Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

3-methyl-2-oxobutanoate hydroxymethyltransferase

Gene

panB

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is tranferred onto alpha-ketoisovalerate to form ketopantoate.1 Publication

Catalytic activityi

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate.1 Publication

Cofactori

Mg2+2 Publications, Co2+2 Publications, Zn2+2 Publications, Ni2+2 Publications, Ca2+2 PublicationsNote: Binds 1 Mg2+ ion per subunit. Can also use Co2+, Zn2+, Ni2+ and Ca2+ to a lesser extent.2 Publications

Kineticsi

  1. KM=240 µM for alpha-ketoisovalerate (at 37 degrees Celsius and pH 7.5)1 Publication
  2. KM=820 µM for 5,10-methylenetetrahydrofolate (at 37 degrees Celsius and pH 7.5)1 Publication
  1. Vmax=1.6 µmol/min/mg enzyme (at 37 degrees Celsius and pH 7.5)1 Publication

pH dependencei

Optimum pH is 7.0-7.5.1 Publication

Pathwayi: (R)-pantothenate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes (R)-pantoate from 3-methyl-2-oxobutanoate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. 3-methyl-2-oxobutanoate hydroxymethyltransferase (panB), 3-methyl-2-oxobutanoate hydroxymethyltransferase (panB)
  2. 2-dehydropantoate 2-reductase (LH57_14090), Putative 2-dehydropantoate 2-reductase (Rv2573)
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 bindingi62Magnesium1
Metal bindingi101MagnesiumBy similarity1
Binding sitei101Alpha-ketoisovalerateBy similarity1
Binding sitei131Alpha-ketoisovalerateBy similarity1
Metal bindingi133Magnesium1
Active sitei199Proton acceptorBy similarity1

GO - Molecular functioni

  • 3-methyl-2-oxobutanoate hydroxymethyltransferase activity Source: MTBBASE
  • magnesium ion binding Source: MTBBASE

GO - Biological processi

  • growth Source: MTBBASE
  • pantothenate biosynthetic process Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Pantothenate biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-6436-MONOMER.
UniPathwayiUPA00028; UER00003.

Names & Taxonomyi

Protein namesi
Recommended name:
3-methyl-2-oxobutanoate hydroxymethyltransferase (EC:2.1.2.11)
Alternative name(s):
Ketopantoate hydroxymethyltransferase
Short name:
KPHMT
Gene namesi
Name:panB
Ordered Locus Names:Rv2225
ORF Names:MTCY427.06
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv2225.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001848642 – 2813-methyl-2-oxobutanoate hydroxymethyltransferaseAdd BLAST280

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1

Post-translational modificationi

Pupylated at an undetermined lysine residue by the prokaryotic ubiquitin-like protein Pup with the help of the ligase PafA, which leads to its degradation by the proteasome. The cross-link involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side-chain amino group of a lysine in PanB.1 Publication

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

PaxDbiP9WIL7.

Interactioni

Subunit structurei

Homodecamer; pentamer of dimers.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv2225.

Structurei

Secondary structure

1281
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi23 – 32Combined sources10
Beta strandi36 – 40Combined sources5
Helixi44 – 51Combined sources8
Turni52 – 54Combined sources3
Beta strandi57 – 60Combined sources4
Helixi64 – 67Combined sources4
Beta strandi72 – 76Combined sources5
Helixi79 – 81Combined sources3
Helixi83 – 92Combined sources10
Beta strandi96 – 101Combined sources6
Helixi111 – 123Combined sources13
Beta strandi128 – 135Combined sources8
Helixi136 – 138Combined sources3
Helixi139 – 148Combined sources10
Beta strandi152 – 157Combined sources6
Helixi176 – 191Combined sources16
Beta strandi194 – 200Combined sources7
Helixi203 – 212Combined sources10
Beta strandi217 – 222Combined sources6
Beta strandi226 – 231Combined sources6
Helixi233 – 236Combined sources4
Helixi254 – 270Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OY0X-ray2.80A/B/C/D/E1-281[»]
ProteinModelPortaliP9WIL7.
SMRiP9WIL7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni62 – 63Alpha-ketoisovalerate bindingBy similarity2

Sequence similaritiesi

Belongs to the PanB family.Curated

Phylogenomic databases

eggNOGiENOG4105CCG. Bacteria.
COG0413. LUCA.
KOiK00606.
OMAiDMLGFFD.
PhylomeDBiP9WIL7.

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.
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR00222. panB. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P9WIL7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEQTIYGAN TPGGSGPRTK IRTHHLQRWK ADGHKWAMLT AYDYSTARIF
60 70 80 90 100
DEAGIPVLLV GDSAANVVYG YDTTVPISID ELIPLVRGVV RGAPHALVVA
110 120 130 140 150
DLPFGSYEAG PTAALAAATR FLKDGGAHAV KLEGGERVAE QIACLTAAGI
160 170 180 190 200
PVMAHIGFTP QSVNTLGGFR VQGRGDAAEQ TIADAIAVAE AGAFAVVMEM
210 220 230 240 250
VPAELATQIT GKLTIPTVGI GAGPNCDGQV LVWQDMAGFS GAKTARFVKR
260 270 280
YADVGGELRR AAMQYAQEVA GGVFPADEHS F
Length:281
Mass (Da):29,336
Last modified:April 16, 2014 - v1
Checksum:iE05CDDC5B7E80932
GO

Mass spectrometryi

Molecular mass is 29202 Da from positions 2 - 281. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP45003.1.
PIRiE70776.
RefSeqiNP_216741.1. NC_000962.3.
WP_003411489.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP45003; CCP45003; Rv2225.
GeneIDi887440.
KEGGimtu:Rv2225.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP45003.1.
PIRiE70776.
RefSeqiNP_216741.1. NC_000962.3.
WP_003411489.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OY0X-ray2.80A/B/C/D/E1-281[»]
ProteinModelPortaliP9WIL7.
SMRiP9WIL7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2225.

Proteomic databases

PaxDbiP9WIL7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP45003; CCP45003; Rv2225.
GeneIDi887440.
KEGGimtu:Rv2225.

Organism-specific databases

TubercuListiRv2225.

Phylogenomic databases

eggNOGiENOG4105CCG. Bacteria.
COG0413. LUCA.
KOiK00606.
OMAiDMLGFFD.
PhylomeDBiP9WIL7.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00003.
BioCyciMTBH37RV:G185E-6436-MONOMER.

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.
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR00222. panB. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPANB_MYCTU
AccessioniPrimary (citable) accession number: P9WIL7
Secondary accession number(s): L0TAJ8, P0A5Q8, Q10505
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: November 2, 2016
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Was identified as a natural substrate of the M.tuberculosis proteasome.
Was identified as a high-confidence drug target.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.