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Q1H384 (GLMM_METFK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. 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:Mfla_0785
OrganismMethylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875) [Complete proteome] [HAMAP]
Taxonomic identifier265072 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaMethylophilalesMethylophilaceaeMethylobacillus

Protein attributes

Sequence length453 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 – 453453Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000301338

Sites

Active site1081Phosphoserine intermediate By similarity
Metal binding1081Magnesium; via phosphate group By similarity
Metal binding2471Magnesium By similarity
Metal binding2491Magnesium By similarity
Metal binding2511Magnesium By similarity

Amino acid modifications

Modified residue1081Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1H384 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: BC1A89917BE99A2D

FASTA45348,525
        10         20         30         40         50         60 
MSRKYFGTDG VRGKVGTFPI TPDFVMRLGY AAGRVLTRMD HHLVPGTKPL VIIGKDTRIS 

        70         80         90        100        110        120 
GYMFETALVS GLCAGGVNVR ITGPLPTPAI AHVTRAQRAQ AGIVISASHN PFDDNGIKFF 

       130        140        150        160        170        180 
SAQGTKLPDE VELAIEAELD QPMELVPTEQ IGRVKRIDDA AGRYIEFCKS TFPNALDLRG 

       190        200        210        220        230        240 
LKIVLDCANG ATYHVAPPVF HELGAEVISI GTQPNGLNIN LNVGSTHPES LQQAVVEHQA 

       250        260        270        280        290        300 
DLGIAFDGDG DRVVMADNQG QLLDGDQLLY IIASHRHQRG RLGGGVVGTL MTNLALEHAL 

       310        320        330        340        350        360 
GKEGIPFQRA KVGDRYVLEL LNANEWQLGG ENSGHILCLD KHSSGDGIIA ALQVLHALRA 

       370        380        390        400        410        420 
SGLSLADWAK RLPLYPQVLI NVKVAQRIDL DSNTALQAAV TSAEGALKGT GRVLLRASGT 

       430        440        450 
EPKIRVMVEG QDRPLVQRLA EEIAAVVQQE AAS 

« Hide

References

[1]"Complete sequence of Methylobacillus flagellatus KT."
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., Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KT / ATCC 51484 / DSM 6875.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000284 Genomic DNA. Translation: ABE49053.1.
RefSeqYP_544894.1. NC_007947.1.

3D structure databases

ProteinModelPortalQ1H384.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1H384.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4000641.
GenomeReviewsGene locus Mfla_0785 in contig CP000284_GR.
KEGGmfa:Mfla_0785.
NMPDRfig|265072.7.peg.788.
PATRIC32267159. VBIMetFla97085_0817.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAPLEDIQV.
PhylomeDBQ1H384.
ProtClustDBCLSK2529299.

Enzyme and pathway databases

BioCycMFLA265072:MFLA_0785-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 nameGLMM_METFK
AccessionPrimary (citable) accession number: Q1H384
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: June 27, 2006
Last modified: January 25, 2012
This is version 42 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