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Q8ETM7 (GLMM_OCEIH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. 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:OB0232
OrganismOceanobacillus iheyensis (strain DSM 14371 / JCM 11309 / KCTC 3954 / HTE831) [Complete proteome] [HAMAP]
Taxonomic identifier221109 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeOceanobacillus

Protein attributes

Sequence length446 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 – 446446Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000147927

Sites

Active site1001Phosphoserine intermediate By similarity
Metal binding1001Magnesium; via phosphate group By similarity
Metal binding2391Magnesium By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity

Amino acid modifications

Modified residue1001Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8ETM7 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 0A2236E82F45DA95

FASTA44648,293
        10         20         30         40         50         60 
MGKFFGTDGV RGVANEGLTP ELAFKLGRFG GYVLTKDSER PRILIGRDTR VSGHMLEGAL 

        70         80         90        100        110        120 
LAGLLSIGAE VMRLGVISTP GVAYLTKATS AQAGVMISAS HNPVEDNGIK FFGPDGFKLT 

       130        140        150        160        170        180 
DAQENEIESL MEGEDNLPRP TGADIGVVND YFEGGQKYLS YLKDTIDNDF EGIHIAIDCA 

       190        200        210        220        230        240 
NGATSSLATH LFADLEADIY SIGSSPDGLN INDGFGSTHP EKLQEFVVEK NADIGLAFDG 

       250        260        270        280        290        300 
DGDRLIAVDE KGNLVDGDKI MFICAKYMHE IGMLRKDTVV STVMSNLGFY KALENIGLNS 

       310        320        330        340        350        360 
NKTSVGDRYV MEEMRQNGYN LGGEQSGHII FLDYITTGDG MLSAIQLVNV MRETGKPLSE 

       370        380        390        400        410        420 
LADEMVVFPQ VLKNVRVMDK NQALSSSVLL DEVDAVEKEL GEDGRVLVRP SGTEPLVRVM 

       430        440 
VEAKTKEECE QYADRIVSVI EQHLGA 

« Hide

References

[1]"Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments."
Takami H., Takaki Y., Uchiyama I.
Nucleic Acids Res. 30:3927-3935(2002) [PubMed: 12235376] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 14371 / JCM 11309 / KCTC 3954 / HTE831.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000028 Genomic DNA. Translation: BAC12188.1.
RefSeqNP_691153.1. NC_004193.1.

3D structure databases

ProteinModelPortalQ8ETM7.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1015394.
GenomeReviewsGene locus OB0232 in contig BA000028_GR.
KEGGoih:OB0232.
NMPDRfig|221109.1.peg.233.
PATRIC22791371. VBIOceIhe82024_0239.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG644964.
OMAPLEDIQV.
PhylomeDBQ8ETM7.

Enzyme and pathway databases

BioCycOIHE221109:OB0232-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_OCEIH
AccessionPrimary (citable) accession number: Q8ETM7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 56 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