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A4WQ91 (GLMM_RHOS5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 36. 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:Rsph17025_0649
OrganismRhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) [Complete proteome] [HAMAP]
Taxonomic identifier349102 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length447 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 – 447447Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_1000068913

Sites

Active site1031Phosphoserine intermediate By similarity
Metal binding1031Magnesium; via phosphate group By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity
Metal binding2461Magnesium By similarity

Amino acid modifications

Modified residue1031Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4WQ91 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 5BFAE861E86C0E44

FASTA44747,718
        10         20         30         40         50         60 
MTRKLFGTDG VRGRANSYPM TAEVALRLGA AAGRYFRPVG AGSPRVVIGK DTRLSGYMLE 

        70         80         90        100        110        120 
NALTAGLTST GMNVLLLGPV PTPAVGFLTR SMRADLGVMI SASHNPHEDN GIKFFGPDGF 

       130        140        150        160        170        180 
KLSDEAEAEI EAILAGEIQP AQPGNIGRAK RIDDGRGRYQ EYCKTTFPAG LRLDGLKVVI 

       190        200        210        220        230        240 
DCANGAAYRA APEVLWELGA EVIPLGVEPD GKNINLRCGS THPEAAAEAV RAHGADVGIC 

       250        260        270        280        290        300 
LDGDADRVII LDEQGRQADG DQIMALFAAR WAEEGRLRDA TLVATVMSNL GLERFLSARG 

       310        320        330        340        350        360 
LRLERTPVGD RYVVEAMRRG GWNLGGEQSG HIVMTDFATT GDGLLAGLQF LAAMAQTGRK 

       370        380        390        400        410        420 
ASELSRSFET VPQLLQNVRY AAGQEPLTAP SVQAVIREAE VRLNGSGRLL IRKSGTEPLI 

       430        440 
RVMAECEDEA LLRDVVEEIV AAVKDAA 

« Hide

References

[1]"Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17025 / ATH 2.4.3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000661 Genomic DNA. Translation: ABP69555.1.
RefSeqYP_001166860.1. NC_009428.1.

3D structure databases

ProteinModelPortalA4WQ91.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4WQ91.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5082993.
GenomeReviewsGene locus Rsph17025_0649 in contig CP000661_GR.
KEGGrsq:Rsph17025_0649.
PATRIC23159441. VBIRhoSph94549_0659.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAIGSAKRI.
PhylomeDBA4WQ91.
ProtClustDBPRK14315.

Enzyme and pathway databases

BioCycRSPH349102:RSPH17025_0649-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_RHOS5
AccessionPrimary (citable) accession number: A4WQ91
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 29, 2007
Last modified: January 25, 2012
This is version 36 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