Skip Header

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

A9VJ42 (A9VJ42_BACWK) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
EC=2.3.1.180 HAMAP MF_01815
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III HAMAP MF_01815
Beta-ketoacyl-ACP synthase III HAMAP MF_01815
Gene names
Name:fabH HAMAP MF_01815
Ordered Locus Names:BcerKBAB4_1082
OrganismBacillus weihenstephanensis (strain KBAB4) [Complete proteome] [HAMAP] EMBL ABY42331.1
Taxonomic identifier315730 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length310 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

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

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP MF_01815 SAAS SAAS013747

Subunit structure

Homodimer By similarity. HAMAP MF_01815 SAAS SAAS013747

Subcellular location

Cytoplasm By similarity HAMAP MF_01815 SAAS SAAS013747.

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. HAMAP MF_01815

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region236 – 2405ACP-binding By similarity HAMAP MF_01815

Sites

Active site1121 By similarity HAMAP MF_01815
Active site2351 By similarity HAMAP MF_01815
Active site2651 By similarity HAMAP MF_01815

Sequences

Sequence LengthMass (Da)Tools
A9VJ42 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 51F7FDB1BB86D42B

FASTA31033,461
        10         20         30         40         50         60 
MNVGILGIGR YVPEKVVTNY DLEKIVDTSD EWIRTRTGIA ERRIADDTID TSYMAVEASK 

        70         80         90        100        110        120 
KALEDAGISG EDIDLILVAT VTPDRAFPAV ACVIQEAIGA KHAAAMDLSA ACAGFMYGMI 

       130        140        150        160        170        180 
TAQQFIQTGT YKNVLVVGSD KLSKIVDWND RNTAVLFGDG AGAIVMGAVS EGKGVLSFEL 

       190        200        210        220        230        240 
GADGSGGKHL YQDEYVMMNG REVFKFAVRQ LGDSCLRVLE KAGLTKEDVD FLVPHQANIR 

       250        260        270        280        290        300 
IMESARERLN LPKEKMSMTI EKFGNTSASS IPIAMVEELQ NGRIQDGDLI ILVGFGGGLT 

       310 
WGAVALRWGK

« Hide

References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000903 Genomic DNA. Translation: ABY42331.1.
RefSeqYP_001643959.1. NC_010184.1.

3D structure databases

ProteinModelPortalA9VJ42.
SMRA9VJ42. Positions 1-309.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9VJ42.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000079146; EBBACP00000077080; EBBACG00000079137.
GeneID5841294.
GenomeReviewsGene locus BcerKBAB4_1082 in contig CP000903_GR.
KEGGbwe:BcerKBAB4_1082.
PATRIC19006684. VBIBacWei55973_1663.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000001269.
HOGENOMHBG649927.
OMAKEIGAIN.
ProtClustDBPRK09352.

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 nameA9VJ42_BACWK
AccessionPrimary (citable) accession number: A9VJ42
Entry history
Integrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: December 14, 2011
This is version 30 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