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Reviewed, UniProtKB/Swiss-Prot P25177 (GLMM_HELPY)

Last modified November 3, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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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 (Campylobacter pylori) [Complete proteome] [HAMAP]
Taxonomic identifier210 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

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Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Post-translational modification

Activated by phosphorylation. Can autophosphorylate in vitro using ATP. HAMAP MF_01554

Sequence similarities

Belongs to the phosphohexose mutase family.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445Phosphoglucosamine mutase HAMAP MF_01554
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

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Sequences

Sequence LengthMass (Da)Tools
P25177-1 [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

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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.

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Cross-references

Sequence databases

M60398 Genomic DNA. Translation: AAA25018.1.
AY353251 Genomic DNA. Translation: AAQ57666.1.
AE000511 Genomic DNA. Translation: AAD07146.1.
PIRC38537.
RefSeqNP_206875.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:3160N.

Genome annotation databases

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

Phylogenomic databases

HOGENOMP25177.
OMAVHDRYIE.

Enzyme and pathway databases

BRENDA5.4.2.10. 1131.

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...

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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: November 3, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Helicobacter pylori

Helicobacter pylori (strain 26695): entries and gene names

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