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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   13-FEB-2019, entry version 144.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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-
RT   aminobutyraldehyde 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,
RP   AND 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
RT   component of ethanol aversion.";
RL   Structure 5:701-711(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3;
CC   -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from
CC       ethanol: 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   UniGene; Bt.44041; -.
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   ProteinModelPortal; P20000; -.
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   eggNOG; COG1012; LUCA.
DR   GeneTree; ENSGT00940000156240; -.
DR   HOGENOM; HOG000271505; -.
DR   HOVERGEN; HBG000097; -.
DR   InParanoid; P20000; -.
DR   KO; K00128; -.
DR   OMA; TFVQEDV; -.
DR   OrthoDB; 153834at2759; -.
DR   TreeFam; TF300455; -.
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 9 organ(s), highest expression level in liver.
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; Complete proteome;
KW   Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase;
KW   Reference proteome; Transit peptide.
FT   TRANSIT       1     21       Mitochondrion.
FT                                {ECO:0000269|PubMed:1449496}.
FT   CHAIN        22    520       Aldehyde dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000007167.
FT   NP_BIND     186    188       NAD. {ECO:0000244|PDB:1A4Z,
FT                                ECO:0000269|PubMed:9195888}.
FT   NP_BIND     212    215       NAD. {ECO:0000244|PDB:1A4Z,
FT                                ECO:0000269|PubMed:9195888}.
FT   NP_BIND     265    270       NAD. {ECO:0000244|PDB:1A4Z,
FT                                ECO:0000269|PubMed:9195888}.
FT   NP_BIND     419    421       NAD. {ECO:0000244|PDB:1A4Z,
FT                                ECO:0000269|PubMed:9195888}.
FT   ACT_SITE    288    288       Proton acceptor.
FT                                {ECO:0000305|PubMed:9195888}.
FT   ACT_SITE    322    322       Nucleophile.
FT                                {ECO:0000305|PubMed:9195888}.
FT   BINDING     245    245       NAD; via carbonyl oxygen.
FT                                {ECO:0000244|PDB:1A4Z,
FT                                ECO:0000269|PubMed:9195888}.
FT   BINDING     288    288       NAD. {ECO:0000244|PDB:1A4Z,
FT                                ECO:0000269|PubMed:9195888}.
FT   SITE        189    189       Transition state stabilizer.
FT                                {ECO:0000269|PubMed:9195888}.
FT   MOD_RES      55     55       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES      76     76       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     162    162       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     371    371       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     378    378       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     386    386       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     429    429       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     431    431       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     444    444       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     454    454       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   CONFLICT    289    289       L -> I (in Ref. 1; no nucleotide entry
FT                                and 3; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT    385    385       A -> L (in Ref. 1; no nucleotide entry
FT                                and 3; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT    409    409       V -> L (in Ref. 1; no nucleotide entry
FT                                and 3; no nucleotide entry).
FT                                {ECO:0000305}.
FT   STRAND       41     46       {ECO:0000244|PDB:1AG8}.
FT   STRAND       47     49       {ECO:0000244|PDB:1A4Z}.
FT   STRAND       56     60       {ECO:0000244|PDB:1AG8}.
FT   TURN         62     64       {ECO:0000244|PDB:1AG8}.
FT   STRAND       67     72       {ECO:0000244|PDB:1AG8}.
FT   HELIX        76     89       {ECO:0000244|PDB:1AG8}.
FT   HELIX        95     98       {ECO:0000244|PDB:1AG8}.
FT   HELIX       101    117       {ECO:0000244|PDB:1AG8}.
FT   HELIX       119    130       {ECO:0000244|PDB:1AG8}.
FT   HELIX       134    139       {ECO:0000244|PDB:1AG8}.
FT   HELIX       141    153       {ECO:0000244|PDB:1AG8}.
FT   TURN        154    158       {ECO:0000244|PDB:1AG8}.
FT   STRAND      161    164       {ECO:0000244|PDB:1AG8}.
FT   STRAND      167    178       {ECO:0000244|PDB:1AG8}.
FT   STRAND      181    185       {ECO:0000244|PDB:1AG8}.
FT   STRAND      188    190       {ECO:0000244|PDB:1AG8}.
FT   HELIX       191    205       {ECO:0000244|PDB:1AG8}.
FT   STRAND      208    213       {ECO:0000244|PDB:1AG8}.
FT   HELIX       219    231       {ECO:0000244|PDB:1AG8}.
FT   STRAND      237    243       {ECO:0000244|PDB:1AG8}.
FT   HELIX       245    253       {ECO:0000244|PDB:1AG8}.
FT   STRAND      260    265       {ECO:0000244|PDB:1AG8}.
FT   HELIX       267    279       {ECO:0000244|PDB:1AG8}.
FT   STRAND      284    288       {ECO:0000244|PDB:1AG8}.
FT   STRAND      294    297       {ECO:0000244|PDB:1AG8}.
FT   HELIX       303    315       {ECO:0000244|PDB:1AG8}.
FT   HELIX       316    319       {ECO:0000244|PDB:1AG8}.
FT   STRAND      327    331       {ECO:0000244|PDB:1AG8}.
FT   HELIX       332    348       {ECO:0000244|PDB:1AG8}.
FT   HELIX       367    383       {ECO:0000244|PDB:1AG8}.
FT   STRAND      386    389       {ECO:0000244|PDB:1AG8}.
FT   STRAND      392    394       {ECO:0000244|PDB:1AG8}.
FT   STRAND      396    398       {ECO:0000244|PDB:1AG8}.
FT   STRAND      404    408       {ECO:0000244|PDB:1AG8}.
FT   HELIX       414    417       {ECO:0000244|PDB:1AG8}.
FT   STRAND      422    430       {ECO:0000244|PDB:1AG8}.
FT   HELIX       433    441       {ECO:0000244|PDB:1AG8}.
FT   STRAND      447    452       {ECO:0000244|PDB:1AG8}.
FT   HELIX       456    465       {ECO:0000244|PDB:1AG8}.
FT   STRAND      469    474       {ECO:0000244|PDB:1AG8}.
FT   STRAND      492    494       {ECO:0000244|PDB:1AG8}.
FT   HELIX       500    503       {ECO:0000244|PDB:1AG8}.
FT   STRAND      506    514       {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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