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C1KWK2 (PANB_LISMC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. 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:Lm4b_01919
OrganismListeria monocytogenes serotype 4b (strain CLIP80459) [Complete proteome] [HAMAP]
Taxonomic identifier568819 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length277 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-Rule MF_00156

Catalytic activity

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate. HAMAP-Rule MF_00156

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_00156

Pathway

Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. HAMAP-Rule MF_00156

Subunit structure

Homodecamer; pentamer of dimers By similarity. HAMAP-Rule MF_00156

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00156.

Sequence similarities

Belongs to the PanB family.

Ontologies

Keywords
   Biological processPantothenate biosynthesis
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpantothenate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function3-methyl-2-oxobutanoate hydroxymethyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2772773-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP-Rule MF_00156
PRO_1000203475

Regions

Region43 – 442Alpha-ketoisovalerate binding By similarity

Sites

Active site1811Proton acceptor By similarity
Metal binding431Magnesium By similarity
Metal binding821Magnesium By similarity
Metal binding1141Magnesium By similarity
Binding site821Alpha-ketoisovalerate By similarity
Binding site1121Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
C1KWK2 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: DDBAE81C7FE16EBF

FASTA27729,839
        10         20         30         40         50         60 
MKRPVDFFAM KENGEKITMI TAYDYPSAKN VEQAEADMIL VGDSLGMVVL GYDSTVPVTM 

        70         80         90        100        110        120 
DDMIHHTKAV KRGAPDTFVV TDMPFMTYHG SVDETIQNAR KIIQESGAHA VKLEGAGEVV 

       130        140        150        160        170        180 
NKIARLTEAG APVVAHLGLT PQSVGLTGSY KVRAKSAQEA QELMDNALAV EAAGAIALVL 

       190        200        210        220        230        240 
EAIPRQLAEK VSKALSIPTI GIGAGVETDG QVLVYHDIIG YGISRRAKFV KAYADIDERI 

       250        260        270 
EPALASYVKE VKAATFPEVK HSFTMAEEDL KGLYGRE 

« Hide

References

[1]"Comparative genomics and transcriptomics of lineages I, II, and III strains of Listeria monocytogenes."
Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B., Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A., Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P. expand/collapse author list , Rusniok C., Buchrieser C., Goebel W., Chakraborty T.
BMC Genomics 13:144-144(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CLIP80459.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM242711 Genomic DNA. Translation: CAS05677.1.
RefSeqYP_002758613.1. NC_012488.1.

3D structure databases

ProteinModelPortalC1KWK2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING634178.Lm4b_01919.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAS05677; CAS05677; Lm4b_01919.
GeneID7704031.
KEGGlmc:Lm4b_01919.
PATRIC20307069. VBILisMon88360_1933.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000078427.
KOK00606.
OMAAIKQYAD.
OrthoDBEOG63C0WN.
ProtClustDBPRK00311.

Enzyme and pathway databases

BioCycLMON568819:GJF9-2847-MONOMER.
UniPathwayUPA00028; UER00003.

Family and domain databases

Gene3D3.20.20.60. 1 hit.
HAMAPMF_00156. PanB.
InterProIPR003700. Pantoate_hydroxy_MeTrfase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERPTHR20881. PTHR20881. 1 hit.
PfamPF02548. Pantoate_transf. 1 hit.
[Graphical view]
PIRSFPIRSF000388. Pantoate_hydroxy_MeTrfase. 1 hit.
SUPFAMSSF51621. SSF51621. 1 hit.
TIGRFAMsTIGR00222. panB. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANB_LISMC
AccessionPrimary (citable) accession number: C1KWK2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 2009
Last modified: February 19, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways