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A1S7U2 (GLMM2_SHEAM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 48. 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 2

EC=5.4.2.10
Gene names
Name:glmM2
Ordered Locus Names:Sama_2243
OrganismShewanella amazonensis (strain ATCC BAA-1098 / SB2B) [Complete proteome] [HAMAP]
Taxonomic identifier326297 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length452 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 – 452452Phosphoglucosamine mutase 2 HAMAP-Rule MF_01554
PRO_0000305671

Sites

Active site1011Phosphoserine intermediate By similarity
Metal binding1011Magnesium; via phosphate group By similarity
Metal binding2451Magnesium By similarity
Metal binding2471Magnesium By similarity
Metal binding2491Magnesium By similarity

Amino acid modifications

Modified residue1011Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1S7U2 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 2F928340908292D2

FASTA45247,825
        10         20         30         40         50         60 
MSRKYFGTDG VRGKVGEFPI TPDFAMKLGW AAGTVMAASG TKEVIIGKDT RLSGYMLESA 

        70         80         90        100        110        120 
MEAGFCAAGV NVALTGPLPT PAIAYLTSTF RADAGVVISA SHNPYYDNGI KFFSNTGTKL 

       130        140        150        160        170        180 
TDEQELEIER LLVSAIEGGA MTCVASDKLG KVRRINDAAG RYIEFCKGTF PNSLSLTGLK 

       190        200        210        220        230        240 
IVVDSAHGAA YHIAKNVYRE LGAEVISIND KPDGININEH CGATHMDSLQ TAVMIHEADL 

       250        260        270        280        290        300 
GIALDGDADR LMMVDSKGQV IDGDALLYLL AKSAQQRGEQ VSGVIGTLMS NLGFEQALAN 

       310        320        330        340        350        360 
LGIPFKRAKV GDRYVVELLK ETGWRLGGEN SGHLLMLDFT TTGDAIVASL QVLRALLESG 

       370        380        390        400        410        420 
AGLADAITEL NMFPQVLINV RLNGNAAVGL SHPSVSDAVA TAESALGNDG RVLLRKSGTE 

       430        440        450 
PLIRVMVEAK DAVKANQYAE LIADAVRAVF PA 

« Hide

References

[1]"Complete sequence of Shewanella amazonensis SB2B."
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., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1098 / SB2B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000507 Genomic DNA. Translation: ABM00449.1.
RefSeqYP_928118.1. NC_008700.1.

3D structure databases

ProteinModelPortalA1S7U2.
ModBaseSearch...

Protein-protein interaction databases

STRING326297.Sama_2243.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM00449; ABM00449; Sama_2243.
GeneID4604493.
KEGGsaz:Sama_2243.
PATRIC23453291. VBISheAma74963_2314.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMATAVMIHE.
ProtClustDBCLSK2516801.

Enzyme and pathway databases

BioCycSAMA326297:GH0T-2373-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 nameGLMM2_SHEAM
AccessionPrimary (citable) accession number: A1S7U2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: February 6, 2007
Last modified: May 1, 2013
This is version 48 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