(data stored in SCRATCH3701 zone)

SWISSPROT: FABI_RICTY

ID   FABI_RICTY              Reviewed;         261 AA.
AC   Q68X10;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 96.
DE   RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] FabI;
DE            Short=ENR;
DE            EC=1.3.1.9;
DE   AltName: Full=NADH-dependent enoyl-ACP reductase;
GN   Name=fabI; OrderedLocusNames=RT0353;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
CC   -!- FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an
CC       enoyl moiety that is covalently linked to an acyl carrier protein
CC       (ACP). Involved in the elongation cycle of fatty acid which are used in
CC       the lipid metabolism (By similarity). {ECO:0000250}.
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, Rhea:RHEA-
CC         COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. FabI subfamily. {ECO:0000305}.
DR   EMBL; AE017197; AAU03832.1; -; Genomic_DNA.
DR   RefSeq; WP_011190816.1; NC_006142.1.
DR   SMR; Q68X10; -.
DR   STRING; 257363.RT0353; -.
DR   EnsemblBacteria; AAU03832; AAU03832; RT0353.
DR   KEGG; rty:RT0353; -.
DR   eggNOG; ENOG4105CSJ; Bacteria.
DR   eggNOG; COG0623; LUCA.
DR   KO; K00208; -.
DR   OMA; GILDMIH; -.
DR   OrthoDB; 762291at2; -.
DR   BioCyc; RTYP257363:G1G0L-359-MONOMER; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000000604; Chromosome.
DR   GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; ISS:UniProtKB.
DR   GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB.
DR   GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
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; Q68X10.
DR   SWISS-2DPAGE; Q68X10.
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; NAD; Oxidoreductase.
FT   CHAIN           1..261
FT                   /note="Enoyl-[acyl-carrier-protein] reductase [NADH] FabI"
FT                   /id="PRO_0000286637"
FT   NP_BIND         21..22
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         66..67
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         193..197
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        147
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        157
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         15
FT                   /note="NAD; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   BINDING         42
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /note="NAD; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /note="Substrate; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   261 AA;  28713 MW;  45A3A9D3F0E6DF9F CRC64;
     MTTRLLQGKK GLITGIANNM SISWAIAQLA KKHGAELWFT YQSEALEKRV KPLAEEIGCN
     FISELDVTDQ KSISNLFNDI KEKWNSFDFL LHGMAFANKN ELKGRYVDTS LENFYNSLHI
     SCYSLLELSR SAETLMHDGG SILTLTYYGA EKVIPNYNIM GVAKAALEAS VKYLANDMGE
     NNIRVNAISA GPIKTLASSA ISDFSTMLKF HASTAPLKRN ITQEDVGGAA VYLFSELSKG
     VTGEIHYVDC GYNIIGSSKL L
//

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