Reviewed,
UniProtKB/Swiss-Prot Q81JF6 (FABH2_BACAN)
Last modified
February 9, 2010.
Version 54.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 2 EC=2.3.1.180 Alternative name(s): 3-oxoacyl-[acyl-carrier-protein] synthase III protein 2 Beta-ketoacyl-ACP synthase III 2 Short name=KAS III 2 | ||||
| Gene names |
| ||||
| Organism | Bacillus anthracis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1392 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 327 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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 | |
| 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 process | Fatty acid biosynthesis Lipid synthesis |
| Cellular component | Cytoplasm |
| Molecular function | Acyltransferase Transferase |
| Technical term | Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | fatty acid biosynthetic process Inferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 3-oxoacyl-[acyl-carrier-protein] synthase activity Inferred from electronic annotation. Source: HAMAP beta-ketoacyl-acyl-carrier-protein synthase III activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 327 | 327 | 3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 2 HAMAP MF_01815 | PRO_0000110394 | |||||
Regions | |||||||||
| Region | 252 – 256 | 5 | ACP-binding By similarity | ||||||
Sites | |||||||||
| Active site | 114 | 1 | By similarity | ||||||
| Active site | 251 | 1 | By similarity | ||||||
| Active site | 281 | 1 | By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. Fraser C.M.Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton. |
| [2] | "Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor. |
| [3] | "Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE016879 Genomic DNA. Translation: AAP25732.1. AE017334 Genomic DNA. Translation: AAT30939.1. AE017225 Genomic DNA. Translation: AAT54008.1. |
| RefSeq | NP_844246.1. YP_018464.1. YP_027957.1. |
3D structure databases | |
| SMR | Q81JF6. Positions 5-325. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1086168. 2817393. 2851898. |
| GenomeReviews | Gene locus BA_1826 in contig AE016879_GR. Gene locus BAS1691 in contig AE017225_GR. Gene locus GBAA_1826 in contig AE017334_GR. |
| KEGG | ban:BA1826. bar:GBAA1826. bat:BAS1691. |
| TIGR | BA_1826. GBAA_1826. |
Phylogenomic databases | |
| HOGENOM | HBG649927. |
| OMA | IESICEK. |
Enzyme and pathway databases | |
| BioCyc | BANT260799:BAS1691-MONOMER. BANT261594:GBAA1826-MONOMER. |
| BRENDA | 2.3.1.180. 267517. |
Family and domain databases | |
| HAMAP | MF_01815. FabH. [Tree] |
| InterPro | IPR013751. ACP_syn_III. IPR013747. ACP_syn_III_C. IPR004655. FabH_synth. IPR016039. Thiolase-like. IPR016038. Thiolase-like_subgr. [Graphical view] |
| Gene3D | G3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits. |
| Pfam | PF08545. ACP_syn_III. 1 hit. PF08541. ACP_syn_III_C. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00747. fabH. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | FABH2_BACAN | ||||||||
| Accession | Primary (citable) accession number: Q81JF6 Secondary accession number(s): Q6I0C9, Q6KUA0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (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 |

Clusters with


