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A3QGV0 (GLMM_SHELP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. 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:Shew_2832
OrganismShewanella loihica (strain ATCC BAA-1088 / PV-4) [Complete proteome] [HAMAP]
Taxonomic identifier323850 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

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-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 – 443443Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_0000305674

Sites

Active site1001Phosphoserine intermediate By similarity
Metal binding1001Magnesium; via phosphate group By similarity
Metal binding2391Magnesium By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity

Amino acid modifications

Modified residue1001Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A3QGV0 [UniParc].

Last modified April 17, 2007. Version 1.
Checksum: C8A1F5A8D8B5141E

FASTA44347,703
        10         20         30         40         50         60 
MRKFFGTDGI RGKVGAGKMT PELALKLGWA AGRVLSRTGT KKVIIGKDTR ISGYLFESAM 

        70         80         90        100        110        120 
EAGLSAAGLN VMLMGPMPTP AVAYLTRTFR AEAGVVISAS HNPYYDNGIK FFSTDGSKLD 

       130        140        150        160        170        180 
DEVELEIERE LEKPLECVES HLLGKVSRIE DAAGRYIEYC KGNFPAEHTL NGLKIVVDCA 

       190        200        210        220        230        240 
HGATYHIAPS VFRELGAEVI TIGDKPDGIN INHEVGATSM GKIRETVIAE KADLGIALDG 

       250        260        270        280        290        300 
DGDRIMMVNR HGKVIDGDEI LYILACDAQD RGVLKGGVVG TLMSNLGLDL ALKARDIPFA 

       310        320        330        340        350        360 
RSKVGDRYVM ELLKEKDWRI GGENSGHILN LDHGTTGDGI VAGILVLAAM CRKQATLEEL 

       370        380        390        400        410        420 
TEGIKMLPQV LVNVRFEGTH NPLEADSVLS AQAEVEAKLG ERGRVLLRKS GTEPLIRVMV 

       430        440 
EGDVASDVKA HANYIAEAIK ALV 

« Hide

References

[1]"Complete sequence of Shewanella loihica PV-4."
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G., Fredrickson J., Tiedje J., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1088 / PV-4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000606 Genomic DNA. Translation: ABO24698.1.
RefSeqYP_001094957.1. NC_009092.1.

3D structure databases

ProteinModelPortalA3QGV0.
ModBaseSearch...

Protein-protein interaction databases

STRING323850.Shew_2832.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO24698; ABO24698; Shew_2832.
GeneID4922339.
KEGGslo:Shew_2832.
PATRIC23517557. VBISheLoi132094_2831.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMATLMSNMS.
ProtClustDBPRK10887.

Enzyme and pathway databases

BioCycSLOI323850:GHQJ-2924-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_SHELP
AccessionPrimary (citable) accession number: A3QGV0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: April 17, 2007
Last modified: May 29, 2013
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