Skip Header

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

A8ERJ6 (FABH_ARCB4) 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:Abu_0295
OrganismArcobacter butzleri (strain RM4018) [Complete proteome] [HAMAP]
Taxonomic identifier367737 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeArcobacter

Protein attributes

Sequence length333 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 – 3333333-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
PRO_1000070213

Regions

Region256 – 2605ACP-binding By similarity

Sites

Active site1141 By similarity
Active site2551 By similarity
Active site2851 By similarity

Sequences

Sequence LengthMass (Da)Tools
A8ERJ6 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 956C4CE41AC1481B

FASTA33335,902
        10         20         30         40         50         60 
MIYAAFRSIG AYIPPKIMSN ADFEKIIDTS DEWITKRTGI KERRIANEGE ASSDLGARAG 

        70         80         90        100        110        120 
ELAIERAAIS KEEIDLVICA TVTPDFLCMP STACLIAAKL GLSNVMAFDV SAACTGFVYA 

       130        140        150        160        170        180 
LNVAKAFIES GMKKNVLIVG AEKYSAILDY TDRTTCFLFG DGAGAAIISA TNDKSESIID 

       190        200        210        220        230        240 
INCSSDGNYE DLIKTPGGGS KNPCSQEVLE NKMACIKMKG NETFKLAVKT LTSDVKTMLE 

       250        260        270        280        290        300 
KHNLTNEDIN HFIPHQANYR IIKAVGEALD LSDEKTVVTV DKYGNTSAAS IPMAMNYAFE 

       310        320        330 
QGKIKAGDTI LFDAFGGGLT WGSALFKFAP IKR 

« Hide

References

[1]"The complete genome sequence and analysis of the Epsilonproteobacterium Arcobacter butzleri."
Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M., Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A., Rogosin A., Stanker L.H., Mandrell R.E.
PLoS ONE 2:E1358-E1358(2007) [PubMed: 18159241] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RM4018.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000361 Genomic DNA. Translation: ABV66570.1.
RefSeqYP_001489239.1. NC_009850.1.

3D structure databases

ProteinModelPortalA8ERJ6.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8ERJ6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5623993.
GenomeReviewsGene locus Abu_0295 in contig CP000361_GR.
KEGGabu:Abu_0295.
PATRIC20961950. VBIArcBut20197_0288.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHBG649927.
OMAMAKISPE.
ProtClustDBPRK09352.

Enzyme and pathway databases

BioCycABUT367737:ABU_0295-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_ARCB4
AccessionPrimary (citable) accession number: A8ERJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 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