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Database: UniProt
Entry: O16518_CAEEL
LinkDB: O16518_CAEEL
Original site: O16518_CAEEL 
ID   O16518_CAEEL            Unreviewed;       493 AA.
AC   O16518;
DT   01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 2.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN   Name=alh-4 {ECO:0000313|EMBL:CCD72037.1,
GN   ECO:0000313|WormBase:T05H4.13a};
GN   ORFNames=CELE_T05H4.13 {ECO:0000313|EMBL:CCD72037.1}, T05H4.13
GN   {ECO:0000313|WormBase:T05H4.13a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD72037.1, ECO:0000313|Proteomes:UP000001940};
RN   [1] {ECO:0000313|EMBL:CCD72037.1, ECO:0000313|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD72037.1,
RC   ECO:0000313|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RA   Sulson J.E., Waterston R.;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492}.
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DR   EMBL; BX284605; CCD72037.1; -; Genomic_DNA.
DR   PIR; T31905; T31905.
DR   RefSeq; NP_741553.1; NM_171471.5.
DR   AlphaFoldDB; O16518; -.
DR   SMR; O16518; -.
DR   EPD; O16518; -.
DR   PeptideAtlas; O16518; -.
DR   EnsemblMetazoa; T05H4.13a.1; T05H4.13a.1; WBGene00000110.
DR   GeneID; 179026; -.
DR   KEGG; cel:CELE_T05H4.13; -.
DR   UCSC; T05H4.13a; c. elegans.
DR   AGR; WB:WBGene00000110; -.
DR   WormBase; T05H4.13a; CE27441; WBGene00000110; alh-4.
DR   HOGENOM; CLU_005391_3_1_1; -.
DR   OrthoDB; 606537at2759; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00000110; Expressed in larva and 4 other cell types or tissues.
DR   ExpressionAtlas; O16518; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; IBA:GO_Central.
DR   CDD; cd07087; ALDH_F3-13-14_CALDH-like; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
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:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
PE   1: Evidence at protein level;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR036492};
KW   Proteomics identification {ECO:0007829|EPD:O16518,
KW   ECO:0007829|PeptideAtlas:O16518};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        462..485
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..428
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        209
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
FT   ACT_SITE        243
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ   SEQUENCE   493 AA;  55567 MW;  99B25D2DA5881015 CRC64;
     MAFTELVETQ RKYFRTGETK PVKFRKQQLL KLKKFIEENR EALSEAVWKD LRRRHESTEI
     LEIGMTIQEI DYFLKNIDDW VKPTHVEKTF TTALDKPVIE KDPKGVVLII SPWNYPVSMI
     LLPMVPAIAA GNTVVIKPSE LSENVAATFE KLIPKYFESK YVTVVNGGIP ETTDLLKERF
     DHILYTGCPP VAKIIMTAAA KHLTPVTLEL GGKCPVVVED DADIDISAKR IAWGKWLNCG
     QTCLAPDYIL VNSTVKPKLV AAIRKYVNEF YGEDVKASKD YARMINQRHF DRISGLLDKT
     QGAVLIGGER DRADLYIPPT VLDVEKSDPF MHDEIFGPVL PIITVQSFSE SLEYIADGEK
     PLAAYIFTRN EAKVKRLLNE TSSGGVTVND VLMHITVDTL PFGGVGVSGM GRYRGKYGFD
     TFTHEKSVLH RGFFGESLLA ARYPPLSQQK LDQMRRLTGK RISLNLMNVA TLPIVMASFV
     FGMLFQKYAR NLH
//
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