(data stored in ACNUC7421 zone)

SWISSPROT: Q5LWR9_RUEPO

ID   Q5LWR9_RUEPO            Unreviewed;       254 AA.
AC   Q5LWR9;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 106.
DE   RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000256|PIRNR:PIRNR000094};
DE            EC=1.3.1.9 {ECO:0000256|PIRNR:PIRNR000094};
GN   Name=fabI-1 {ECO:0000313|EMBL:AAV93443.1};
GN   OrderedLocusNames=SPO0113 {ECO:0000313|EMBL:AAV93443.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93443.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93443.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93443.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(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; CP000031; AAV93443.1; -; Genomic_DNA.
DR   RefSeq; WP_011045886.1; NC_003911.12.
DR   STRING; 246200.SPO0113; -.
DR   EnsemblBacteria; AAV93443; AAV93443; SPO0113.
DR   KEGG; sil:SPO0113; -.
DR   eggNOG; ENOG4105CSJ; Bacteria.
DR   eggNOG; COG0623; LUCA.
DR   KO; K00208; -.
DR   OMA; VATAMHV; -.
DR   OrthoDB; 762291at2; -.
DR   BioCyc; RPOM246200:G1G48-114-MONOMER; -.
DR   Proteomes; UP000001023; Chromosome.
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; Q5LWR9.
DR   SWISS-2DPAGE; Q5LWR9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
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   ECO:0000313|EMBL:AAV93443.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023}.
FT   NP_BIND      19     20       NAD. {ECO:0000256|PIRSR:PIRSR000094-3}.
FT   NP_BIND      64     65       NAD. {ECO:0000256|PIRSR:PIRSR000094-3}.
FT   ACT_SITE    145    145       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000094-1}.
FT   ACT_SITE    155    155       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000094-1}.
FT   BINDING      13     13       NAD; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000094-3}.
FT   BINDING      92     92       NAD; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000094-3}.
FT   BINDING     162    162       NAD. {ECO:0000256|PIRSR:PIRSR000094-3}.
SQ   SEQUENCE   254 AA;  27230 MW;  5D6BE606B4C1850F CRC64;
     MGLLDGKRGL VVGIANERSI ASGCAQAFHR EGAELAVTYL NEKARPFVQP VAEALDAEIF
     MPLDVTADAE MDALFEAIAS SWGRLDFILH SVAYCPKEDL HGNVLDCSRE GFSAAMDISV
     HSFMRLARRA RPLMQNGGCL LTVSYYGAEK VVDHYNVMGP VKAALESTVK YMAAELGPEG
     IRVNALSPGP LMTRAASGIA HFDALIDEAR ARAPQQRLVT IEDVGNMAAG LVSDAARNVT
     GNISYVDAGY HVMS
//

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