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Protein

3-methyl-2-oxobutanoate hydroxymethyltransferase

Gene

panB

Organism
Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264)
Status
Reviewed-Annotation score: Annotation score: 3 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.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), 3-methyl-2-oxobutanoate hydroxymethyltransferase (panB)
  2. 2-dehydropantoate 2-reductase (panE-1), 2-dehydropantoate 2-reductase (panE-2)
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

BioCyciBTHA271848:GJMY-1311-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:BTH_I1311
OrganismiBurkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264)
Taxonomic identifieri271848 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
Proteomesi
  • UP000001930 Componenti: Chromosome I

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 – 2712713-methyl-2-oxobutanoate hydroxymethyltransferasePRO_0000297237Add
BLAST

Interactioni

Subunit structurei

Homodecamer; pentamer of dimers.UniRule annotation

Structurei

Secondary structure

1
271
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 2310Combined sources
Beta strandi27 – 315Combined sources
Helixi35 – 439Combined sources
Beta strandi47 – 515Combined sources
Helixi55 – 584Combined sources
Beta strandi63 – 653Combined sources
Helixi70 – 8213Combined sources
Beta strandi86 – 927Combined sources
Helixi101 – 11313Combined sources
Beta strandi117 – 1226Combined sources
Helixi125 – 1273Combined sources
Helixi128 – 1369Combined sources
Beta strandi141 – 1477Combined sources
Helixi149 – 1513Combined sources
Helixi152 – 1554Combined sources
Helixi165 – 18117Combined sources
Beta strandi184 – 1907Combined sources
Helixi193 – 20210Combined sources
Beta strandi207 – 2126Combined sources
Beta strandi216 – 2216Combined sources
Helixi223 – 2264Combined sources
Helixi248 – 26013Combined sources
Helixi267 – 2693Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VAVX-ray1.80A/B/C/D/E/F/G/H/I/J1-271[»]
ProteinModelPortaliQ2SYZ1.
SMRiQ2SYZ1. Positions 12-270.
ModBaseiSearch...
MobiDBiSearch...

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

HOGENOMiHOG000078427.
KOiK00606.
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.
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR00222. panB. 1 hit.

Sequencei

Sequence statusi: Complete.

Q2SYZ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTYLQESSRP AVTVPKLQAM REAGEKIAML TCYDASFAAL LDRANVDVQL
60 70 80 90 100
IGDSLGNVLQ GQTTTLPVTL DDIAYHTACV ARAQPRALIV ADLPFGTYGT
110 120 130 140 150
PADAFASAVK LMRAGAQMVK FEGGEWLAET VRFLVERAVP VCAHVGLTPQ
160 170 180 190 200
SVHAFGGFKV QGKTEAGAAQ LLRDARAVEE AGAQLIVLEA VPTLVAAEVT
210 220 230 240 250
RELSIPTIGI GAGAECSGQV LVLHDMLGVF PGKRPRFVKD FMQGQPSIFA
260 270
AVEAYVRAVK DGSFPGPEHS F
Length:271
Mass (Da):28,726
Last modified:July 24, 2007 - v2
Checksum:iA3D42CB528EFFC99
GO

Sequence cautioni

The sequence ABC38840 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000086 Genomic DNA. Translation: ABC38840.1. Different initiation.
RefSeqiWP_025369782.1. NZ_CM000438.1.

Genome annotation databases

EnsemblBacteriaiABC38840; ABC38840; BTH_I1311.
KEGGibte:BTH_I1311.
PATRICi19305538. VBIBurTha36512_4078.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000086 Genomic DNA. Translation: ABC38840.1. Different initiation.
RefSeqiWP_025369782.1. NZ_CM000438.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VAVX-ray1.80A/B/C/D/E/F/G/H/I/J1-271[»]
ProteinModelPortaliQ2SYZ1.
SMRiQ2SYZ1. Positions 12-270.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABC38840; ABC38840; BTH_I1311.
KEGGibte:BTH_I1311.
PATRICi19305538. VBIBurTha36512_4078.

Phylogenomic databases

HOGENOMiHOG000078427.
KOiK00606.
OrthoDBiPOG091H02K8.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00003.
BioCyciBTHA271848:GJMY-1311-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_BURTA
AccessioniPrimary (citable) accession number: Q2SYZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: July 24, 2007
Last modified: September 7, 2016
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.