ALDH2_HORSE
ID ALDH2_HORSE Reviewed; 500 AA.
AC P12762;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 115.
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;
GN Name=ALDH2;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3350012; DOI=10.1111/j.1432-1033.1988.tb13920.x;
RA Johansson J., von Bahr-Lindstroem H., Jeck R., Woenckhaus C., Joernvall H.;
RT "Mitochondrial aldehyde dehydrogenase from horse liver. Correlations of the
RT same species variants for both the cytosolic and the mitochondrial forms of
RT an enzyme.";
RL Eur. J. Biochem. 172:527-533(1988).
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}.
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DR PIR; S00364; S00364.
DR AlphaFoldDB; P12762; -.
DR SMR; P12762; -.
DR STRING; 9796.ENSECAP00000015826; -.
DR PaxDb; P12762; -.
DR PeptideAtlas; P12762; -.
DR InParanoid; P12762; -.
DR SABIO-RK; P12762; -.
DR UniPathway; UPA00780; UER00768.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; ISS:UniProtKB.
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:0018547; F:nitroglycerin reductase activity; ISS:UniProtKB.
DR GO; GO:0008957; F:phenylacetaldehyde dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0046185; P:aldehyde catabolic process; ISS:UniProtKB.
DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:1903179; P:regulation of dopamine biosynthetic process; ISS:UniProtKB.
DR GO; GO:1905627; P:regulation of serotonin biosynthetic process; ISS:UniProtKB.
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 Acetylation; Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..500
FT /note="Aldehyde dehydrogenase, mitochondrial"
FT /id="PRO_0000056467"
FT ACT_SITE 268
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 302
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 245..250
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 169
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P20000"
FT MOD_RES 35
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 56
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 142
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 358
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 366
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 409
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 411
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 424
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 434
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT VARIANT 1
FT /note="A -> L"
FT VARIANT 1
FT /note="A -> S"
SQ SEQUENCE 500 AA; 54166 MW; 7F95364A73383B24 CRC64;
AAAATQAVPA PNQQPEVFYN QIFINNEWHD AVSKKTFPTV NPSTGEVICQ VAAGDKEDVD
RAVKAARAAF QLGSPWRRMD ASDRGRLLNR LADLIERDRT YLAALETLDN GKPYVISYLV
DLDMVLKCLR YYAGWADKYH GKTIPIDGDF FSYTRHEPVG VCGQIIPWNF PLLMQAAKLG
PALATGNVVV MKVAEQTPLT ALYVANLTKE AGFPPGVVNV VPGFGPTAGA AIASHEDVDK
VAFTGSTEVG HLIQVAAGRS NLKKVTLELG GKSPNIIVSD ADMDWAVEQA HFALFFNQGQ
CCGAGSRTFV QEDVYAEFVE RSVARAKSRV VGNPFDSQTE QGPQVDETQF NKVLGYIKSG
KEEGAKLLCG GGAAADRGYF IQPTVFGDVQ DGMTIAKEEI FGPVMQILKF KTIEEVVGRA
NNSKYGLAAA VFTKDLDKAN YLSQALQAGT VWINCYDVFG AQSPFGGYKM SGNGRELGEY
GLQAYTEVKT VTIKVPQKNS
