ID   AL3A1_HUMAN             Reviewed;         453 AA.
AC   P30838; A8K828; Q9BT37;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 3.
DT   27-MAR-2024, entry version 208.
DE   RecName: Full=Aldehyde dehydrogenase, dimeric NADP-preferring;
DE            EC=1.2.1.5 {ECO:0000269|PubMed:1737758, ECO:0000269|PubMed:22021038};
DE   AltName: Full=ALDHIII;
DE   AltName: Full=Aldehyde dehydrogenase 3;
DE   AltName: Full=Aldehyde dehydrogenase family 3 member A1;
GN   Name=ALDH3A1; Synonyms=ALDH3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-134.
RC   TISSUE=Stomach;
RA   Schuuring E.M.D., Verhoeven E., Eckey R., Vos H.L., Michalides R.J.A.;
RT   "Cloning and complete nucleotide sequence of a cDNA encoding the full-
RT   length open reading frame of the human aldehyde dehydrogenase type III
RT   gene.";
RL   Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   TISSUE=Stomach;
RX   PubMed=1737758; DOI=10.1016/s0021-9258(19)50690-1;
RA   Hsu L.C., Chang W.-C., Shibuya A., Yoshida A.;
RT   "Human stomach aldehyde dehydrogenase cDNA and genomic cloning, primary
RT   structure, and expression in Escherichia coli.";
RL   J. Biol. Chem. 267:3030-3037(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Stomach;
RX   PubMed=8493892; DOI=10.1007/978-1-4615-2904-0_16;
RA   Hsu L.C., Yoshida A.;
RT   "Human stomach aldehyde dehydrogenase, ALDH3.";
RL   Adv. Exp. Med. Biol. 328:141-152(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-134.
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-134.
RC   TISSUE=Cervix, and Tongue;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-134.
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-134.
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   PROTEIN SEQUENCE OF 62-453.
RC   TISSUE=Stomach;
RX   PubMed=2037078; DOI=10.1016/0014-5793(91)80559-l;
RA   Yin S.-J., Vagelopoulos N., Wang S.-L., Joernvall H.;
RT   "Structural features of stomach aldehyde dehydrogenase distinguish dimeric
RT   aldehyde dehydrogenase as a 'variable' enzyme. 'Variable' and 'constant'
RT   enzymes within the alcohol and aldehyde dehydrogenase families.";
RL   FEBS Lett. 283:85-88(1991).
RN   [10]
RP   CHARACTERIZATION.
RX   PubMed=1905102; DOI=10.1007/978-1-4684-5901-2_6;
RA   Eckey R., Timmann R., Hempel J., Agarwal D.P., Goedde H.W.;
RT   "Biochemical, immunological, and molecular characterization of a 'high Km'
RT   aldehyde dehydrogenase.";
RL   Adv. Exp. Med. Biol. 284:43-52(1991).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-178 AND LYS-194, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH INHIBITOR, CATALYTIC
RP   ACTIVITY, MUTAGENESIS OF CYS-244, AND ACTIVE SITE.
RX   PubMed=22021038; DOI=10.1074/jbc.m111.293597;
RA   Khanna M., Chen C.H., Kimble-Hill A., Parajuli B., Perez-Miller S.,
RA   Baskaran S., Kim J., Dria K., Vasiliou V., Mochly-Rosen D., Hurley T.D.;
RT   "Discovery of a novel class of covalent inhibitor for aldehyde
RT   dehydrogenases.";
RL   J. Biol. Chem. 286:43486-43494(2011).
RN   [15]
RP   VARIANT ALA-329.
RX   PubMed=9250352; DOI=10.1046/j.1469-1809.1997.6130235.x;
RA   Tsukamoto N., Chang C., Yoshida A.;
RT   "Mutations associated with Sjogren-Larsson syndrome.";
RL   Ann. Hum. Genet. 61:235-242(1997).
CC   -!- FUNCTION: ALDHs play a major role in the detoxification of alcohol-
CC       derived acetaldehyde (Probable). They are involved in the metabolism of
CC       corticosteroids, biogenic amines, neurotransmitters, and lipid
CC       peroxidation (Probable). Oxidizes medium and long chain aldehydes into
CC       non-toxic fatty acids (PubMed:1737758). Preferentially oxidizes
CC       aromatic aldehyde substrates (PubMed:1737758). Comprises about 50
CC       percent of corneal epithelial soluble proteins (By similarity). May
CC       play a role in preventing corneal damage caused by ultraviolet light
CC       (By similarity). {ECO:0000250|UniProtKB:P47739,
CC       ECO:0000269|PubMed:1737758, ECO:0000305}.
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=1.2.1.5; Evidence={ECO:0000269|PubMed:1737758,
CC         ECO:0000269|PubMed:22021038};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NAD(+) + octanal = 2 H(+) + NADH + octanoate;
CC         Xref=Rhea:RHEA:44100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P47739};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Note=Has a high Km for acetaldehyde.;
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22021038}.
