ID V4BKT6_LOTGI Unreviewed; 503 AA.
AC V4BKT6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN ORFNames=LOTGIDRAFT_229102 {ECO:0000313|EMBL:ESO89209.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO89209.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESO89209.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492,
CC ECO:0000256|RuleBase:RU003345}.
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DR EMBL; KB202619; ESO89209.1; -; Genomic_DNA.
DR RefSeq; XP_009060246.1; XM_009061998.1.
DR AlphaFoldDB; V4BKT6; -.
DR STRING; 225164.V4BKT6; -.
DR EnsemblMetazoa; LotgiT229102; LotgiP229102; LotgiG229102.
DR GeneID; 20247896; -.
DR KEGG; lgi:LOTGIDRAFT_229102; -.
DR CTD; 20247896; -.
DR HOGENOM; CLU_005391_3_1_1; -.
DR OMA; AVANCIV; -.
DR OrthoDB; 606537at2759; -.
DR Proteomes; UP000030746; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
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:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 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.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR036492,
KW ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000030746};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 469..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..426
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 210
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 244
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ SEQUENCE 503 AA; 55943 MW; A573A9571D43DD52 CRC64;
MANYNKVITE LHETFLTGKT KTYEWRDRQL RQLLKLIEEN GKAIEDALFK DLHKHANEAQ
IMETGMVKND LINAINSLSD WMKPDMVKKD LLVAMDTCFI QSEPFGVTLI LGAWNYPIQL
TLLPLIGAIA AGNCAVVKPS ELSHYTALVL EDLIPKYLDT ECIKVINGAV PETTALLKER
FDLIFYTGNN VVAKIVMAAA AKNLTPVILE LGGKSPVYID KNIDYNTVAR RLVWGKAINS
GQTCIAPDYV LCTTDVQNKI IEEMKKVVND FYGDPSKSEY YGRIINDRHF ERVKSLLKGV
NIAIGGNVNE KERLISPTVL KDVKTTDHVM QSEIFGPILP IVTVQNEDEA IEYINSGEKP
LALYVFSSND KIVNKFLSQT SSGGVCVNDT LLHAGIQTLP FGGVGHSGIG GYHGKFSFDV
FSHKRSVLKR GLGMEFVNNI RYPPYTEKKM KILNLLTGKK VKKTGIMSFL PFVLFGTFLA
FVFKSVGVEA IAARIKPLLG KKD
//
