Reviewed,
UniProtKB/Swiss-Prot Q9JXF1 (BICOA_NEIMB)
Last modified
November 3, 2009.
Version 44.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Bifunctional enzyme birA/coaX Including the following 2 domains: 1- Recommended name: Biotin--[acetyl-CoA-carboxylase] synthetase EC=6.3.4.15 Alternative name(s): Biotin--protein ligase 2- Recommended name: Type III pantothenate kinase EC=2.7.1.33 Alternative name(s): Pantothenic acid kinase PanK-III | ||||
| Gene names |
| ||||
| Organism | Neisseria meningitidis serogroup B [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 491 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria |
Protein attributes
| Sequence length | 592 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Activates biotin to form biotinyl-5'-adenylate and transfers the biotin moiety to biotin-accepting proteins By similarity. Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis By similarity. |
| Catalytic activity | ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]. HAMAP MF_01274 ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate. HAMAP MF_01274 |
| Cofactor | Monovalent cations By similarity. |
| Pathway | Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. HAMAP MF_01274 |
| Subcellular location | Cytoplasm Potential. |
| Sequence similarities | In the N-terminal section; belongs to the biotin--protein ligase family. In the C-terminal section; belongs to the type III pantothenate kinase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Coenzyme A biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Biotin Nucleotide-binding |
| Molecular function | Kinase Ligase Transferase |
| Technical term | Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | coenzyme A biosynthetic process Inferred from electronic annotation. Source: HAMAP positive regulation of transcriptionInferred from electronic annotation. Source: InterPro protein modification processInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: HAMAP biotin-[acetyl-CoA-carboxylase] ligase activityInferred from electronic annotation. Source: EC pantothenate kinase activityInferred from electronic annotation. Source: HAMAP transcription activator activityInferred 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 – 592 | 592 | Bifunctional enzyme birA/coaX HAMAP MF_01274 | PRO_0000270884 | |||||
Regions | |||||||||
| Nucleotide binding | 344 – 351 | 8 | ATP By similarity | ||||||
| Region | 1 – 329 | 329 | Biotin--protein ligase HAMAP MF_01274 | ||||||
| Region | 336 – 592 | 257 | Type III pantothenate kinase HAMAP MF_01274 | ||||||
| Region | 433 – 436 | 4 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 435 | 1 | Proton acceptor Potential | ||||||
| Binding site | 426 | 1 | Substrate By similarity | ||||||
| Binding site | 458 | 1 | ATP Potential | ||||||
| Binding site | 508 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Complete genome sequence of Neisseria meningitidis serogroup B strain MC58." Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., White O. Venter J.C.Science 287:1809-1815(2000) [PubMed: 10710307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MC58 / Serogroup B. |
Cross-references
Sequence databases | |
|---|---|
| AE002098 Genomic DNA. Translation: AAF42394.1. | |
| PIR | B81009. |
| RefSeq | NP_275065.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1BIA based on UniProtKB P06709. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 903989. |
| GenomeReviews | Gene locus NMB2075 in contig AE002098_GR. |
| KEGG | nme:NMB2075. |
| NMPDR | fig|122586.1.peg.1999. |
| TIGR | NMB2075. |
Phylogenomic databases | |
| HOGENOM | Q9JXF1. |
| OMA | HECASSN. |
Enzyme and pathway databases | |
| BioCyc | NMEN122586:NMB_2075-MON. |
| BRENDA | 2.7.1.33. 293828. 6.3.4.15. 293828. |
Family and domain databases | |
| HAMAP | MF_01274. Fused. [Tree] |
| InterPro | IPR004619. Baf. IPR004408. Biotin_CoA_COase_ligase. IPR003142. BPL_C. IPR004143. BPL_LipA_LipB. [Graphical view] |
| PANTHER | PTHR12835. BirA_ligase. 1 hit. |
| Pfam | PF02237. BPL_C. 1 hit. PF03099. BPL_LipA_LipB. 1 hit. PF03309. Bvg_acc_factor. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00671. baf. 1 hit. TIGR00121. birA_ligase. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | BICOA_NEIMB | ||||||||
| Accession | Primary (citable) accession number: Q9JXF1 | ||||||||
| 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


