ID A0A0S2JZ86_9GAMM Unreviewed; 405 AA.
AC A0A0S2JZ86;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=long-chain-fatty-acyl-CoA reductase {ECO:0000256|ARBA:ARBA00013020};
DE EC=1.2.1.50 {ECO:0000256|ARBA:ARBA00013020};
GN ORFNames=PP2015_922 {ECO:0000313|EMBL:ALO41440.1};
OS Pseudoalteromonas phenolica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=161398 {ECO:0000313|EMBL:ALO41440.1, ECO:0000313|Proteomes:UP000061457};
RN [1] {ECO:0000313|EMBL:ALO41440.1, ECO:0000313|Proteomes:UP000061457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 12086 {ECO:0000313|EMBL:ALO41440.1,
RC ECO:0000313|Proteomes:UP000061457};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: LuxC is the fatty acid reductase enzyme responsible for
CC synthesis of the aldehyde substrate for the luminescent reaction
CC catalyzed by luciferase. {ECO:0000256|ARBA:ARBA00003277}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty aldehyde + CoA + NADP(+) = a long-chain
CC fatty acyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:15437,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17176, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:83139; EC=1.2.1.50;
CC Evidence={ECO:0000256|ARBA:ARBA00000747};
CC -!- PATHWAY: Lipid metabolism; fatty acid reduction for biolumincescence.
CC {ECO:0000256|ARBA:ARBA00004908}.
CC -!- SIMILARITY: Belongs to the LuxC family.
CC {ECO:0000256|ARBA:ARBA00010915}.
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DR EMBL; CP013187; ALO41440.1; -; Genomic_DNA.
DR RefSeq; WP_058029180.1; NZ_PNBV01000005.1.
DR AlphaFoldDB; A0A0S2JZ86; -.
DR STRING; 161398.PP2015_922; -.
DR KEGG; pphe:PP2015_922; -.
DR PATRIC; fig|161398.10.peg.938; -.
DR OrthoDB; 7156875at2; -.
DR UniPathway; UPA00569; -.
DR Proteomes; UP000061457; Chromosome I.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050062; F:long-chain-fatty-acyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR008670; CoA_reduct_LuxC.
DR Pfam; PF05893; LuxC; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
PE 3: Inferred from homology;
KW Luminescence {ECO:0000256|ARBA:ARBA00023223};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000061457}.
SQ SEQUENCE 405 AA; 45650 MW; 7D259087612B531E CRC64;
MIHIPNSIQT QCELVLGDWT SFHCRPETVW HERTIDFLTS LSTEIRRHPE AKSSPDLMAL
AFWLRKSHLL SMRRECHTAE LSMGLGLTFH ICPSNVPINF AYSLAFALLA GNSCVLRLSS
KSNRATEIVL QTLTDLINKP ENFSIAKRIL LLSYQYNDDI SAFWFSKAAG KVIWGGDSTI
NKMRQFPTPP RSREVAFADR YSFCVINAEY VLSIDNNQLQ SECQNIFNDI YQLDQAGCSS
PQLCIWVGSN NSILQAKGKI WQNVSIIAAK KRTDVNDIQV LNKFVNTCDA IIDHDQVTKV
DIISPQLTLI TVDKLNIAQH QFRGTSGQIY EASIQSLDEL VPLINEKVQT LSYLGIDKYA
LQELIINNNL TGIDRIVPTG KALNMHNLWD GYDIIAGLSR TITIE
//
