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Q39JC5 (PANB2_BURS3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. 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 2

EC=2.1.2.11
Alternative name(s):
Ketopantoate hydroxymethyltransferase 2
Short name=KPHMT 2
Gene names
Name:panB2
Ordered Locus Names:Bcep18194_A3842
OrganismBurkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194)) [Complete proteome] [HAMAP]
Taxonomic identifier269483 [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 2 HAMAP MF_00156
PRO_0000297236

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
Q39JC5 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 07EF436360F36A6C

FASTA27128,686
        10         20         30         40         50         60 
MTYLQESSRP AVTVPKLQAM RDAGEKIAML TCYDASFSAL LDRSGVDVLL IGDSLGNVLQ 

        70         80         90        100        110        120 
GHTTTLPVSL DDIAYHTACV ARAQPRALIM ADLPFGTYGT PAEAFASSVK LMRAGAQMVK 

       130        140        150        160        170        180 
LEGGEWLAET IRFLVERAVP VCAHVGLTPQ SVHAFGGFKV QGKTEAGAAQ LLRDARAVEA 

       190        200        210        220        230        240 
AGAQVVLLEA VPTLIGSEVT HMLRVPTIGI GAGADCSGQV LVLHDMLGVF PGKRPRFVKD 

       250        260        270 
FMQGEPNIQA AVEAYVRAVK DGSFPGPEHS F 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia sp. 383."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 383.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000151 Genomic DNA. Translation: ABB07441.1.
RefSeqYP_368085.1. NC_007510.1.

3D structure databases

ProteinModelPortalQ39JC5.
SMRQ39JC5. Positions 12-271.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ39JC5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3749026.
GenomeReviewsGene locus Bcep18194_A3842 in contig CP000151_GR.
KEGGbur:Bcep18194_A3842.
NMPDRfig|269483.3.peg.4559.
PATRIC19285008. VBIBurSp120713_1936.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0413.
HOGENOMHBG299908.
OMAYDATFAH.
ProtClustDBPRK00311.

Enzyme and pathway databases

BioCycBSP36773:BCEP18194_A3842-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 namePANB2_BURS3
AccessionPrimary (citable) accession number: Q39JC5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: November 22, 2005
Last modified: January 25, 2012
This is version 43 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