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Reviewed, UniProtKB/Swiss-Prot A8EVP8 (PANB_ARCB4)

Last modified November 3, 2009. Version 22. 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: Abu_1775
OrganismArcobacter butzleri (strain RM4018) [Complete proteome] [HAMAP]
Taxonomic identifier367737 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeArcobacter

Protein attributes

Sequence length269 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 – 2692693-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP MF_00156
PRO_1000096940

Regions

Region50 – 512Alpha-ketoisovalerate binding By similarity

Sites

Active site1871Proton acceptor By similarity
Metal binding501Magnesium By similarity
Metal binding891Magnesium By similarity
Metal binding1201Magnesium By similarity
Binding site891Alpha-ketoisovalerate By similarity
Binding site1181Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
A8EVP8-1 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: C4E53F57B5C5E7C9

FASTA26929,857
        10         20         30         40         50         60 
MSIIKNNFEK MNITKIKNSK NNKKLTVITA YDALFAKLFE EIADMILVGD SLNMSFAGRP 

        70         80         90        100        110        120 
DTLSATLEQM IYHTNAVCNG AKNAFVIIDM PFGTYINKDE ALKNCVEVYR QTNANAVKIE 

       130        140        150        160        170        180 
GGEDKADIIK HLTSNAVAVM GHIGLMPQYV RSEGGYKVRG KTKEDEEQLI RDAIAVEKAG 

       190        200        210        220        230        240 
AFSIVVEGVK SDVAKKITQA VNIPIIGIGA GVDTDGQVLV WSDMLGFFEE FKPKFVRHYL 

       250        260 
DGAELVKEAV NQYRNDVQDK SFPSKEEEY 

« Hide

References

[1]"The complete genome sequence and analysis of the Epsilonproteobacterium Arcobacter butzleri."
Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M., Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A., Rogosin A., Stanker L.H., Mandrell R.E.
PLoS ONE 2:E1358-E1358(2007) [PubMed: 18159241] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000361 Genomic DNA. Translation: ABV68021.1.
RefSeqYP_001490691.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA8EVP8.

Genome annotation databases

GeneID5625318.
GenomeReviewsGene locus Abu_1775 in contig CP000361_GR.
KEGGabu:Abu_1775.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAYATPEQT.

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_ARCB4
AccessionPrimary (citable) accession number: A8EVP8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 13, 2007
Last modified: November 3, 2009
This is version 22 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