CC   -!- INTERACTION:
CC       P30838; O75344: FKBP6; NbExp=3; IntAct=EBI-3905126, EBI-744771;
CC       P30838; Q9NUX5: POT1; NbExp=2; IntAct=EBI-3905126, EBI-752420;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P47739}.
CC   -!- TISSUE SPECIFICITY: High levels in stomach, esophagus and lung; low
CC       level in the liver and kidney.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; M74542; AAA51696.1; -; mRNA.
DR   EMBL; M77477; AAB46377.1; -; mRNA.
DR   EMBL; S61044; AAB26658.1; -; mRNA.
DR   EMBL; BT007102; AAP35766.1; -; mRNA.
DR   EMBL; AK292193; BAF84882.1; -; mRNA.
DR   EMBL; AK314584; BAG37160.1; -; mRNA.
DR   EMBL; AC005722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471212; EAW50909.1; -; Genomic_DNA.
DR   EMBL; BC004370; AAH04370.1; -; mRNA.
DR   EMBL; BC008892; AAH08892.1; -; mRNA.
DR   EMBL; BC021194; AAH21194.1; -; mRNA.
DR   CCDS; CCDS11212.1; -.
DR   PIR; A42584; A42584.
DR   RefSeq; NP_000682.3; NM_000691.4.
DR   RefSeq; NP_001128639.1; NM_001135167.1.
DR   RefSeq; NP_001128640.1; NM_001135168.1.
DR   PDB; 3SZA; X-ray; 1.48 A; A/B=1-453.
DR   PDB; 3SZB; X-ray; 1.51 A; A/B=1-453.
DR   PDB; 4H80; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-453.
DR   PDB; 4L1O; X-ray; 2.30 A; A/B=1-453.
DR   PDB; 4L2O; X-ray; 1.94 A; A/B/E/G=1-453.
DR   PDB; 8BB8; X-ray; 1.80 A; A/B=2-453.
DR   PDBsum; 3SZA; -.
DR   PDBsum; 3SZB; -.
DR   PDBsum; 4H80; -.
DR   PDBsum; 4L1O; -.
DR   PDBsum; 4L2O; -.
DR   PDBsum; 8BB8; -.
DR   AlphaFoldDB; P30838; -.
DR   SMR; P30838; -.
DR   BioGRID; 106720; 93.
DR   IntAct; P30838; 16.
DR   STRING; 9606.ENSP00000411821; -.
DR   BindingDB; P30838; -.
DR   ChEMBL; CHEMBL3578; -.
DR   DrugBank; DB00157; NADH.
DR   GlyGen; P30838; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P30838; -.
DR   PhosphoSitePlus; P30838; -.
DR   SwissPalm; P30838; -.
DR   BioMuta; ALDH3A1; -.
DR   DMDM; 311033473; -.
DR   EPD; P30838; -.
DR   jPOST; P30838; -.
DR   MassIVE; P30838; -.
DR   MaxQB; P30838; -.
DR   PaxDb; 9606-ENSP00000411821; -.
DR   PeptideAtlas; P30838; -.
DR   PRIDE; P30838; -.
DR   ProteomicsDB; 54741; -.
DR   Pumba; P30838; -.
DR   Antibodypedia; 26030; 522 antibodies from 40 providers.
DR   DNASU; 218; -.
DR   Ensembl; ENST00000225740.11; ENSP00000225740.6; ENSG00000108602.18.
DR   Ensembl; ENST00000444455.5; ENSP00000388469.1; ENSG00000108602.18.
DR   Ensembl; ENST00000457500.6; ENSP00000411821.2; ENSG00000108602.18.
DR   GeneID; 218; -.
DR   KEGG; hsa:218; -.
DR   MANE-Select; ENST00000225740.11; ENSP00000225740.6; NM_000691.5; NP_000682.3.
DR   UCSC; uc002gwj.4; human.
DR   AGR; HGNC:405; -.
DR   CTD; 218; -.
DR   DisGeNET; 218; -.
DR   GeneCards; ALDH3A1; -.
DR   HGNC; HGNC:405; ALDH3A1.
DR   HPA; ENSG00000108602; Tissue enhanced (esophagus, salivary gland, stomach).
DR   MIM; 100660; gene.
DR   neXtProt; NX_P30838; -.
DR   OpenTargets; ENSG00000108602; -.
DR   PharmGKB; PA24697; -.
DR   VEuPathDB; HostDB:ENSG00000108602; -.
DR   eggNOG; KOG2456; Eukaryota.
DR   GeneTree; ENSGT00940000162101; -.
DR   InParanoid; P30838; -.
DR   OMA; EPCIQGQ; -.
DR   OrthoDB; 606537at2759; -.
DR   PhylomeDB; P30838; -.
DR   TreeFam; TF314264; -.
DR   BRENDA; 1.2.1.5; 2681.
DR   PathwayCommons; P30838; -.
DR   Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
DR   SABIO-RK; P30838; -.
DR   SignaLink; P30838; -.
