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Q39I86 (FABH_BURS3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. 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:Bcep18194_A4233
OrganismBurkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194)) [Complete proteome] [HAMAP]
Taxonomic identifier269483 [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_1000070225

Regions

Region257 – 2615ACP-binding By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q39I86 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 9544EA3DF63E7F8C

FASTA32935,062
        10         20         30         40         50         60 
MAQSTLYSRV LGTGSYLPPD RVTNQQLTDR LAKEGIETSD EWIVARTGIH ARHFAAPDVT 

        70         80         90        100        110        120 
TSDLALEASR RAIEAAGIDP QSIDLIIVAT STPDFVFPST ACLLQNKLGI KNGGAAFDVQ 

       130        140        150        160        170        180 
AVCSGFAYAM ATADSFIRSG QHRTALVIGA ETFSRILDFK DRTTCVLFGD GAGAVILSAS 

       190        200        210        220        230        240 
EEPGVLGSAL HADGSYSHIL CTPGNVNRGV IEGSAFLYMD GQAVFKLAVN VLEKVAIEAL 

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

       310        320 
RDGRIQRGQH VLIEGVGGGF TWGASVFRY 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia sp. 383."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 383.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000151 Genomic DNA. Translation: ABB07830.1.
RefSeqYP_368474.1. NC_007510.1.

3D structure databases

ProteinModelPortalQ39I86.
SMRQ39I86. Positions 6-329.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ39I86.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3749428.
GenomeReviewsGene locus Bcep18194_A4233 in contig CP000151_GR.
KEGGbur:Bcep18194_A4233.
NMPDRfig|269483.3.peg.5453.
PATRIC19285825. VBIBurSp120713_2335.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHBG649927.
OMARILNFLA.
ProtClustDBPRK09352.

Enzyme and pathway databases

BioCycBSP36773:BCEP18194_A4233-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_BURS3
AccessionPrimary (citable) accession number: Q39I86
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 22, 2005
Last modified: January 25, 2012
This is version 48 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