(data stored in ACNUC7421 zone)

SWISSPROT: Q13IW2_PARXL

ID   Q13IW2_PARXL            Unreviewed;       257 AA.
AC   Q13IW2;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 95.
DE   RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000256|PIRNR:PIRNR000094};
DE            EC=1.3.1.9 {ECO:0000256|PIRNR:PIRNR000094};
GN   ORFNames=Bxe_C0050 {ECO:0000313|EMBL:ABE35977.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE35977.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE35977.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE35977.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000272; ABE35977.1; -; Genomic_DNA.
DR   RefSeq; WP_011493237.1; NZ_CP008761.1.
DR   STRING; 266265.Bxe_C0050; -.
DR   EnsemblBacteria; ABE35977; ABE35977; Bxe_C0050.
DR   GeneID; 4009597; -.
DR   KEGG; bxb:DR64_8374; -.
DR   KEGG; bxe:Bxe_C0050; -.
DR   PATRIC; fig|266265.5.peg.7830; -.
DR   eggNOG; ENOG4105CSJ; Bacteria.
DR   eggNOG; COG0623; LUCA.
DR   KO; K00208; -.
DR   OMA; ARRISGN; -.
DR   OrthoDB; 762291at2; -.
DR   BioCyc; BXEN266265:BXE_RS37005-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 3.
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   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; Q13IW2.
DR   SWISS-2DPAGE; Q13IW2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
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:ABE35977.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   NP_BIND      22     23       NAD. {ECO:0000256|PIRSR:PIRSR000094-3}.
FT   NP_BIND      67     68       NAD. {ECO:0000256|PIRSR:PIRSR000094-3}.
FT   NP_BIND     194    198       NAD. {ECO:0000256|PIRSR:PIRSR000094-3}.
FT   BINDING      16     16       NAD; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000094-3}.
FT   BINDING      95     95       NAD; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000094-3}.
FT   BINDING      98     98       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000256|PIRSR:
FT                                PIRSR000094-2}.
FT   BINDING     165    165       NAD. {ECO:0000256|PIRSR:PIRSR000094-3}.
SQ   SEQUENCE   257 AA;  27255 MW;  84B65BE0D584E7A8 CRC64;
     MNGIIDLSGK RGLVVGIANE HSIAAGCARM FRAIGAEIAV TYLNDKAEPY VRAVAETLPA
     SLVMPCDVTV PGQLEAVFAR ISREWGKLDF VLHSIAFAPA VDLHASLVDC SAEGFALAMD
     VSCHSFIRMT RLALPLMAEG GSLMTVSFYG AERAVDHYNL MGPVKAALES SVRYLAVDLA
     PRRVHVHAIS AGAVKTRAAS GLDHFDVLLD EVRARTPARH LVTIDEIGRI AAVLASDAGM
     TLTGSTLYAD AGFHVVA
//

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