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G8UG37 (G8UG37_BACCE) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 11. Feed History...

Clusters with 100%, 90%, 50% identity | 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 HAMAP-Rule MF_01815
EC=2.3.1.180 HAMAP-Rule MF_01815
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III HAMAP-Rule MF_01815
Beta-ketoacyl-ACP synthase III HAMAP-Rule MF_01815
Gene names
Name:fabH HAMAP-Rule MF_01815
ORF Names:bcf_08950 EMBL AEW54912.1
OrganismBacillus cereus F837/76 EMBL AEW54912.1
Taxonomic identifier347495 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group ›

Protein attributes

Sequence length327 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-Rule MF_01815

Catalytic activity

Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2. HAMAP-Rule MF_01815 SAAS SAAS004655

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP-Rule MF_01815 SAAS SAAS004655

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01815 SAAS SAAS004655

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01815 SAAS SAAS004655.

Domain

The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH By similarity. HAMAP-Rule MF_01815

Sequence similarities

Belongs to the FabH family. HAMAP-Rule MF_01815

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1141 By similarity HAMAP-Rule MF_01815
Active site2511 By similarity HAMAP-Rule MF_01815
Active site2811 By similarity HAMAP-Rule MF_01815

Sequences

Sequence LengthMass (Da)Tools
G8UG37 [UniParc].

Last modified February 22, 2012. Version 1.
Checksum: 9A10DC162C28EA8B

FASTA32736,108
        10         20         30         40         50         60 
MHSKSRITAI GTYVPNQILS NNDLEKMIDT NDEWIVQRTG MKERRIASKD EYSSHLAIQA 

        70         80         90        100        110        120 
IENLCTTFKK NLEDIDCIIV ATTTADYVFP SVACQIQQHF NIPHTIAFDL NATCAGFTYG 

       130        140        150        160        170        180 
LHVGNSLITS GSHKKVLVVA TETLSKVTDY TDRTTCILFG DGAGAILLER DENKPSFIAA 

       190        200        210        220        230        240 
HMGTNGHGGI HLYRTNLSTT LNGTPLQTNE KIVQNGREVY KWATRTVPAG IKELLHTANM 

       250        260        270        280        290        300 
QIDAIDWFIP HSVNLRMIES ICEKTEIPIQ KTLTSVKYMG NTSSASIPLA LDLARKEGKL 

       310        320 
NNGETLLLYG FGGGLTHLGL IVEWDLN

« Hide

References

[1]"Complete Genome Sequence of the Highly Hemolytic Strain Bacillus cereus F837/76."
Auger S., Galleron N., Segurens B., Dossat C., Bolotin A., Wincker P., Sorokin A.
J. Bacteriol. 194:1630-1630(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: F837/76 EMBL AEW54912.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP003187 Genomic DNA. Translation: AEW54912.1.
RefSeqYP_005118425.1. NC_016779.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEW54912; AEW54912; bcf_08950.
GeneID11681695.
KEGGbcf:bcf_08950.

Phylogenomic databases

KOK00648.

Enzyme and pathway databases

UniPathwayUPA00094.

Family and domain databases

Gene3D3.40.47.10. 2 hits.
HAMAPMF_01815. FabH.
InterProIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
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 nameG8UG37_BACCE
AccessionPrimary (citable) accession number: G8UG37
Entry history
Integrated into UniProtKB/TrEMBL: February 22, 2012
Last sequence update: February 22, 2012
Last modified: April 3, 2013
This is version 11 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info