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A5CU74 (GLMM_CLAM3) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 32. 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:CMM_2578
OrganismClavibacter michiganensis subsp. michiganensis (strain NCPPB 382) [Complete proteome] [HAMAP]
Taxonomic identifier443906 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrobacteriaceaeClavibacter

Protein attributes

Sequence length437 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 – 437437Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_1000068899

Sites

Active site931Phosphoserine intermediate By similarity
Metal binding931Magnesium; via phosphate group By similarity
Metal binding2301Magnesium By similarity
Metal binding2321Magnesium By similarity
Metal binding2341Magnesium By similarity

Amino acid modifications

Modified residue931Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5CU74 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: C5EFB5AFD02579D4

FASTA43745,704
        10         20         30         40         50         60 
MPRLFGTDGV RGLANGETIT ADLALRLAQA AAHVLGQDAR DPRVSGEFIA AAVAAGLASS 

        70         80         90        100        110        120 
GVDVFDAGVI PTPATAYLIA DFDADFGVMI SASHNPAPDN GIKFFAAGGR KLADELEDRI 

       130        140        150        160        170        180 
EAQLSRPVLL PTGADVGRIR RFADAEDRYV LHLLGTLQHR LDGIHVVLDC AHGAAAGISP 

       190        200        210        220        230        240 
EVFTDAGARV TVIGNDPDGM NINDRVGSTH LDLLAEAVLA HGADVGIAHD GDADRCLAVD 

       250        260        270        280        290        300 
HTGAIIDGDQ IMAVLALSMA RRGLLAERTL VATVMSNLGL RIAMAENDIT VMQTRVGDRY 

       310        320        330        340        350        360 
VLEAMNEGGY SLGGEQSGHL VIAEHATTGD GILTGIQLLG EMAATGKSLH ELASVMTVYP 

       370        380        390        400        410        420 
QVMINVRGVD RDRVGDDAEL NAAVARAEAE LGDTGRILMR ASGTEPMIRV MVEAADQATA 

       430 
ERHAEELAAL VTERLAI 

« Hide

References

[1]"The genome sequence of the tomato-pathogenic actinomycete Clavibacter michiganensis subsp. michiganensis NCPPB382 reveals a large island involved in pathogenicity."
Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M., Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., Kirchner O., Krause L., Linke B., McHardy A., Meyer F., Pohle S., Rueckert C. expand/collapse author list , Schneiker S., Zellermann E.-M., Puehler A., Eichenlaub R., Kaiser O., Bartels D.
J. Bacteriol. 190:2138-2149(2008) [PubMed: 18192381] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCPPB 382.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM711867 Genomic DNA. Translation: CAN02661.1.
RefSeqYP_001223323.1. NC_009480.1.

3D structure databases

ProteinModelPortalA5CU74.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5CU74.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5174761.
GenomeReviewsGene locus CMM_2578 in contig AM711867_GR.
KEGGcmi:CMM_2578.
PATRIC21455999. VBIClaMic82482_2697.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAGVGSTHL.
ProtClustDBPRK14318.

Enzyme and pathway databases

BioCycCMIC443906:CMM_2578-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. 2 hits.
TIGRFAMsTIGR01455. GlmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_CLAM3
AccessionPrimary (citable) accession number: A5CU74
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 12, 2007
Last modified: December 14, 2011
This is version 32 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