UniProtKB - P32056 (GMM_ECOLI)
Protein
GDP-mannose mannosyl hydrolase
Gene
gmm
Organism
Escherichia coli (strain K12)
Status
Functioni
Hydrolyzes both GDP-mannose and GDP-glucose. Could participate in the regulation of cell wall biosynthesis by influencing the concentration of GDP-mannose or GDP-glucose in the cell. Might also be involved in the biosynthesis of the slime polysaccharide colanic acid.2 Publications
Catalytic activityi
Cofactori
Mg2+UniRule annotation3 PublicationsNote: Binds 1 Mg2+ ion per subunit.UniRule annotation3 Publications
Kineticsi
GDP-alpha-D-mannose is likely to be the biological substrate, but the Kcat/KM obtained with GDP-alpha-D-glucose is very similar to that with GDP-alpha-D-mannose.
- KM=0.3 mM for GDP-mannose1 Publication
- KM=1.9 mM for GDP-glucose1 Publication
- Vmax=1.6 µmol/min/mg enzyme with GDP-mannose as substrate1 Publication
- Vmax=7.5 µmol/min/mg enzyme with GDP-glucose as substrate1 Publication
pH dependencei
Optimum pH is 9.3.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 8 | SubstrateUniRule annotation2 Publications | 1 | |
Binding sitei | 36 | SubstrateUniRule annotation2 Publications | 1 | |
Metal bindingi | 49 | Magnesium; via carbonyl oxygenUniRule annotation2 Publications | 1 | |
Metal bindingi | 69 | MagnesiumUniRule annotation2 Publications | 1 | |
Metal bindingi | 122 | MagnesiumUniRule annotation2 Publications | 1 | |
Sitei | 123 | Critical for catalysis | 1 |
GO - Molecular functioni
- GDP-glucosidase activity Source: EcoCyc
- GDP-mannose mannosyl hydrolase activity Source: UniProtKB-UniRule
- magnesium ion binding Source: EcoCyc
- manganese ion binding Source: EcoCyc
GO - Biological processi
- lipopolysaccharide biosynthetic process Source: UniProtKB-KW
Keywordsi
Molecular function | Hydrolase |
Biological process | Lipopolysaccharide biosynthesis |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:GDPMANMANHYDRO-MONOMER MetaCyc:GDPMANMANHYDRO-MONOMER |
SABIO-RKi | P32056 |
Names & Taxonomyi
Protein namesi | Recommended name: GDP-mannose mannosyl hydrolaseUniRule annotation (EC:3.6.1.-UniRule annotation)Short name: GDPMHUniRule annotation Alternative name(s): Colanic acid biosynthesis protein WcaH |
Gene namesi | Name:gmmUniRule annotation Synonyms:nudD, wcaH, yefC Ordered Locus Names:b2051, JW5335 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 21 | D → A: Increases Km for GDP-mannose 5-fold. Reduces activity 120-fold. 1 Publication | 1 | |
Mutagenesisi | 21 | D → N: Increases Km for GDP-mannose 9-fold. Reduces activity 400-fold. 1 Publication | 1 | |
Mutagenesisi | 36 | R → Q: Increases Km for GDP-mannose 9-fold. Reduces activity 24-fold. 1 Publication | 1 | |
Mutagenesisi | 51 | R → K: Increases Km for GDP-mannose 40-fold. Reduces activity 10-fold. 1 Publication | 1 | |
Mutagenesisi | 51 | R → Q: Increases Km for GDP-mannose 40-fold. Reduces activity 300-fold. 1 Publication | 1 | |
Mutagenesisi | 64 | R → Q: Increases Km for GDP-mannose 80-fold. Reduces activity 24-fold. 1 Publication | 1 | |
Mutagenesisi | 69 | E → Q: Increases Km for GDP-mannose 10-fold. Increases Km for magnesium 40-fold. Reduces activity 150-fold. | 1 | |
Mutagenesisi | 87 | H → Q: Increases Km for GDP-mannose 4-fold. Reduces activity 200-fold. 1 Publication | 1 | |
Mutagenesisi | 101 | H → Q: Increases Km for GDP-mannose 14-fold. Reduces activity 7-fold. 1 Publication | 1 | |
Mutagenesisi | 102 | Y → F: Increases Km for GDP-mannose 7-fold. Reduces activity 100-fold. 1 Publication | 1 | |
Mutagenesisi | 123 | H → Q: Increases Km for GDP-mannose 5-fold. Reduces activity 2000-fold. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB04315, Guanosine-5'-Diphosphate |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000056983 | 1 – 159 | GDP-mannose mannosyl hydrolaseAdd BLAST | 159 |
Proteomic databases
PaxDbi | P32056 |
PRIDEi | P32056 |
Interactioni
Subunit structurei
Homodimer.
