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A2SF93 (GLMM_METPP) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 39. 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:Mpe_A1270
OrganismMethylibium petroleiphilum (strain PM1) [Complete proteome] [HAMAP]
Taxonomic identifier420662 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesMethylibium

Protein attributes

Sequence length457 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 – 457457Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000301337

Sites

Active site1061Phosphoserine intermediate By similarity
Metal binding1061Magnesium; via phosphate group By similarity
Metal binding2451Magnesium By similarity
Metal binding2471Magnesium By similarity
Metal binding2491Magnesium By similarity

Amino acid modifications

Modified residue1061Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A2SF93 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: 7D2E75174F8E010B

FASTA45748,254
        10         20         30         40         50         60 
MSRTYFGTDG IRGAVGQAPI TPDFVLRLGH AVGRVLKSQQ TSPASRPTVL IGKDTRISGY 

        70         80         90        100        110        120 
MLESALEAGF ASAGVDVLLT GPLPTPGVAY LTRALRLSLG VVISASHNPY GDNGIKFFSA 

       130        140        150        160        170        180 
KGEKLPDSWE QQVEATVEEA AQWVDSSGLG KARRLDDAQG RYIEFCKSTV AGELSLKGLK 

       190        200        210        220        230        240 
LVVDGAHGAA YQVAPAVFHE LGAEVISIGC NPNGLNINDG FGATHPEALV SAVQAHQADY 

       250        260        270        280        290        300 
GIALDGDADR LQLVDATGRL YNGDELLYLM TLDRLAAEPS EDAAPSRVGV PGVVGTLMTN 

       310        320        330        340        350        360 
LAVEQALAAR GVAFVRAKVG DRYVLEELLA RGWQLGGEGS GHLIALDKHT TGDGLVSALQ 

       370        380        390        400        410        420 
VLQAVVRSGR TLAQLLEGLT LFPQVLLNVR LQPGQDWKAS AALAEAQRES LAELGERGRI 

       430        440        450 
LIRPSGTEPL LRVMVEASDA ALAQRCAQRM ADAVRRA 

« Hide

References

[1]"Whole-genome analysis of the methyl tert-butyl ether-degrading beta-proteobacterium Methylibium petroleiphilum PM1."
Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., Hristova K.R.
J. Bacteriol. 189:1931-1945(2007) [PubMed: 17158667] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PM1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000555 Genomic DNA. Translation: ABM94232.1.
RefSeqYP_001020467.1. NC_008825.1.

3D structure databases

ProteinModelPortalA2SF93.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2SF93.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4785847.
GenomeReviewsGene locus Mpe_A1270 in contig CP000555_GR.
KEGGmpt:Mpe_A1270.
NMPDRfig|279263.3.peg.1595.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAPLEDIQV.
PhylomeDBA2SF93.
ProtClustDBPRK10887.

Enzyme and pathway databases

BioCycMPET420662:MPE_A1270-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_METPP
AccessionPrimary (citable) accession number: A2SF93
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: March 6, 2007
Last modified: November 16, 2011
This is version 39 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