ALDH2_PIG
ID ALDH2_PIG Reviewed; 521 AA.
AC Q2XQV4;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Aldehyde dehydrogenase, mitochondrial;
DE EC=1.2.1.3;
DE AltName: Full=ALDH class 2;
DE AltName: Full=ALDH-E2;
DE Flags: Precursor;
GN Name=ALDH2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ji Y., Bennett B.M.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Is capable of converting retinaldehyde to retinoic acid.
CC {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; DQ266356; ABB70228.1; -; mRNA.
DR RefSeq; NP_001038076.1; NM_001044611.2.
DR AlphaFoldDB; Q2XQV4; -.
DR SMR; Q2XQV4; -.
DR STRING; 9823.ENSSSCP00000010556; -.
DR PaxDb; Q2XQV4; -.
DR PeptideAtlas; Q2XQV4; -.
DR PRIDE; Q2XQV4; -.
DR Ensembl; ENSSSCT00000055390; ENSSSCP00000053451; ENSSSCG00000009889.
DR Ensembl; ENSSSCT00025069501; ENSSSCP00025029933; ENSSSCG00025050497.
DR Ensembl; ENSSSCT00035044779; ENSSSCP00035017930; ENSSSCG00035033776.
DR Ensembl; ENSSSCT00040009144; ENSSSCP00040003586; ENSSSCG00040006895.
DR Ensembl; ENSSSCT00045006276; ENSSSCP00045004257; ENSSSCG00045003770.
DR Ensembl; ENSSSCT00055023290; ENSSSCP00055018413; ENSSSCG00055011877.
DR Ensembl; ENSSSCT00060076086; ENSSSCP00060032896; ENSSSCG00060055813.
DR Ensembl; ENSSSCT00065034412; ENSSSCP00065014281; ENSSSCG00065025693.
DR Ensembl; ENSSSCT00070014826; ENSSSCP00070012258; ENSSSCG00070007644.
DR GeneID; 733685; -.
DR KEGG; ssc:733685; -.
DR CTD; 217; -.
DR VGNC; VGNC:106442; ALDH2.
DR eggNOG; KOG2450; Eukaryota.
DR GeneTree; ENSGT00940000156240; -.
DR HOGENOM; CLU_005391_0_1_1; -.
DR InParanoid; Q2XQV4; -.
DR OMA; HGIGYYP; -.
DR OrthoDB; 153834at2759; -.
DR TreeFam; TF300455; -.
DR Reactome; R-SSC-380612; Metabolism of serotonin.
DR Reactome; R-SSC-71384; Ethanol oxidation.
DR UniPathway; UPA00780; UER00768.
DR Proteomes; UP000008227; Chromosome 14.
DR Proteomes; UP000314985; Chromosome 14.
DR Bgee; ENSSSCG00000009889; Expressed in liver and 47 other tissues.
DR ExpressionAtlas; Q2XQV4; baseline and differential.
DR Genevisible; Q2XQV4; SS.
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: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 2: Evidence at transcript level;
KW Acetylation; Mitochondrion; NAD; Oxidoreductase; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 22..521
FT /note="Aldehyde dehydrogenase, mitochondrial"
FT /id="PRO_0000312492"
FT ACT_SITE 289
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 323
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 266..271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 190
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P20000"
FT MOD_RES 56
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 77
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 163
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 372
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 379
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 387
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 430
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 432
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 445
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 455
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
SQ SEQUENCE 521 AA; 56921 MW; 12913E10ECD560A7 CRC64;
MLRPAALAAA RLVLRQGRRL LSAAPTQAVP APNQQPEIFY NQIFINNEWH DAISKKTFPT
VNPSTGDVIC HVAEGDKEDV DRAVEAARAA FQLGSPWRRL DASDRGRLLN RLADLIERDR
TYLAALETLD NGKPYVISYL VDLDMVLKCL RYYAGWADKY HGKTLPIDGD YFSYTRHEPV
GVCGQIIPWN FPLLMQAWKL GPALATGNVV VMKVSEQTPL TALYVANLIK EAGFPPGVVN
IVPGYGPTAG AAIASHEDVD KVAFTGSTEV GHLIQVAAGK SNLKRVTLEL GGKSPNIIMS
DADMDWAVEQ AHFALFFNQG QCCCAGSRTF VQEDIYAEFV ERSVARARSR VVGNPFDSRT
EQGPQIDETQ FKKILGYIKS GKEEGAKLLC GGGAAADRGY FIQPTVFGDV QDGMTIAKEE
IFGPVMQILK FKTIEEVIGR ANNSKYGLAA AVFTKDLDKA NYLSQALQAG TVWVNCYDVF
GAQSPFGGYK LSGSGRELGE YGLQAYTEVK TVTVKVPQKN S
