ID A0A2A8HTW6_9SPHN Unreviewed; 491 AA.
AC A0A2A8HTW6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=B2G71_12240 {ECO:0000313|EMBL:PEQ12394.1};
OS Novosphingobium sp. PC22D.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1962403 {ECO:0000313|EMBL:PEQ12394.1, ECO:0000313|Proteomes:UP000220675};
RN [1] {ECO:0000313|EMBL:PEQ12394.1, ECO:0000313|Proteomes:UP000220675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC22D {ECO:0000313|EMBL:PEQ12394.1,
RC ECO:0000313|Proteomes:UP000220675};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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}.
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:PEQ12394.1}.
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DR EMBL; MWMO01000007; PEQ12394.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A8HTW6; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00569; -.
DR Proteomes; UP000220675; 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 InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
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:UP000220675}.
SQ SEQUENCE 491 AA; 54233 MW; 291D004B77D5DA62 CRC64;
MAKRPISYAV LRGKVIETDL VEFGGRGGDI TFLAPDPHAI ADQIPIASPR LMEDLYEISL
EDILDYLAEL GERLHLKDNP YLQEALEYSY ATAPTTKPIM DGFFHDMPFM FDKDRIRGMV
DFNIGIDYLE GWKTTDINGS RVGIRAYGAR TLHIVAGNGP VLGALTVIRG AVTRGDTIIK
VPSNDPFTTG AIARTMVDMA PDHPVTKHLA VAYWRGGDEA LESRLYQPHN IEKICAWGGF
ASVKHVTKYI QPGIELISLD PKRSASIVGG EALDDDAMMN EAANRIATDV ATGNQTACAA
CRMVYVTCGT DDEGVAKLRQ LGQKTYDAMM RLPEALTTKP KRYDPELKSQ VDMLRLSDDF
YTVIGGEDGE GAVLVSHTPD RVEFWEYLAD RTVNLIPVDT IDEVLDVVDA YTQTVGVYPE
SLREIVRHKG ALHGGQRFVS LGYAFNGPGL VGPQDGIEPM RRIVKWIISE EPLPGRKPFW
ECSNEEIKVV A
//
