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Reviewed, UniProtKB/Swiss-Prot A7I3D6 (FABH_CAMHC)

Last modified November 3, 2009. Version 15. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: CHAB381_1492
OrganismCampylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A) [Complete proteome] [HAMAP]
Taxonomic identifier360107 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

Subcellular location

Cytoplasm Probable.

Domain

The last Arg residue of the ACP-binding site is essential for the weak association between ACP/acpP and fabH By similarity.

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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

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

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3333333-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
PRO_1000056335

Regions

Region259 – 2635ACP-binding By similarity

Sites

Active site1141 By similarity
Active site2581 By similarity
Active site2881 By similarity

Sequences

Sequence LengthMass (Da)Tools
A7I3D6-1 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: C7D1A3ACE66F5470

FASTA33335,873
        10         20         30         40         50         60 
MKNAAMLSIG AYVPPYELSN FDLEKMVETS DEWIVKRTGI HTRHIAKNET AGDMAAKAAD 

        70         80         90        100        110        120 
LAISRSGISK EEIDAIICAT ITPDFFCMPS TACITAEKLG LNKGITAFDI SAACSGFIYL 

       130        140        150        160        170        180 
LEIGSALIKS GAKKNVLIIG TEKLSSIVDW KDRATCVLFG DGAGAAVLSC MDNKNNGISK 

       190        200        210        220        230        240 
PYGIIDIHTA SDGNKAELLM TPTKNSNIKD IADENLGFLH MKGNEVFKIA VQTLSNDVVK 

       250        260        270        280        290        300 
ILKKNNVKPE EIDLFVPHQA NFRIIEAVKN RLNFTDNQCV VTVGKYGNTS SASIPIALNE 

       310        320        330 
AYENGRLKNG SLILLDAFGG GFTWGSALIR FGL 

« Hide

References

[1]"Complete genome sequence of Campylobacter hominis ATCC BAA-381, a commensal isolated from the human gastrointestinal tract."
Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Nelson K.E.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000776 Genomic DNA. Translation: ABS52499.1.
RefSeqYP_001407027.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA7I3D6.

Genome annotation databases

GeneID5408858.
GenomeReviewsGene locus CHAB381_1492 in contig CP000776_GR.
KEGGcha:CHAB381_1492.
NMPDRfig|360107.5.peg.1458.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAYSRITGT.

Family and domain databases

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

Entry information

Entry nameFABH_CAMHC
AccessionPrimary (citable) accession number: A7I3D6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 11, 2007
Last modified: November 3, 2009
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents