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Q64UB9 (PANB_BACFR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

EC=2.1.2.11
Alternative name(s):
Ketopantoate hydroxymethyltransferase
Short name=KPHMT
Gene names
Name:panB
Ordered Locus Names:BF2163
OrganismBacteroides fragilis (strain YCH46) [Complete proteome] [HAMAP]
Taxonomic identifier295405 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length273 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 – 2732733-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156
PRO_0000184812

Regions

Region53 – 542Alpha-ketoisovalerate binding By similarity

Sites

Active site1911Proton acceptor By similarity
Metal binding531Magnesium By similarity
Metal binding921Magnesium By similarity
Metal binding1241Magnesium By similarity
Binding site921Alpha-ketoisovalerate By similarity
Binding site1221Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q64UB9 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: F7EABB8AF3842932

FASTA27329,807
        10         20         30         40         50         60 
MAGYISDDTR KVTTHRLIEM KQRGEKISML TSYDYTMAQI VDGAGIDVIL VGDSASNVMA 

        70         80         90        100        110        120 
GNVTTLPITL DQMIYHGKSV VRGVKRAMVV VDMPFGSYQG NEMEGLASAI RIMKESHADA 

       130        140        150        160        170        180 
LKLEGGEEII DTVKRILSAG IPVMGHLGLM PQSINKYGTY TVRAKDDAEA EKLIRDAHLL 

       190        200        210        220        230        240 
EEAGCFGLVL EKIPAALASR VASELTIPVI GIGAGGDVDG QVLVIQDMLG MNNGFRPRFL 

       250        260        270 
RRYADLYTVM TDAISHYVSD VKNCDFPNEK EQY 

« Hide

References

[1]"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation."
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004) [PubMed: 15466707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YCH46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006841 Genomic DNA. Translation: BAD48910.1.
RefSeqYP_099444.1. NC_006347.1.

3D structure databases

ProteinModelPortalQ64UB9.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3084164.
GenomeReviewsGene locus BF2163 in contig AP006841_GR.
KEGGbfr:BF2163.
PATRIC21049978. VBIBacFra17906_2101.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG299908.
OMAYDATFAH.
PhylomeDBQ64UB9.
ProtClustDBPRK00311.

Enzyme and pathway databases

BioCycBFRA295405:BF2163-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 namePANB_BACFR
AccessionPrimary (citable) accession number: Q64UB9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 46 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