ID AL1A1_HUMAN Reviewed; 501 AA.
AC P00352; O00768; Q5SYR1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 224.
DE RecName: Full=Aldehyde dehydrogenase 1A1 {ECO:0000305|PubMed:19296407};
DE EC=1.2.1.19 {ECO:0000250|UniProtKB:P24549};
DE EC=1.2.1.28 {ECO:0000269|PubMed:17175089, ECO:0000269|PubMed:19296407};
DE EC=1.2.1.3 {ECO:0000269|PubMed:12941160, ECO:0000269|PubMed:15623782, ECO:0000269|PubMed:17175089, ECO:0000269|PubMed:19296407};
DE EC=1.2.1.36 {ECO:0000250|UniProtKB:P51647};
DE AltName: Full=3-deoxyglucosone dehydrogenase {ECO:0000305|PubMed:17175089};
DE AltName: Full=ALDH-E1;
DE AltName: Full=ALHDII;
DE AltName: Full=Aldehyde dehydrogenase family 1 member A1 {ECO:0000312|HGNC:HGNC:402};
DE AltName: Full=Aldehyde dehydrogenase, cytosolic {ECO:0000303|PubMed:2591967};
DE AltName: Full=Retinal dehydrogenase 1 {ECO:0000250|UniProtKB:P51647};
DE Short=RALDH 1 {ECO:0000250|UniProtKB:P51647};
DE Short=RalDH1 {ECO:0000250|UniProtKB:P51647};
GN Name=ALDH1A1 {ECO:0000312|HGNC:HGNC:402};
GN Synonyms=ALDC, ALDH1 {ECO:0000312|HGNC:HGNC:402},
GN PUMB1 {ECO:0000312|HGNC:HGNC:402};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2591967; DOI=10.1016/0888-7543(89)90127-4;
RA Hsu L.C., Chang W.-C., Yoshida A.;
RT "Genomic structure of the human cytosolic aldehyde dehydrogenase gene.";
RL Genomics 5:857-865(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-121.
RC TISSUE=Liver;
RX PubMed=8214422; DOI=10.1111/j.1530-0277.1993.tb00849.x;
RA Zheng C.F., Wang T.T., Weiner H.;
RT "Cloning and expression of the full-length cDNAs encoding human liver class
RT 1 and class 2 aldehyde dehydrogenase.";
RL Alcohol. Clin. Exp. Res. 17:828-831(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC TISSUE=Lens;
RX PubMed=19296407; DOI=10.1080/15287390802706371;
RA Xiao T., Shoeb M., Siddiqui M.S., Zhang M., Ramana K.V., Srivastava S.K.,
RA Vasiliou V., Ansari N.H.;
RT "Molecular cloning and oxidative modification of human lens ALDH1A1:
RT implication in impaired detoxification of lipid aldehydes.";
RL J. Toxicol. Environ. Health Part A 72:577-584(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-177.
RG NIEHS SNPs program;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RX PubMed=8493914; DOI=10.1007/978-1-4615-2904-0_5;
RA Yoshida A., Hsu L.C., Yanagawa Y.;
RT "Biological role of human cytosolic aldehyde dehydrogenase 1: hormonal
RT response, retinal oxidation and implication in testicular feminization.";
RL Adv. Exp. Med. Biol. 328:37-44(1993).
RN [10]
RP PROTEIN SEQUENCE OF 2-501, AND ACETYLATION AT SER-2.
RC TISSUE=Liver;
RX PubMed=6723659; DOI=10.1111/j.1432-1033.1984.tb08150.x;
RA Hempel J., von Bahr-Lindstroem H., Joernvall H.;
RT "Aldehyde dehydrogenase from human liver. Primary structure of the
RT cytoplasmic isoenzyme.";
RL Eur. J. Biochem. 141:21-35(1984).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 162-501.
RX PubMed=4015823; DOI=10.1016/0741-8329(85)90024-2;
RA Yoshida A., Ikawa M., Hsu L.C., Tani K.;
RT "Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases.";
RL Alcohol 2:103-106(1985).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 162-501.
RC TISSUE=Liver;
RX PubMed=2987944; DOI=10.1073/pnas.82.11.3771;
RA Hsu L.C., Tani K., Fujiyoshi T., Kurachi K., Yoshida A.;
RT "Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:3771-3775(1985).
RN [13]
RP PROTEIN SEQUENCE OF 266-273, ACTIVE SITE, AND NAD-BINDING.
