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A9HB20 (GLMM_GLUDA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. 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:GDI0812, Gdia_1205
OrganismGluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5) [Complete proteome] [HAMAP]
Taxonomic identifier272568 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconacetobacter

Protein attributes

Sequence length452 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 – 452452Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_1000201105

Sites

Active site1041Phosphoserine intermediate By similarity
Metal binding1041Magnesium; via phosphate group By similarity
Metal binding2451Magnesium By similarity
Metal binding2471Magnesium By similarity
Metal binding2491Magnesium By similarity

Amino acid modifications

Modified residue1041Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A9HB20 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 8E5A0D0D63B31511

FASTA45248,393
        10         20         30         40         50         60 
MSKTRHLFGT DGIRGLANQD PMTVEIAQKL GQAAGLRFTR GVHRHRVLLG KDTRLSGYMI 

        70         80         90        100        110        120 
ECALVSGFLS AGMDVTLVGP MPTPAIAMLT RSLRADLGVM ISASHNPFGD NGIKLFGPDG 

       130        140        150        160        170        180 
FKLSDETEAE IEELMRSDLA GRLAAPDRIG RASRLNDAAG RYIENAKASF PRGRRLDGLR 

       190        200        210        220        230        240 
IVIDCANGAA YRVAPTALWE LGAEVIRIGC EPDGININEQ CGSTKPESLC EAVVAHGAHI 

       250        260        270        280        290        300 
GIALDGDADR VLIADEKGRL IDGDQILALI ARSWGRQGRL NSAQIVATVM SNMGLARCLE 

       310        320        330        340        350        360 
GLGLELVRTA VGDRYVVERM RELGANLGGE QSGHMVLSDF ATTGDGLVAA LQVLAVLVEE 

       370        380        390        400        410        420 
GRPASEVCRM FTPFPQMLRN VRFTGKSPLH APSVQDARRR AEAELGTAGR LLLRESGTEP 

       430        440        450 
LVRVMAEAED PALVERIVAE MCEAIDSAQV VA 

« Hide

References

[1]"Gluconacetobacter diazotrophicus Pal5 complete genome."
Bertalan M., Baldani I.J., Ferreira P.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49037 / DSM 5601 / PAl5.
[2]"Complete sequence of chromosome of Gluconacetobacter diazotrophicus PAl 5."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Triplett E.W.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49037 / DSM 5601 / PAl5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001189 Genomic DNA. Translation: ACI50988.1.
AM889285 Genomic DNA. Translation: CAP54755.1.
RefSeqYP_001601093.1. NC_010125.1.
YP_002275603.1. NC_011365.1.

3D structure databases

ProteinModelPortalA9HB20.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9HB20.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5789498.
6974609.
GenomeReviewsGene locus GDI0812 in contig AM889285_GR.
Gene locus Gdia_1205 in contig CP001189_GR.
KEGGgdi:GDI_0812.
gdj:Gdia_1205.
PATRIC22050778. VBIGluDia203729_1195.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG644964.
OMALENTIPE.
ProtClustDBPRK14315.

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_GLUDA
AccessionPrimary (citable) accession number: A9HB20
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 5, 2008
Last modified: January 25, 2012
This is version 37 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