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Protein

3-methyl-2-oxobutanoate hydroxymethyltransferase

Gene

panB

Organism
Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CIP 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424))
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 (panE)
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 bindingi53 – 531MagnesiumUniRule annotation
Metal bindingi92 – 921MagnesiumUniRule annotation
Binding sitei92 – 921Alpha-ketoisovalerateUniRule annotation
Binding sitei120 – 1201Alpha-ketoisovalerateUniRule annotation
Metal bindingi122 – 1221MagnesiumUniRule annotation
Active sitei189 – 1891Proton 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

BioCyciCTAI164546:GJNE-2553-MONOMER.
CTAI977880:GLC7-2553-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:RALTA_A2559
OrganismiCupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CIP 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424))
Taxonomic identifieri977880 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
Proteomesi
  • UP000001692 Componenti: Chromosome 1

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 – 2732733-methyl-2-oxobutanoate hydroxymethyltransferasePRO_1000096959Add
BLAST

Proteomic databases

PRIDEiB3R6G5.

Interactioni

Subunit structurei

Homodecamer; pentamer of dimers.UniRule annotation

Protein-protein interaction databases

STRINGi977880.RALTA_A2559.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 542Alpha-ketoisovalerate bindingUniRule annotation

Sequence similaritiesi

Belongs to the PanB family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CCG. Bacteria.
COG0413. LUCA.
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.

B3R6G5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYLLDPSRK TITIPKLQAM RDAGEKIAML TAYDSSFAAL LDYCGVEMIL
60 70 80 90 100
VGDSLGNVMQ GQQTTLPVTL EQMAYHTECA ARGNQTALLL TDLPFGTYPT
110 120 130 140 150
PEAAFASAVT LMKAGAQMVK LEGGDWLAPI VKFLVERSIP VCAHIGLTPQ
160 170 180 190 200
SVHALGGFKV QGKTDAGAAQ LRRDALALQA AGAQVVLMEA VPAALAGEIT
210 220 230 240 250
QSLAVPTIGI GAGADCSGQV LVLQDMLNIY PGRKAKFVRN FMDGQPSIEA
260 270
AVRAYVAAVK DGSFPAAEHT FSA
Length:273
Mass (Da):28,671
Last modified:September 2, 2008 - v1
Checksum:iFD46B5A07D7E6D6C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU633749 Genomic DNA. Translation: CAQ70490.1.
RefSeqiWP_012353786.1. NC_010528.1.

Genome annotation databases

EnsemblBacteriaiCAQ70490; CAQ70490; RALTA_A2559.
KEGGicti:RALTA_A2559.
PATRICi21531766. VBICupTai42494_2522.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU633749 Genomic DNA. Translation: CAQ70490.1.
RefSeqiWP_012353786.1. NC_010528.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi977880.RALTA_A2559.

Proteomic databases

PRIDEiB3R6G5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAQ70490; CAQ70490; RALTA_A2559.
KEGGicti:RALTA_A2559.
PATRICi21531766. VBICupTai42494_2522.

Phylogenomic databases

eggNOGiENOG4105CCG. Bacteria.
COG0413. LUCA.
HOGENOMiHOG000078427.
KOiK00606.
OMAiMAAGAQM.
OrthoDBiEOG63C0WN.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00003.
BioCyciCTAI164546:GJNE-2553-MONOMER.
CTAI977880:GLC7-2553-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: DSM 17343 / BCRC 17206 / CIP 107171 / LMG 19424 / R1.

Entry informationi

Entry nameiPANB_CUPTR
AccessioniPrimary (citable) accession number: B3R6G5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 2, 2008
Last modified: May 11, 2016
This is version 57 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.