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A0RRK2 (GLMM_CAMFF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 47. 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:CFF8240_1717
OrganismCampylobacter fetus subsp. fetus (strain 82-40) [Complete proteome] [HAMAP]
Taxonomic identifier360106 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter ›

Protein attributes

Sequence length446 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 – 446446Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_0000301296

Sites

Active site991Phosphoserine intermediate By similarity
Metal binding991Magnesium; via phosphate group By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity
Metal binding2461Magnesium By similarity

Amino acid modifications

Modified residue991Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A0RRK2 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: EBD0D00E65F329B6

FASTA44648,865
        10         20         30         40         50         60 
MKLFGTDGVR GRAGEKLNAM TAMRLAMAAG IYFRKNSITN KILVGKDTRK SGYMIETAIV 

        70         80         90        100        110        120 
AGLTAVGYNV IQIGPMPTPA IAFLTEDMRC DAGIMISASH NPFDDNGIKF FDSFGNKLSV 

       130        140        150        160        170        180 
EAEQAIENIF FHNEIIENNQ KIGLEIGQSK RIDDVIGRYI VHIKNSFPKS LTLKGLRVVL 

       190        200        210        220        230        240 
DVANGAVYKV APTVFSELGA ETIVLNDEPN GGNINDGCGA LHPENLAKEV KRLRADIGFA 

       250        260        270        280        290        300 
FDGDADRLVV VDENAKVVDG DALLGVLATY LDENKMLDKK EIVATVMSNA ALDDYLAKHK 

       310        320        330        340        350        360 
IKLLRSNVGD KFVLEMMKEN GINFGGEQSG HIIFSDFSKT GDGLVSALQV SACLLAKNKK 

       370        380        390        400        410        420 
ASEIFGSIKA YPQKLSNLKI IEKRPLDELK GLKELEDELK KLGIRTLFRY SGTENVIRLL 

       430        440 
LEGKDEALVT KKIAEVEKFF IKALNE

« Hide

References

[1]"Sequence of Campylobacter fetus subsp. fetus 82-40."
Fouts D.E., Nelson K.E.
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 82-40.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000487 Genomic DNA. Translation: ABK83123.1.
RefSeqYP_892835.1. NC_008599.1.

3D structure databases

ProteinModelPortalA0RRK2.
ModBaseSearch...

Protein-protein interaction databases

STRING360106.CFF8240_1717.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK83123; ABK83123; CFF8240_1717.
GeneID4538587.
KEGGcff:CFF8240_1717.
PATRIC20037952. VBICamFet25865_1670.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMASGHIILF.
ProtClustDBPRK14324.

Enzyme and pathway databases

BioCycCFET360106:GHTH-1721-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. 2 hits.
TIGRFAMsTIGR01455. glmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_CAMFF
AccessionPrimary (citable) accession number: A0RRK2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: January 9, 2007
Last modified: May 1, 2013
This is version 47 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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