Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8XHZ5 (GLMM_CLOPE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoglucosamine mutase

EC=5.4.2.10
Gene names
Name:glmM
Ordered Locus Names:CPE2329
OrganismClostridium perfringens [Complete proteome] [HAMAP]
Taxonomic identifier1502 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length448 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate By similarity. HAMAP MF_01554_B

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP MF_01554_B

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01554_B

Post-translational modification

Activated by phosphorylation By similarity. HAMAP MF_01554_B

Sequence similarities

Belongs to the phosphohexose mutase family.

Ontologies

Keywords
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: InterPro

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 448448Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000147874

Sites

Active site1001Phosphoserine intermediate By similarity
Metal binding1001Magnesium; via phosphate group By similarity
Metal binding2401Magnesium By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity

Amino acid modifications

Modified residue1001Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8XHZ5 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: EE3B76AC6C206B1D

FASTA44848,355
        10         20         30         40         50         60 
MSRLFGTDGV RGIANTELTA ELAYNLGRAG AYVLTEGTHK PKILVAKDTR ISGDMLEAAL 

        70         80         90        100        110        120 
VAGILSVGAE AVCLGVVPTP AVAHLTRVYG ADAGVMISAS HNPVEYNGIK FFDDKGYKLS 

       130        140        150        160        170        180 
DDLEDEIQRV IESGFENVPS PTGANLGREI IEKAALEDYI SFAKDTIGIS LEGLRVALDC 

       190        200        210        220        230        240 
ANGASHEAAV RAFRELGAEI FVINDNPDGT NINENCGSTH PEELMEYVVK KKCHMGFAFD 

       250        260        270        280        290        300 
GDADRCLAVD EQGNLVDGDF ILTICAKYLK ELGRLKDDTL VVTVMSNLGL MIACKNEKIN 

       310        320        330        340        350        360 
TAVTKVGDRY VLEEMLAKGY SLGGEQSGHI IFLDHNSTGD GLVTALQVAS IVKRTGKSLF 

       370        380        390        400        410        420 
ELKNVMKVLP QVLVNAKVPN NMKNIHEEDE EIIAEIKKME AALDGCGRVL IRPSGTEPLV 

       430        440 
RVMLEGENQA EIDEMAHNLA KMIEAKCN 

« Hide

References

[1]"Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater."
Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.
Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002) [PubMed: 11792842] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 13 / Type A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000016 Genomic DNA. Translation: BAB82035.1.
RefSeqNP_563245.1. NC_003366.1.

3D structure databases

ProteinModelPortalQ8XHZ5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID990691.
GenomeReviewsGene locus CPE2329 in contig BA000016_GR.
KEGGcpe:CPE2329.
NMPDRfig|195102.1.peg.2392.
PATRIC19498715. VBICloPer59675_2400.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG644964.
OMAESTDNIM.
PhylomeDBQ8XHZ5.
ProtClustDBPRK14316.

Enzyme and pathway databases

BioCycCPER195102:CPE2329-MONOMER.

Family and domain databases

HAMAPMF_01554_B. GlmM_B.
[Tree]
InterProIPR005844. 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.
[Graphical view]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
KOK03431.
PfamPF02878. 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]
PRINTSPR00509. PGMPMM.
SUPFAMSSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
TIGRFAMsTIGR01455. GlmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_CLOPE
AccessionPrimary (citable) accession number: Q8XHZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2002
Last modified: January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families