Q5WGA3 (PANB_BACSK) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 46.
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: 3-methyl-2-oxobutanoate hydroxymethyltransferase EC=2.1.2.11 Alternative name(s): Ketopantoate hydroxymethyltransferase Short name=KPHMT | ||||
| Gene names |
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| Organism | Bacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 66692 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 279 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is tranferred onto alpha-ketoisovalerate to form ketopantoate By similarity. HAMAP MF_00156 |
| Catalytic activity | 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate. HAMAP MF_00156 |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. HAMAP MF_00156 |
| Pathway | Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. HAMAP MF_00156 |
| Subunit structure | Homodecamer; pentamer of dimers By similarity. HAMAP MF_00156 |
| Subcellular location | Cytoplasm Potential HAMAP MF_00156. |
| Sequence similarities | Belongs to the PanB family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pantothenate biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | Magnesium Metal-binding |
| Molecular function | Methyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | pantothenate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 3-methyl-2-oxobutanoate hydroxymethyltransferase activity Inferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW methyltransferase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 279 | 279 | 3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156 | PRO_0000184815 | |||||
Regions | |||||||||
| Region | 43 – 44 | 2 | Alpha-ketoisovalerate binding By similarity | ||||||
Sites | |||||||||
| Active site | 181 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 43 | 1 | Magnesium By similarity | ||||||
| Metal binding | 82 | 1 | Magnesium By similarity | ||||||
| Metal binding | 114 | 1 | Magnesium By similarity | ||||||
| Binding site | 82 | 1 | Alpha-ketoisovalerate By similarity | ||||||
| Binding site | 112 | 1 | Alpha-ketoisovalerate By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16." Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K. Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KSM-K16. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AP006627 Genomic DNA. Translation: BAD64602.1. |
| RefSeq | YP_175563.1. NC_006582.1. |
3D structure databases | |
| ProteinModelPortal | Q5WGA3. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q5WGA3. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000046648; EBBACP00000045409; EBBACG00000046639. |
| GeneID | 3202071. |
| GenomeReviews | Gene locus ABC2067 in contig AP006627_GR. |
| KEGG | bcl:ABC2067. |
| NMPDR | fig|66692.3.peg.2371. |
| PATRIC | 18923678. VBIBacCla58185_2202. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0413. |
| GeneTree | EBGT00050000000505. |
| HOGENOM | HBG299908. |
| OMA | YDATFAH. |
| ProtClustDB | PRK00311. |
Enzyme and pathway databases | |
| BioCyc | BCLA66692:ABC2067-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00156. PanB. [Tree] |
| InterPro | IPR003700. Pantoate_hydroxy_MeTrfase. IPR015813. Pyrv/PenolPyrv_Kinase. [Graphical view] |
| Gene3D | G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit. |
| KO | K00606. |
| PANTHER | PTHR20881. Pantoate_transf. 1 hit. |
| Pfam | PF02548. Pantoate_transf. 1 hit. [Graphical view] |
| PIRSF | PIRSF000388. Pantoate_hydroxy_MeTrfase. 1 hit. |
| SUPFAM | SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit. |
| TIGRFAMs | TIGR00222. PanB. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | PANB_BACSK | ||||||||
| Accession | Primary (citable) accession number: Q5WGA3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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