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Q6G5P7 (GLMM_BARHE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. 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:BH14740
OrganismBartonella henselae (strain ATCC 49882 / Houston 1) (Rochalimaea henselae) [Complete proteome] [HAMAP]
Taxonomic identifier283166 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length459 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 – 459459Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000147848

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
Q6G5P7 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 46B1FF13458E6247

FASTA45950,233
        10         20         30         40         50         60 
MPQKYFGTDG IRGKANVFPM TPDFAMKVGM AVGILFRSQN QSRRVVIGKD TRLSGYMLEN 

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

       130        140        150        160        170        180 
LSDEIEEKIE QLIDTDLSKS LASCAEIGYA KRVEGDIYRY IEYAKRTLPR DVRLDNLRIV 

       190        200        210        220        230        240 
VDCANGAAYK AAPRALWELG AEVFAINDTP NGTNINHKCG STDLASLKQK VHEVRADVGI 

       250        260        270        280        290        300 
ALDGDGDRVL LVDEKAQTVD GDQLIAVIAE HWHKNGRLQS KGVVTTIMSN LGLERFLNSK 

       310        320        330        340        350        360 
GLDLVRTKVG DRYVVDAMRK KGYNVGGEAS GHIVLSDFGT TGDGLVAALQ ILACMQEIQI 

       370        380        390        400        410        420 
PMSHLCQRFE PVPQIFKNVM IKNKNVLKKN PVKTAIEQAT QRLGKKARLV IRASGTEPVI 

       430        440        450 
RIMGEGDERE MLDAVVTEMV DIITHHDTLS KACASLERS 

« 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: ATCC 49882 / Houston 1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX897699 Genomic DNA. Translation: CAF28237.1.
RefSeqYP_034174.1. NC_005956.1.

3D structure databases

ProteinModelPortalQ6G5P7.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2866034.
GenomeReviewsGene locus BH14740 in contig BX897699_GR.
KEGGbhe:BH14740.
NMPDRfig|283166.1.peg.1302.
PATRIC20547160. VBIBarHen29080_1688.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG644964.
OMAGVGSTHL.
PhylomeDBQ6G5P7.
ProtClustDBPRK10887.

Enzyme and pathway databases

BioCycBHEN283166:BH14740-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_BARHE
AccessionPrimary (citable) accession number: Q6G5P7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 19, 2004
Last modified: January 25, 2012
This is version 47 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