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Q8X929 (PANB_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 82. 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:Z0145, ECs0138
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length264 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 – 2642643-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP-Rule MF_00156
PRO_0000184843

Regions

Region45 – 462Alpha-ketoisovalerate binding By similarity

Sites

Active site1811Proton acceptor By similarity
Metal binding451Magnesium By similarity
Metal binding841Magnesium By similarity
Metal binding1141Magnesium By similarity
Binding site841Alpha-ketoisovalerate By similarity
Binding site1121Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8X929 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: D93FF23EBEF8D090

FASTA26428,310
        10         20         30         40         50         60 
MKPTTIASLQ KCKQEKKRFA TITAYDYSFA KLFAEEGLNV MLVGDSLGMT VQGHESTLPV 

        70         80         90        100        110        120 
TVEDIAYHTT AVRRGAPNCL LLADLPFMAY ATPEQAFENA ATVMRAGANM VKIEGGEWLV 

       130        140        150        160        170        180 
ETVKMLTERA VPVCGHLGLT PQSVNIFGGY KVQGRGDEAS DRLLSDALAL EAAGAQLLVL 

       190        200        210        220        230        240 
ECVPVELAKR ITEALAIPVI GIGAGNVTDG QILVMHDAFG ITGGHIPKFA KNFLAETGDI 

       250        260 
RAAVRQYMAE VESGVYPGEE HSFH 

« Hide

References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG54438.1.
BA000007 Genomic DNA. Translation: BAB33561.1.
PIRB85497.
B90646.
RefSeqNP_285830.1. NC_002655.2.
NP_308165.1. NC_002695.1.

3D structure databases

ProteinModelPortalQ8X929.
SMRQ8X929. Positions 3-264.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z0145.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG54438; AAG54438; Z0145.
BAB33561; BAB33561; BAB33561.
GeneID913736.
956841.
KEGGece:Z0145.
ecs:ECs0138.
PATRIC18349218. VBIEscCol44059_0139.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0413.
HOGENOMHOG000078427.
KOK00606.
OMAEKIAMIT.
OrthoDBEOG63C0WN.

Enzyme and pathway databases

BioCycECOL386585:GJFA-135-MONOMER.
ECOO157:PANB-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_ECO57
AccessionPrimary (citable) accession number: Q8X929
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: March 1, 2002
Last modified: May 14, 2014
This is version 82 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