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Q9CNJ0 (GLMM_PASMU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 66. 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:PM0440
OrganismPasteurella multocida (strain Pm70) [Complete proteome] [HAMAP]
Taxonomic identifier272843 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Pasteurella ›

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-Rule MF_01554

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP-Rule MF_01554

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Post-translational modification

Activated by phosphorylation By similarity.

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: HAMAP

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_0000147929

Sites

Active site1021Phosphoserine intermediate By similarity
Metal binding1021Magnesium; via phosphate group By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity

Amino acid modifications

Modified residue1021Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CNJ0 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 2A8B974B1B097091

FASTA44447,328
        10         20         30         40         50         60 
MAERKYFGTD GVRGKVGTFP ITPDFALKLG WAAGKVLATQ GSRTVLIGKD TRISGYMLES 

        70         80         90        100        110        120 
ALEAGLAAAG LSAAFTGPMP TPAIAYLTRT FRAEAGIVIS ASHNPYYDNG IKFFSAQGTK 

       130        140        150        160        170        180 
LPDDVEEAIE AMLDEPMDCV ESAELGRASR INDAVGRYIE FCKGTFPAHL SLENYKIVVD 

       190        200        210        220        230        240 
CAHGATYHIA PNVMRELGAE VIEIGAKPNG LNINEKCGAT DIKALQEKVL EVKADVGLAY 

       250        260        270        280        290        300 
DGDGDRLIMV DHLGNKVDGD QVLFIIAREA LRAGHLKGGV VGTLMSNMSL ELALKQLGIP 

       310        320        330        340        350        360 
FVRANVGDRY VLEKMQEKGW LLGGENSGHI IILDKNTTGD GIIASLAVLS AMVQHNLSLN 

       370        380        390        400        410        420 
ELASAVPLFP QVLINVRFAG GDNPLESAAV KAVAAEVEKR LAGKGRILLR KSGTEPLIRV 

       430        440 
MVECEDGALA QQCAEQIADV VRAN

« Hide

References

[1]"Complete genomic sequence of Pasteurella multocida Pm70."
May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pm70.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE004439 Genomic DNA. Translation: AAK02524.1.
RefSeqNP_245377.1. NC_002663.1.

3D structure databases

ProteinModelPortalQ9CNJ0.
ModBaseSearch...

Protein-protein interaction databases

STRING272843.PM0440.

Proteomic databases

PRIDEQ9CNJ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK02524; AAK02524; PM0440.
GeneID1243787.
KEGGpmu:PM0440.
PATRIC22870056. VBIPasMul88067_0452.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMATLMSNMS.
ProtClustDBPRK10887.

Family and domain databases

Gene3D3.40.120.10. 3 hits.
HAMAPMF_01554_B. GlmM_B.
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]
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_PASMU
AccessionPrimary (citable) accession number: Q9CNJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: June 1, 2001
Last modified: May 1, 2013
This is version 66 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

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