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Database: UniProt/SWISS-PROT
Entry: ALDH2_BOVIN
LinkDB: ALDH2_BOVIN
Original site: ALDH2_BOVIN 
ID   ALDH2_BOVIN             Reviewed;         520 AA.
AC   P20000; Q1LZC6;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   12-AUG-2020, entry version 151.
DE   RecName: Full=Aldehyde dehydrogenase, mitochondrial;
DE            EC=1.2.1.3;
DE   AltName: Full=ALDH class 2;
DE   AltName: Full=ALDH-E2;
DE   AltName: Full=ALDHI;
DE   Flags: Precursor;
GN   Name=ALDH2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=1689984; DOI=10.1016/0003-9861(90)90590-u;
RA   Guan K., Weiner H.;
RT   "Sequence of the precursor of bovine liver mitochondrial aldehyde
RT   dehydrogenase as determined from its cDNA, its gene, and its
RT   functionality.";
RL   Arch. Biochem. Biophys. 277:351-360(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 92-520.
RX   PubMed=2540003; DOI=10.1111/j.1432-1033.1989.tb14616.x;
RA   Farres J., Guan K.-L., Weiner H.;
RT   "Primary structures of rat and bovine liver mitochondrial aldehyde
RT   dehydrogenases deduced from cDNA sequences.";
RL   Eur. J. Biochem. 180:67-74(1989).
RN   [4]
RP   PROTEIN SEQUENCE OF 22-34.
RC   TISSUE=Brain;
RX   PubMed=1449496; DOI=10.1016/0006-291x(92)91530-4;
RA   Lee J.E., Cho Y.D.;
RT   "Purification and characterization of bovine brain gamma-aminobutyraldehyde
RT   dehydrogenase.";
RL   Biochem. Biophys. Res. Commun. 189:450-454(1992).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 22-520 IN COMPLEX WITH NAD, AND
RP   SITE.
RX   PubMed=9195888; DOI=10.1016/s0969-2126(97)00224-4;
RA   Steinmetz C.G., Xie P., Weiner H., Hurley T.D.;
RT   "Structure of mitochondrial aldehyde dehydrogenase: the genetic component
RT   of ethanol aversion.";
RL   Structure 5:701-711(1997).
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;
CC   -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol:
CC       step 2/2.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
DR   EMBL; BC116084; AAI16085.1; -; mRNA.
DR   PIR; S09030; S09030.
DR   RefSeq; NP_001068835.1; NM_001075367.1.
DR   PDB; 1A4Z; X-ray; 2.75 A; A/B/C/D=22-520.
DR   PDB; 1AG8; X-ray; 2.65 A; A/B/C/D=22-520.
DR   PDBsum; 1A4Z; -.
DR   PDBsum; 1AG8; -.
DR   SMR; P20000; -.
DR   STRING; 9913.ENSBTAP00000011521; -.
DR   PaxDb; P20000; -.
DR   PeptideAtlas; P20000; -.
DR   PRIDE; P20000; -.
DR   Ensembl; ENSBTAT00000011521; ENSBTAP00000011521; ENSBTAG00000008743.
DR   GeneID; 508629; -.
DR   KEGG; bta:508629; -.
DR   CTD; 217; -.
DR   eggNOG; KOG2450; Eukaryota.
DR   GeneTree; ENSGT00940000156240; -.
DR   HOGENOM; CLU_005391_0_1_1; -.
DR   InParanoid; P20000; -.
DR   KO; K00128; -.
DR   OMA; NYIVGGL; -.
DR   OrthoDB; 153834at2759; -.
DR   TreeFam; TF300455; -.
DR   Reactome; R-BTA-380612; Metabolism of serotonin.
DR   Reactome; R-BTA-71384; Ethanol oxidation.
DR   SABIO-RK; P20000; -.
DR   UniPathway; UPA00780; UER00768.
DR   EvolutionaryTrace; P20000; -.
DR   Proteomes; UP000009136; Chromosome 17.
DR   Bgee; ENSBTAG00000008743; Expressed in lung and 18 other tissues.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; ISS:CAFA.
