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B0S2Q1 (GLMM_FINM2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 32. 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:FMG_1223
OrganismFinegoldia magna (strain ATCC 29328) (Peptostreptococcus magnus) [Complete proteome] [HAMAP]
Taxonomic identifier334413 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiales Family XI. Incertae Sedis › Finegoldia

Protein attributes

Sequence length449 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 – 449449Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_1000201100

Sites

Active site991Phosphoserine intermediate By similarity
Metal binding991Magnesium; via phosphate group By similarity
Metal binding2391Magnesium By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity

Amino acid modifications

Modified residue991Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
B0S2Q1 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 2D844D3B6E0E3523

FASTA44949,923
        10         20         30         40         50         60 
MGKYFGTDGI RGVAGEDLTV ELAYKLARAA CYKLKDVDNK LIVIGKDTRI SGDMLEAALI 

        70         80         90        100        110        120 
SGITSMGFDV YRLGVIPTPA VAYLTRFYNA CCGIVISASH NPYEFNGIKY FSNEGFKLKD 

       130        140        150        160        170        180 
SLEEEIEYLI DHQDEIDLKV TGEKVGRVYE EECARDTYIN YLLSRVDLDL TGVKVSLDCG 

       190        200        210        220        230        240 
YGATSEIAPI IFNRLNADVT VTNTEYDGKN INFKCGSTNP EVISNLVKIS ESDMGFSFDG 

       250        260        270        280        290        300 
DGDRLIACDE TGEIMDGDHV ICAVGHFLKE NNKLKNNAVV GTVMTNIGLI KSLKEIGVDV 

       310        320        330        340        350        360 
IKTQVGDRYV LEEMRKNGYI IGGEQSGHII FIEDNTTGDG ILSAIKLAEI AVKSKQKLSE 

       370        380        390        400        410        420 
MNNLMTSFPQ VLVNAKVNNE YKKVYKDDEV INQKIAELEH EFKDEGRVLI RPSGTEPLIR 

       430        440 
VMIEGENQEY LEKKAIELKD LIEERCELI

« Hide

References

[1]"Complete genome sequence of Finegoldia magna, an anaerobic opportunistic pathogen."
Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K., Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.
DNA Res. 15:39-47(2008) [PubMed: 18263572] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29328.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP008971 Genomic DNA. Translation: BAG08641.1.
RefSeqYP_001692531.1. NC_010376.1.

3D structure databases

ProteinModelPortalB0S2Q1.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0S2Q1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6020062.
GenomeReviewsGene locus FMG_1223 in contig AP008971_GR.
KEGGfma:FMG_1223.
PATRIC21888131. VBIFinMag33027_1426.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG644964.
OMAGVGSTHL.

Enzyme and pathway databases

BioCycFMAG334413:FMG_1223-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. 2 hits.
TIGRFAMsTIGR01455. GlmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_FINM2
AccessionPrimary (citable) accession number: B0S2Q1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 8, 2008
Last modified: January 25, 2012
This is version 32 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

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