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A1VQI3 (GLMM_POLNA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. 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:Pnap_2609
OrganismPolaromonas naphthalenivorans (strain CJ2) [Complete proteome] [HAMAP]
Taxonomic identifier365044 [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_0000301353

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
A1VQI3 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: EFABE6A480DEA79D

FASTA44347,567
        10         20         30         40         50         60 
MNRKYFGTDG IRGTVGEAPI TPDFVLRLAH AVGRVLRRTE ARPTVLIGKD TRISGYMLES 

        70         80         90        100        110        120 
ALESGFNSAG VDVVLLGPLP TPGVAYLTRA QRASLGVVIS ASHNPFADNG IKFFSAQGNK 

       130        140        150        160        170        180 
LNDEWEFEVE ATLKEEPVWA DSASLGKTRR LDDAAGRYIE FCKSTFAHDL TLKGLKIVVD 

       190        200        210        220        230        240 
GAHGAAYQIA PMVFHELGAE VIAIGCAPDG LNINDGVGAT HPQALVNAVL ANKADYGIAL 

       250        260        270        280        290        300 
DGDADRLQMV DAQGRLFNGD EVLYLMVNER LSRGEKVPGT VGTLMTNMAV EVALKAKGVE 

       310        320        330        340        350        360 
FVRAKVGDRY ILEELERRGW LLGGEGSGHM LALDKHTTGD GLISALQVLQ ACARSNQTLA 

       370        380        390        400        410        420 
QLLSEVVLFP QTLINVRLKP GQDWKNSAEL AAQTKAAEIE LGDSGRILIR ASGTEPLLRV 

       430        440 
MVEARDAEQA RACAERVADA VRS 

« Hide

References

[1]"Complete sequence of chromosome 1 of Polaromonas naphthalenivorans CJ2."
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., Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Madsen E.L., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CJ2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000529 Genomic DNA. Translation: ABM37911.1.
RefSeqYP_982832.1. NC_008781.1.

3D structure databases

ProteinModelPortalA1VQI3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1VQI3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4690087.
GenomeReviewsGene locus Pnap_2609 in contig CP000529_GR.
KEGGpna:Pnap_2609.
PATRIC22949887. VBIPolNap76733_3476.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAESTDNIM.
PhylomeDBA1VQI3.
ProtClustDBPRK10887.

Enzyme and pathway databases

BioCycPNAP365044:PNAP_2609-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. 3 hits.
TIGRFAMsTIGR01455. GlmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_POLNA
AccessionPrimary (citable) accession number: A1VQI3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: February 6, 2007
Last modified: December 14, 2011
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