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Reviewed, UniProtKB/Swiss-Prot A5VS47 (GLMM_BRUO2)

Last modified November 3, 2009. Version 19. 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: BOV_1634
OrganismBrucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512) [Complete proteome] [HAMAP]
Taxonomic identifier444178 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length451 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 – 451451Phosphoglucosamine mutase HAMAP MF_01554
PRO_0000305634

Sites

Active site1021Phosphoserine intermediate By similarity
Metal binding1021Magnesium; via phosphate group By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity
Metal binding2471Magnesium By similarity

Amino acid modifications

Modified residue1021Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5VS47-1 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: ADA445AE3D805CD5

FASTA45148,569
        10         20         30         40         50         60 
MTRKFFGTDG IRGQANSFPM TPEIAMKVGM AVGYIFRRKG QASRVVIGKD TRRSGYMLEN 

        70         80         90        100        110        120 
ALVAGFTAAG MDVFLLGPIP TPAVAMLCRS LRADIGVMIS ASHNPFYDNG IKLFGPDGFK 

       130        140        150        160        170        180 
LSDQIELQIE AMIEGDMTPF LASHGDVGRA KRVDGDIYRY IEFAKRTLPR NISLNGLRVV 

       190        200        210        220        230        240 
VDCANGAGYK VAPAALWELG AEVITINNEP NGININEDCG STHPIGLMKK VHEVRADVGI 

       250        260        270        280        290        300 
ALDGDADRVL LVDENGTVID GDQLMAVIAE SWAASNRLEG GGIVATVMSN LGLERFLADR 

       310        320        330        340        350        360 
NLTLARTKVG DRYVVEHMRE HGFNVGGEQS GHIVLSDFAT TGDGLISALQ ILAVAQEQNK 

       370        380        390        400        410        420 
PISDVCRKFQ PVPQLLKNVR TTGGKPLENK RVKSAIDEAK ERLGGQGRLV IRPSGTEPLI 

       430        440        450 
RVMAEGDDRG LVEKVVNDII DVISSESSAA A 

« Hide

References

[1]Paulsen I.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000708 Genomic DNA. Translation: ABQ60403.1.
RefSeqYP_001259544.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5202053.
GenomeReviewsGene locus BOV_1634 in contig CP000708_GR.
KEGGbov:BOV_1634.
TIGRBOV_1634.

Phylogenomic databases

OMAVHDRYIE.

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. 1 hit.
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_BRUO2
AccessionPrimary (citable) accession number: A5VS47
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: July 10, 2007
Last modified: November 3, 2009
This is version 19 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