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Q255P2 (GLMM_CHLFF) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoglucosamine mutase

EC=5.4.2.10
Gene names
Name:glmM
Ordered Locus Names:CF0224
OrganismChlamydophila felis (strain Fe/C-56) [Complete proteome] [HAMAP]
Taxonomic identifier264202 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila

Protein attributes

Sequence length458 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 – 458458Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000301299

Sites

Active site1061Phosphoserine intermediate By similarity
Metal binding1061Magnesium; via phosphate group By similarity
Metal binding2471Magnesium By similarity
Metal binding2491Magnesium By similarity
Metal binding2511Magnesium By similarity

Amino acid modifications

Modified residue1061Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q255P2 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 9AD5BD035E2EA52B

FASTA45849,681
        10         20         30         40         50         60 
MTREIKPLFG TDGVRGRANH EPMTVEMSVL LGKAVAGVLQ ECKPGRHRVV VGKDTRLSGY 

        70         80         90        100        110        120 
MFENALIAGL TSMGIETLVL GPIPTPGVAF ITRAYRADAG IMISASHNPY WDNGIKIFSS 

       130        140        150        160        170        180 
EGFKISDVIE RRIEQMVAFK EFGNLPEDYA VGKNKRVVDA MGRYIEFAKA TFPRGRTLNG 

       190        200        210        220        230        240 
LKIVLDCAHG AAYKVAPSVF EELDAEVICY GCEPTGSNIN DNCGALFPSV IQKAVIEHKA 

       250        260        270        280        290        300 
DVGIALDGDG DRIIMVNEKG HIVDGDMILS ICANDLKKKG ILHGNRIVAT VMTNFGVLKY 

       310        320        330        340        350        360 
LENVGIDTLI SPVGDRHVLQ NMLEYEANLG GEQSGHMIFL DYNTTGDGIV SALQVLRIMI 

       370        380        390        400        410        420 
ESESTLSDLT SPIVKSPQAL INVAVKEKIP LDTLPLVQEA LRDVRSSLGD SGRVLLRYSG 

       430        440        450 
TENICRVMVE GLKKHQVDSL AKTIADIVDS ELGVGIIE 

« Hide

References

[1]"Genome sequence of the cat pathogen, Chlamydophila felis."
Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H., Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H., Hattori M., Kuhara S., Shirai M.
DNA Res. 13:15-23(2006) [PubMed: 16766509] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Fe/C-56.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006861 Genomic DNA. Translation: BAE80996.1.
RefSeqYP_515141.1. NC_007899.1.

3D structure databases

HSSPHSSP built from PDB template 2DKD based on UniProtKB Q9P4V2.
ProteinModelPortalQ255P2.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ255P2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3958956.
GenomeReviewsGene locus CF0224 in contig AP006861_GR.
KEGGcfe:CF0224.
PATRIC20204019. VBIChlFel51660_0232.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAIGSAKRI.
PhylomeDBQ255P2.
ProtClustDBPRK14314.

Enzyme and pathway databases

BioCycCFEL264202:CF0224-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_CHLFF
AccessionPrimary (citable) accession number: Q255P2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: April 18, 2006
Last modified: January 25, 2012
This is version 41 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