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Q73S29 (GLMM_MYCPA) 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:MAP_4247
OrganismMycobacterium paratuberculosis [Complete proteome] [HAMAP]
Taxonomic identifier1770 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)

Protein attributes

Sequence length444 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 – 444444Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000147917

Sites

Active site1021Phosphoserine intermediate By similarity
Metal binding1021Magnesium; via phosphate group By similarity
Metal binding2391Magnesium By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity

Amino acid modifications

Modified residue1021Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q73S29 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 3ABB15297818CCDE

FASTA44445,365
        10         20         30         40         50         60 
MGRLFGTDGV RGVANRELTA ELALALGAAA ARQLASGSAP GRRVAVIGRD PRASGEMLEA 

        70         80         90        100        110        120 
AVIAGLTSQG VDALRVGVLP TPAVAYLTGA YDADFGVMIS ASHNPMPDNG IKIFGPGGHK 

       130        140        150        160        170        180 
LDDGTEDRIE ALVGDAGPRP VGAGIGRVID AEDAADRYLR HLSKASTLRL DGLTVVVDCA 

       190        200        210        220        230        240 
HGAASAVAPR AYRAAGARVI AINADPNGLN INDNCGSTHL DSLRAAVVAH RADLGLAHDG 

       250        260        270        280        290        300 
DADRCLAVDA DGNLVDGDHI MVVLALAMRE AGELASDTLV TTVMSNLGLH LAMRSAGITV 

       310        320        330        340        350        360 
RTTGVGDRYV VEELRAGDFS LGGEQSGHIV MPALGSTGDG IVTGLRLMTR MAQTGSPLSD 

       370        380        390        400        410        420 
LASAMQTLPQ VLINVTVADK ATAATAPSVQ TAVGQAAAEL GDTGRILLRP SGTEPMIRVM 

       430        440 
VEAPEKDIAQ RLATRVAEAV SAAR 

« Hide

References

[1]"The complete genome sequence of Mycobacterium avium subspecies paratuberculosis."
Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., Kanjilal S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005) [PubMed: 16116077] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-968 / K-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016958 Genomic DNA. Translation: AAS06797.1.
RefSeqNP_963181.1. NC_002944.2.

3D structure databases

ProteinModelPortalQ73S29.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000039191; EBMYCP00000037580; EBMYCG00000039186.
GeneID2717767.
GenomeReviewsGene locus MAP_4247 in contig AE016958_GR.
KEGGmpa:MAP4247.
NMPDRfig|262316.1.peg.4247.
PATRIC18001440. VBIMycAvi108102_4521.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000015909.
HOGENOMHBG644964.
OMAGVGSTHL.
ProtClustDBPRK14318.

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_MYCPA
AccessionPrimary (citable) accession number: Q73S29
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 5, 2004
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