UniRule annotation3 PublicationsProtein-protein interaction databases
BioGRIDi | 4261145, 369 interactors |
STRINGi | 511145.b2051 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P32056 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P32056 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 13 – 153 | Nudix hydrolaseUniRule annotationAdd BLAST | 141 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 2 – 3 | Substrate binding | 2 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 50 – 71 | Nudix boxAdd BLAST | 22 |
Sequence similaritiesi
Belongs to the Nudix hydrolase family.UniRule annotation
Phylogenomic databases
eggNOGi | COG1051, Bacteria |
HOGENOMi | CLU_037162_12_0_6 |
InParanoidi | P32056 |
PhylomeDBi | P32056 |
Family and domain databases
CDDi | cd03430, GDPMH, 1 hit |
HAMAPi | MF_00941, GDPMH_gmm, 1 hit |
InterProi | View protein in InterPro IPR033715, GDPMH IPR028613, GDPMH_Gmm IPR015797, NUDIX_hydrolase-like_dom_sf IPR020084, NUDIX_hydrolase_CS IPR000086, NUDIX_hydrolase_dom |
Pfami | View protein in Pfam PF00293, NUDIX, 1 hit |
PIRSFi | PIRSF037599, GDPMH, 1 hit |
SUPFAMi | SSF55811, SSF55811, 1 hit |
PROSITEi | View protein in PROSITE PS51462, NUDIX, 1 hit PS00893, NUDIX_BOX, 1 hit |
i Sequence
Sequence statusi: Complete.
P32056-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MFLRQEDFAT VVRSTPLVSL DFIVENSRGE FLLGKRTNRP AQGYWFVPGG
60 70 80 90 100
RVQKDETLEA AFERLTMAEL GLRLPITAGQ FYGVWQHFYD DNFSGTDFTT
110 120 130 140 150
HYVVLGFRFR VSEEELLLPD EQHDDYRWLT SDALLASDNV HANSRAYFLA
EKRTGVPGL
Sequence cautioni
The sequence AAC77844 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
Mass spectrometryi
Molecular mass is 18472±67 Da. Determined by MALDI. 1 Publication
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U38473 Genomic DNA Translation: AAC77844.1 Different initiation. U00096 Genomic DNA Translation: AAC75112.2 AP009048 Genomic DNA Translation: BAA15907.2 |
PIRi | E55239 |
RefSeqi | NP_416555.2, NC_000913.3 WP_001393539.1, NZ_LN832404.1 |
Genome annotation databases
EnsemblBacteriai | AAC75112; AAC75112; b2051 BAA15907; BAA15907; BAA15907 |
GeneIDi | 946559 |
KEGGi | ecj:JW5335 eco:b2051 |
PATRICi | fig|511145.12.peg.2128 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U38473 Genomic DNA Translation: AAC77844.1 Different initiation. U00096 Genomic DNA Translation: AAC75112.2 AP009048 Genomic DNA Translation: BAA15907.2 |
PIRi | E55239 |
RefSeqi | NP_416555.2, NC_000913.3 WP_001393539.1, NZ_LN832404.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1RYA | X-ray | 1.30 | A/B | 1-159 | [»] | |
2GT2 | X-ray | 2.00 | A/B/C/D | 1-159 | [»] | |
2GT4 | X-ray | 2.30 | A/B/C | 1-159 | [»] | |
SMRi | P32056 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4261145, 369 interactors |
STRINGi | 511145.b2051 |
Chemistry databases
DrugBanki | DB04315, Guanosine-5'-Diphosphate |
Proteomic databases
PaxDbi | P32056 |
PRIDEi | P32056 |
Genome annotation databases
EnsemblBacteriai | AAC75112; AAC75112; b2051 BAA15907; BAA15907; BAA15907 |
GeneIDi | 946559 |
KEGGi | ecj:JW5335 eco:b2051 |
PATRICi | fig|511145.12.peg.2128 |
Organism-specific databases
EchoBASEi | EB1737 |
Phylogenomic databases
eggNOGi | COG1051, Bacteria |
HOGENOMi | CLU_037162_12_0_6 |
InParanoidi | P32056 |
PhylomeDBi | P32056 |
Enzyme and pathway databases
BioCyci | EcoCyc:GDPMANMANHYDRO-MONOMER MetaCyc:GDPMANMANHYDRO-MONOMER |
SABIO-RKi | P32056 |
Miscellaneous databases
EvolutionaryTracei | P32056 |
PROi | PR:P32056 |
Family and domain databases
CDDi | cd03430, GDPMH, 1 hit |
HAMAPi | MF_00941, GDPMH_gmm, 1 hit |
InterProi | View protein in InterPro IPR033715, GDPMH IPR028613, GDPMH_Gmm IPR015797, NUDIX_hydrolase-like_dom_sf IPR020084, NUDIX_hydrolase_CS IPR000086, NUDIX_hydrolase_dom |
Pfami | View protein in Pfam PF00293, NUDIX, 1 hit |
PIRSFi | PIRSF037599, GDPMH, 1 hit |
SUPFAMi | SSF55811, SSF55811, 1 hit |
PROSITEi | View protein in PROSITE PS51462, NUDIX, 1 hit PS00893, NUDIX_BOX, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | GMM_ECOLI | |
Accessioni | P32056Primary (citable) accession number: P32056 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1993 |
Last sequence update: | March 27, 2002 | |
Last modified: | April 7, 2021 | |
This is version 152 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families