Q2YPI1 (PANB_BRUA2) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 40.
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 |
| ||||
| Organism | Brucella abortus (strain 2308) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 359391 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella |
Protein attributes
| Sequence length | 275 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 – 275 | 275 | 3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156 | PRO_0000297227 | |||||
Regions | |||||||||
| Region | 49 – 50 | 2 | Alpha-ketoisovalerate binding By similarity | ||||||
Sites | |||||||||
| Active site | 187 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 49 | 1 | Magnesium By similarity | ||||||
| Metal binding | 88 | 1 | Magnesium By similarity | ||||||
| Metal binding | 120 | 1 | Magnesium By similarity | ||||||
| Binding site | 88 | 1 | Alpha-ketoisovalerate By similarity | ||||||
| Binding site | 118 | 1 | Alpha-ketoisovalerate By similarity | ||||||
Sequences
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References
| [1] | "Whole-genome analyses of speciation events in pathogenic Brucellae." Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E. Infect. Immun. 73:8353-8361(2005) [PubMed: 16299333] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 2308. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM040264 Genomic DNA. Translation: CAJ10316.1. |
| RefSeq | YP_413827.1. NC_007618.1. |
3D structure databases | |
| ProteinModelPortal | Q2YPI1. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q2YPI1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 3788835. |
| GenomeReviews | Gene locus BAB1_0360 in contig AM040264_GR. |
| KEGG | bmf:BAB1_0360. |
| PATRIC | 17843588. VBIBruMel86222_0379. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0413. |
| HOGENOM | HBG299908. |
| OMA | MAHVGLM. |
| ProtClustDB | PRK00311. |
Enzyme and pathway databases | |
| BioCyc | BMEL359391:BAB1_0360-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_BRUA2 | ||||||||
| Accession | Primary (citable) accession number: Q2YPI1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Brucella abortus strain 2308 Brucella abortus (strain 2308): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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