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P65655 (PANB_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BR0330, BS1330_I0331
OrganismBrucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]
Taxonomic identifier204722 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length275 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 – 2752753-methyl-2-oxobutanoate hydroxymethyltransferase HAMAP-Rule MF_00156
PRO_0000184827

Regions

Region49 – 502Alpha-ketoisovalerate binding By similarity

Sites

Active site1871Proton acceptor By similarity
Metal binding491Magnesium By similarity
Metal binding881Magnesium By similarity
Metal binding1201Magnesium By similarity
Binding site881Alpha-ketoisovalerate By similarity
Binding site1181Alpha-ketoisovalerate By similarity

Sequences

Sequence LengthMass (Da)Tools
P65655 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: F73117B84258FE26

FASTA27529,418
        10         20         30         40         50         60 
MSAPVTRKRL TPKVIQAMKG ECPIVSLTAY TTPVARLLDP HCDLLLVGDS LGMVLYGMES 

        70         80         90        100        110        120 
TLAVTLDMMI MHGQAVMRGT SHACVIVDMP FGSYQESKEQ AFRNAARVMQ ETGCDGVKLE 

       130        140        150        160        170        180 
GGEEMAETVA FLVRRGIPVF GHVGLMPQQV NTVGGFRSLG RGDDEAGKIR RDAQAIAQAG 

       190        200        210        220        230        240 
AFAVVIEGTV EPLAREITAL IDIPTVGIGA SSACDGQVLV SDDMLGLFQD FTPRFVKRFA 

       250        260        270 
HLAPQVSQAA EAYAEEVRAR RFPGPEHVFG AKPGA 

« Hide

References

[1]"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts."
Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. expand/collapse author list , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.
[2]"Revised genome sequence of Brucella suis 1330."
Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.
J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014291 Genomic DNA. Translation: AAN29279.1.
CP002997 Genomic DNA. Translation: AEM17692.1.
RefSeqNP_697364.1. NC_004310.3.
YP_005615184.1. NC_017251.1.

3D structure databases

ProteinModelPortalP65655.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING204722.BR0330.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN29279; AAN29279; BR0330.
AEM17692; AEM17692; BS1330_I0331.
GeneID1165991.
12136650.
KEGGbms:BR0330.
bsi:BS1330_I0331.
PATRIC17788949. VBIBruSui107850_0343.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0413.
HOGENOMHOG000078427.
KOK00606.
OMAAIKQYAD.
OrthoDBEOG63C0WN.
ProtClustDBPRK00311.

Enzyme and pathway databases

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_BRUSU
AccessionPrimary (citable) accession number: P65655
Secondary accession number(s): G0K686, Q8YFD0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: February 19, 2014
This is version 64 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

Brucella suis

Brucella suis (strain 1330): entries and gene names