FABG_RICPR
ID FABG_RICPR Reviewed; 241 AA.
AC P50941;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 125.
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=RP762;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
RC STRAIN=Madrid E;
RX PubMed=8132476; DOI=10.1128/jb.176.6.1777-1781.1994;
RA Dunkin S.M., Winkler H.H., Wood D.O.;
RT "Isolation and characterization of the Rickettsia prowazekii recA gene.";
RL J. Bacteriol. 176:1777-1781(1994).
RN [3]
RP IDENTIFICATION.
RX PubMed=8662004; DOI=10.1007/bf02352282;
RA Andersson S.G.E., Sharp P.M.;
RT "Codon usage and base composition in Rickettsia prowazekii.";
RL J. Mol. Evol. 42:525-536(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS), AND SUBUNIT.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase
RT Rickettsia prowazekii.";
RL Submitted (FEB-2009) 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.4}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AJ235273; CAA15190.1; -; Genomic_DNA.
DR EMBL; U01959; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR PIR; F71636; F71636.
DR RefSeq; NP_221114.1; NC_000963.1.
DR RefSeq; WP_010886363.1; NC_000963.1.
DR PDB; 3F9I; X-ray; 2.25 A; A/B=1-241.
DR PDBsum; 3F9I; -.
DR AlphaFoldDB; P50941; -.
DR SMR; P50941; -.
DR STRING; 272947.RP762; -.
DR EnsemblBacteria; CAA15190; CAA15190; CAA15190.
DR KEGG; rpr:RP762; -.
DR PATRIC; fig|272947.5.peg.798; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_3_5; -.
DR OMA; KMPERDY; -.
DR BRENDA; 1.1.1.100; 5447.
DR UniPathway; UPA00094; -.
DR EvolutionaryTrace; P50941; -.
DR Proteomes; UP000002480; Chromosome.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; ISS:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; ISS:UniProtKB.
DR GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB.
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;
KW Reference proteome.
FT CHAIN 1..241
FT /note="3-oxoacyl-[acyl-carrier-protein] reductase FabG"
FT /id="PRO_0000054679"
FT ACT_SITE 148
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 13..16
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 57..58
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 148..152
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:3F9I"
FT TURN 12..15
FT /evidence="ECO:0007829|PDB:3F9I"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:3F9I"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:3F9I"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:3F9I"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:3F9I"
FT HELIX 64..72
FT /evidence="ECO:0007829|PDB:3F9I"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:3F9I"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:3F9I"
FT HELIX 109..125
FT /evidence="ECO:0007829|PDB:3F9I"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:3F9I"
FT HELIX 146..166
FT /evidence="ECO:0007829|PDB:3F9I"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:3F9I"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:3F9I"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:3F9I"
FT HELIX 209..220
FT /evidence="ECO:0007829|PDB:3F9I"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:3F9I"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:3F9I"
SQ SEQUENCE 241 AA; 25759 MW; E43B8711545B8295 CRC64;
MIDLTGKTSL ITGASSGIGS AIARLLHKLG SKVIISGSNE EKLKSLGNAL KDNYTIEVCN
LANKEECSNL ISKTSNLDIL VCNAGITSDT LAIRMKDQDF DKVIDINLKA NFILNREAIK
KMIQKRYGRI INISSIVGIA GNPGQANYCA SKAGLIGMTK SLSYEVATRG ITVNAVAPGF
IKSDMTDKLN EKQREAIVQK IPLGTYGIPE DVAYAVAFLA SNNASYITGQ TLHVNGGMLM
V
