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B4UDZ3 (PANB_ANASK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. 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

EC=2.1.2.11
Alternative name(s):
Ketopantoate hydroxymethyltransferase
Short name=KPHMT
Gene names
Name:panB
Ordered Locus Names:AnaeK_3740
OrganismAnaeromyxobacter sp. (strain K) [Complete proteome] [HAMAP]
Taxonomic identifier447217 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length306 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 – 3063063-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156
PRO_1000096939

Regions

Region53 – 542Alpha-ketoisovalerate binding By similarity

Sites

Active site1951Proton acceptor By similarity
Metal binding531Magnesium By similarity
Metal binding961Magnesium By similarity
Metal binding1281Magnesium By similarity
Binding site961Alpha-ketoisovalerate By similarity
Binding site1261Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
B4UDZ3 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: EE4D6C07B3BF21FB

FASTA30632,293
        10         20         30         40         50         60 
MSSHPPAPRK HVTIHELRRM KESGERIAMV TAYDATAARL VAVAGVDAVL VGDSLGMAVQ 

        70         80         90        100        110        120 
GHESTLPVTL DQMVYHSAMV RRGLARGDGR AHLVTDMSFG SYQASADEAV KAAMRLVAEG 

       130        140        150        160        170        180 
GAEAVKLEGG AEFGEVIRRI VRAGVPVMGH IGLTPQSVHK MGGYVVQGKD SEKAQQILRD 

       190        200        210        220        230        240 
ARALEAAGCY ALVLECIPSE LARIVTSQLR VPTIGIGAGP HCDGQVLVLN DLLGLDASFT 

       250        260        270        280        290        300 
PRFVKRFGEV GAAVQDAVGA YVGEVKARAF PDDAHSFHSS SVRLVPVERH AEAAEEEPPD 


AIGAPI 

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References

[1]"Complete sequence of Anaeromyxobacter sp. K."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikiva G., Beliaev A.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001131 Genomic DNA. Translation: ACG74951.1.
RefSeqYP_002136080.1. NC_011145.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB4UDZ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6787429.
GenomeReviewsGene locus AnaeK_3740 in contig CP001131_GR.
KEGGank:AnaeK_3740.
PATRIC20942229. VBIAnaSp90767_3784.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG299908.
OMAYDATFAH.
ProtClustDBPRK00311.

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_ANASK
AccessionPrimary (citable) accession number: B4UDZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: January 25, 2012
This is version 27 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