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Q9PKF7 (FABG_CHLMU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:TC_0508
OrganismChlamydia muridarum (strain MoPn / Nigg) [Complete proteome] [HAMAP]
Taxonomic identifier243161 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

Sequence similarities

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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2482483-oxoacyl-[acyl-carrier-protein] reductase FabG
PRO_0000054669

Regions

Nucleotide binding14 – 174NADP By similarity
Nucleotide binding65 – 662NADP By similarity
Nucleotide binding157 – 1615NADP By similarity

Sites

Active site1571Proton acceptor By similarity
Binding site921NADP; via carbonyl oxygen By similarity
Binding site1441Substrate By similarity
Binding site1901NADP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PKF7 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 1F5C8968CB05FF58

FASTA24825,977
        10         20         30         40         50         60 
MNSLLVNKAA IVTGGSRGIG FGIAKLFAEH GANVQIWGIN EEAGKSAAQD LSDKTGSKVS 

        70         80         90        100        110        120 
FALVDVSKND MVSAQVQKFL AEYGTIDVVV NNAGITRDSL LMRMSEEEWS SVIDTNLGSI 

       130        140        150        160        170        180 
YNVCSAVIRP MIKARSGAIV NISSIVGLRG SPGQTNYAAA KAGIIGFSKA LSKEVGSKNI 

       190        200        210        220        230        240 
RVNCIAPGFI DTDMTKGLSD NLKNEWLKGV PLGRVGTPEE IAMAALFLAS NQSSYITGQV 


LSVDGGMA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002160 Genomic DNA. Translation: AAF39350.1.
PIRE81695.
RefSeqNP_296885.1. NC_002620.2.

3D structure databases

ProteinModelPortalQ9PKF7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243161.TC0508.

Proteomic databases

PRIDEQ9PKF7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF39350; AAF39350; TC_0508.
GeneID1245868.
KEGGcmu:TC_0508.
PATRIC20372460. VBIChlMur19118_0546.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1028.
KOK00059.
OMAVTCKELD.
OrthoDBEOG6N3CR8.

Enzyme and pathway databases

BioCycCMUR243161:GHYU-529-MONOMER.
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]
PIRSFPIRSF000126. 11-beta-HSD1. 1 hit.
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
TIGRFAMsTIGR01830. 3oxo_ACP_reduc. 1 hit.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFABG_CHLMU
AccessionPrimary (citable) accession number: Q9PKF7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 87 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways