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Reviewed, UniProtKB/Swiss-Prot A7GJJ9 (FABH_CLOBL)

Last modified November 3, 2009. Version 13. 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: CLI_3829
OrganismClostridium botulinum (strain Langeland / NCTC 10281 / Type F) [Complete proteome] [HAMAP]
Taxonomic identifier441772 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length326 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 – 3263263-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
PRO_1000056345

Regions

Region252 – 2565ACP-binding By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
A7GJJ9-1 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: A19B3463F9437AE7

FASTA32635,788
        10         20         30         40         50         60 
MSNISVIGTG SYVPNNIITN DFLSTIVDTS DEWIRTRTGI LERRISKGEN TIYMATESAK 

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

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

       190        200        210        220        230        240 
SNGLKGEHLT CGVLKANNTP NKNDRLEKNN FIKMNGKEIF RFAVGAMNET ICNIQEKTKW 

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

       310        320 
NKQDKIILVG FGGGLTFGGV AIVWSI 

« Hide

References

[1]Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000728 Genomic DNA. Translation: ABS41342.1.
RefSeqYP_001392959.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA7GJJ9.

Genome annotation databases

GeneID5402679.
GenomeReviewsGene locus CLI_3829 in contig CP000728_GR.
KEGGcbf:CLI_3829.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAYIVPHQA.

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_CLOBL
AccessionPrimary (citable) accession number: A7GJJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 11, 2007
Last modified: November 3, 2009
This is version 13 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