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Reviewed, UniProtKB/Swiss-Prot Q6MHI3 (PANB_BDEBA)

Last modified November 3, 2009. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: Bd3560
OrganismBdellovibrio bacteriovorus [Complete proteome] [HAMAP]
Taxonomic identifier959 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaBdellovibrionalesBdellovibrionaceaeBdellovibrio

Protein attributes

Sequence length263 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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.

Subcellular location

Cytoplasm Potential.

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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3-methyl-2-oxobutanoate hydroxymethyltransferase activity

Inferred from electronic annotation. Source: HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2632633-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156
PRO_0000184820

Regions

Region43 – 442Alpha-ketoisovalerate binding By similarity

Sites

Active site1801Proton acceptor By similarity
Metal binding431Magnesium By similarity
Metal binding821Magnesium By similarity
Metal binding1131Magnesium By similarity
Binding site821Alpha-ketoisovalerate By similarity
Binding site1111Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6MHI3-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 5CB495EA041E5351

FASTA26328,276
        10         20         30         40         50         60 
MKTILDFHDK KSKKQKISMI TCYDYSFARI VADSDIDCIL VGDSLAMVML GHSTTLDVSA 

        70         80         90        100        110        120 
SVMAHHTAAV VRGAGDKFVI ADLPFMSYRK GLTANMTAVE KVMKAGAHAV KLEGAAGNLK 

       130        140        150        160        170        180 
LVRHLVDSGV PVMGHLGLTP QSVNQLGGFK VQGRDEKAQK KILEAALQLQ DAGAFSVVLE 

       190        200        210        220        230        240 
CVPSKLAKEI TAALEIPTIG IGAGVDCDGQ VLVLQDMLGM NQGFKPKFVK TYLDGFNTIK 

       250        260 
GALNQYHQEV STEIFPSEKE SYS 

« Hide

References

[1]"A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a genomic perspective."
Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C., Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E., Schuster S.C.
Science 303:689-692(2004) [PubMed: 14752164] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15356 / HD100 / DSM 50701 / NCIB 9529.

Cross-references

Sequence databases

BX842655 Genomic DNA. Translation: CAE78349.1.
RefSeqNP_970290.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2737239.
GenomeReviewsGene locus Bd3560 in contig BX842601_GR.
KEGGbba:Bd3560.
NMPDRfig|264462.1.peg.3263.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ6MHI3.
OMAYATPEQT.

Enzyme and pathway databases

BioCycBBAC264462:BD3560-MON.
BRENDA2.1.2.11. 3459.

Family and domain databases

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

Entry information

Entry namePANB_BDEBA
AccessionPrimary (citable) accession number: Q6MHI3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: July 5, 2004
Last modified: November 3, 2009
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents