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Database: UniProt
Entry: A0A196MV70_9SPHN
LinkDB: A0A196MV70_9SPHN
Original site: A0A196MV70_9SPHN 
ID   A0A196MV70_9SPHN        Unreviewed;       474 AA.
AC   A0A196MV70;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   11-DEC-2019, entry version 11.
DE   RecName: Full=Acyl-CoA reductase {ECO:0000256|PIRNR:PIRNR009414};
DE            EC=1.2.1.50 {ECO:0000256|PIRNR:PIRNR009414};
GN   ORFNames=A7Q26_00470 {ECO:0000313|EMBL:OAN59314.1};
OS   Sphingobium sp. TCM1.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=453246 {ECO:0000313|EMBL:OAN59314.1, ECO:0000313|Proteomes:UP000078322};
RN   [1] {ECO:0000313|EMBL:OAN59314.1, ECO:0000313|Proteomes:UP000078322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TCM1 {ECO:0000313|EMBL:OAN59314.1,
RC   ECO:0000313|Proteomes:UP000078322};
RA   Takahashi S.;
RT   "Draft Genome Sequences of Sphingobium sp. strain TCM1 and Sphingomonas sp.
RT   strain TDK1, Haloalkyl Organophosphorus Flame Retardant-Degrading
RT   Bacteria.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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|PIRNR:PIRNR009414};
CC   -!- SIMILARITY: Belongs to the LuxC family.
CC       {ECO:0000256|PIRNR:PIRNR009414}.
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:OAN59314.1}.
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DR   EMBL; LXVX01000001; OAN59314.1; -; Genomic_DNA.
DR   RefSeq; WP_066854936.1; NZ_LXVX01000001.1.
DR   EnsemblBacteria; OAN59314; OAN59314; A7Q26_00470.
DR   Proteomes; UP000078322; 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:InterPro.
DR   CDD; cd07080; ALDH_Acyl-CoA-Red_LuxC; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR008670; CoA_reduct_LuxC.
DR   Pfam; PF05893; LuxC; 1.
DR   PIRSF; PIRSF009414; LuxC; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|PIRNR:PIRNR009414};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR009414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078322}.
SQ   SEQUENCE   474 AA;  52046 MW;  CAD742281B9A2DF0 CRC64;
     MTVVEKNAAI AQAPVEPIQV RHFVRGRLVE GDAVRHRSRD LGVDFVTPEI DLNALVAQRS
     ELPPLYDVPT TEIVDFLVEA GRRMDFETNP YLREALEHTV KVNPLPRRVV ENLFRRARHF
     LTRDGLMSSI ETSFLNPAAL DGWVARIDAH GNRGALRAFP TRMVHMLAGN SPTGCISSIA
     QGALVKAVNL FKMPSSDPFT CVAMLRTMAD VDPNHPVVKS MSAVYWRGGD TRIEGALYRP
     QYFDKIVAWG GGDAIRNVIQ YIGPGLQMVS FDPKTSISMI GAEAFVSPDV IEQVAQAAAI
     DVATMNQEAC LASRFLFVEG ERAGIETFCA RLQEQLGIDR ETASAIGQPP PREVREEIEM
     RQMMGDDCKV WGKPDGRGLV ILTDEPVDFH PSNKTANVVH VASLDDAIAH VNVATQTIGV
     YPPERKAALR DRLASAGAQR VVRLGGAAKH VAGGTHDGMF PMQHLVRWMS EEDA
//
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