DR   SIGNOR; P30838; -.
DR   BioGRID-ORCS; 218; 15 hits in 1156 CRISPR screens.
DR   ChiTaRS; ALDH3A1; human.
DR   EvolutionaryTrace; P30838; -.
DR   GeneWiki; Aldehyde_dehydrogenase_3_family,_member_A1; -.
DR   GenomeRNAi; 218; -.
DR   Pharos; P30838; Tchem.
DR   PRO; PR:P30838; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P30838; Protein.
DR   Bgee; ENSG00000108602; Expressed in nasal cavity epithelium and 151 other cell types or tissues.
DR   ExpressionAtlas; P30838; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:LIFEdb.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR   GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; TAS:Reactome.
DR   GO; GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; IDA:CACAO.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; IDA:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR   CDD; cd07132; ALDH_F3AB; 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   InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR   PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43570:SF15; ALDEHYDE DEHYDROGENASE, DIMERIC NADP-PREFERRING; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
DR   Genevisible; P30838; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Lipid metabolism; NAD; NADP; Oxidoreductase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..453
FT                   /note="Aldehyde dehydrogenase, dimeric NADP-preferring"
FT                   /id="PRO_0000056470"
FT   ACT_SITE        210
FT                   /evidence="ECO:0000269|PubMed:22021038"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000269|PubMed:22021038"
FT   BINDING         188..193
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         178
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         194
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VARIANT         134
FT                   /note="S -> A (in dbSNP:rs887241)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1,
FT                   ECO:0000269|Ref.4, ECO:0000269|Ref.7"
FT                   /id="VAR_018981"
FT   VARIANT         309
FT                   /note="G -> E (in dbSNP:rs3744692)"
FT                   /id="VAR_018982"
FT   VARIANT         329
FT                   /note="P -> A (in allele ALDH3A1*2; dbSNP:rs2228100)"
FT                   /evidence="ECO:0000269|PubMed:9250352"
FT                   /id="VAR_011303"
FT   MUTAGEN         244
FT                   /note="C->S: Abolishes activity."
FT                   /evidence="ECO:0000269|PubMed:22021038"
FT   CONFLICT        12
FT                   /note="R -> P (in Ref. 2; AAB46377 and 3; AAB26658)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        27
FT                   /note="I -> F (in Ref. 1; AAA51696)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        170
FT                   /note="V -> L (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        436
FT                   /note="D -> E (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           3..16
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   TURN            17..20
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   HELIX           23..39
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   HELIX           41..52
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   HELIX           56..61
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   HELIX           64..82
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   HELIX           91..93
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   STRAND          96..104
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   STRAND          106..111
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   STRAND          114..116
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   HELIX           119..130
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   STRAND          134..138
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   STRAND          141..143
FT                   /evidence="ECO:0007829|PDB:4L2O"
FT   HELIX           144..157
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   TURN            160..162
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   HELIX           170..176
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   STRAND          182..188
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   HELIX           190..201
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   TURN            202..204
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   STRAND          207..210
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   STRAND          216..219
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   HELIX           225..237
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   HELIX           238..241
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   STRAND          249..252
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   HELIX           254..256
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   HELIX           257..272
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   HELIX           276..278
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   HELIX           288..298
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   STRAND          301..305
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   TURN            311..314
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   STRAND          319..323
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   HELIX           329..331
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   STRAND          337..344
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   HELIX           348..357
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   STRAND          362..367
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   HELIX           371..380
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   STRAND          384..389
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   HELIX           393..395
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   HELIX           406..408
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   HELIX           416..421
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   STRAND          423..430
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   HELIX           437..442
FT                   /evidence="ECO:0007829|PDB:3SZA"
FT   STRAND          443..445
FT                   /evidence="ECO:0007829|PDB:3SZA"
SQ   SEQUENCE   453 AA;  50395 MW;  D35C488A022FAACA CRC64;
     MSKISEAVKR ARAAFSSGRT RPLQFRIQQL EALQRLIQEQ EQELVGALAA DLHKNEWNAY
     YEEVVYVLEE IEYMIQKLPE WAADEPVEKT PQTQQDELYI HSEPLGVVLV IGTWNYPFNL
     TIQPMVGAIA AGNSVVLKPS ELSENMASLL ATIIPQYLDK DLYPVINGGV PETTELLKER
     FDHILYTGST GVGKIIMTAA AKHLTPVTLE LGGKSPCYVD KNCDLDVACR RIAWGKFMNS
     GQTCVAPDYI LCDPSIQNQI VEKLKKSLKE FYGEDAKKSR DYGRIISARH FQRVMGLIEG
     QKVAYGGTGD AATRYIAPTI LTDVDPQSPV MQEEIFGPVL PIVCVRSLEE AIQFINQREK
     PLALYMFSSN DKVIKKMIAE TSSGGVAAND VIVHITLHSL PFGGVGNSGM GSYHGKKSFE
     TFSHRRSCLV RPLMNDEGLK VRYPPSPAKM TQH
//