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Protein

3-methyl-2-oxobutanoate hydroxymethyltransferase

Gene

panB

Organism
Neisseria meningitidis serogroup B (strain MC58)
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.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. no protein annotated in this organism
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 bindingi43MagnesiumUniRule annotation1
Metal bindingi82MagnesiumUniRule annotation1
Binding sitei82Alpha-ketoisovalerate1
Binding sitei111Alpha-ketoisovalerate1
Metal bindingi113MagnesiumUniRule annotation1
Active sitei179Proton 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:NMB0870
OrganismiNeisseria meningitidis serogroup B (strain MC58)
Taxonomic identifieri122586 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
Proteomesi
  • UP000000425 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_00001848671 – 2633-methyl-2-oxobutanoate hydroxymethyltransferaseAdd BLAST263

Proteomic databases

PaxDbiQ9JZW6.

Interactioni

Subunit structurei

Homodecamer; pentamer of dimers.1 Publication

Protein-protein interaction databases

STRINGi122586.NMB0870.

Structurei

Secondary structure

1263
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 13Combined sources10
Beta strandi17 – 21Combined sources5
Helixi25 – 33Combined sources9
Beta strandi38 – 41Combined sources4
Helixi45 – 48Combined sources4
Beta strandi53 – 55Combined sources3
Helixi60 – 73Combined sources14
Beta strandi75 – 82Combined sources8
Beta strandi87 – 90Combined sources4
Helixi92 – 104Combined sources13
Beta strandi108 – 113Combined sources6
Helixi116 – 118Combined sources3
Helixi119 – 127Combined sources9
Beta strandi132 – 138Combined sources7
Helixi140 – 142Combined sources3
Helixi158 – 170Combined sources13
Beta strandi174 – 180Combined sources7
Helixi183 – 192Combined sources10
Beta strandi197 – 202Combined sources6
Beta strandi206 – 211Combined sources6
Helixi213 – 216Combined sources4
Beta strandi220 – 223Combined sources4
Helixi238 – 250Combined sources13
Helixi257 – 259Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1O66X-ray1.75A/B/C/D/E2-263[»]
1O68X-ray2.10A/B/C/D/E2-263[»]
ProteinModelPortaliQ9JZW6.
SMRiQ9JZW6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JZW6.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni43 – 44Alpha-ketoisovalerate binding2

Sequence similaritiesi

Belongs to the PanB family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CCG. Bacteria.
COG0413. LUCA.
HOGENOMiHOG000078427.
KOiK00606.
OMAiQMAYHTE.
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.

Q9JZW6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MITVNTLQKM KAAGEKIAML TAYESSFAAL MDDAGVEMLL VGDSLGMAVQ
60 70 80 90 100
GRKSTLPVSL RDMCYHTECV ARGAKNAMIV SDLPFGAYQQ SKEQAFAAAA
110 120 130 140 150
ELMAAGAHMV KLEGGVWMAE TTEFLQMRGI PVCAHIGLTP QSVFAFGGYK
160 170 180 190 200
VQGRGGKAQA LLNDAKAHDD AGAAVVLMEC VLAELAKKVT ETVSCPTIGI
210 220 230 240 250
GAGADCDGQV LVMHDMLGIF PGKTAKFVKN FMQGHDSVQA AVRAYVAEVK
260
AKTFPAAEHI FAD
Length:263
Mass (Da):27,739
Last modified:October 1, 2000 - v1
Checksum:iB863D8238F320317
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE002098 Genomic DNA. Translation: AAF41281.1.
PIRiF81148.
RefSeqiNP_273911.1. NC_003112.2.
WP_002222670.1. NC_003112.2.

Genome annotation databases

EnsemblBacteriaiAAF41281; AAF41281; NMB0870.
GeneIDi902986.
KEGGinme:NMB0870.
PATRICi20357133. VBINeiMen85645_1083.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE002098 Genomic DNA. Translation: AAF41281.1.
PIRiF81148.
RefSeqiNP_273911.1. NC_003112.2.
WP_002222670.1. NC_003112.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1O66X-ray1.75A/B/C/D/E2-263[»]
1O68X-ray2.10A/B/C/D/E2-263[»]
ProteinModelPortaliQ9JZW6.
SMRiQ9JZW6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi122586.NMB0870.

Proteomic databases

PaxDbiQ9JZW6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF41281; AAF41281; NMB0870.
GeneIDi902986.
KEGGinme:NMB0870.
PATRICi20357133. VBINeiMen85645_1083.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00028; UER00003.

Miscellaneous databases

EvolutionaryTraceiQ9JZW6.

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_NEIMB
AccessioniPrimary (citable) accession number: Q9JZW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: October 1, 2000
Last modified: November 2, 2016
This is version 101 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

3D-structure, Complete proteome, Reference 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.