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P25177 (GLMM_HELPY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Synonyms:ureC
Ordered Locus Names:HP_0075
OrganismHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Taxonomic identifier85962 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. Ref.4

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. Can autophosphorylate in vitro using ATP. HAMAP MF_01554_B

Sequence similarities

Belongs to the phosphohexose mutase family.

Ontologies

Keywords
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference 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 – 445445Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000147899

Sites

Active site991Phosphoserine intermediate By similarity
Metal binding991Magnesium; via phosphate group By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity
Metal binding2461Magnesium By similarity

Amino acid modifications

Modified residue991Phosphoserine; by autocatalysis Probable

Experimental info

Sequence conflict1241K → R in AAA25018. Ref.1
Sequence conflict1341E → G in AAA25018. Ref.1
Sequence conflict1461V → I in AAQ57666. Ref.2
Sequence conflict1611A → V in AAQ57666. Ref.2
Sequence conflict2161D → E Ref.1
Sequence conflict2161D → E Ref.2
Sequence conflict2731S → T in AAQ57666. Ref.2
Sequence conflict2821V → I in AAA25018. Ref.1
Sequence conflict2861N → S in AAQ57666. Ref.2
Sequence conflict3181Q → R Ref.1
Sequence conflict3181Q → R Ref.2
Sequence conflict3591Q → L in AAA25018. Ref.1
Sequence conflict3641A → R in AAA25018. Ref.1
Sequence conflict3741S → N Ref.1
Sequence conflict3741S → N Ref.2
Sequence conflict3931S → N in AAA25018. Ref.1
Sequence conflict4311S → L in AAQ57666. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P25177 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: C0A52D904FFDAF20

FASTA44549,086
        10         20         30         40         50         60 
MKIFGTDGVR GKAGVKLTPM FVMRLGIAAG LYFKKHSQTN KILIGKDTRK SGYMVENALV 

        70         80         90        100        110        120 
SALTSIGYNV IQIGPMPTPA IAFLTEDMRC DAGIMISASH NPFEDNGIKF FNSYGYKLKE 

       130        140        150        160        170        180 
EEEKAIEEIF HDEELLHSSY KVGESVGSAK RIDDVIGRYI AHLKHSFPKH LNLQSLRIVL 

       190        200        210        220        230        240 
DTANGAAYKV APVVFSELGA DVLVINDEPN GCNINDQCGA LHPNQLSQEV KKYRADLGFA 

       250        260        270        280        290        300 
FDGDADRLVV VDNLGNIVHG DKLLGVLGVY QKSKNALSSQ AVVATNMSNL ALKEYLKSQD 

       310        320        330        340        350        360 
LELKHCAIGD KFVSECMQLN KANFGGEQSG HIIFSDYAKT GDGLVCALQV SALVLESKQV 

       370        380        390        400        410        420 
SSVALNPFEL YPQSLVNLNV QKKPPLESLK GYSALLKELD KLEIRHLIRY SGTENKLRIL 

       430        440 
LEAKDEKLLE SKMQELKEFF EGHLC

« Hide

References

« Hide 'large scale' references
[1]"Shuttle cloning and nucleotide sequences of Helicobacter pylori genes responsible for urease activity."
Labigne A., Cussac V., Courcoux P.
J. Bacteriol. 173:1920-1931(1991) [PubMed: 2001995] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 85P.
[2]"Gene cloning and expression of glmM in E. coli."
She F.F., Zhang J., Ding H.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487.
[3]"The complete genome sequence of the gastric pathogen Helicobacter pylori."
Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. expand/collapse author list , Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.
Nature 388:539-547(1997) [PubMed: 9252185] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700392 / 26695.
[4]"The Helicobacter pylori ureC gene codes for a phosphoglucosamine mutase."
De Reuse H., Labigne A., Mengin-Lecreulx D.
J. Bacteriol. 179:3488-3493(1997) [PubMed: 9171391] [Abstract]
Cited for: FUNCTION AS A PHOSPHOGLUCOSAMINE MUTASE.
[5]"Autophosphorylation of phosphoglucosamine mutase from Escherichia coli."
Jolly L., Pompeo F., van Heijenoort J., Fassy F., Mengin-Lecreulx D.
J. Bacteriol. 182:1280-1285(2000) [PubMed: 10671448] [Abstract]
Cited for: AUTOPHOSPHORYLATION AT A SERINE RESIDUE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M60398 Genomic DNA. Translation: AAA25018.1.
AY353251 Genomic DNA. Translation: AAQ57666.1.
AE000511 Genomic DNA. Translation: AAD07146.1.
PIRC38537.
RefSeqNP_206875.1. NC_000915.1.

3D structure databases

ProteinModelPortalP25177.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-3160N.
MINTMINT-176642.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID900169.
GenomeReviewsGene locus HP_0075 in contig AE000511_GR.
KEGGhpy:HP0075.
NMPDRfig|85962.1.peg.73.
PATRIC20591355. VBIHelPyl33062_0078.
TIGRHP_0075.

Phylogenomic databases

HOGENOMHBG644964.
OMAIGSAKRI.
ProtClustDBPRK14324.

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_HELPY
AccessionPrimary (citable) accession number: P25177
Secondary accession number(s): Q6V395
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: November 1, 1997
Last modified: January 25, 2012
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Helicobacter pylori

Helicobacter pylori (strain 26695): entries and gene names

SIMILARITY comments

Index of protein domains and families

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