Q73AV4 (PANB_BACC1) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 51.
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 | Bacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 222523 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 278 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 – 278 | 278 | 3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156 | PRO_0000184809 | |||||
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 genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1." Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D. Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10987. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE017194 Genomic DNA. Translation: AAS40597.1. |
| RefSeq | NP_977989.1. NC_003909.8. |
3D structure databases | |
| ProteinModelPortal | Q73AV4. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q73AV4. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000028851; EBBACP00000028201; EBBACG00000028842. |
| GeneID | 2752037. |
| GenomeReviews | Gene locus BCE_1668 in contig AE017194_GR. |
| KEGG | bca:BCE_1668. |
| NMPDR | fig|222523.1.peg.1661. |
| PATRIC | 18852161. VBIBacCer118379_1584. |
| TIGR | BCE_1668. |
Phylogenomic databases | |
| eggNOG | COG0413. |
| GeneTree | EBGT00050000000505. |
| HOGENOM | HBG299908. |
| OMA | YDATFAH. |
| ProtClustDB | PRK00311. |
Enzyme and pathway databases | |
| BioCyc | BCER405917:BCE_1668-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_BACC1 | ||||||||
| Accession | Primary (citable) accession number: Q73AV4 | ||||||||
| 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 |

Clusters with