(data stored in ACNUC29543 zone)

SWISSPROT: B2JMM8_PARP8

ID   B2JMM8_PARP8            Unreviewed;       259 AA.
AC   B2JMM8;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000256|PIRNR:PIRNR000094};
DE            EC=1.3.1.9 {ECO:0000256|PIRNR:PIRNR000094};
GN   OrderedLocusNames=Bphy_3687 {ECO:0000313|EMBL:ACC72822.1};
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC72822.1, ECO:0000313|Proteomes:UP000001192};
RN   [1] {ECO:0000313|Proteomes:UP000001192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC   {ECO:0000313|Proteomes:UP000001192};
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A.,
RA   Melkonian R., James E.K., Young J.P., Bena G., Hauser L., Land M.,
RA   Kyrpides N., Bruce D., Chain P., Copeland A., Pitluck S., Woyke T.,
RA   Lizotte-Waniewski M., Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad
RT   host range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP]
CC         + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925,
CC         Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785;
CC         EC=1.3.1.9; Evidence={ECO:0000256|PIRNR:PIRNR000094};
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family. FabI subfamily. {ECO:0000256|PIRNR:PIRNR000094}.
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DR   EMBL; CP001044; ACC72822.1; -; Genomic_DNA.
DR   RefSeq; WP_012402995.1; NC_010623.1.
DR   STRING; 391038.Bphy_3687; -.
DR   EnsemblBacteria; ACC72822; ACC72822; Bphy_3687.
DR   GeneID; 27743353; -.
DR   KEGG; bph:Bphy_3687; -.
DR   eggNOG; ENOG4105CSJ; Bacteria.
DR   eggNOG; COG0623; LUCA.
DR   KO; K00208; -.
DR   OMA; VATAMHV; -.
DR   OrthoDB; 762291at2; -.
DR   BioCyc; BPHY391038:G1GBS-3782-MONOMER; -.
DR   Proteomes; UP000001192; Chromosome 2.
DR   GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd05372; ENR_SDR; 1.
DR   InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR43159:SF2; PTHR43159:SF2; 1.
DR   PIRSF; PIRSF000094; Enoyl-ACP_rdct; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
DR   PRODOM; B2JMM8.
DR   SWISS-2DPAGE; B2JMM8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001192};
KW   Fatty acid biosynthesis {ECO:0000256|PIRNR:PIRNR000094};
KW   Fatty acid metabolism {ECO:0000256|PIRNR:PIRNR000094};
KW   Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000094};
KW   Lipid metabolism {ECO:0000256|PIRNR:PIRNR000094};
KW   NAD {ECO:0000256|PIRNR:PIRNR000094, ECO:0000256|PIRSR:PIRSR000094-3};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000094};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001192}.
FT   NP_BIND      24     25       NAD. {ECO:0000256|PIRSR:PIRSR000094-3}.
FT   NP_BIND      69     70       NAD. {ECO:0000256|PIRSR:PIRSR000094-3}.
FT   ACT_SITE    150    150       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000094-1}.
FT   ACT_SITE    160    160       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000094-1}.
FT   BINDING      18     18       NAD; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000094-3}.
FT   BINDING      97     97       NAD; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000094-3}.
FT   BINDING     100    100       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000256|PIRSR:
FT                                PIRSR000094-2}.
FT   BINDING     167    167       NAD. {ECO:0000256|PIRSR:PIRSR000094-3}.
SQ   SEQUENCE   259 AA;  27531 MW;  79DA6E8C0573038F CRC64;
     MERPTGQVLA GSKALIVGIA NEHSIAYGCA RAFRELGADL AITYLNDKAK PYVEPLAQEL
     GATLLLPLDV SKPGELEAVF DAVRTTWGRL DVAVHSIAFA PKADLQGGLL NSSPEGFSVA
     MDISCHSFIR MARLAAPLMD DGGSLFAMSY LGASRVVPNY DLMGPVKAAL EASCRYLAHE
     LGPKRIRVHP ISPGPLKTRA ASGLKDFDLL LNEAAERAPI GELVDIMDVG YTCAFLATPY
     ARRMTGNTVF VDGGVSIIG
//

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