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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)DescriptionActionsGraphical viewLength
Metal bindingi53MagnesiumUniRule annotation1
Metal bindingi92MagnesiumUniRule annotation1
Binding sitei92Alpha-ketoisovalerateUniRule annotation1
Binding sitei120Alpha-ketoisovalerateUniRule annotation1
Metal bindingi122MagnesiumUniRule annotation1
Active sitei189Proton 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: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)DescriptionActionsGraphical viewLength
ChainiPRO_00002972371 – 2713-methyl-2-oxobutanoate hydroxymethyltransferaseAdd BLAST271

Interactioni

Subunit structurei

Homodecamer; pentamer of dimers.UniRule annotation

Structurei

Secondary structure

1271
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 23Combined sources10
Beta strandi27 – 31Combined sources5
Helixi35 – 43Combined sources9
Beta strandi47 – 51Combined sources5
Helixi55 – 58Combined sources4
Beta strandi63 – 65Combined sources3
Helixi70 – 82Combined sources13
Beta strandi86 – 92Combined sources7
Helixi101 – 113Combined sources13
Beta strandi117 – 122Combined sources6
Helixi125 – 127Combined sources3
Helixi128 – 136Combined sources9
Beta strandi141 – 147Combined sources7
Helixi149 – 151Combined sources3
Helixi152 – 155Combined sources4
Helixi165 – 181Combined sources17
Beta strandi184 – 190Combined sources7
Helixi193 – 202Combined sources10
Beta strandi207 – 212Combined sources6
Beta strandi216 – 221Combined sources6
Helixi223 – 226Combined sources4
Helixi248 – 260Combined sources13
Helixi267 – 269Combined sources3

3D structure databases

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

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni53 – 54Alpha-ketoisovalerate bindingUniRule annotation2

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3VAVX-ray1.80A/B/C/D/E/F/G/H/I/J1-271[»]
ProteinModelPortaliQ2SYZ1.
SMRiQ2SYZ1.
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.

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: November 2, 2016
This is version 74 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.