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A4JCP8 (FABH_BURVG) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

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

EC=2.3.1.41
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III
Beta-ketoacyl-ACP synthase III
Short name=KAS III
Gene names
Name:fabH
Ordered Locus Names:Bcep1808_1040
OrganismBurkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia (strain R1808)) [Complete proteome] [HAMAP]
Taxonomic identifier269482 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length329 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. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids By similarity. HAMAP MF_01815

Catalytic activity

Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]. HAMAP MF_01815

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP MF_01815

Subunit structure

Homodimer By similarity. HAMAP MF_01815

Subcellular location

Cytoplasm Probable HAMAP MF_01815.

Domain

The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH By similarity. HAMAP MF_01815

Sequence similarities

Belongs to the FabH family.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Lipid synthesis
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Multifunctional enzyme
Gene Ontology (GO)
   Biological processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3-oxoacyl-[acyl-carrier-protein] synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3293293-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
PRO_1000070227

Regions

Region257 – 2615ACP-binding By similarity

Sites

Active site1231 By similarity
Active site2561 By similarity
Active site2861 By similarity

Sequences

Sequence LengthMass (Da)Tools
A4JCP8 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: 66AFDB0C30B65D6D

FASTA32934,985
        10         20         30         40         50         60 
MAQSTLYSRV LGTGSYLPPD RVTNQQLADR LAKEGIETSD EWIVARTGIH ARHFAAPDVT 

        70         80         90        100        110        120 
TSDLAYQAAR RAIEAADIDP QSIDLIIVAT STPDFVFPST ACLLQNKLGI KSGGAAFDVQ 

       130        140        150        160        170        180 
AVCSGFAYAM AMADSFIRGG QHRTALVVGA ETFSRILDFK DRTTCVLFGD GAGAVILSAS 

       190        200        210        220        230        240 
EEPGVLGSAL HADGSYSNIL CTPGNVNRGV IEGSAFLHMD GQAVFKLAVN VLEKVAVEAL 

       250        260        270        280        290        300 
AKANLAPEQI DWLIPHQANI RIMTSTCRKL GLPQERMVVT VDQHGNTSAA SIPMALDVAV 

       310        320 
RDGRIQRGQH VLIEGVGGGF TWGASVFRF 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Tiedje J., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: G4 / LMG 22486.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000614 Genomic DNA. Translation: ABO54051.1.
RefSeqYP_001118886.1. NC_009256.1.

3D structure databases

ProteinModelPortalA4JCP8.
SMRA4JCP8. Positions 6-329.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4JCP8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4952746.
GenomeReviewsGene locus Bcep1808_1040 in contig CP000614_GR.
KEGGbvi:Bcep1808_1040.
PATRIC19320589. VBIBurVie89221_5274.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHBG649927.
OMARILNFLA.
ProtClustDBPRK09352.

Enzyme and pathway databases

BioCycBVIE269482:BCEP1808_1040-MONOMER.

Family and domain databases

HAMAPMF_01815. FabH.
[Tree]
InterProIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
KOK00648.
PfamPF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]
SUPFAMSSF53901. Thiolase-like. 1 hit.
TIGRFAMsTIGR00747. FabH. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFABH_BURVG
AccessionPrimary (citable) accession number: A4JCP8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 1, 2007
Last modified: December 14, 2011
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families