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P50941 (FABG_RICPR) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-oxoacyl-[acyl-carrier-protein] reductase FabG

EC=1.1.1.100
Alternative name(s):
3-ketoacyl-acyl carrier protein reductase
Beta-Ketoacyl-acyl carrier protein reductase
Beta-ketoacyl-ACP reductase
Gene names
Name:fabG
Ordered Locus Names:RP762
OrganismRickettsia prowazekii (strain Madrid E) [Reference proteome] [HAMAP]
Taxonomic identifier272947 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length241 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis By similarity.

Catalytic activity

(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Homotetramer. Ref.4

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2412413-oxoacyl-[acyl-carrier-protein] reductase FabG
PRO_0000054679

Regions

Nucleotide binding13 – 164NADP By similarity
Nucleotide binding57 – 582NADP By similarity
Nucleotide binding148 – 1525NADP By similarity

Sites

Active site1481Proton acceptor By similarity
Binding site381NADP By similarity
Binding site831NADP; via carbonyl oxygen By similarity
Binding site1351Substrate By similarity
Binding site1811NADP; via amide nitrogen and carbonyl oxygen By similarity

Secondary structure

................................... 241
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P50941 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: E43B8711545B8295

FASTA24125,759
        10         20         30         40         50         60 
MIDLTGKTSL ITGASSGIGS AIARLLHKLG SKVIISGSNE EKLKSLGNAL KDNYTIEVCN 

        70         80         90        100        110        120 
LANKEECSNL ISKTSNLDIL VCNAGITSDT LAIRMKDQDF DKVIDINLKA NFILNREAIK 

       130        140        150        160        170        180 
KMIQKRYGRI INISSIVGIA GNPGQANYCA SKAGLIGMTK SLSYEVATRG ITVNAVAPGF 

       190        200        210        220        230        240 
IKSDMTDKLN EKQREAIVQK IPLGTYGIPE DVAYAVAFLA SNNASYITGQ TLHVNGGMLM 


V 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Rickettsia prowazekii and the origin of mitochondria."
Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G.
Nature 396:133-140(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Madrid E.
[2]"Isolation and characterization of the Rickettsia prowazekii recA gene."
Dunkin S.M., Winkler H.H., Wood D.O.
J. Bacteriol. 176:1777-1781(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
Strain: Madrid E.
[3]"Codon usage and base composition in Rickettsia prowazekii."
Andersson S.G.E., Sharp P.M.
J. Mol. Evol. 42:525-536(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[4]"Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase rickettsia prowazekII."
Joint center for strIuctural genomics (JCSG)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS), SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ235273 Genomic DNA. Translation: CAA15190.1.
U01959 Unassigned DNA. No translation available.
PIRF71636.
RefSeqNP_221114.1. NC_000963.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3F9IX-ray2.25A/B1-241[»]
ProteinModelPortalP50941.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272947.RP762.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAA15190; CAA15190; CAA15190.
GeneID883564.
KEGGrpr:RP762.
PATRIC17902389. VBIRicPro72556_0798.

Phylogenomic databases

eggNOGCOG1028.
KOK00059.
OMATSELRES.
OrthoDBEOG6N3CR8.
ProtClustDBPRK05653.

Enzyme and pathway databases

UniPathwayUPA00094.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR011284. 3oxo_ACP_reduc.
IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
TIGRFAMsTIGR01830. 3oxo_ACP_reduc. 1 hit.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP50941.

Entry information

Entry nameFABG_RICPR
AccessionPrimary (citable) accession number: P50941
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 30, 2000
Last modified: November 13, 2013
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Rickettsia prowazekii

Rickettsia prowazekii (strain Madrid E): entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways