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Protein

Phosphoglucosamine mutase

Gene

glmM

Organism
Mycobacterium leprae (strain TN)
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)DescriptionActionsGraphical viewLength
Active sitei102Phosphoserine intermediateUniRule annotation1
Metal bindingi102Magnesium; via phosphate groupUniRule annotation1
Metal bindingi240MagnesiumUniRule annotation1
Metal bindingi242MagnesiumUniRule annotation1
Metal bindingi244MagnesiumUniRule annotation1

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:ML0366
OrganismiMycobacterium leprae (strain TN)
Taxonomic identifieri272631 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000000806 Componenti: Chromosome

Organism-specific databases

LepromaiML0366.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001479161 – 463Phosphoglucosamine mutaseAdd BLAST463

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei102PhosphoserineUniRule annotation1

Post-translational modificationi

Activated by phosphorylation.UniRule annotation

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

STRINGi272631.ML0366.

Structurei

3D structure databases

ProteinModelPortaliQ49869.
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.

Q49869-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRLFGTDGV RGVANRELTP ELVLALGAAA ARCLANSGEP GRRVAVIGRD
60 70 80 90 100
PRASGEMLEA AVIAGLTSAG VDALRVGVLP TPAVAYLTGA YDADFGVMIS
110 120 130 140 150
ASHNPMVDNG IKIFGPGGHK LDDDTEDQIE DLVTGGPGLR PAGVAIGRVI
160 170 180 190 200
DAEDATERYL RHVGKASTIR LDGLTVVVDC AHGAASSAAP RAYRAAGARV
210 220 230 240 250
IAINADPNGI NINDRCGSTD LGSLRSAVLA HRADLGLAHD GDADRCLAVD
260 270 280 290 300
ANGDLVDGDA IMVVLALAMQ EAGELSSNTL VTTVMSNLGL HLAMRSVGVI
310 320 330 340 350
VRTTDVGDRY VLEELRAGDF SLGGEQSGHI VMPALGSTGD GIITGLRLMT
360 370 380 390 400
RMVQTSSSLA ALASAMRALP QVLINVEVAD KTTAAAAPLV QTAVETAEVE
410 420 430 440 450
LGNTGRILLR PSGTEPMIRV MVEAAEEDVA HRVATRVAAA VSAQGSPLRC
460
WNPDAISGVE LRL
Length:463
Mass (Da):47,644
Last modified:November 1, 1996 - v1
Checksum:iC0F1D18BB7697AC2
GO

Sequence cautioni

The sequence AAA17297 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00020 Genomic DNA. Translation: AAA17306.1.
U00020 Genomic DNA. Translation: AAA17297.1. Different initiation.
AL583918 Genomic DNA. Translation: CAC29874.1.
PIRiS72992.
RefSeqiNP_301362.1. NC_002677.1.
WP_010907686.1. NC_002677.1.

Genome annotation databases

EnsemblBacteriaiCAC29874; CAC29874; CAC29874.
GeneIDi909025.
KEGGimle:ML0366.
PATRICi18051338. VBIMycLep78757_0618.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00020 Genomic DNA. Translation: AAA17306.1.
U00020 Genomic DNA. Translation: AAA17297.1. Different initiation.
AL583918 Genomic DNA. Translation: CAC29874.1.
PIRiS72992.
RefSeqiNP_301362.1. NC_002677.1.
WP_010907686.1. NC_002677.1.

3D structure databases

ProteinModelPortaliQ49869.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272631.ML0366.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC29874; CAC29874; CAC29874.
GeneIDi909025.
KEGGimle:ML0366.
PATRICi18051338. VBIMycLep78757_0618.

Organism-specific databases

LepromaiML0366.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiGLMM_MYCLE
AccessioniPrimary (citable) accession number: Q49869
Secondary accession number(s): Q49862
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: November 1, 1996
Last modified: September 7, 2016
This is version 95 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.