ID   ALDH2_PONAB             Reviewed;         517 AA.
AC   Q5RF00;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-MAY-2023, entry version 84.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for clearance of cellular formaldehyde, a cytotoxic
CC       and carcinogenic metabolite that induces DNA damage.
CC       {ECO:0000250|UniProtKB:P05091}.
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   -!- 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; CR857362; CAH89657.1; -; mRNA.
DR   RefSeq; NP_001124747.1; NM_001131275.1.
DR   AlphaFoldDB; Q5RF00; -.
DR   SMR; Q5RF00; -.
DR   STRING; 9601.ENSPPYP00000005665; -.
DR   GeneID; 100171596; -.
DR   KEGG; pon:100171596; -.
DR   CTD; 217; -.
DR   eggNOG; KOG2450; Eukaryota.
DR   InParanoid; Q5RF00; -.
DR   OrthoDB; 2291791at2759; -.
DR   Proteomes; UP000001595; 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:0106435; F:carboxylesterase 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:1903179; P:regulation of dopamine biosynthetic process; ISS:UniProtKB.
DR   GO; GO:1905627; P:regulation of serotonin biosynthetic process; ISS:UniProtKB.
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:SF233; ALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 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   2: Evidence at transcript level;
KW   Acetylation; Mitochondrion; NAD; Oxidoreductase; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..17
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           18..517
FT                   /note="Aldehyde dehydrogenase, mitochondrial"
FT                   /id="PRO_0000312493"
FT   ACT_SITE        285
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        319
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         262..267
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            186
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P20000"
FT   MOD_RES         52
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
FT   MOD_RES         78
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
FT   MOD_RES         159
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
FT   MOD_RES         368
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
FT   MOD_RES         383
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
FT   MOD_RES         426
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
FT   MOD_RES         428
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
FT   MOD_RES         451
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
SQ   SEQUENCE   517 AA;  56380 MW;  E8F74D4CFA27220E CRC64;
     MLRAAARFGP RLGRRLLSAA ATQAVPAPNQ QPEVFCNQIF INNEWHDAVS RKTFPTVNPS
     TGEVICQVAE GDKEDVDKAV KAARAAFQLG SPWRRMDASH RGRLLNRLAD LIERDRTYLA
     ALETLDNGKP YVISYLVDLD MVLKCLRYYA GWADKYHGKT IPIDGDFFSY TRHEPVGVCG
     QIIPWNFPLL MQAWKLGPAL ATGNVVVMKV AEQTPLTALY VANLIKEAGF PPGVVNIVPG
     FGPTAGAAIA SHEDVDKVAF TGSTEIGRVI QVAAGSSNLK RVTLELGGKS PNIIMSDADM
     DWAVEQAHFA LFFNQGQCCC AGSRTFVQED IYDEFVERSV ARAKSRVVGN PFDSKTEQGP
     QVDETQFKKI LGYINTGKQE GAKLLCGGGI AADRGYFIQP TVFGDVQDGM TIAKEEIFGP
     VMQILKFKTI EEVVGRANNS TYGLAAAVFT KDLDKANYLS QALQAGTVWV NCYNVFGAQS
     PFGGYKMSGS GRELGEYGLQ AYTEVKTVTV KVPQKNS
//