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Protein

Phosphoglucosamine mutase

Gene

glmM

Organism
Verminephrobacter eiseniae (strain EF01-2)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.UniRule annotation

Catalytic activityi

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei102 – 1021Phosphoserine intermediateUniRule annotation
Metal bindingi102 – 1021Magnesium; via phosphate groupUniRule annotation
Metal bindingi241 – 2411MagnesiumUniRule annotation
Metal bindingi243 – 2431MagnesiumUniRule annotation
Metal bindingi245 – 2451MagnesiumUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciVEIS391735:GHY5-209-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglucosamine mutaseUniRule annotation (EC:5.4.2.10UniRule annotation)
Gene namesi
Name:glmMUniRule annotation
Ordered Locus Names:Veis_0209
OrganismiVerminephrobacter eiseniae (strain EF01-2)
Taxonomic identifieri391735 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeVerminephrobacter
Proteomesi
  • UP000000374 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 460460Phosphoglucosamine mutasePRO_0000301401Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei102 – 1021PhosphoserineUniRule annotation

Post-translational modificationi

Activated by phosphorylation.UniRule annotation

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiA1WEE4.

Interactioni

Protein-protein interaction databases

STRINGi391735.Veis_0209.

Structurei

3D structure databases

ProteinModelPortaliA1WEE4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphohexose mutase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107QJF. Bacteria.
COG1109. LUCA.
HOGENOMiHOG000268678.
KOiK03431.
OMAiFNLGGEQ.
OrthoDBiPOG091H02H5.

Family and domain databases

CDDicd05802. GlmM. 1 hit.
Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
HAMAPiMF_01554_B. GlmM_B. 1 hit.
InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR005841. Alpha-D-phosphohexomutase_SF.
IPR006352. GlmM_bact.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
TIGRFAMsiTIGR01455. glmM. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A1WEE4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRQHFGTDG IRGTVGQPPI TPDFVLRLAH AVGRVLRQTQ ERPVVLIGKD
60 70 80 90 100
TRISGYMLES ALESGFNSAG VDVVLLGPLP TPGVAYLTCA QRASLGVVIS
110 120 130 140 150
ASHNPYPDNG IKFFSAQGSK LSDAWEQAVE TALGEPPAWT NSANLGKARR
160 170 180 190 200
LNDAAERYIE FCKNTFAQDL SLKGLKIVLD AAHGAAYQVG PKVLRELEAE
210 220 230 240 250
VIAIGCSPDG LNINHEVGAT HPDTLVRAVH AHHADYGIAL DGDADRVLIV
260 270 280 290 300
DATGRLYNGD ELLYLMVADR MGRDEHVPGV VGTLMTNRAV ELALQARGVE
310 320 330 340 350
FVRAKVGDRY ILEELTRRDW ALGGEGSGHL LALDRHTTGD GIGSALQVLQ
360 370 380 390 400
ACVRSRSTLA QLLAAVTLYP QVLLNVRLPP DQDWTTNRLL ADAIQAVEQQ
410 420 430 440 450
LGASGRVLIR ASGTEPLLRV MVEARDAQLA DSCAQRLANA ARAGWQGHTS
460
LKNAPPMGAN
Length:460
Mass (Da):49,302
Last modified:February 6, 2007 - v1
Checksum:i519D881E97121162
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000542 Genomic DNA. Translation: ABM56001.1.
RefSeqiWP_011808020.1. NC_008786.1.

Genome annotation databases

EnsemblBacteriaiABM56001; ABM56001; Veis_0209.
KEGGivei:Veis_0209.
PATRICi24013702. VBIVerEis120356_0256.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000542 Genomic DNA. Translation: ABM56001.1.
RefSeqiWP_011808020.1. NC_008786.1.

3D structure databases

ProteinModelPortaliA1WEE4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi391735.Veis_0209.

Proteomic databases

PRIDEiA1WEE4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM56001; ABM56001; Veis_0209.
KEGGivei:Veis_0209.
PATRICi24013702. VBIVerEis120356_0256.

Phylogenomic databases

eggNOGiENOG4107QJF. Bacteria.
COG1109. LUCA.
HOGENOMiHOG000268678.
KOiK03431.
OMAiFNLGGEQ.
OrthoDBiPOG091H02H5.

Enzyme and pathway databases

BioCyciVEIS391735:GHY5-209-MONOMER.

Family and domain databases

CDDicd05802. GlmM. 1 hit.
Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
HAMAPiMF_01554_B. GlmM_B. 1 hit.
InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR005841. Alpha-D-phosphohexomutase_SF.
IPR006352. GlmM_bact.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
TIGRFAMsiTIGR01455. glmM. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGLMM_VEREI
AccessioniPrimary (citable) accession number: A1WEE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: February 6, 2007
Last modified: September 7, 2016
This is version 66 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

Complete proteome, Reference proteome

Documents

  1. 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.