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A7FPM6 (FABH_CLOB1) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 30. 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:CLB_3684
OrganismClostridium botulinum (strain ATCC 19397 / Type A) [Complete proteome] [HAMAP]
Taxonomic identifier441770 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length326 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 – 3263263-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
PRO_1000056343

Regions

Region252 – 2565ACP-binding By similarity

Sites

Active site1121 By similarity
Active site2511 By similarity
Active site2811 By similarity

Sequences

Sequence LengthMass (Da)Tools
A7FPM6 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 7BE182C66B07F344

FASTA32635,813
        10         20         30         40         50         60 
MSNISVIGTG SYVPNNIITN DFLSTIVDTS DEWIRTRTGI LERRISKGEN TIYMATESAK 

        70         80         90        100        110        120 
EAIKNANIEA NDLDLIIVAT LTPDNFMPST ACSVQKEIGA MNALCFDISA ACSGFIYGLE 

       130        140        150        160        170        180 
IACSMLKNSF RNKALIIGAE NLSKIVDWED RNTCVLFGDG AGSAILSKTK EEGILEFHSG 

       190        200        210        220        230        240 
SNGLKGEHLT CGVLKANNTP NKNDSLEKNN FIKMNGKEIF RFAVGAMNET IYNIQEKTKW 

       250        260        270        280        290        300 
DLNEVKYIIS HQANSRIIEY TAKKLNTEKD KFYMNLDKYG NTSAASIPIA LDEMNKRGLL 

       310        320 
NKQDKIILVG FGGGLTFGGV AIVWSI 

« Hide

References

[1]"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids."
Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
PLoS ONE 2:E1271-E1271(2007) [PubMed: 18060065] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19397 / Type A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000726 Genomic DNA. Translation: ABS33769.1.
RefSeqYP_001385916.1. NC_009697.1.

3D structure databases

ProteinModelPortalA7FPM6.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7FPM6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5395624.
GenomeReviewsGene locus CLB_3684 in contig CP000726_GR.
KEGGcba:CLB_3684.
PATRIC19361910. VBICloBot110701_3537.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHBG649927.
OMAKEIGAIN.
ProtClustDBCLSK972443.

Enzyme and pathway databases

BioCycCBOT441770:CLB_3684-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_CLOB1
AccessionPrimary (citable) accession number: A7FPM6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 11, 2007
Last modified: December 14, 2011
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