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Protein

3-methyl-2-oxobutanoate hydroxymethyltransferase

Gene

panB

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
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. 2-dehydropantoate 2-reductase (SAV2443), 2-dehydropantoate 2-reductase (SAV2600)
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 bindingi43 – 431MagnesiumUniRule annotation
Metal bindingi82 – 821MagnesiumUniRule annotation
Binding sitei82 – 821Alpha-ketoisovalerateUniRule annotation
Binding sitei112 – 1121Alpha-ketoisovalerateUniRule annotation
Metal bindingi114 – 1141MagnesiumUniRule annotation
Active sitei179 – 1791Proton 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

BioCyciSAUR158878:GJJ5-2667-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:SAV2599
OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
Taxonomic identifieri158878 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000002481 Componenti: Chromosome

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 – 2722723-methyl-2-oxobutanoate hydroxymethyltransferasePRO_0000184889Add
BLAST

Proteomic databases

PaxDbiQ931E6.

2D gel databases

World-2DPAGE0002:Q931E6.

Interactioni

Subunit structurei

Homodecamer; pentamer of dimers.UniRule annotation

Protein-protein interaction databases

STRINGi158878.SAV2599.

Structurei

3D structure databases

ProteinModelPortaliQ931E6.
SMRiQ931E6. Positions 3-260.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni43 – 442Alpha-ketoisovalerate bindingUniRule annotation

Sequence similaritiesi

Belongs to the PanB family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CCG. Bacteria.
COG0413. LUCA.
HOGENOMiHOG000078427.
KOiK00606.
OMAiRPQGKNI.
OrthoDBiEOG63C0WN.
PhylomeDBiQ931E6.

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.

Q931E6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTVSLLIDM KQKQTKISMV TAYDFPSAKQ VEAAGIDMIL VGDSLGMTVL
60 70 80 90 100
GYESTVQVTL ADMIHHGRAV RRGAPNTFVV VDMPIGAVGI SMTQDLNHAL
110 120 130 140 150
KLYQETNANA IKAEGAHITP FIEKATAIGI PVVAHLGLTP QSVGVMGYKL
160 170 180 190 200
QGATKEAAEQ LILDAKNVEQ AGAVALVLEA IPNDLAEEIS KHLTIPVIGI
210 220 230 240 250
GAGKGTDGQV LVYHDMLNYG VEHKAKFVKQ FADFSVGVDG LKQYDQEVKS
260 270
GAFPSEEYTY KKKIMNEVNN ND
Length:272
Mass (Da):29,241
Last modified:December 1, 2001 - v1
Checksum:iACEE2E048074F8D5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB58761.1.
RefSeqiWP_000860041.1. NC_002758.2.

Genome annotation databases

EnsemblBacteriaiBAB58761; BAB58761; SAV2599.
KEGGisav:SAV2599.
PATRICi19566134. VBIStaAur52173_2693.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB58761.1.
RefSeqiWP_000860041.1. NC_002758.2.

3D structure databases

ProteinModelPortaliQ931E6.
SMRiQ931E6. Positions 3-260.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi158878.SAV2599.

2D gel databases

World-2DPAGE0002:Q931E6.

Proteomic databases

PaxDbiQ931E6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB58761; BAB58761; SAV2599.
KEGGisav:SAV2599.
PATRICi19566134. VBIStaAur52173_2693.

Phylogenomic databases

eggNOGiENOG4105CCG. Bacteria.
COG0413. LUCA.
HOGENOMiHOG000078427.
KOiK00606.
OMAiRPQGKNI.
OrthoDBiEOG63C0WN.
PhylomeDBiQ931E6.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00003.
BioCyciSAUR158878:GJJ5-2667-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Mu50 / ATCC 700699.

Entry informationi

Entry nameiPANB_STAAM
AccessioniPrimary (citable) accession number: Q931E6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: December 1, 2001
Last modified: March 16, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

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.