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Q8KA28 (FABB_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. 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] synthase 1

EC=2.3.1.41
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase I
Beta-ketoacyl-ACP synthase I
Short name=KAS I
Gene names
Name:fabB
Ordered Locus Names:BUsg_084
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length407 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids By similarity.

Catalytic activity

Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the beta-ketoacyl-ACP synthases family.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function3-oxoacyl-[acyl-carrier-protein] synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4074073-oxoacyl-[acyl-carrier-protein] synthase 1
PRO_0000180309

Sites

Active site1641 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8KA28 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: CBCFC30445A34679

FASTA40744,523
        10         20         30         40         50         60 
MKRVVITGFG IISSIGNNKK EVLNSLYNGI SGITFSEEMK ESGMRSQVWG NIKLENKKFF 

        70         80         90        100        110        120 
KKNKISRFMN NGSIYAFLSM EQAIKDANLQ TKQYQKNPRI GIIAGSGGGF PKYHIQGIDA 

       130        140        150        160        170        180 
IRSNRGLNSV SPYIAIKAMN SGISACLSTL FKIYGVNYSI SSACATSGHC IGNAFELIKF 

       190        200        210        220        230        240 
GKQDLIFAGG GEEVSWELAY EFDAMKALSS NFNKNPTKSS RVYDVNRDGF VISGGGGIIV 

       250        260        270        280        290        300 
IEELNCALSR SAHIYAEIIG YAATSDGKDM VVPSGDGAVR CMNLAKKQNK MLFIDYLNVH 

       310        320        330        340        350        360 
GTSTKIGDLI ELEAIKKSFF HEKKPMISAT KSMTGHALGV SGVHEIIYTL LMMKYNFIAP 

       370        380        390        400 
SINIETIEPS ADNMNIVQKT FHKKIKTALS NSFGFGGTNV SLILKKY 

« 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: AAM67654.1.
RefSeqNP_660443.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8KA28.
SMRQ8KA28. Positions 1-406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg084.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67654; AAM67654; BUsg_084.
GeneID1005901.
KEGGbas:BUsg084.
PATRIC21246943. VBIBucAph100086_0086.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0304.
KOK00647.
OMANYLAMEQ.
OrthoDBEOG6DG2SR.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-93-MONOMER.
UniPathwayUPA00094.

Family and domain databases

Gene3D3.40.47.10. 2 hits.
InterProIPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamPF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
SUPFAMSSF53901. SSF53901. 2 hits.
PROSITEPS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFABB_BUCAP
AccessionPrimary (citable) accession number: Q8KA28
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: May 14, 2014
This is version 75 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