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B1XGY6 (GLMM_ECODH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 38. 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:ECDH10B_3350
OrganismEscherichia coli (strain K12 / DH10B) [Complete proteome] [HAMAP]
Taxonomic identifier316385 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length445 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 – 445445Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_1000201090

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
B1XGY6 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: ECDF9A0378A980EC

FASTA44547,544
        10         20         30         40         50         60 
MSNRKYFGTD GIRGRVGDAP ITPDFVLKLG WAAGKVLARH GSRKIIIGKD TRISGYMLES 

        70         80         90        100        110        120 
ALEAGLAAAG LSALFTGPMP TPAVAYLTRT FRAEAGIVIS ASHNPFYDNG IKFFSIDGTK 

       130        140        150        160        170        180 
LPDAVEEAIE AEMEKEISCV DSAELGKASR IVDAAGRYIE FCKATFPNEL SLSELKIVVD 

       190        200        210        220        230        240 
CANGATYHIA PNVLRELGAN VIAIGCEPNG VNINAEVGAT DVRALQARVL AEKADLGIAF 

       250        260        270        280        290        300 
DGDGDRVIMV DHEGNKVDGD QIMYIIAREG LRQGQLRGGA VGTLMSNMGL ELALKQLGIP 

       310        320        330        340        350        360 
FARAKVGDRY VLEKMQEKGW RIGAENSGHV ILLDKTTTGD GIVAGLQVLA AMARNHMSLH 

       370        380        390        400        410        420 
DLCSGMKMFP QILVNVRYTA GSGDPLEHES VKAVTAEVEA ALGNRGRVLL RKSGTEPLIR 

       430        440 
VMVEGEDEAQ VTEFAHRIAD AVKAV 

« Hide

References

[1]"The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse."
Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B., Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B., Posfai G., Weinstock G.M., Blattner F.R.
J. Bacteriol. 190:2597-2606(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / DH10B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000948 Genomic DNA. Translation: ACB04253.1.
RefSeqYP_001732031.1. NC_010473.1.

3D structure databases

ProteinModelPortalB1XGY6.
SMRB1XGY6. Positions 5-444.
ModBaseSearch...

Protein-protein interaction databases

STRING316385.ECDH10B_3350.

Proteomic databases

PRIDEB1XGY6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB04253; ACB04253; ECDH10B_3350.
GeneID6059875.
KEGGecd:ECDH10B_3350.
PATRIC18466625. VBIEscCol59506_3373.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMAKVIAIGC.
ProtClustDBPRK10887.

Enzyme and pathway databases

BioCycECOL316385:GJ8B-3212-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_ECODH
AccessionPrimary (citable) accession number: B1XGY6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 20, 2008
Last modified: May 1, 2013
This is version 38 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