RX PubMed=3676276; DOI=10.1021/bi00392a015;
RA Abriola D.P., Fields R., Stein S., Mackerell A.D. Jr., Pietruszko R.;
RT "Active site of human liver aldehyde dehydrogenase.";
RL Biochemistry 26:5679-5684(1987).
RN [14]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Erythrocyte;
RX PubMed=2776714; DOI=10.1159/000469006;
RA Agarwal D.P., Cohn P., Goedde H.W., Hempel J.;
RT "Aldehyde dehydrogenase from human erythrocytes: structural relationship to
RT the liver cytosolic isozyme.";
RL Enzyme 42:47-52(1989).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12941160; DOI=10.1089/104454903322216671;
RA Manzer R., Qamar L., Estey T., Pappa A., Petersen D.R., Vasiliou V.;
RT "Molecular cloning and baculovirus expression of the rabbit corneal
RT aldehyde dehydrogenase (ALDH1A1) cDNA.";
RL DNA Cell Biol. 22:329-338(2003).
RN [16]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15623782; DOI=10.1167/iovs.04-0120;
RA Choudhary S., Xiao T., Vergara L.A., Srivastava S., Nees D.,
RA Piatigorsky J., Ansari N.H.;
RT "Role of aldehyde dehydrogenase isozymes in the defense of rat lens and
RT human lens epithelial cells against oxidative stress.";
RL Invest. Ophthalmol. Vis. Sci. 46:259-267(2005).
RN [17]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=17175089; DOI=10.1016/j.biochi.2006.11.005;
RA Collard F., Vertommen D., Fortpied J., Duester G., Van Schaftingen E.;
RT "Identification of 3-deoxyglucosone dehydrogenase as aldehyde dehydrogenase
RT 1A1 (retinaldehyde dehydrogenase 1).";
RL Biochimie 89:369-373(2007).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-91; LYS-128; LYS-252; LYS-353;
RP LYS-367; LYS-410; LYS-419; LYS-435 AND LYS-495, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-337 AND SER-413, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP INTERACTION WITH PRMT3, AND REGION.
RX PubMed=33495566; DOI=10.1038/s42003-020-01644-3;
RA Verma M., Khan M.I.K., Kadumuri R.V., Chakrapani B., Awasthi S., Mahesh A.,
RA Govindaraju G., Chavali P.L., Rajavelu A., Chavali S., Dhayalan A.;
RT "PRMT3 interacts with ALDH1A1 and regulates gene-expression by inhibiting
RT retinoic acid signaling.";
RL Commun. Biol. 4:109-109(2021).
RN [23] {ECO:0007744|PDB:5AC2}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH DUOCARMYCIN ANALOG,
RP FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF CYS-302.
RX PubMed=26373694; DOI=10.1002/anie.201505749;
RA Koch M.F., Harteis S., Blank I.D., Pestel G., Tietze L.F., Ochsenfeld C.,
RA Schneider S., Sieber S.A.;
RT "Structural, biochemical, and computational studies reveal the mechanism of
RT selective aldehyde dehydrogenase 1A1 inhibition by cytotoxic duocarmycin
RT analogues.";
RL Angew. Chem. Int. Ed. Engl. 54:13550-13554(2015).
RN [24] {ECO:0007744|PDB:4WB9, ECO:0007744|PDB:4WJ9}
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF VARIANT SER-121 ALONE AND IN
RP COMPLEX WITH NADH, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=25450233; DOI=10.1016/j.cbi.2014.10.028;
RA Morgan C.A., Hurley T.D.;
RT "Development of a high-throughput in vitro assay to identify selective
RT inhibitors for human ALDH1A1.";
RL Chem. Biol. Interact. 234:29-37(2015).
RN [25] {ECO:0007744|PDB:4WP7, ECO:0007744|PDB:4WPN, ECO:0007744|PDB:4X4L}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITORS,
RP AND MUTAGENESIS OF GLY-458.
RX PubMed=25634381; DOI=10.1021/jm501900s;
RA Morgan C.A., Hurley T.D.;
RT "Characterization of two distinct structural classes of selective aldehyde
RT dehydrogenase 1A1 inhibitors.";
RL J. Med. Chem. 58:1964-1975(2015).
