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Reviewed, UniProtKB/Swiss-Prot B7GIY9 (GLMM_ANOFW)

Last modified July 28, 2009. Version 7. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphoglucosamine mutase
    EC=5.4.2.10
Gene names
Name: glmM
Ordered Locus Names: Aflv_0151
OrganismAnoxybacillus flavithermus (strain DSM 21510 / WK1) [Complete proteome] [HAMAP]
Taxonomic identifier491915 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeAnoxybacillus

Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate By similarity.

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP 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: UniProtKB-KW

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 447447Phosphoglucosamine mutase HAMAP MF_01554
PRO_1000201057

Sites

Active site1001Phosphoserine intermediate By similarity
Metal binding1001Magnesium; via phosphate group By similarity
Metal binding2401Magnesium By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity

Amino acid modifications

Modified residue1001Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
B7GIY9-1 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 7C5A04D02033D22C

FASTA44748,285
        10         20         30         40         50         60 
MGKYFGTDGV RGIANSELTP ELAFKIGRFG GYVLTKDKER PKVLIGRDTR ISGHMLEGAL 

        70         80         90        100        110        120 
VAGLLSIGAE VMRLGVISTP GVAYLTKALG AQAGVMISAS HNPVQDNGIK FFGPDGFKLS 

       130        140        150        160        170        180 
DEQELEIEAL LDSEQDTLPR PIGKDLGQVN DYFEGGQKYL QYLKQTVDED FSGIHVALDC 

       190        200        210        220        230        240 
AHGATSALAT HLFADLDADV STMGASPNGL NINDGVGSTH PEALAAFVKE KGADVGLAFD 

       250        260        270        280        290        300 
GDGDRLIAVD ENGQIVDGDQ IMYICAKYLN EQGRLKHQTV VSTVMSNLGF YKALEAQGIK 

       310        320        330        340        350        360 
SVQTAVGDRY VVEEMKKNGY NLGGEQSGHI IFLDYNTTGD GLLTALQLVN IMKVTKKPLS 

       370        380        390        400        410        420 
ELAGEMKKYP QKLVNVKVTD KQEAIANEEV QRVIREVEEE MAGNGRILVR PSGTEPLVRV 

       430        440 
MAEAPTNELC DQYVERIAAV IRERFGA 

« Hide

References

[1]"Encapsulated in silica: genome, proteome and physiology of the thermophilic bacterium Anoxybacillus flavithermus WK1."
Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A., Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V., Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.
Genome Biol. 9:RESEARCH161.1-RESEARCH161.16(2008) [PubMed: 19014707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000922 Genomic DNA. Translation: ACJ32535.1.
RefSeqYP_002314520.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID7036363.
GenomeReviewsGene locus Aflv_0151 in contig CP000922_GR.
KEGGafl:Aflv_0151.

Organism-specific databases

CMRSearch...

Family and domain databases

HAMAPMF_01554.
[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. A-D-PHexomutase_N.
IPR006352. GlmM.
[Graphical view]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
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.
TIGRFAMsTIGR01455. glmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_ANOFW
AccessionPrimary (citable) accession number: B7GIY9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: July 28, 2009
This is version 7 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents