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Reviewed, UniProtKB/Swiss-Prot Q7WMD0 (GLMM_BORBR)

Last modified February 9, 2010. Version 39. 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: BB1462
OrganismBordetella bronchiseptica (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]
Taxonomic identifier518 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

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

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP MF_01554

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01554

Post-translational modification

Activated by phosphorylation By similarity. HAMAP MF_01554

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 – 452452Phosphoglucosamine mutase HAMAP MF_01554
PRO_0000147854

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
Q7WMD0-1 [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
BX640441 Genomic DNA. Translation: CAE31959.1.
RefSeqNP_888007.1.

3D structure databases

SMRQ7WMD0. Positions 4-444.
ModBaseSearch...

Genome annotation databases

GeneID2663878.
KEGGbbr:BB1462.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG644964.
OMASTHPEAM.
PhylomeDBQ7WMD0.

Enzyme and pathway databases

BioCycBBRO257310:BB1462-MONOMER.
BRENDA5.4.2.10. 413.

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. 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_BORBR
AccessionPrimary (citable) accession number: Q7WMD0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 1, 2003
Last modified: February 9, 2010
This is version 39 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