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Protein

Phosphoglucosamine mutase

Gene

glmM

Organism
Mycobacterium ulcerans (strain Agy99)
Status
Reviewed-Annotation score: Annotation score: 2 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 bindingi240 – 2401MagnesiumUniRule annotation
Metal bindingi242 – 2421MagnesiumUniRule annotation
Metal bindingi244 – 2441MagnesiumUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglucosamine mutaseUniRule annotation (EC:5.4.2.10UniRule annotation)
Gene namesi
Name:glmMUniRule annotation
Ordered Locus Names:MUL_0866
OrganismiMycobacterium ulcerans (strain Agy99)
Taxonomic identifieri362242 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000000765 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 445445Phosphoglucosamine mutasePRO_0000301344Add
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

Structurei

3D structure databases

ProteinModelPortaliA0PMD3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphohexose mutase family.UniRule annotation

Phylogenomic databases

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.

A0PMD3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRLFGTDGV RGVANRELTA ELALALGAAT AQHLASSTGP GRRVAVVGRD
60 70 80 90 100
PRASGEMLEA AVIAGLTSQG VDALRVGVLP TPAVAYLTGA YDADFGVMIS
110 120 130 140 150
ASHNPMPDNG IKIFGPGGHK LDDATENRIE SLVAAGPGLR PVGSEIGRVI
160 170 180 190 200
DAEDAADRYL RHVSKACTTR LDGLTVVVDC AHGAASEVGP RAYRAAGARV
210 220 230 240 250
IEINADPNGL NINDDCGSTH LEAIRAAVLA HGADLGVAHD GDADRCLAVD
260 270 280 290 300
ANGDLVDGDA IMVVLALAMQ EAGELASDTL VTTVMSNLGL HLAMREAGVN
310 320 330 340 350
VRTTGVGDRY VLEELRAGDY SLGGEQSGHI VMPGLGSTGD GIVTGLRLMT
360 370 380 390 400
RMVATGASLA ALASRMQTLP QVLINVQVTD KATAAAAPSV QAAVDRAETE
410 420 430 440
LGDTGRILLR PSGTEPLIRV MVEAADEEAA HRLATSVADA VSAAG
Length:445
Mass (Da):45,415
Last modified:January 9, 2007 - v1
Checksum:iF1DCCEBF1A529ABC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000325 Genomic DNA. Translation: ABL03502.1.

Genome annotation databases

EnsemblBacteriaiABL03502; ABL03502; MUL_0866.
KEGGimul:MUL_0866.
PATRICi18168432. VBIMycUlc37413_1078.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000325 Genomic DNA. Translation: ABL03502.1.

3D structure databases

ProteinModelPortaliA0PMD3.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABL03502; ABL03502; MUL_0866.
KEGGimul:MUL_0866.
PATRICi18168432. VBIMycUlc37413_1078.

Phylogenomic databases

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]
ProtoNetiSearch...

Entry informationi

Entry nameiGLMM_MYCUA
AccessioniPrimary (citable) accession number: A0PMD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: January 9, 2007
Last modified: September 7, 2016
This is version 68 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

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.