Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q0HWV8 (GLMM2_SHESR)

Last modified November 3, 2009. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphoglucosamine mutase 2
    EC=5.4.2.10
Gene names
Name: glmM2
Ordered Locus Names: Shewmr7_1398
OrganismShewanella sp. (strain MR-7) [Complete proteome] [HAMAP]
Taxonomic identifier60481 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate By similarity.

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP 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: UniProtKB-KW

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 450450Phosphoglucosamine mutase 2 HAMAP MF_01554
PRO_0000305678

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
Q0HWV8-1 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: CC05BCA27B679295

FASTA45047,824
        10         20         30         40         50         60 
MSRKYFGTDG VRGKVGTFPI TPDFAMKLGW AAGTVLASTG TKEVLIGKDT RISGYMLESA 

        70         80         90        100        110        120 
MEAGFSAAGV NVALIGPMPT PAVAYLASTF RADAGVVISA SHNPFYDNGI KFFSNTGTKL 

       130        140        150        160        170        180 
NDAQELEIEA LLEQALEHNA LQCVASEKLG KVRRIDDAAG RYIEFCKGTF PNHLSLAGLK 

       190        200        210        220        230        240 
IVVDSAHGAA YHIAPNVYRE LGAEVISIND KPNGVNINDH CGATHLDSLQ SAVMIHEADL 

       250        260        270        280        290        300 
GIALDGDADR VMFVDHNGHV VDGDEILFIL AQAAYQKGEM QGGVVGTLMS NLGLELALKQ 

       310        320        330        340        350        360 
MGIPFLRAKV GDRYVVEQLK ETGWQLGGEG SGHILSLQHA STGDGIVASL QVLKAILESG 

       370        380        390        400        410        420 
KRLAELKAGM TKLPQVLINV RLTSGSADSI LSKDSVKQAV ITAEEVLGNQ GRVLLRKSGT 

       430        440        450 
EPLIRVMVES TDISLTQQQA EYIAQAVKVA 

« Hide

References

[1]"Complete sequence of chromosome 1 of Shewanella sp. MR-7."
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., Kiss H., 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., Nealson K., Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000444 Genomic DNA. Translation: ABI42397.1.
RefSeqYP_737454.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ0HWV8.

Genome annotation databases

GeneID4258567.
GenomeReviewsGene locus Shewmr7_1398 in contig CP000444_GR.
KEGGshm:Shewmr7_1398.
NMPDRfig|60481.10.peg.1330.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ0HWV8.
OMANTIPEDL.

Family and domain databases

HAMAPMF_01554.
[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. A-D-PHexomutase_N.
IPR006352. GlmM.
[Graphical view]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
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.
TIGRFAMsTIGR01455. glmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM2_SHESR
AccessionPrimary (citable) accession number: Q0HWV8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 3, 2006
Last modified: November 3, 2009
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents