ID   AL7A1_CAEEL             Reviewed;         531 AA.
AC   P46562;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Putative aldehyde dehydrogenase family 7 member A1 homolog;
DE            EC=1.2.1.3;
DE   AltName: Full=ALH-9;
GN   Name=alh-9; ORFNames=F01F1.6;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; BX284603; CCD65988.1; -; Genomic_DNA.
DR   PIR; T15944; T15944.
DR   RefSeq; NP_498263.2; NM_065862.3.
DR   AlphaFoldDB; P46562; -.
DR   SMR; P46562; -.
DR   BioGRID; 41042; 39.
DR   DIP; DIP-25437N; -.
DR   IntAct; P46562; 2.
DR   STRING; 6239.F01F1.6.2; -.
DR   iPTMnet; P46562; -.
DR   EPD; P46562; -.
DR   PaxDb; P46562; -.
DR   PeptideAtlas; P46562; -.
DR   EnsemblMetazoa; F01F1.6.1; F01F1.6.1; WBGene00000115.
DR   EnsemblMetazoa; F01F1.6.2; F01F1.6.2; WBGene00000115.
DR   GeneID; 175820; -.
DR   KEGG; cel:CELE_F01F1.6; -.
DR   UCSC; F01F1.6.1; c. elegans.
DR   CTD; 175820; -.
DR   WormBase; F01F1.6; CE39486; WBGene00000115; alh-9.
DR   eggNOG; KOG2453; Eukaryota.
DR   GeneTree; ENSGT00940000154938; -.
DR   HOGENOM; CLU_005391_1_2_1; -.
DR   InParanoid; P46562; -.
DR   OMA; DAWKVYM; -.
DR   OrthoDB; 692580at2759; -.
DR   PhylomeDB; P46562; -.
DR   Reactome; R-CEL-6798163; Choline catabolism.
DR   Reactome; R-CEL-71064; Lysine catabolism.
DR   SignaLink; P46562; -.
DR   PRO; PR:P46562; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00000115; Expressed in adult organism and 4 other tissues.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006081; P:cellular aldehyde metabolic 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; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR044638; ALDH7A1-like.
DR   PANTHER; PTHR43521; PTHR43521; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..531
FT                   /note="Putative aldehyde dehydrogenase family 7 member A1
FT                   homolog"
FT                   /id="PRO_0000056499"
FT   ACT_SITE        286
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        320
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   BINDING         264..269
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            185
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   531 AA;  57013 MW;  2FEA6B882C790BBF CRC64;
     MNRLLSSGMS AATLQTRMAS QLLINDSKYG FLKELGLTEN NAGVFHGKWA ASGQVVQSFA
     PANNSPIANV QNGNVQDYEI AISEAKKAYN DWCEVPAPRR GEIVRQIGDK LRTQLQNLGK
     LVSLEMGKIS AEGVGEVQEY VDICDYATGL SRSLEGKIFP SERPGHALLE QWNPLGVVGV
     ISAFNFPCAV YGWNNALALV TGNSVVWKPA PSTPLTAIAV TKLVEEVLVA NNVNPALCSL
     VCGEGDVGQA LVKDKRVNLV SFTGSSEIGK IVGQQVQARF GKLLLELGGN NAIIVNEDAD
     LNMVVPATVF AAVGTAGQRC TTTRRLIVHD KVYDQVLERL KKAYAQFESR IGCPLDSNTI
     IGPLHNQQAV GKYKASVAEA VASGGKIEYG GKVLERDGNF VLPTIVTGLK HDSPVVLRET
     FAPILYVLKF STLEEAIAIN NEVDQGLSSS LFTTNIQNVF KWMGPKGSDC GIVNVNIPTS
     GAEIGGAFGG EKETGGGRES GSDSWRQYMR RSTCTINYSK ELPLAQGIKF E