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Reviewed, UniProtKB/Swiss-Prot Q6FYQ7 (GLMM_BARQU)

Last modified November 3, 2009. Version 35. 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: BQ11740
OrganismBartonella quintana (Rochalimaea quintana) [Complete proteome] [HAMAP]
Taxonomic identifier803 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length459 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 – 459459Phosphoglucosamine mutase HAMAP MF_01554
PRO_0000147849

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
Q6FYQ7-1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: F2D519773F534588

FASTA45949,802
        10         20         30         40         50         60 
MAQKYFGTDG IRGKANVFPM TPDFAMKVGM AVGVLFRSQR QSRRVVIGKD TRLSGYMLEN 

        70         80         90        100        110        120 
ALVSGFTAAG MEAFLLGPVP TPAVAMLCRS LRADLGVMIS ASHNPFYDNG IKLFGPDGFK 

       130        140        150        160        170        180 
LSDEIEKKIE QLIDTDLSKS LASCAEIGYA KRVEGDIYRY IEYAKRTLPR DVRLDALRIV 

       190        200        210        220        230        240 
VDCANGAAYK AAPRALWELG AEVFAINDAP NGTNINQKCG STDLASLKQK VHEVRADVGI 

       250        260        270        280        290        300 
ALDGDGDRVL IVDEKAQTVD GDQLIAVIAE HWHKTGRLQG NGVVTTIMSN LGLERFLNRK 

       310        320        330        340        350        360 
GLELVRTNVG DRYVVDAMRQ KGYNIGGEAS GHIVLSDFGT TGDGLVAALQ ILACMQESQS 

       370        380        390        400        410        420 
SMSHLCKRFE PVPQILKNVT IKNKNVLKKN QVKTAIDQAT QRLGNEARLV IRASGTEPVI 

       430        440        450 
RIMGEGDERE VLDAVVAEMV DVIAHHDALS KVGASLEGS 

« Hide

References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Toulouse.

Cross-references

Sequence databases

BX897700 Genomic DNA. Translation: CAF26633.1.
RefSeqYP_032707.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2866668.
GenomeReviewsGene locus BQ11740 in contig BX897700_GR.
KEGGbqu:BQ11740.
NMPDRfig|283165.1.peg.977.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ6FYQ7.
OMAVHDRYIE.

Enzyme and pathway databases

BioCycBQUI283165:BQ11740-MON.
BRENDA5.4.2.10. 292235.

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. 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_BARQU
AccessionPrimary (citable) accession number: Q6FYQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 19, 2004
Last modified: November 3, 2009
This is version 35 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