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Protein

3-methyl-2-oxobutanoate hydroxymethyltransferase

Gene

panB

Organism
Pectobacterium carotovorum subsp. carotovorum (strain PC1)
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 (PC1_1035), 2-dehydropantoate 2-reductase (PC1_1469)
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)DescriptionActionsGraphical viewLength
Metal bindingi45MagnesiumUniRule annotation1
Metal bindingi84MagnesiumUniRule annotation1
Binding sitei84Alpha-ketoisovalerateUniRule annotation1
Binding sitei112Alpha-ketoisovalerateUniRule annotation1
Metal bindingi114MagnesiumUniRule annotation1
Active sitei181Proton acceptorUniRule annotation1

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

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:PC1_3118
OrganismiPectobacterium carotovorum subsp. carotovorum (strain PC1)
Taxonomic identifieri561230 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesPectobacteriaceaePectobacterium
Proteomesi
  • UP000002736 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10002034761 – 2653-methyl-2-oxobutanoate hydroxymethyltransferaseAdd BLAST265

Proteomic databases

PRIDEiC6DC47.

Interactioni

Subunit structurei

Homodecamer; pentamer of dimers.UniRule annotation

Protein-protein interaction databases

STRINGi561230.PC1_3118.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni45 – 46Alpha-ketoisovalerate bindingUniRule annotation2

Sequence similaritiesi

Belongs to the PanB family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CCG. Bacteria.
COG0413. LUCA.
HOGENOMiHOG000078427.
KOiK00606.
OMAiDMLGFFD.
OrthoDBiPOG091H02K8.

Family and domain databases

CDDicd06557. KPHMT-like. 1 hit.
Gene3Di3.20.20.60. 1 hit.
HAMAPiMF_00156. PanB. 1 hit.
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.
TIGRFAMsiTIGR00222. panB. 1 hit.

Sequencei

Sequence statusi: Complete.

C6DC47-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPTTISHLR QWKQEQRKFA TITAYDASFS RLFFEQGIRV MLVGDSLGMT
60 70 80 90 100
VQGHDSTLPV TTSDIVYHTQ CVRRGAPLAL VLSDMPFMTY ATPEQTFSQA
110 120 130 140 150
AELMRAGANM VKLEGGSWLA PTVKMLTERA VPVCGHLGLT PQSVNIFGGY
160 170 180 190 200
KIQGRSESDA NQLLADALAL EEAGAQLLVL ECVPVALAKR VTDALSIPVI
210 220 230 240 250
GIGAGNVTDG QILVMHDAFG ITGDNTPKFA KNFLAQSGGD IRAAVGLYAQ
260
EVEQGIYPAE EHSFH
Length:265
Mass (Da):28,552
Last modified:September 1, 2009 - v1
Checksum:i40F112C2BBA7F7B0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001657 Genomic DNA. Translation: ACT14141.1.
RefSeqiWP_015841286.1. NC_012917.1.

Genome annotation databases

EnsemblBacteriaiACT14141; ACT14141; PC1_3118.
KEGGipct:PC1_3118.
PATRICi20490938. VBIPecCar70489_3138.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001657 Genomic DNA. Translation: ACT14141.1.
RefSeqiWP_015841286.1. NC_012917.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi561230.PC1_3118.

Proteomic databases

PRIDEiC6DC47.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACT14141; ACT14141; PC1_3118.
KEGGipct:PC1_3118.
PATRICi20490938. VBIPecCar70489_3138.

Phylogenomic databases

eggNOGiENOG4105CCG. Bacteria.
COG0413. LUCA.
HOGENOMiHOG000078427.
KOiK00606.
OMAiDMLGFFD.
OrthoDBiPOG091H02K8.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00003.

Family and domain databases

CDDicd06557. KPHMT-like. 1 hit.
Gene3Di3.20.20.60. 1 hit.
HAMAPiMF_00156. PanB. 1 hit.
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.
TIGRFAMsiTIGR00222. panB. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPANB_PECCP
AccessioniPrimary (citable) accession number: C6DC47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 1, 2009
Last modified: November 30, 2016
This is version 53 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.