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A6WQD3 (GLMM2_SHEB8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. 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:Shew185_2888
OrganismShewanella baltica (strain OS185) [Complete proteome] [HAMAP]
Taxonomic identifier402882 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length450 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 – 450450Phosphoglucosamine mutase 2 HAMAP MF_01554_B
PRO_0000343598

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
A6WQD3 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 86220AB0613B8EEE

FASTA45047,851
        10         20         30         40         50         60 
MSRKYFGTDG VRGKVGEFPI TPDFAMKLGW AAGTVLASTG TKEVLIGKDT RSSGYMLESA 

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

       130        140        150        160        170        180 
NDAQELEIEA LLEKALNQNA MQCVASEKLG KVRRIDDAAG RYIEFCKGTF PNHLSLAGLK 

       190        200        210        220        230        240 
IVIDSAHGAA YHIAPNVYRE LGAEVISIND KPNGVNINDH CGATHLDSLQ TAVMVHEADL 

       250        260        270        280        290        300 
GIALDGDADR VMFVDHNGHV VDGDEILFIL AQAAHSKGEM TGGVVGTLMS NLGLELALKQ 

       310        320        330        340        350        360 
MDIPFVRAKV GDRYVVEQLK RTGWQLGGEG SGHILSLQHA STGDGIVASL QVLKAVLESQ 

       370        380        390        400        410        420 
KSLSEIKAGM TKLPQVLINV RLATADADSI LATTSVKQAV IKAEEFLGDQ GRVLLRKSGT 

       430        440        450 
EPLIRVMVES TDNIMTQTQA EYIADAVRAA 

« Hide

References

[1]"Complete sequence of chromosome of Shewanella baltica OS185."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Brettar I., Rodrigues J., Konstantinidis K., Tiedje J., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OS185.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000753 Genomic DNA. Translation: ABS09022.1.
RefSeqYP_001367085.1. NC_009665.1.

3D structure databases

ProteinModelPortalA6WQD3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6WQD3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5369563.
GenomeReviewsGene locus Shew185_2888 in contig CP000753_GR.
KEGGsbm:Shew185_2888.
PATRIC23462717. VBISheBal127872_3128.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAESTDNIM.
ProtClustDBCLSK2516801.

Enzyme and pathway databases

BioCycSBAL402882:SHEW185_2888-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 nameGLMM2_SHEB8
AccessionPrimary (citable) accession number: A6WQD3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: August 21, 2007
Last modified: January 25, 2012
This is version 31 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