CC -!- FUNCTION: Cytosolic dehydrogenase that catalyzes the irreversible
CC oxidation of a wide range of aldehydes to their corresponding
CC carboxylic acid (PubMed:19296407, PubMed:12941160, PubMed:15623782,
CC PubMed:17175089, PubMed:26373694, PubMed:25450233). Functions
CC downstream of retinol dehydrogenases and catalyzes the oxidation of
CC retinaldehyde into retinoic acid, the second step in the oxidation of
CC retinol/vitamin A into retinoic acid (By similarity). This pathway is
CC crucial to control the levels of retinol and retinoic acid, two
CC important molecules which excess can be teratogenic and cytotoxic (By
CC similarity). Also oxidizes aldehydes resulting from lipid peroxidation
CC like (E)-4-hydroxynon-2-enal/HNE, malonaldehyde and hexanal that form
CC protein adducts and are highly cytotoxic. By participating for instance
CC to the clearance of (E)-4-hydroxynon-2-enal/HNE in the lens epithelium
CC prevents the formation of HNE-protein adducts and lens opacification
CC (PubMed:19296407, PubMed:12941160, PubMed:15623782). Functions also
CC downstream of fructosamine-3-kinase in the fructosamine degradation
CC pathway by catalyzing the oxidation of 3-deoxyglucosone, the
CC carbohydrate product of fructosamine 3-phosphate decomposition, which
CC is itself a potent glycating agent that may react with lysine and
CC arginine side-chains of proteins (PubMed:17175089). Has also an
CC aminobutyraldehyde dehydrogenase activity and is probably part of an
CC alternative pathway for the biosynthesis of GABA/4-aminobutanoate in
CC midbrain, thereby playing a role in GABAergic synaptic transmission (By
CC similarity). {ECO:0000250|UniProtKB:P24549,
CC ECO:0000269|PubMed:12941160, ECO:0000269|PubMed:15623782,
CC ECO:0000269|PubMed:17175089, ECO:0000269|PubMed:19296407,
CC ECO:0000269|PubMed:25450233, ECO:0000269|PubMed:26373694}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3; Evidence={ECO:0000269|PubMed:12941160,
CC ECO:0000269|PubMed:15623782, ECO:0000269|PubMed:17175089,
CC ECO:0000269|PubMed:19296407};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16186;
CC Evidence={ECO:0000305|PubMed:19296407};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2
CC H(+) + NADH; Xref=Rhea:RHEA:42080, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17898, ChEBI:CHEBI:35291,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.36;
CC Evidence={ECO:0000250|UniProtKB:P51647};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42081;
CC Evidence={ECO:0000250|UniProtKB:P51647};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-cis-retinal + H2O + NAD(+) = 9-cis-retinoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:42084, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78273,
CC ChEBI:CHEBI:78630; Evidence={ECO:0000250|UniProtKB:P51647};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42085;
CC Evidence={ECO:0000250|UniProtKB:P51647};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-cis-retinal + H2O + NAD(+) = 11-cis-retinoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:47132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16066, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:87435; Evidence={ECO:0000250|UniProtKB:P51647};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47133;
CC Evidence={ECO:0000250|UniProtKB:P51647};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-cis-retinal + H2O + NAD(+) = 13-cis-retinoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:67332, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:45487, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:169952; Evidence={ECO:0000250|UniProtKB:Q8HYE4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67333;
CC Evidence={ECO:0000250|UniProtKB:Q8HYE4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-deoxyglucosone + H2O + NAD(+) = 2-dehydro-3-deoxy-D-
CC gluconate + 2 H(+) + NADH; Xref=Rhea:RHEA:67244, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:57990, ChEBI:CHEBI:60777;
CC Evidence={ECO:0000269|PubMed:17175089};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67245;
CC Evidence={ECO:0000305|PubMed:17175089};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-hydroxynon-2-enal + H2O + NAD(+) = (E)-4-hydroxynon-2-
CC enoate + 2 H(+) + NADH; Xref=Rhea:RHEA:67248, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58968, ChEBI:CHEBI:142920;
CC Evidence={ECO:0000269|PubMed:12941160, ECO:0000269|PubMed:15623782,
CC ECO:0000269|PubMed:19296407};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67249;
CC Evidence={ECO:0000269|PubMed:15623782};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + malonaldehyde + NAD(+) = 3-oxopropanoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:67252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33190, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:566274; Evidence={ECO:0000269|PubMed:12941160,
CC ECO:0000269|PubMed:19296407};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67253;
CC Evidence={ECO:0000305|PubMed:19296407};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexanal + NAD(+) = 2 H(+) + hexanoate + NADH;
CC Xref=Rhea:RHEA:67276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17120, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:88528; Evidence={ECO:0000269|PubMed:12941160};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67277;
CC Evidence={ECO:0000305|PubMed:12941160};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + propanal = 2 H(+) + NADH + propanoate;
CC Xref=Rhea:RHEA:67256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17153, ChEBI:CHEBI:17272, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:12941160,
CC ECO:0000269|PubMed:19296407};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67257;
CC Evidence={ECO:0000305|PubMed:19296407};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetaldehyde + H2O + NAD(+) = acetate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:25294, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000269|PubMed:19296407};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25295;
CC Evidence={ECO:0000305|PubMed:19296407};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:11840, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16150, ChEBI:CHEBI:17169, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.28;
CC Evidence={ECO:0000269|PubMed:17175089, ECO:0000269|PubMed:19296407};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11841;
CC Evidence={ECO:0000305|PubMed:19296407};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264,
CC ChEBI:CHEBI:59888; EC=1.2.1.19;
CC Evidence={ECO:0000250|UniProtKB:P24549};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106;
CC Evidence={ECO:0000250|UniProtKB:P24549};
CC -!- ACTIVITY REGULATION: Inhibited by citral, disulfiram, and cyanamide.
CC Activated by diethylstilbestrol (PubMed:19296407). Inhibited by
CC duocarmycin analogs (PubMed:26373694). {ECO:0000269|PubMed:19296407,
CC ECO:0000269|PubMed:26373694}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=59.4 uM for NAD (at pH 8.0) {ECO:0000269|PubMed:19296407};
CC KM=85 uM for NAD (at pH 7.1 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:17175089};
CC KM=2 uM for benzaldehyde (at pH 7.1 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:17175089};
CC KM=4.8 uM for (E)-4-hydroxynon-2-enal (at pH 8.0)
CC {ECO:0000269|PubMed:19296407};
CC KM=17.9 uM for (E)-4-hydroxynon-2-enal (at pH 8.0 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:12941160};
CC KM=114.4 uM for malonaldehyde (at pH 8.0 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:12941160};
CC KM=3.5 uM for malonaldehyde (at pH 8.0)
CC {ECO:0000269|PubMed:19296407};
CC KM=95 uM for 3-deoxyglucosone (at pH 7.1 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:17175089};
CC KM=238.2 uM for acetaldehyde (at pH 8.0)
CC {ECO:0000269|PubMed:19296407};
CC KM=121.4 uM for propanal (at pH 8.0) {ECO:0000269|PubMed:19296407};
CC KM=137.2 uM for propanal (at pH 8.0 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:12941160};
CC KM=15 uM for propanal (at pH 7.5) {ECO:0000269|PubMed:25450233};
CC KM=13.4 uM for hexanal (at pH 8.0 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:12941160};
CC KM=142.2 uM for benzaldehyde (at pH 8.0)
CC {ECO:0000269|PubMed:19296407};
CC KM=177.1 uM for trans-2-heptenal (at pH 8.0)
CC {ECO:0000269|PubMed:19296407};
CC Vmax=254.6 nmol/min/mg enzyme with (E)-4-hydroxynon-2-enal (at pH 8.0
CC and 25 degrees Celsius) {ECO:0000269|PubMed:12941160};
CC Vmax=135 nmol/min/mg enzyme with (E)-4-hydroxynon-2-enal (at pH 8.0)
CC {ECO:0000269|PubMed:19296407};
CC Vmax=564.9 nmol/min/mg enzyme with malonaldehyde (at pH 8.0 and 25
CC degrees Celsius) {ECO:0000269|PubMed:12941160};
CC Vmax=381.6 nmol/min/mg enzyme with malonaldehyde (at pH 8.0)
CC {ECO:0000269|PubMed:19296407};
CC Vmax=45 nmol/min/mg enzyme with 3-deoxyglucosone (at pH 7.1 and 30
CC degrees Celsius) {ECO:0000269|PubMed:17175089};
CC Vmax=631.4 nmol/min/mg enzyme with acetaldehyde (at pH 8.0)
CC {ECO:0000269|PubMed:19296407};
CC Vmax=747.3 nmol/min/mg enzyme with propanal (at pH 8.0 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:12941160};
CC Vmax=445.3 nmol/min/mg enzyme with propanal (at pH 8.0)
CC {ECO:0000269|PubMed:19296407};
CC Vmax=707.1 nmol/min/mg enzyme with hexanal (at pH 8.0 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:12941160};
CC Vmax=750.3 nmol/min/mg enzyme with benzaldehyde (at pH 8.0)
CC {ECO:0000269|PubMed:19296407};
CC Vmax=72 nmol/min/mg enzyme with benzaldehyde (at pH 7.1 and 30
CC degrees Celsius) {ECO:0000269|PubMed:17175089};
CC Vmax=155.8 nmol/min/mg enzyme with trans-2-heptenal (at pH 8.0)
CC {ECO:0000269|PubMed:19296407};
CC pH dependence:
CC Optimum pH is 7.1-9 for the 3-deoxyglucosone dehydrogenase activity.
CC {ECO:0000269|PubMed:17175089};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000250|UniProtKB:P51647}.
CC -!- SUBUNIT: Homotetramer (By similarity). Interacts with PRMT3; the
CC interaction is direct, inhibits ALDH1A1 aldehyde dehydrogenase activity
CC and is independent of the methyltransferase activity of PRMT3
CC (PubMed:33495566). {ECO:0000250|UniProtKB:P51977,
CC ECO:0000269|PubMed:33495566}.
CC -!- INTERACTION:
CC P00352; P09172: DBH; NbExp=3; IntAct=EBI-752170, EBI-8589586;
CC P00352; P14136: GFAP; NbExp=3; IntAct=EBI-752170, EBI-744302;
CC P00352; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-752170, EBI-1055254;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12941160}.
CC Cell projection, axon {ECO:0000250|UniProtKB:P24549}.
CC -!- TISSUE SPECIFICITY: Expressed by erythrocytes (at protein level).
CC {ECO:0000269|PubMed:17175089}.
CC -!- PTM: The N-terminus is blocked most probably by acetylation.
CC {ECO:0000250|UniProtKB:P15437}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/aldh1a1/";
CC ---------------------------------------------------------------------------
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DR EMBL; M31994; AAA51692.1; -; Genomic_DNA.
DR EMBL; M31982; AAA51692.1; JOINED; Genomic_DNA.
DR EMBL; M31983; AAA51692.1; JOINED; Genomic_DNA.
DR EMBL; M31984; AAA51692.1; JOINED; Genomic_DNA.
DR EMBL; M31985; AAA51692.1; JOINED; Genomic_DNA.
DR EMBL; M31986; AAA51692.1; JOINED; Genomic_DNA.
DR EMBL; M31987; AAA51692.1; JOINED; Genomic_DNA.
DR EMBL; M31988; AAA51692.1; JOINED; Genomic_DNA.
DR EMBL; M31989; AAA51692.1; JOINED; Genomic_DNA.
DR EMBL; M31990; AAA51692.1; JOINED; Genomic_DNA.
DR EMBL; M31991; AAA51692.1; JOINED; Genomic_DNA.
DR EMBL; M31992; AAA51692.1; JOINED; Genomic_DNA.
DR EMBL; AF003341; AAC51652.1; -; mRNA.
DR EMBL; AY390731; AAR92229.1; -; mRNA.
DR EMBL; BT006921; AAP35567.1; -; mRNA.
DR EMBL; AY338497; AAP88039.1; -; Genomic_DNA.
DR EMBL; AL591031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471089; EAW62543.1; -; Genomic_DNA.
DR EMBL; BC001505; AAH01505.1; -; mRNA.
DR EMBL; S61235; AAD13925.1; -; Genomic_DNA.
DR EMBL; M26761; AAA35518.1; -; mRNA.
DR EMBL; K03000; AAA51695.1; -; mRNA.
DR CCDS; CCDS6644.1; -.
DR PIR; A33371; DEHUE1.
DR RefSeq; NP_000680.2; NM_000689.4.
DR PDB; 4WB9; X-ray; 2.07 A; A=1-501.
DR PDB; 4WJ9; X-ray; 1.74 A; A=1-501.
DR PDB; 4WP7; X-ray; 1.80 A; A=1-501.
DR PDB; 4WPN; X-ray; 1.95 A; A=1-501.
DR PDB; 4X4L; X-ray; 1.85 A; A=1-501.
DR PDB; 5AC2; X-ray; 1.85 A; A=1-501.
DR PDB; 5L2M; X-ray; 1.70 A; A=1-501.
DR PDB; 5L2N; X-ray; 1.70 A; A=1-501.
DR PDB; 5L2O; X-ray; 2.05 A; A/B/C/D/E/F/G/H=1-501.
DR PDB; 5TEI; X-ray; 2.10 A; A=1-501.
DR PDB; 6DUM; X-ray; 2.00 A; A=1-501.
DR PDB; 7JWS; X-ray; 1.60 A; A=1-501.
DR PDB; 7JWT; X-ray; 1.80 A; A=1-501.
DR PDB; 7JWU; X-ray; 1.90 A; A=1-501.
DR PDB; 7JWV; X-ray; 1.60 A; A=1-501.
DR PDB; 7JWW; X-ray; 1.60 A; A=1-501.
DR PDB; 7UM9; X-ray; 1.80 A; A=1-501.
DR PDB; 8D46; EM; 2.84 A; A/B/C/D=1-501.
DR PDB; 8DNO; EM; 3.40 A; A/B/C/D=1-501.
DR PDB; 8ENE; EM; 2.64 A; A/B/C/D=1-501.
DR PDB; 8PVH; EM; 2.90 A; A=2-501.
DR PDB; 8WFQ; X-ray; 3.50 A; A/B/C/D/E/F/G/H=1-501.
DR PDBsum; 4WB9; -.
DR PDBsum; 4WJ9; -.
DR PDBsum; 4WP7; -.
DR PDBsum; 4WPN; -.
DR PDBsum; 4X4L; -.
DR PDBsum; 5AC2; -.
DR PDBsum; 5L2M; -.
DR PDBsum; 5L2N; -.
DR PDBsum; 5L2O; -.
DR PDBsum; 5TEI; -.
DR PDBsum; 6DUM; -.
DR PDBsum; 7JWS; -.
DR PDBsum; 7JWT; -.
DR PDBsum; 7JWU; -.
DR PDBsum; 7JWV; -.
DR PDBsum; 7JWW; -.
DR PDBsum; 7UM9; -.
DR PDBsum; 8D46; -.
DR PDBsum; 8DNO; -.
DR PDBsum; 8ENE; -.
DR PDBsum; 8PVH; -.
DR PDBsum; 8WFQ; -.
DR AlphaFoldDB; P00352; -.
DR EMDB; EMD-17966; -.
DR EMDB; EMD-27176; -.
DR EMDB; EMD-27575; -.
DR EMDB; EMD-28271; -.
DR SMR; P00352; -.
DR BioGRID; 106718; 69.
DR IntAct; P00352; 12.
DR STRING; 9606.ENSP00000297785; -.
DR BindingDB; P00352; -.
DR ChEMBL; CHEMBL3577; -.
DR DrugBank; DB04447; 1,4-Dithiothreitol.
DR DrugBank; DB09462; Glycerin.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB00755; Tretinoin.
DR DrugBank; DB00162; Vitamin A.
DR DrugCentral; P00352; -.
DR GlyGen; P00352; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P00352; -.
DR MetOSite; P00352; -.
DR PhosphoSitePlus; P00352; -.
DR SwissPalm; P00352; -.
DR BioMuta; ALDH1A1; -.
DR DMDM; 118495; -.
DR DOSAC-COBS-2DPAGE; P00352; -.
DR REPRODUCTION-2DPAGE; IPI00218914; -.
DR REPRODUCTION-2DPAGE; P00352; -.
DR SWISS-2DPAGE; P00352; -.
DR UCD-2DPAGE; P00352; -.
DR EPD; P00352; -.
DR jPOST; P00352; -.
DR MassIVE; P00352; -.
DR PaxDb; 9606-ENSP00000297785; -.
DR PeptideAtlas; P00352; -.
DR ProteomicsDB; 51235; -.
DR Pumba; P00352; -.
DR Antibodypedia; 1064; 1149 antibodies from 47 providers.
DR DNASU; 216; -.
DR Ensembl; ENST00000297785.8; ENSP00000297785.3; ENSG00000165092.13.
DR GeneID; 216; -.
DR KEGG; hsa:216; -.
DR MANE-Select; ENST00000297785.8; ENSP00000297785.3; NM_000689.5; NP_000680.2.
DR AGR; HGNC:402; -.
DR CTD; 216; -.
DR DisGeNET; 216; -.
DR GeneCards; ALDH1A1; -.
DR HGNC; HGNC:402; ALDH1A1.
DR HPA; ENSG00000165092; Tissue enhanced (liver).
DR MIM; 100640; gene.
DR neXtProt; NX_P00352; -.
DR OpenTargets; ENSG00000165092; -.
DR PharmGKB; PA24692; -.
DR VEuPathDB; HostDB:ENSG00000165092; -.
DR eggNOG; KOG2450; Eukaryota.
DR GeneTree; ENSGT00940000154609; -.
DR HOGENOM; CLU_005391_0_2_1; -.
DR InParanoid; P00352; -.
DR OMA; GTYAINW; -.
DR OrthoDB; 2291791at2759; -.
DR PhylomeDB; P00352; -.
DR TreeFam; TF300455; -.
DR BioCyc; MetaCyc:HS09183-MONOMER; -.
DR BRENDA; 1.2.1.36; 2681.
DR PathwayCommons; P00352; -.
DR Reactome; R-HSA-5365859; RA biosynthesis pathway.
DR Reactome; R-HSA-70350; Fructose catabolism.
DR Reactome; R-HSA-71384; Ethanol oxidation.
DR SABIO-RK; P00352; -.
DR SignaLink; P00352; -.
DR SIGNOR; P00352; -.
DR UniPathway; UPA00912; -.
DR BioGRID-ORCS; 216; 10 hits in 1159 CRISPR screens.
DR ChiTaRS; ALDH1A1; human.
DR GeneWiki; ALDH1A1; -.
DR GenomeRNAi; 216; -.
DR Pharos; P00352; Tchem.
DR PRO; PR:P00352; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P00352; Protein.
DR Bgee; ENSG00000165092; Expressed in bronchial epithelial cell and 201 other cell types or tissues.
DR ExpressionAtlas; P00352; baseline and differential.
DR Genevisible; P00352; HS.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0106373; F:3-deoxyglucosone dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0005497; F:androgen binding; TAS:ProtInc.
DR GO; GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:RHEA.
DR GO; GO:0005096; F:GTPase activator activity; TAS:UniProtKB.
DR GO; GO:0051287; F:NAD binding; ISS:CAFA.
DR GO; GO:0001758; F:retinal dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; TAS:ProtInc.
DR GO; GO:0110095; P:cellular detoxification of aldehyde; IMP:UniProtKB.
DR GO; GO:0030392; P:fructosamine catabolic process; IDA:UniProtKB.
DR GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0036438; P:maintenance of lens transparency; ISS:UniProtKB.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0001523; P:retinoid metabolic process; ISS:UniProtKB.
DR GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07141; ALDH_F1AB_F2_RALDH1; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR PANTHER; PTHR11699:SF140; ALDEHYDE DEHYDROGENASE 1A1; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell projection; Cytoplasm;
KW Direct protein sequencing; Lipid metabolism; NAD; Nucleotide-binding;
KW Oxidoreductase; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6723659,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..501
FT /note="Aldehyde dehydrogenase 1A1"
FT /id="PRO_0000056415"
FT REGION 336..501
FT /note="Mediates interaction with PRMT3"
FT /evidence="ECO:0000269|PubMed:33495566"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008,
FT ECO:0000269|PubMed:3676276"
FT ACT_SITE 303
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008,
FT ECO:0000269|PubMed:3676276"
FT BINDING 167..170
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:25450233,
FT ECO:0000269|PubMed:25634381, ECO:0007744|PDB:4WB9,
FT ECO:0007744|PDB:4X4L"
FT BINDING 193..196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:25450233,
FT ECO:0000269|PubMed:25634381, ECO:0007744|PDB:4WB9,
FT ECO:0007744|PDB:4X4L"
FT BINDING 226..227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:25450233,
FT ECO:0000269|PubMed:25634381, ECO:0007744|PDB:4WB9,
FT ECO:0007744|PDB:4X4L"
FT BINDING 246..247
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:25450233,
FT ECO:0000269|PubMed:25634381, ECO:0007744|PDB:4WB9,
FT ECO:0007744|PDB:4X4L"
FT BINDING 269..271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:25450233,
FT ECO:0000269|PubMed:25634381, ECO:0007744|PDB:4WB9,
FT ECO:0007744|PDB:4X4L"
FT BINDING 349..353
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:25450233,
FT ECO:0000269|PubMed:25634381, ECO:0007744|PDB:4WB9,
FT ECO:0007744|PDB:4X4L"
FT BINDING 400..402
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:25450233,
FT ECO:0000269|PubMed:25634381, ECO:0007744|PDB:4WB9,
FT ECO:0007744|PDB:4X4L"
FT SITE 170
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P20000"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:6723659,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 91
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 252
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 337
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 353
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 367
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 410
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 419
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 435
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 495
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 121
FT /note="N -> S (in dbSNP:rs1049981)"
FT /evidence="ECO:0000269|PubMed:8214422"
FT /id="VAR_048901"
FT VARIANT 125
FT /note="G -> R (in dbSNP:rs11554423)"
FT /id="VAR_048902"
FT VARIANT 177
FT /note="I -> F (in dbSNP:rs8187929)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_017778"
FT MUTAGEN 302
FT /note="C->A,S: Does not prevent inhibition by duocarmycin
FT analogs."
