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A0K4T1 (PANB1_BURCH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3-methyl-2-oxobutanoate hydroxymethyltransferase 1

EC=2.1.2.11
Alternative name(s):
Ketopantoate hydroxymethyltransferase 1
Short name=KPHMT 1
Gene names
Name:panB1
Ordered Locus Names:Bcen2424_0755
OrganismBurkholderia cenocepacia (strain HI2424) [Complete proteome] [HAMAP]
Taxonomic identifier331272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length271 AA.
Sequence statusComplete.
Protein existenceInferred 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 processPantothenate biosynthesis
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpantothenate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3-methyl-2-oxobutanoate hydroxymethyltransferase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2712713-methyl-2-oxobutanoate hydroxymethyltransferase 1 HAMAP MF_00156
PRO_0000297229

Regions

Region53 – 542Alpha-ketoisovalerate binding By similarity

Sites

Active site1891Proton acceptor By similarity
Metal binding531Magnesium By similarity
Metal binding921Magnesium By similarity
Metal binding1221Magnesium By similarity
Binding site921Alpha-ketoisovalerate By similarity
Binding site1201Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
A0K4T1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: CFB5B95BE8E50996

FASTA27128,752
        10         20         30         40         50         60 
MTYLQESSRP AVTVPKLQAM RDAGEKIAML TCYDASFSAL LDRAGTDVLL IGDSLGNVLQ 

        70         80         90        100        110        120 
GHTTTLPVSI DDIAYHTACV ARAQPRALVV ADLPFGTYGT PVDAFANAVK LMRAGAQMVK 

       130        140        150        160        170        180 
LEGGEWLADT IRFLVERSVP VCAHLGLTPQ SVHAFGGFKV QGKTEAGAAQ LLRDARAIED 

       190        200        210        220        230        240 
AGAQLVVLEA VPTLVAAEVT HMLKIPTIGI GAGVDCSGQV LVLHDMLGVF PGKRPRFVKD 

       250        260        270 
FMQGQPNIQA AVEAYVSAVK DRSFPGPEHS F 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia cenocepacia HI2424."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., LiPuma J.J., Gonzalez C.F., Konstantinidis K., Tiedje J.M., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HI2424.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000458 Genomic DNA. Translation: ABK07508.1.
RefSeqYP_834401.1. NC_008542.1.

3D structure databases

ProteinModelPortalA0K4T1.
SMRA0K4T1. Positions 12-270.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0K4T1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4450580.
GenomeReviewsGene locus Bcen2424_0755 in contig CP000458_GR.
KEGGbch:Bcen2424_0755.
PATRIC19058729. VBIBurCen15205_0757.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0413.
HOGENOMHBG299908.
OMAYDATFAH.
ProtClustDBPRK00311.

Enzyme and pathway databases

BioCycBCEN331272:BCEN2424_0755-MONOMER.

Family and domain databases

HAMAPMF_00156. PanB.
[Tree]
InterProIPR003700. Pantoate_hydroxy_MeTrfase.
IPR015813. Pyrv/PenolPyrv_Kinase.
[Graphical view]
Gene3DG3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
KOK00606.
PANTHERPTHR20881. Pantoate_transf. 1 hit.
PfamPF02548. Pantoate_transf. 1 hit.
[Graphical view]
PIRSFPIRSF000388. Pantoate_hydroxy_MeTrfase. 1 hit.
SUPFAMSSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMsTIGR00222. PanB. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANB1_BURCH
AccessionPrimary (citable) accession number: A0K4T1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: December 12, 2006
Last modified: December 14, 2011
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families