FABG_STAAM
ID FABG_STAAM Reviewed; 246 AA.
AC P0A0H9; Q99QK7;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase FabG;
DE EC=1.1.1.100;
DE AltName: Full=3-ketoacyl-acyl carrier protein reductase;
DE AltName: Full=Beta-Ketoacyl-acyl carrier protein reductase;
DE AltName: Full=Beta-ketoacyl-ACP reductase;
GN Name=fabG; OrderedLocusNames=SAV1231;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND SUBUNIT.
RA Anderson S.M., Wawrzak Z., Onopriyenko O., Edwards A., Anderson W.F.,
RA Savchenko A.;
RT "Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, FabG,
RT from Staphylococcus aureus.";
RL Submitted (SEP-2010) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP
CC substrates to beta-hydroxyacyl-ACP products, the first reductive step
CC in the elongation cycle of fatty acid biosynthesis. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; BA000017; BAB57393.1; -; Genomic_DNA.
DR PDB; 3OSU; X-ray; 1.90 A; A/B=1-246.
DR PDBsum; 3OSU; -.
DR AlphaFoldDB; P0A0H9; -.
DR SMR; P0A0H9; -.
DR World-2DPAGE; 0002:P0A0H9; -.
DR PaxDb; P0A0H9; -.
DR EnsemblBacteria; BAB57393; BAB57393; SAV1231.
DR KEGG; sav:SAV1231; -.
DR HOGENOM; CLU_010194_1_3_9; -.
DR OMA; KMPERDY; -.
DR PhylomeDB; P0A0H9; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000002481; Chromosome.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR011284; 3oxo_ACP_reduc.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01830; 3oxo_ACP_reduc; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase.
FT CHAIN 1..246
FT /note="3-oxoacyl-[acyl-carrier-protein] reductase FabG"
FT /id="PRO_0000054684"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 11..14
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 62..63
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 154..158
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:3OSU"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:3OSU"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:3OSU"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:3OSU"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:3OSU"
FT HELIX 66..80
FT /evidence="ECO:0007829|PDB:3OSU"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:3OSU"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:3OSU"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:3OSU"
FT HELIX 115..131
FT /evidence="ECO:0007829|PDB:3OSU"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:3OSU"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:3OSU"
FT HELIX 152..172
FT /evidence="ECO:0007829|PDB:3OSU"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:3OSU"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:3OSU"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:3OSU"
FT HELIX 197..204
FT /evidence="ECO:0007829|PDB:3OSU"
FT HELIX 215..225
FT /evidence="ECO:0007829|PDB:3OSU"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:3OSU"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:3OSU"
SQ SEQUENCE 246 AA; 26146 MW; 2BD7CA319D3A37C5 CRC64;
MKMTKSALVT GASRGIGRSI ALQLAEEGYN VAVNYAGSKE KAEAVVEEIK AKGVDSFAIQ
ANVADADEVK AMIKEVVSQF GSLDVLVNNA GITRDNLLMR MKEQEWDDVI DTNLKGVFNC
IQKATPQMLR QRSGAIINLS SVVGAVGNPG QANYVATKAG VIGLTKSAAR ELASRGITVN
AVAPGFIVSD MTDALSDELK EQMLTQIPLA RFGQDTDIAN TVAFLASDKA KYITGQTIHV
NGGMYM
