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Q8K9J5 (FABG_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BUsg_339
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length244 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.

Miscellaneous

Calcium ions stabilize the structure, and may inhibit FabG activity by obstructing access to the active site By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2442443-oxoacyl-[acyl-carrier-protein] reductase FabG
PRO_0000054667

Regions

Nucleotide binding12 – 154NADP By similarity
Nucleotide binding59 – 602NADP By similarity
Nucleotide binding151 – 1555NADP By similarity

Sites

Active site1511Proton acceptor By similarity
Metal binding501Calcium 1; via carbonyl oxygen; shared with dimeric partner By similarity
Metal binding531Calcium 1; via carbonyl oxygen; shared with dimeric partner By similarity
Metal binding1451Calcium 2 By similarity
Metal binding2331Calcium 3; shared with dimeric partner By similarity
Metal binding2341Calcium 3; via carbonyl oxygen; shared with dimeric partner By similarity
Binding site371NADP By similarity
Binding site861NADP; via carbonyl oxygen By similarity
Binding site1381Substrate By similarity
Binding site1841NADP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8K9J5 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 14526C91CDC54D5A

FASTA24426,939
        10         20         30         40         50         60 
MKIEKKTALV TGANQGLGKE IAIKLSQKGI QVIGTSTTVD GVKTINKYLK KNGFGFILDL 

        70         80         90        100        110        120 
KDTDSILEKM KEICQKKYSI DILINNAGIT SDNLLVYMSN KEWENVIKIN LTSVFYMSKS 

       130        140        150        160        170        180 
VIRSMIKKRY GRIVTIGSVI GYLGNRGQIN YSASKSGLIG FHKSLALEVA QKGITVNIVS 

       190        200        210        220        230        240 
PGFIKTNLTK NLNVFQYKKH LSKIPMKRIG TAEEIANAVI FLSSEKASYI TGQTIHVNGG 


MYMT 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM67893.1.
RefSeqNP_660682.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8K9J5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg339.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67893; AAM67893; BUsg_339.
GeneID1005569.
KEGGbas:BUsg339.
PATRIC21247493. VBIBucAph100086_0353.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1028.
KOK00059.
OMAMESAMGE.
OrthoDBEOG6N3CR8.
ProtClustDBCLSK441831.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-356-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]
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...

Entry information

Entry nameFABG_BUCAP
AccessionPrimary (citable) accession number: Q8K9J5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 1, 2002
Last modified: November 13, 2013
This is version 81 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

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names