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Protein

3-methyl-2-oxobutanoate hydroxymethyltransferase

Gene

panB

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Status
Reviewed-Annotation score: Annotation score: 4 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+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

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)
  2. 2-dehydropantoate 2-reductase (Cgl1089)
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 bindingi50 – 501MagnesiumBy similarity
Metal bindingi89 – 891MagnesiumBy similarity
Binding sitei89 – 891Alpha-ketoisovalerateBy similarity
Binding sitei119 – 1191Alpha-ketoisovalerateBy similarity
Metal bindingi121 – 1211MagnesiumBy similarity
Active sitei187 – 1871Proton acceptorBy similarity

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 hydroxymethyltransferase (EC:2.1.2.11)
Alternative name(s):
Ketopantoate hydroxymethyltransferase
Short name:
KPHMT
Gene namesi
Name:panB
Ordered Locus Names:Cgl0114, cg0149
OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Taxonomic identifieri196627 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000000582 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2692693-methyl-2-oxobutanoate hydroxymethyltransferasePRO_0000184838Add
BLAST

Interactioni

Subunit structurei

Homodecamer; pentamer of dimers.By similarity

Protein-protein interaction databases

STRINGi196627.NCgl0113.

Structurei

3D structure databases

ProteinModelPortaliQ9X712.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 512Alpha-ketoisovalerate bindingBy similarity

Sequence similaritiesi

Belongs to the PanB family.Curated

Phylogenomic databases

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

Q9X712-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGIDAKKIR TRHFREAKVN GQKVSVLTSY DALSARIFDE AGVDMLLVGD
60 70 80 90 100
SAANVVLGRD TTLSITLDEM IVLAKAVTIA TKRALVVVDL PFGTYEVSPN
110 120 130 140 150
QAVESAIRVM RETGAAAVKI EGGVEIAQTI RRIVDAGIPV VGHIGYTPQS
160 170 180 190 200
EHSLGGHVVQ GRGASSGKLI ADARALEQAG AFAVVLEMVP AEAAREVTED
210 220 230 240 250
LSITTIGIGA GNGTDGQVLV WQDAFGLNRG KKPRFVREYA TLGDSLHDAA
260
QAYIADIHAG TFPGEAESF
Length:269
Mass (Da):28,324
Last modified:April 23, 2003 - v2
Checksum:iC494D4FF3D2A0047
GO

Sequence cautioni

The sequence BAB97507.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA65397.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAF18682.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96580 Genomic DNA. Translation: CAA65397.1. Different initiation.
BA000036 Genomic DNA. Translation: BAB97507.1. Different initiation.
BX927148 Genomic DNA. Translation: CAF18682.1. Different initiation.
PIRiT47119.
RefSeqiNP_599367.1. NC_003450.3.
WP_011013400.1. NC_006958.1.

Genome annotation databases

EnsemblBacteriaiBAB97507; BAB97507; BAB97507.
CAF18682; CAF18682; cg0149.
GeneIDi1021087.
KEGGicgb:cg0149.
cgl:NCgl0113.
PATRICi21492276. VBICorGlu203724_0117.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96580 Genomic DNA. Translation: CAA65397.1. Different initiation.
BA000036 Genomic DNA. Translation: BAB97507.1. Different initiation.
BX927148 Genomic DNA. Translation: CAF18682.1. Different initiation.
PIRiT47119.
RefSeqiNP_599367.1. NC_003450.3.
WP_011013400.1. NC_006958.1.

3D structure databases

ProteinModelPortaliQ9X712.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196627.NCgl0113.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB97507; BAB97507; BAB97507.
CAF18682; CAF18682; cg0149.
GeneIDi1021087.
KEGGicgb:cg0149.
cgl:NCgl0113.
PATRICi21492276. VBICorGlu203724_0117.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00028; UER00003.

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

« Hide 'large scale' publications
  1. "D-pantothenate synthesis in Corynebacterium glutamicum and use of panBC and genes encoding L-valine synthesis for D-pantothenate overproduction."
    Eggeling L., Sahm H.
    Appl. Environ. Microbiol. 65:1973-1979(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY.
    Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
  2. "The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
    Ikeda M., Nakagawa S.
    Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Entry informationi

Entry nameiPANB_CORGL
AccessioniPrimary (citable) accession number: Q9X712
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: April 23, 2003
Last modified: November 11, 2015
This is version 101 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

Complete proteome, Reference 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.