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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi43 – 431MagnesiumUniRule annotation
Metal bindingi82 – 821MagnesiumUniRule annotation
Binding sitei82 – 821Alpha-ketoisovalerate
Binding sitei111 – 1111Alpha-ketoisovalerate
Metal bindingi113 – 1131MagnesiumUniRule annotation
Active sitei179 – 1791Proton 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

BioCyciNMEN122586:GHGG-903-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: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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2632633-methyl-2-oxobutanoate hydroxymethyltransferasePRO_0000184867Add
BLAST

Proteomic databases

PaxDbiQ9JZW6.

Interactioni

Subunit structurei

Homodecamer; pentamer of dimers.1 Publication

Protein-protein interaction databases

STRINGi122586.NMB0870.

Structurei

Secondary structure

1
263
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1310Combined sources
Beta strandi17 – 215Combined sources
Helixi25 – 339Combined sources
Beta strandi38 – 414Combined sources
Helixi45 – 484Combined sources
Beta strandi53 – 553Combined sources
Helixi60 – 7314Combined sources
Beta strandi75 – 828Combined sources
Beta strandi87 – 904Combined sources
Helixi92 – 10413Combined sources
Beta strandi108 – 1136Combined sources
Helixi116 – 1183Combined sources
Helixi119 – 1279Combined sources
Beta strandi132 – 1387Combined sources
Helixi140 – 1423Combined sources
Helixi158 – 17013Combined sources
Beta strandi174 – 1807Combined sources
Helixi183 – 19210Combined sources
Beta strandi197 – 2026Combined sources
Beta strandi206 – 2116Combined sources
Helixi213 – 2164Combined sources
Beta strandi220 – 2234Combined sources
Helixi238 – 25013Combined sources
Helixi257 – 2593Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O66X-ray1.75A/B/C/D/E2-263[»]
1O68X-ray2.10A/B/C/D/E2-263[»]
ProteinModelPortaliQ9JZW6.
SMRiQ9JZW6. Positions 1-261.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JZW6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni43 – 442Alpha-ketoisovalerate binding

Sequence similaritiesi

Belongs to the PanB family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CCG. Bacteria.
COG0413. LUCA.
HOGENOMiHOG000078427.
KOiK00606.
OMAiMAAGAQM.
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.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1O66X-ray1.75A/B/C/D/E2-263[»]
1O68X-ray2.10A/B/C/D/E2-263[»]
ProteinModelPortaliQ9JZW6.
SMRiQ9JZW6. Positions 1-261.
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.
OMAiMAAGAQM.
OrthoDBiEOG63C0WN.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00003.
BioCyciNMEN122586:GHGG-903-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9JZW6.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MC58.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-263 IN COMPLEX WITH SUBSTRATE AND SODIUM ION, SUBUNIT.

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 11, 2015
This is version 98 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.