ID J2PVC6_9PSED Unreviewed; 798 AA.
AC J2PVC6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=PMI23_03857 {ECO:0000313|EMBL:EJM33856.1};
OS Pseudomonas sp. GM24.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144326 {ECO:0000313|EMBL:EJM33856.1, ECO:0000313|Proteomes:UP000007503};
RN [1] {ECO:0000313|EMBL:EJM33856.1, ECO:0000313|Proteomes:UP000007503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM24 {ECO:0000313|EMBL:EJM33856.1,
RC ECO:0000313|Proteomes:UP000007503};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJM33856.1}.
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DR EMBL; AKJR01000168; EJM33856.1; -; Genomic_DNA.
DR RefSeq; WP_007918117.1; NZ_AKJR01000168.1.
DR AlphaFoldDB; J2PVC6; -.
DR PATRIC; fig|1144326.3.peg.3752; -.
DR UniPathway; UPA00569; -.
DR Proteomes; UP000007503; Unassembled WGS sequence.
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 Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR008670; CoA_reduct_LuxC.
DR PANTHER; PTHR43845; BLR5969 PROTEIN; 1.
DR PANTHER; PTHR43845:SF1; BLR5969 PROTEIN; 1.
DR Pfam; PF05893; LuxC; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
PE 3: Inferred from homology;
KW Luminescence {ECO:0000256|ARBA:ARBA00023223};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ SEQUENCE 798 AA; 87111 MW; 605377D31EAD260C CRC64;
MYLINGELHA DVDLDNALAL LQQTLPQRLS TPLDSATVLT AAAHFAGQLH NAELPLDDEQ
RQVLIDFCQP HALQHKLERE LGDQAESLRR VDYQHSRFER WSPLGLVVHV TPANAPLLAC
CALIESLLAG NINWLRPSSS DQGLTARLLH TLVQCDPSGE LRHYVAVLPV ATAQIGRLCK
MANGVSAWGG EAALQAIRQQ LPPGCRWIDW GHRISFAYLT PQAASPQALD ALVDEVCRLD
QQACSSPQWL LVDSDDPAVL QAIGNELAKA FERRAGQWPA LIPTVQEASE ITTRTLMTRL
SQSFSAVTAQ VWSAPGWRVI WSHDQLLAPS PLFRTVLLKP LPRARLTQNL LPWRNVLQSC
ALMCDEAQIG ALSRTLIAAG VSRIAPIDAI HDGYDGEPHD GVYALQRLSR RVSVSVAPTQ
LPTHMTLDRP ACKPTLAGLA ITDKAAFIAR PTTAAAQLFF RSGGSSGTPA LAGYSYRDFQ
RQIRATADGL FAAGLDPSRD KVMNLFFSGG LYGGFFSFAK VLETLGASHL PMGAPADDDY
GDIAQVIIEQ QVTVLIGMPS SLHRLFLNEQ QRLSRYGAIE KVFLGGEHIS EQCRELLQRC
GVASIRSAVY GSVDAGPCGH ACAATGDGVF HLMDAIQHLE IVALEEDVPV VGNEIGRLLF
TSKAREGQQV QRYEVGDTGR WLPGDCACGL SSPRFELLQR HGRLLRIGSD FICLNELGRH
LQAPFQLHLD HAPDGLERLL VRSPAAPADL LLRLEGYATL TSLVRAGLLT VQTQTCETQQ
FDRNRHSGKI PAVVDARR
//