FT /evidence="ECO:0000269|PubMed:26373694"
FT MUTAGEN 458
FT /note="G->N: No significant effect on aldehyde
FT dehydrogenase activity. Prevents the inhibition by ALDH1A1-
FT specific inhibitors."
FT /evidence="ECO:0000269|PubMed:25634381"
FT CONFLICT 162
FT /note="V -> I (in Ref. 11; AAA35518 and 12; AAA51695)"
FT /evidence="ECO:0000305"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:7JWS"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:7JWS"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:7JWS"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:7JWS"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:7JWS"
FT HELIX 57..70
FT /evidence="ECO:0007829|PDB:7JWS"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:7JWS"
FT HELIX 82..98
FT /evidence="ECO:0007829|PDB:7JWS"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:7JWS"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:7JWS"
FT HELIX 122..136
FT /evidence="ECO:0007829|PDB:7JWS"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:7JWS"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:5L2O"
FT STRAND 148..159
FT /evidence="ECO:0007829|PDB:7JWS"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:7JWS"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:7JWS"
FT HELIX 172..185
FT /evidence="ECO:0007829|PDB:7JWS"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:7JWS"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:8ENE"
FT HELIX 200..212
FT /evidence="ECO:0007829|PDB:7JWS"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:7JWS"
FT HELIX 226..234
FT /evidence="ECO:0007829|PDB:7JWS"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:7JWS"
FT HELIX 248..260
FT /evidence="ECO:0007829|PDB:7JWS"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:8ENE"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:7JWS"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:7JWS"
FT HELIX 284..296
FT /evidence="ECO:0007829|PDB:7JWS"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:7JWS"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:7JWS"
FT HELIX 313..327
FT /evidence="ECO:0007829|PDB:7JWS"
FT HELIX 348..363
FT /evidence="ECO:0007829|PDB:7JWS"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:7JWS"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:7JWS"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:7JWS"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:7JWS"
FT STRAND 403..412
FT /evidence="ECO:0007829|PDB:7JWS"
FT HELIX 414..422
FT /evidence="ECO:0007829|PDB:7JWS"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:8ENE"
FT STRAND 428..433
FT /evidence="ECO:0007829|PDB:7JWS"
FT HELIX 437..446
FT /evidence="ECO:0007829|PDB:7JWS"
FT STRAND 450..455
FT /evidence="ECO:0007829|PDB:7JWS"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:7JWS"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:7JWS"
FT HELIX 479..483
FT /evidence="ECO:0007829|PDB:7JWS"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:7JWS"
FT STRAND 487..495
FT /evidence="ECO:0007829|PDB:7JWS"
SQ SEQUENCE 501 AA; 54862 MW; B26464DC7168348E CRC64;
MSSSGTPDLP VLLTDLKIQY TKIFINNEWH DSVSGKKFPV FNPATEEELC QVEEGDKEDV
DKAVKAARQA FQIGSPWRTM DASERGRLLY KLADLIERDR LLLATMESMN GGKLYSNAYL
NDLAGCIKTL RYCAGWADKI QGRTIPIDGN FFTYTRHEPI GVCGQIIPWN FPLVMLIWKI
GPALSCGNTV VVKPAEQTPL TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDID
KVAFTGSTEV GKLIKEAAGK SNLKRVTLEL GGKSPCIVLA DADLDNAVEF AHHGVFYHQG
QCCIAASRIF VEESIYDEFV RRSVERAKKY ILGNPLTPGV TQGPQIDKEQ YDKILDLIES
GKKEGAKLEC GGGPWGNKGY FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSLDDVIKR
ANNTFYGLSA GVFTKDIDKA ITISSALQAG TVWVNCYGVV SAQCPFGGFK MSGNGRELGE
YGFHEYTEVK TVTVKISQKN S
//
