Q81JG3 (ACPS_BACAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 63.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Holo-[acyl-carrier-protein] synthase Short name=Holo-ACP synthase EC=2.7.8.7 Alternative name(s): 4'-phosphopantetheinyl transferase AcpS | ||||
| Gene names |
| ||||
| Organism | Bacillus anthracis | ||||
| Taxonomic identifier | 1392 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 119 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein By similarity. HAMAP MF_00101 |
| Catalytic activity | CoA-(4'-phosphopantetheine) + apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier-protein]. HAMAP MF_00101 |
| Cofactor | Magnesium By similarity. HAMAP MF_00101 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00101. |
| Sequence similarities | Belongs to the P-Pant transferase superfamily. AcpS family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid biosynthesis Lipid synthesis |
| Cellular component | Cytoplasm |
| Ligand | Magnesium Metal-binding |
| Molecular function | Transferase |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW macromolecule biosynthetic processInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | holo-[acyl-carrier-protein] synthase activity Inferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 119 | 119 | Holo-[acyl-carrier-protein] synthase HAMAP MF_00101 | PRO_0000175606 | ||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||
| Metal binding | 8 | 1 | Magnesium By similarity | |||||||||||||||||||||||||||
| Metal binding | 58 | 1 | Magnesium By similarity | |||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||
| Beta strand | 8 – 11 | 4 | ||||||||||||||||||||||||||||
| Helix | 12 – 19 | 8 | ||||||||||||||||||||||||||||
| Helix | 25 – 29 | 5 | ||||||||||||||||||||||||||||
| Helix | 32 – 38 | 7 | ||||||||||||||||||||||||||||
| Helix | 45 – 50 | 6 | ||||||||||||||||||||||||||||
| Helix | 54 – 63 | 10 | ||||||||||||||||||||||||||||
| Helix | 74 – 76 | 3 | ||||||||||||||||||||||||||||
| Beta strand | 78 – 81 | 4 | ||||||||||||||||||||||||||||
| Beta strand | 87 – 90 | 4 | ||||||||||||||||||||||||||||
| Beta strand | 94 – 103 | 10 | ||||||||||||||||||||||||||||
| Beta strand | 105 – 115 | 11 | ||||||||||||||||||||||||||||
Sequences
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. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AE016879 Genomic DNA. Translation: AAP24289.1. AE017334 Genomic DNA. Translation: AAT29331.1. AE017225 Genomic DNA. Translation: AAT52572.1. | ||||||||||||
| RefSeq | NP_842803.1. NC_003997.3. YP_016856.1. NC_007530.2. YP_026521.1. NC_005945.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q81JG3. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | EBBACT00000012442; EBBACP00000012198; EBBACG00000012434. EBBACT00000016469; EBBACP00000016090; EBBACG00000016461. EBBACT00000021271; EBBACP00000020756; EBBACG00000021262. | ||||||||||||
| GeneID | 1087043. 2819988. 2850731. | ||||||||||||
| GenomeReviews | Gene locus BA_0250 in contig AE016879_GR. Gene locus BAS0236 in contig AE017225_GR. Gene locus GBAA_0250 in contig AE017334_GR. | ||||||||||||
| KEGG | ban:BA_0250. bar:GBAA_0250. bat:BAS0236. | ||||||||||||
| TIGR | BA_0250. GBAA_0250. | ||||||||||||
Phylogenomic databases | |||||||||||||
| GeneTree | EBGT00050000001692. | ||||||||||||
| HOGENOM | HBG734479. | ||||||||||||
| OMA | VHVSITH. | ||||||||||||
| ProtClustDB | PRK00070. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | BANT260799:BAS0236-MONOMER. BANT261594:GBAA0250-MONOMER. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_00101. AcpS. [Tree] | ||||||||||||
| InterPro | IPR008278. 4-PPantetheinyl_Trfase. IPR002582. ACPS. IPR004568. PPantethiene-prot_Trfase. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.90.470.20. G3DSA:3.90.470.20. 1 hit. | ||||||||||||
| KO | K00997. | ||||||||||||
| Pfam | PF01648. ACPS. 1 hit. [Graphical view] | ||||||||||||
| ProDom | PD004282. PPantethiene-prot_Trfase. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||
| SUPFAM | SSF56214. 4-PPT_transf. 1 hit. | ||||||||||||
| TIGRFAMs | TIGR00516. AcpS. 1 hit. TIGR00556. Pantethn_trn. 1 hit. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | ACPS_BACAN | ||||||||
| Accession | Primary (citable) accession number: Q81JG3 Secondary accession number(s): Q6I4F9, Q6KY61 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

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