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Q89AG9 (FABG_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 74. 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:bbp_321
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length245 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 – 2452453-oxoacyl-[acyl-carrier-protein] reductase FabG
PRO_0000054668

Regions

Nucleotide binding12 – 154NADP By similarity
Nucleotide binding60 – 612NADP By similarity
Nucleotide binding152 – 1565NADP By similarity

Sites

Active site1521Proton acceptor By similarity
Metal binding511Calcium 1; via carbonyl oxygen; shared with dimeric partner By similarity
Metal binding541Calcium 1; via carbonyl oxygen; shared with dimeric partner By similarity
Metal binding1461Calcium 2 By similarity
Metal binding2341Calcium 3; shared with dimeric partner By similarity
Metal binding2351Calcium 3; via carbonyl oxygen; shared with dimeric partner By similarity
Binding site381NADP By similarity
Binding site871NADP; via carbonyl oxygen By similarity
Binding site1391Substrate By similarity
Binding site1851NADP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q89AG9 [UniParc].

Last modified May 30, 2003. Version 1.
Checksum: 6B94C5520D69157E

FASTA24526,788
        10         20         30         40         50         60 
MKTTKKIAVI TGANRGLGKG IAEELSNTNN ITVIGTSTSQ KGCKIINKYL KNNGIGIKLD 

        70         80         90        100        110        120 
ITNPNEITKT MDFVYKNFGR VDILINNAGI IRDKLLINMK TQDWNSVLNV NLNSIFYMSK 

       130        140        150        160        170        180 
SVIRNMIKNK QGKIITIGSV IAHIGNCGQT NYSAAKLGLV GFHKSLALEL APKGITVNMI 

       190        200        210        220        230        240 
APGLIKTGMT NNLSQKQLSK YLSKIPMKRL GTIKEISKIT LFLISNDANY ITGQVIHVNG 


GMYMP 

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016826 Genomic DNA. Translation: AAO27043.1.
RefSeqNP_777938.1. NC_004545.1.

3D structure databases

ProteinModelPortalQ89AG9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224915.bbp321.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO27043; AAO27043; bbp_321.
GeneID1058479.
KEGGbab:bbp321.
PATRIC21245431. VBIBucAph80364_0315.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1028.
KOK00059.
OMAEGIEGWI.
OrthoDBEOG6N3CR8.

Enzyme and pathway databases

BioCycBAPH224915:GJ9D-321-MONOMER.
UniPathwayUPA00094.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. 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.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFABG_BUCBP
AccessionPrimary (citable) accession number: Q89AG9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2003
Last sequence update: May 30, 2003
Last modified: May 14, 2014
This is version 74 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