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Q7W8R3 (GLMM_BORPA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. 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:BPP2069
OrganismBordetella parapertussis [Complete proteome] [HAMAP]
Taxonomic identifier519 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

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_0000147855

Sites

Active site1121Phosphoserine intermediate By similarity
Metal binding1121Magnesium; via phosphate group By similarity
Metal binding2511Magnesium By similarity
Metal binding2531Magnesium By similarity
Metal binding2551Magnesium By similarity

Amino acid modifications

Modified residue1121Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7W8R3 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 223B0A42E412CD42

FASTA45248,300
        10         20         30         40         50         60 
MSQRKYFGTD GVRGEVGGPV INAAFALRLG YAAGRVLARE HREHASGRGR NRPQVVIGKD 

        70         80         90        100        110        120 
TRISGYMLES ALEAGLSAAG IDVLLAGPVP TPAVAYLTRT LRLAAGIVIS ASHNPYQDNG 

       130        140        150        160        170        180 
IKFFSAHGMK LPDDIEAAIE QALDEPLGCV GSEELGRARR MADAQGRYIE FCKSTFPHDL 

       190        200        210        220        230        240 
DLNGLKLVVD AAHGAAYNVA PHVFRELGAE VHAIGVSPDG FNINKGVGAL HPESLAEEVR 

       250        260        270        280        290        300 
ARGADLGIAL DGDADRLQMV DGTGRIYNGD ELLYAIVRER MQRGPVAGVV GTLMTNYGLE 

       310        320        330        340        350        360 
RQLQQIGVGF ERANVGDRYV LEQMQARGWL YGGESSGHLL CLDCHTTGDG TIAALQVLTA 

       370        380        390        400        410        420 
LRRADATLAE WVADLRMYPQ KMINVPLAPG LDWKTHDGLA RARGAVEAEL AGRGRVLIRA 

       430        440        450 
SGTEPKLRLM VEAEDEALAQ ASAQKLADSL GA

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX640429 Genomic DNA. Translation: CAE37369.1.
RefSeqNP_884327.1. NC_002928.3.

3D structure databases

ProteinModelPortalQ7W8R3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1666808.
GenomeReviewsGene locus BPP2069 in contig BX470249_GR.
KEGGbpa:BPP2069.
PATRIC21147957. VBIBorPar43418_2175.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG644964.
OMAPLEDIQV.
PhylomeDBQ7W8R3.
ProtClustDBPRK10887.

Enzyme and pathway databases

BioCycBPAR257311:BPP2069-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_BORPA
AccessionPrimary (citable) accession number: Q7W8R3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 50 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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