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Q821Z6 (GLMM_CHLCV) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. 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:CCA_00789
OrganismChlamydophila caviae [Complete proteome] [HAMAP]
Taxonomic identifier83557 [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_0000147871

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
Q821Z6 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 23DC95E6F93FFDA0

FASTA45849,670
        10         20         30         40         50         60 
MTREEKQLFG TDGIRGRANY EPMTVELSVL LGKAVAGVLQ ERKPGKHRVV VGKDTRLSGY 

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

       130        140        150        160        170        180 
EGFKISDVIE RRIEQMVACR DFGNFPEDYA VGKNKRVVDA MGRYIEFAKA TFPKGRTLKG 

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

       250        260        270        280        290        300 
DVGIALDGDG DRIIMVNEKG HIVDGDMILS ICASDLKKKA LLNGNRVVAT VMTNFGVLKY 

       310        320        330        340        350        360 
LESLGIETLI SSVGDRHVLQ NMLEHEANLG GEQSGHMIFL DYNTTGDGIV SALQVLRIMI 

       370        380        390        400        410        420 
ESESTLSDLT SLIVKSPQAL INVSVKEKIP LDTLPIVQEA LRDVRSSLGD SGRVLLRYSG 

       430        440        450 
TENICRVMVE GLKKHQVDSL AKTIADIVDS ELGAGIIE 

« Hide

References

[1]"Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): examining the role of niche-specific genes in the evolution of the Chlamydiaceae."
Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O., Salzberg S.L., Hsia R.-C., McClarty G. expand/collapse author list , Rank R.G., Bavoil P.M., Fraser C.M.
Nucleic Acids Res. 31:2134-2147(2003) [PubMed: 12682364] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GPIC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015925 Genomic DNA. Translation: AAP05530.1.
RefSeqNP_829652.1. NC_003361.3.

3D structure databases

ProteinModelPortalQ821Z6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1218474.
GenomeReviewsGene locus CCA_00789 in contig AE015925_GR.
KEGGcca:CCA00789.
PATRIC20270711. VBIChlCav107360_0836.
TIGRCCA_00789.

Phylogenomic databases

HOGENOMHBG644964.
OMAIGSAKRI.
PhylomeDBQ821Z6.
ProtClustDBPRK14314.

Enzyme and pathway databases

BioCycCCAV227941:CCA_00789-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_CHLCV
AccessionPrimary (citable) accession number: Q821Z6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 53 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