P31057 (PANB_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 123.
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 | Escherichia coli (strain K12) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 83333 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 264 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is tranferred onto alpha-ketoisovalerate to form ketopantoate. Ref.7 |
| Catalytic activity | 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate. HAMAP-Rule MF_00156 |
| Cofactor | Binds 1 magnesium ion per subunit. Can also use manganese, cobalt and zinc to a lesser extent. Ref.8 |
| Enzyme regulation | Inhibited by isovalerate, pyruvate, 3-methyl-2-butanone, and valine. Partially inhibited by formaldehyde and tetrahydrofolate below or near the KM value. Also inhibited by later intermediates pantoate, pantothenate and coenzyme A. Ref.8 |
| Pathway | Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. HAMAP-Rule MF_00156 |
| Subunit structure | |
| Subcellular location | Cytoplasm Potential HAMAP-Rule MF_00156. |
| Sequence similarities | Belongs to the PanB family. |
| Biophysicochemical properties | Kinetic parameters: KM=0.16 mM for ketopantoate Ref.8 KM=0.18 mM for L-tetrahydrofolate KM=1.0 mM for alpha-ketoisovalerate (at 37 degrees Celsius and pH 6.8) KM=2.9 mM for alpha-ketobutyrate (at 37 degrees Celsius and pH 6.8) KM=5.9 mM for formaldehyde KM=5.9 mM for alpha-keto-beta-methylvalerate (at 37 degrees Celsius and pH 6.8) KM=25 mM for alpha-ketovalerate (at 37 degrees Celsius and pH 6.8) Vmax=8.25 µmol/min/mg enzyme for the forward reaction Vmax=7.3 µmol/min/mg enzyme for the reverse reaction Vmax=4 µmol/min/mg enzyme with alpha-ketobutyrate as substrate (at 37 degrees Celsius and pH 6.8) Vmax=2.8 µmol/min/mg enzyme with alpha-ketoisovalerate as substrate (at 37 degrees Celsius and pH 6.8) Vmax=2 µmol/min/mg enzyme with alpha-ketovalerate as substrate (at 37 degrees Celsius and pH 6.8) Vmax=0.43 µmol/min/mg enzyme with alpha-keto-beta-methylvalerate as substrate (at 37 degrees Celsius and pH 6.8) pH dependence: Optimum pH is 7.0-7.6. Stable from pH 5.0 to 10.0. Rapidly inactivated below pH 4.5. Temperature dependence: Optimum temperature is 70-80 degrees Celsius. |
| Mass spectrometry | Molecular mass is 28234 Da from positions 1 - 264. Determined by ESI. Ref.9 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pantothenate biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | Magnesium Metal-binding |
| Molecular function | Methyltransferase Transferase |
| Technical term | 3D-structure Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | pantothenate biosynthetic process from valine Inferred from mutant phenotype Ref.7. Source: EcoCyc |
| Cellular_component | cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB membraneInferred from direct assay PubMed 16858726. Source: UniProtKB |
| Molecular_function | 3-methyl-2-oxobutanoate hydroxymethyltransferase activity Inferred from direct assay Ref.7. Source: EcoCyc magnesium ion bindingInferred from direct assay Ref.8. Source: EcoCyc 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 – 264 | 264 | 3-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP-Rule MF_00156 | PRO_0000184841 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 45 – 46 | 2 | Alpha-ketoisovalerate binding HAMAP-Rule MF_00156 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Active site | 181 | 1 | Proton acceptor | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 45 | 1 | Magnesium | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 84 | 1 | Magnesium | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 114 | 1 | Magnesium By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 84 | 1 | Alpha-ketoisovalerate | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 112 | 1 | Alpha-ketoisovalerate | |||||||||||||||||||||||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 7 – 8 | 2 | SL → AS in CAA46505. Ref.2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 12 | 1 | Y → C in CAA46505. Ref.2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 15 | 1 | E → D in CAA46505. Ref.2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 63 | 1 | A → E in CAA46505. Ref.2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 124 | 1 | Q → K in CAA46505. Ref.2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 6 – 15 | 10 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 19 – 23 | 5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 27 – 36 | 10 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 40 – 43 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 47 – 50 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 55 – 57 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 62 – 75 | 14 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 79 – 84 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 89 – 92 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 93 – 105 | 13 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 109 – 112 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 117 – 119 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 120 – 128 | 9 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 133 – 139 | 7 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 141 – 143 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 144 – 147 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 157 – 173 | 17 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 177 – 182 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 185 – 194 | 10 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 199 – 204 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 208 – 213 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 215 – 218 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 235 – 237 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 240 – 252 | 13 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 259 – 261 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Nucleotide sequence of the Escherichia coli panBCD gene cluster." Merkel W.K., Nichols B.P. Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [2] | "Cloning and sequencing of the Escherichia coli panB gene, which encodes ketopantoate hydroxymethyltransferase, and overexpression of the enzyme." Jones C.E., Brook J.M., Buck D., Abell C., Smith A.G. J. Bacteriol. 175:2125-2130(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15. Strain: K12. |
| [3] | "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Fujita N., Mori H., Yura T., Ishihama A. Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [4] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [5] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [6] | "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-12. Strain: K12 / EMG2. |
| [7] | "Ketopantoate hydroxymethyltransferase. I. Purification and role in pantothenate biosynthesis." Teller J.H., Powers S.G., Snell E.E. J. Biol. Chem. 251:3780-3785(1976) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. |
| [8] | "Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and regulatory properties." Powers S.G., Snell E.E. J. Biol. Chem. 251:3786-3793(1976) [PubMed] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, COFACTOR, SUBUNIT. |
| [9] | "Structure of E. coli ketopantoate hydroxymethyl transferase complexed with ketopantoate and Mg2+, solved by locating 160 selenomethionine sites." von Delft F., Inoue T., Saldanha S.A., Ottenhof H.H., Schmitzberger F., Birch L.M., Dhanaraj V., Witty M., Smith A.G., Blundell T.L., Abell C. Structure 11:985-996(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ITS PRODUCT AND MAGNESIUM IONS, REACTION MECHANISM, MASS SPECTROMETRY, SUBUNIT. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | L17086 Genomic DNA. Translation: AAA24271.1. X65538 Genomic DNA. Translation: CAA46505.1. U00096 Genomic DNA. Translation: AAC73245.1. AP009048 Genomic DNA. Translation: BAB96711.1. | ||||||||||||
| PIR | F64736. | ||||||||||||
| RefSeq | NP_414676.1. NC_000913.2. YP_488437.1. NC_007779.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P31057. | ||||||||||||
| SMR | P31057. Positions 3-264. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| DIP | DIP-10436N. | ||||||||||||
| IntAct | P31057. 8 interactions. | ||||||||||||
| MINT | MINT-1249247. | ||||||||||||
| STRING | 511145.b0134. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | P31057. | ||||||||||||
| PRIDE | P31057. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | AAC73245; AAC73245; b0134. BAB96711; BAB96711; BAB96711. | ||||||||||||
| GeneID | 12932389. 944839. | ||||||||||||
| KEGG | ecj:Y75_p0131. eco:b0134. | ||||||||||||
| PATRIC | 32115373. VBIEscCol129921_0138. | ||||||||||||
Organism-specific databases | |||||||||||||
| EchoBASE | EB1626. | ||||||||||||
| EcoGene | EG11675. panB. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG0413. | ||||||||||||
| HOGENOM | HOG000078427. | ||||||||||||
| KO | K00606. | ||||||||||||
| OMA | CYDASFA. | ||||||||||||
| ProtClustDB | PRK00311. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | EcoCyc:3-CH3-2-OXOBUTANOATE-OH-CH3-XFER-MONOMER. ECOL316407:JW0130-MONOMER. MetaCyc:3-CH3-2-OXOBUTANOATE-OH-CH3-XFER-MONOMER. | ||||||||||||
| UniPathway | UPA00028; UER00003. | ||||||||||||
Gene expression databases | |||||||||||||
| Genevestigator | P31057. | ||||||||||||
Family and domain databases | |||||||||||||
| Gene3D | 3.20.20.60. 1 hit. | ||||||||||||
| HAMAP | MF_00156. PanB. | ||||||||||||
| InterPro | IPR003700. Pantoate_hydroxy_MeTrfase. IPR015813. Pyrv/PenolPyrv_Kinase. [Graphical view] | ||||||||||||
| PANTHER | PTHR20881. PTHR20881. 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... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | P31057. | ||||||||||||
Entry information
| Entry name | PANB_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P31057 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
