Skip Header

Contribute Send feedback
Read comments (?) or add your own

A8FKB7 (FABH_CAMJ8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. 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] 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:C8J_0305
OrganismCampylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828) [Complete proteome] [HAMAP]
Taxonomic identifier407148 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length324 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 – 3243243-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
PRO_1000073680

Regions

Region247 – 2515ACP-binding By similarity

Sites

Active site1141 By similarity
Active site2461 By similarity
Active site2761 By similarity

Sequences

Sequence LengthMass (Da)Tools
A8FKB7 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 7774F8A82451709B

FASTA32435,192
        10         20         30         40         50         60 
MLKASLKSIA SYIPEKILSN ADLEKMVDTT DEWITRRTGI KERRIASENE NTSDLGTKAA 

        70         80         90        100        110        120 
LKAIKRANLK PEDIDAILVA TLSPDYFTMP STACKIASNL GLVNISAFDI SAACSGFIYL 

       130        140        150        160        170        180 
LEQAKALVES GLKKNVLIIG AEKTSSIMDY NDRSICILFG DGAGAGVVSL DNENHILDVH 

       190        200        210        220        230        240 
TASNGNYGDL LMTQRSQKSN LCQTLSMQMK GNEVFKIAVN TLSNDVVEIL AKNNILAQEI 

       250        260        270        280        290        300 
DLFIPHQANL RIIKAVQEKL NLSDEKCVIT VQKYGNTSAA SIPMAMNDAY EEGRLKKGDL 

       310        320 
ILLDAFGGGF TWGSALLKFG GENF 

« Hide

References

[1]"The complete genome sequence of Campylobacter jejuni strain 81116 (NCTC11828)."
Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M., van Vliet A.H.M.
J. Bacteriol. 189:8402-8403(2007) [PubMed: 17873037] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 81116 / NCTC 11828.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000814 Genomic DNA. Translation: ABV51904.1.
RefSeqYP_001481881.1. NC_009839.1.

3D structure databases

ProteinModelPortalA8FKB7.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8FKB7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5618283.
GenomeReviewsGene locus C8J_0305 in contig CP000814_GR.
KEGGcju:C8J_0305.
PATRIC20054180. VBICamJej119085_0313.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHBG649927.
OMADAYIRGG.
ProtClustDBPRK09352.

Enzyme and pathway databases

BioCycCJEJ407148:C8J_0305-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_CAMJ8
AccessionPrimary (citable) accession number: A8FKB7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: November 13, 2007
Last modified: January 25, 2012
This is version 30 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