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A7MIM5 (GLMM_CROS8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 37. 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:ESA_03567
OrganismCronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii) [Complete proteome] [HAMAP]
Taxonomic identifier290339 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCronobacter

Protein attributes

Sequence length445 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. HAMAP-Rule MF_01554

Post-translational modification

Activated by phosphorylation By similarity. HAMAP-Rule MF_01554

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 – 445445Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_1000068906

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
A7MIM5 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: AB09A56D9A90A1C5

FASTA44547,843
        10         20         30         40         50         60 
MSNRKYFGTD GIRGRVGDAP ITPDFVLKLG WAAGKVLARH GSRKVIIGKD TRISGYMLES 

        70         80         90        100        110        120 
ALEAGLAAAG LSALFTGPMP TPAVAYLTRT FRAEAGIVIS ASHNPFYDNG IKFFSIEGTK 

       130        140        150        160        170        180 
LPDEVEEAIE AELEKEISCV DSAELGKASR IVDAAGRYIE FCKGTFPNEL SLNGLKIVVD 

       190        200        210        220        230        240 
CANGATYHIA PNVLRELGAR VVTIGSEPDG LNINEKCGAT DVRLLQERVV AEKADLGIAF 

       250        260        270        280        290        300 
DGDGDRVIMV DHEGNKVDGD QILYIIAREG LRQGQLRGGA VGTLMSNMGL EVALKQLGIP 

       310        320        330        340        350        360 
FARAKVGDRY VLEKMQEKGW RIGAENSGHV ILLDKTTTGD GIVAALQVLT AIARNHMSLH 

       370        380        390        400        410        420 
DLCSGMKLFP QILVNVRFTP GSGDPLEHDT VKAVTEEVEQ ALGKRGRVLL RKSGTEPLIR 

       430        440 
VMVEGENEAQ VTEFAHRIAD AVKAV 

« Hide

References

[1]"Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic hybridization analysis with other Cronobacter species."
Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L., Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A., Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K., McClelland M., Forsythe S.J.
PLoS ONE 5:E9556-E9556(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-894.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000783 Genomic DNA. Translation: ABU78778.1.
RefSeqYP_001439614.1. NC_009778.1.

3D structure databases

ProteinModelPortalA7MIM5.
ModBaseSearch...

Protein-protein interaction databases

STRING290339.ESA_03567.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABU78778; ABU78778; ESA_03567.
GeneID5550809.
KEGGesa:ESA_03567.
PATRIC20398828. VBICroSak107175_3173.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMAKVIAIGC.
ProtClustDBPRK10887.

Enzyme and pathway databases

BioCycCSAK290339:GJ80-3557-MONOMER.

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_CROS8
AccessionPrimary (citable) accession number: A7MIM5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 2, 2007
Last modified: May 1, 2013
This is version 37 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