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Q129M7 (GLMM_POLSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. 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:Bpro_2850
OrganismPolaromonas sp. (strain JS666 / ATCC BAA-500) [Complete proteome] [HAMAP]
Taxonomic identifier296591 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaePolaromonas

Protein attributes

Sequence length443 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 – 443443Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000301354

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
Q129M7 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 52ECE925D412CAD4

FASTA44347,470
        10         20         30         40         50         60 
MTRKYFGTDG IRGTVGQPPI TPDFVLRLAH AVGRVLRRVE SRPTVLIGKD TRISGYMLES 

        70         80         90        100        110        120 
ALESGFNSAG VDVVLLGPLP TPGVAYLTRA QRASLGVVIS ASHNAYPDNG IKFFSAQGTK 

       130        140        150        160        170        180 
LSDEWELAVE AALEEPPVWV DSATLGKARR LDDAAGRYIE FCKSTFAHDL TLKGLKIVVD 

       190        200        210        220        230        240 
GAHGAAYHIA PKVFHELGAE VIAIGCAPDG LNINHEVGAT HPEALITAVK ANQADYGIAL 

       250        260        270        280        290        300 
DGDADRLQMV DADGRLFNGD EVLFLMVSER LARGEKVPGT VGTLMTNMAV ELALKSRGVE 

       310        320        330        340        350        360 
FVRAKVGDRY VLEELEKRGW LLGGEGSGHL LALDKHTTGD GLISALQVLQ ACVRSGKTIA 

       370        380        390        400        410        420 
QLLGDVVLFP QTLVNVRLKP GQDWKASEKL ALETKAVEAE LGDTGRLLIR ASGTEPLLRV 

       430        440 
MVEARDARQA KACAERVADT VRS 

« Hide

References

[1]"Complete sequence of chromosome of Polaromonas sp. JS666."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Munk A.C., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JS666 / ATCC BAA-500.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000316 Genomic DNA. Translation: ABE44765.1.
RefSeqYP_549663.1. NC_007948.1.

3D structure databases

ProteinModelPortalQ129M7.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ129M7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4014500.
GenomeReviewsGene locus Bpro_2850 in contig CP000316_GR.
KEGGpol:Bpro_2850.
NMPDRfig|296591.1.peg.5441.
PATRIC22958868. VBIPolSp102244_2894.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAPLEDIQV.
PhylomeDBQ129M7.
ProtClustDBPRK10887.

Enzyme and pathway databases

BioCycPSP296591:BPRO_2850-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.
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. 3 hits.
TIGRFAMsTIGR01455. GlmM. 1 hit.
PROSITEPS00710. PGM_PMM. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_POLSJ
AccessionPrimary (citable) accession number: Q129M7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: August 22, 2006
Last modified: January 25, 2012
This is version 45 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