DR   GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 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   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 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; Direct protein sequencing; Mitochondrion; NAD;
KW   Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT         1..21
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:1449496"
FT   CHAIN           22..520
FT                   /note="Aldehyde dehydrogenase, mitochondrial"
FT                   /id="PRO_0000007167"
FT   NP_BIND         186..188
FT                   /note="NAD"
FT                   /evidence="ECO:0000244|PDB:1A4Z,
FT                   ECO:0000269|PubMed:9195888"
FT   NP_BIND         212..215
FT                   /note="NAD"
FT                   /evidence="ECO:0000244|PDB:1A4Z,
FT                   ECO:0000269|PubMed:9195888"
FT   NP_BIND         265..270
FT                   /note="NAD"
FT                   /evidence="ECO:0000244|PDB:1A4Z,
FT                   ECO:0000269|PubMed:9195888"
FT   NP_BIND         419..421
FT                   /note="NAD"
FT                   /evidence="ECO:0000244|PDB:1A4Z,
FT                   ECO:0000269|PubMed:9195888"
FT   ACT_SITE        288
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000305|PubMed:9195888"
FT   ACT_SITE        322
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305|PubMed:9195888"
FT   BINDING         245
FT                   /note="NAD; via carbonyl oxygen"
FT                   /evidence="ECO:0000244|PDB:1A4Z,
FT                   ECO:0000269|PubMed:9195888"
FT   BINDING         288
FT                   /note="NAD"
FT                   /evidence="ECO:0000244|PDB:1A4Z,
FT                   ECO:0000269|PubMed:9195888"
FT   SITE            189
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000269|PubMed:9195888"
FT   MOD_RES         55
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
FT   MOD_RES         76
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
FT   MOD_RES         162
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
FT   MOD_RES         371
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
FT   MOD_RES         378
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
FT   MOD_RES         386
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
FT   MOD_RES         429
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
FT   MOD_RES         431
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
FT   MOD_RES         444
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
FT   MOD_RES         454
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
FT   CONFLICT        289
FT                   /note="L -> I (in Ref. 1; no nucleotide entry and 3; no
FT                   nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        385
FT                   /note="A -> L (in Ref. 1; no nucleotide entry and 3; no
FT                   nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        409
FT                   /note="V -> L (in Ref. 1; no nucleotide entry and 3; no
FT                   nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   STRAND          41..46
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   STRAND          47..49
FT                   /evidence="ECO:0000244|PDB:1A4Z"
FT   STRAND          56..60
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   TURN            62..64
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   STRAND          67..72
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   HELIX           76..89
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   HELIX           95..98
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   HELIX           101..117
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   HELIX           119..130
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   HELIX           134..139
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   HELIX           141..153
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   TURN            154..158
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   STRAND          161..164
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   STRAND          167..178
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   STRAND          181..185
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   STRAND          188..190
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   HELIX           191..205
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   STRAND          208..213
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   HELIX           219..231
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   STRAND          237..243
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   HELIX           245..253
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   STRAND          260..265
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   HELIX           267..279
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   STRAND          284..288
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   STRAND          294..297
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   HELIX           303..315
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   HELIX           316..319
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   STRAND          327..331
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   HELIX           332..348
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   HELIX           367..383
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   STRAND          386..389
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   STRAND          392..394
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   STRAND          396..398
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   STRAND          404..408
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   HELIX           414..417
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   STRAND          422..430
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   HELIX           433..441
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   STRAND          447..452
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   HELIX           456..465
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   STRAND          469..474
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   STRAND          492..494
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   HELIX           500..503
FT                   /evidence="ECO:0000244|PDB:1AG8"
FT   STRAND          506..514
FT                   /evidence="ECO:0000244|PDB:1AG8"
SQ   SEQUENCE   520 AA;  56653 MW;  713FC1EE8F82B2C4 CRC64;
     MLRAVALAAA RLGPRQGRRL LSAATQAVPT PNQQPEVLYN QIFINNEWHD AVSKKTFPTV
     NPSTGDVICH VAEGDKADVD RAVKAARAAF QLGSPWRRMD ASERGRLLNR LADLIERDRT
     YLAALETLDN GKPYIISYLV DLDMVLKCLR YYAGWADKYH GKTIPIDGDY FSYTRHEPVG
     VCGQIIPWNF PLLMQAWKLG PALATGNVVV MKVAEQTPLT ALYVANLIKE AGFPPGVVNV
     IPGFGPTAGA AIASHEDVDK VAFTGSTEVG HLIQVAAGKS NLKRVTLELG GKSPNIIMSD
     ADMDWAVEQA HFALFFNQGQ CCCAGSRTFV QEDIYAEFVE RSVARAKSRV VGNPFDSRTE
     QGPQVDETQF KKVLGYIKSG KEEGAKLLCG GGAAADRGYF IQPTVFGDVQ DGMTIAKEEI
     FGPVMQILKF KSMEEVVGRA NNSKYGLAAA VFTKDLDKAN YLSQALQAGT VWVNCYDVFG
     AQSPFGGYKL SGSGRELGEY GLQAYTEVKT VTVRVPQKNS
//
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