FABI_STAAR
ID FABI_STAAR Reviewed; 256 AA.
AC Q6GI75;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADPH] FabI;
DE Short=ENR;
DE EC=1.3.1.39;
DE AltName: Full=NADPH-dependent enoyl-ACP reductase;
GN Name=fabI; OrderedLocusNames=SAR0978;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) IN COMPLEX WITH NADP AND INHIBITOR,
RP AND SUBUNIT.
RX PubMed=19768684; DOI=10.1002/prot.22581;
RA Priyadarshi A., Kim E.E., Hwang K.Y.;
RT "Structural insights into Staphylococcus aureus enoyl-ACP reductase (FabI),
RT in complex with NADP and triclosan.";
RL Proteins 78:480-486(2010).
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] + NADP(+) = a (2E)-enoyl-[ACP] +
CC H(+) + NADPH; Xref=Rhea:RHEA:22564, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.39;
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:19768684}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. FabI subfamily. {ECO:0000305}.
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DR EMBL; BX571856; CAG39983.1; -; Genomic_DNA.
DR RefSeq; WP_000933195.1; NC_002952.2.
DR PDB; 3GNS; X-ray; 2.71 A; A=1-256.
DR PDB; 3GNT; X-ray; 2.75 A; A/B=1-256.
DR PDB; 3GR6; X-ray; 2.28 A; A/D/G/J=1-256.
DR PDB; 4FS3; X-ray; 1.80 A; A=1-256.
DR PDBsum; 3GNS; -.
DR PDBsum; 3GNT; -.
DR PDBsum; 3GR6; -.
DR PDBsum; 4FS3; -.
DR AlphaFoldDB; Q6GI75; -.
DR SMR; Q6GI75; -.
DR BindingDB; Q6GI75; -.
DR ChEMBL; CHEMBL3994; -.
DR DrugBank; DB11155; Triclocarban.
DR DrugBank; DB08604; Triclosan.
DR DrugCentral; Q6GI75; -.
DR KEGG; sar:SAR0978; -.
DR HOGENOM; CLU_010194_10_1_9; -.
DR OMA; GILDMIH; -.
DR OrthoDB; 762291at2; -.
DR BRENDA; 1.3.1.39; 3352.
DR UniPathway; UPA00094; -.
DR EvolutionaryTrace; Q6GI75; -.
DR Proteomes; UP000000596; Chromosome.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; ISS:UniProtKB.
DR GO; GO:0047117; F:enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR GO; GO:0030497; P:fatty acid elongation; 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; PTHR43159; 1.
DR PIRSF; PIRSF000094; Enoyl-ACP_rdct; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; NAD; NADP; Nucleotide-binding;
KW Oxidoreductase.
FT CHAIN 1..256
FT /note="Enoyl-[acyl-carrier-protein] reductase [NADPH] FabI"
FT /id="PRO_0000407979"
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 13
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19768684"
FT BINDING 19..20
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19768684"
FT BINDING 40..44
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19768684"
FT BINDING 66..67
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19768684"
FT BINDING 94
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19768684"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19768684"
FT BINDING 193..197
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19768684"
FT SITE 40
FT /note="Critical for cofactor specificity"
FT /evidence="ECO:0000250"
FT SITE 41
FT /note="Critical for cofactor specificity"
FT /evidence="ECO:0000250"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:4FS3"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:3GNS"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:4FS3"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:4FS3"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:4FS3"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:4FS3"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:4FS3"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:4FS3"
FT HELIX 70..84
FT /evidence="ECO:0007829|PDB:4FS3"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:4FS3"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:4FS3"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:4FS3"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:4FS3"
FT HELIX 123..133
FT /evidence="ECO:0007829|PDB:4FS3"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:4FS3"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:4FS3"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:4FS3"
FT HELIX 158..178
FT /evidence="ECO:0007829|PDB:4FS3"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:4FS3"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:4FS3"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:4FS3"
FT HELIX 204..214
FT /evidence="ECO:0007829|PDB:4FS3"
FT HELIX 223..234
FT /evidence="ECO:0007829|PDB:4FS3"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:4FS3"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:4FS3"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:4FS3"
SQ SEQUENCE 256 AA; 27992 MW; 69487F3F410B9A15 CRC64;
MLNLENKTYV IMGIANKRSI AFGVAKVLDQ LGAKLVFTYR KERSRKELEK LLEQLNQPEA
HLYQIDVQSD EEVINGFEQI GKDVGNIDGV YHSIAFANME DLRGRFSETS REGFLLAQDI
SSYSLTIVAH EAKKLMPEGG SIVATTYLGG EFAVQNYNVM GVAKASLEAN VKYLALDLGP
DNIRVNAISA GPIRTLSAKG VGGFNTILKE IEERAPLKRN VDQVEVGKTA AYLLSDLSSG
VTGENIHVDS GFHAIK
