Skip Header

Contribute Send feedback
Read comments (?) or add your own

A7ZB08 (GLMM_CAMC1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoglucosamine mutase

EC=5.4.2.10
Gene names
Name:glmM
Ordered Locus Names:Ccon26_00450
ORF Names:CCC13826_1807
OrganismCampylobacter concisus (strain 13826) [Complete proteome] [HAMAP]
Taxonomic identifier360104 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

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 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 – 446446Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_1000073570

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
A7ZB08 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 679CD710DDC60D0B

FASTA44648,781
        10         20         30         40         50         60 
MKLFGTDGVR GKAGEKLSAQ TSMRLAMAAG IYFRKTSATN VILVGKDTRK SGYMIETAIV 

        70         80         90        100        110        120 
AGLTAVGYNV LQIGPMPTPA IAFLTENMRC DAGIMISASH NPYYDNGIKF FDSFGNKLDE 

       130        140        150        160        170        180 
TIEAEIEKIF YDDELIANAQ KTMTEIGANK RIDDVIGRYI VQIKNSFPKE LNLKNLRVVL 

       190        200        210        220        230        240 
DVANGAAYKV APTVFSELGA DVIVINNEPN GSNINQNCGA LHPEDLASEV KRLRADIGFA 

       250        260        270        280        290        300 
FDGDADRLVV VDENGEVVHG DAILGSLAAF LHEQKALKGG AIVATVMSNA ALDDYLKAHK 

       310        320        330        340        350        360 
IKLLRSNVGD KYVLEMMKEN GINFGGEQSG HVIFNDYAKT GDGLVTSMQV VAMMLKKGKK 

       370        380        390        400        410        420 
ASEIFGELKP YPQILLNLKI TEKKPLDKIE GLKELEASLA KEGIRSLFRY SGTENLIRLL 

       430        440 
LEGKNQTLVE KRMDEVEKFF VKALNA 

« Hide

References

[1]"Genome sequence of Campylobacter concisus 13826 isolated from human feces."
Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., On S., Nelson K.E.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 13826.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000792 Genomic DNA. Translation: EAT99044.1.
RefSeqYP_001465966.1. NC_009802.1.

3D structure databases

ProteinModelPortalA7ZB08.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7ZB08.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5597052.
GenomeReviewsGene locus Ccon26_00450 in contig CP000792_GR.
KEGGcco:CCC13826_1807.
PATRIC20026229. VBICamCon95352_0083.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAIGSAKRI.
ProtClustDBPRK14324.

Enzyme and pathway databases

BioCycCCON360104:CCC13826_1807-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_CAMC1
AccessionPrimary (citable) accession number: A7ZB08
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 23, 2007
Last modified: January 25, 2012
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