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Protein

3-methyl-2-oxobutanoate hydroxymethyltransferase

Gene

panB

Organism
Salmonella heidelberg (strain SL476)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is tranferred onto alpha-ketoisovalerate to form ketopantoate.UniRule annotation

Catalytic activityi

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Pathwayi: (R)-pantothenate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes (R)-pantoate from 3-methyl-2-oxobutanoate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. 3-methyl-2-oxobutanoate hydroxymethyltransferase (panB)
  2. no protein annotated in this organism
This subpathway is part of the pathway (R)-pantothenate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-pantoate from 3-methyl-2-oxobutanoate, the pathway (R)-pantothenate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi45 – 451MagnesiumUniRule annotation
Metal bindingi84 – 841MagnesiumUniRule annotation
Binding sitei84 – 841Alpha-ketoisovalerateUniRule annotation
Binding sitei112 – 1121Alpha-ketoisovalerateUniRule annotation
Metal bindingi114 – 1141MagnesiumUniRule annotation
Active sitei180 – 1801Proton acceptorUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Pantothenate biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciSENT454169:GHYG-207-MONOMER.
UniPathwayiUPA00028; UER00003.

Names & Taxonomyi

Protein namesi
Recommended name:
3-methyl-2-oxobutanoate hydroxymethyltransferaseUniRule annotation (EC:2.1.2.11UniRule annotation)
Alternative name(s):
Ketopantoate hydroxymethyltransferaseUniRule annotation
Short name:
KPHMTUniRule annotation
Gene namesi
Name:panBUniRule annotation
Ordered Locus Names:SeHA_C0214
OrganismiSalmonella heidelberg (strain SL476)
Taxonomic identifieri454169 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2632633-methyl-2-oxobutanoate hydroxymethyltransferasePRO_1000097004Add
BLAST

Proteomic databases

PRIDEiB4TK05.

Interactioni

Subunit structurei

Homodecamer; pentamer of dimers.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB4TK05.
SMRiB4TK05. Positions 3-263.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 462Alpha-ketoisovalerate bindingUniRule annotation

Sequence similaritiesi

Belongs to the PanB family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000078427.
KOiK00606.
OMAiMAAGAQM.
OrthoDBiEOG63C0WN.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
HAMAPiMF_00156. PanB.
InterProiIPR003700. Pantoate_hydroxy_MeTrfase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERiPTHR20881. PTHR20881. 1 hit.
PfamiPF02548. Pantoate_transf. 1 hit.
[Graphical view]
PIRSFiPIRSF000388. Pantoate_hydroxy_MeTrfase. 1 hit.
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR00222. panB. 1 hit.

Sequencei

Sequence statusi: Complete.

B4TK05-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPTTISLLQ KCKQEKKRFA TITAYDYSFA KLFADEGINV MLVGDSLGMT
60 70 80 90 100
IQGHDSTLPV TVEDIAYHTR AVRRGAPNCL LLSDLPFMAY ATPEQACENA
110 120 130 140 150
AIVMRAGANM VKIEGGAWLV DTVKMLTERA VPVCGHLGLT PQSVNIFGGY
160 170 180 190 200
KIQGRGDAGQ VLLDDALALE AAGAQLLVLE CVPVELAKRV TEALSIPVIG
210 220 230 240 250
IGAGNVTDGQ ILVMHDAFGI TGGHIPKFAK NFLAEAGDMR AAVQQYMAEV
260
ESGVYPGEEH SFH
Length:263
Mass (Da):28,105
Last modified:September 23, 2008 - v1
Checksum:iD4913FBDB5577603
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001120 Genomic DNA. Translation: ACF67119.1.
RefSeqiWP_000805487.1. NC_011083.1.

Genome annotation databases

EnsemblBacteriaiACF67119; ACF67119; SeHA_C0214.
KEGGiseh:SeHA_C0214.
PATRICi18508290. VBISalEnt43179_0277.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001120 Genomic DNA. Translation: ACF67119.1.
RefSeqiWP_000805487.1. NC_011083.1.

3D structure databases

ProteinModelPortaliB4TK05.
SMRiB4TK05. Positions 3-263.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiB4TK05.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACF67119; ACF67119; SeHA_C0214.
KEGGiseh:SeHA_C0214.
PATRICi18508290. VBISalEnt43179_0277.

Phylogenomic databases

HOGENOMiHOG000078427.
KOiK00606.
OMAiMAAGAQM.
OrthoDBiEOG63C0WN.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00003.
BioCyciSENT454169:GHYG-207-MONOMER.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
HAMAPiMF_00156. PanB.
InterProiIPR003700. Pantoate_hydroxy_MeTrfase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERiPTHR20881. PTHR20881. 1 hit.
PfamiPF02548. Pantoate_transf. 1 hit.
[Graphical view]
PIRSFiPIRSF000388. Pantoate_hydroxy_MeTrfase. 1 hit.
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR00222. panB. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Comparative genomics of 28 Salmonella enterica isolates: evidence for CRISPR-mediated adaptive sublineage evolution."
    Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., Leclerc J.E., Ravel J., Cebula T.A.
    J. Bacteriol. 193:3556-3568(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SL476.

Entry informationi

Entry nameiPANB_SALHS
AccessioniPrimary (citable) accession number: B4TK05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: November 11, 2015
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.