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B5Z751 (B5Z751_HELPG) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Bifunctional protein GlmU HAMAP-Rule MF_01631
Gene names
Name:glmU HAMAP-Rule MF_01631 EMBL ACI27400.1
Ordered Locus Names:HPG27_641 EMBL ACI27400.1
OrganismHelicobacter pylori (strain G27) [Complete proteome] [HAMAP] EMBL ACI27400.1
Taxonomic identifier563041 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter ›

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain By similarity. HAMAP-Rule MF_01631 SAAS SAAS005882

Catalytic activity

Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate. HAMAP-Rule MF_01631 SAAS SAAS005882

UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine. HAMAP-Rule MF_01631 SAAS SAAS005882

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01631 SAAS SAAS005882

Pathway

Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. HAMAP-Rule MF_01631 SAAS SAAS005882

Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. HAMAP-Rule MF_01631 SAAS SAAS005882

Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. HAMAP-Rule MF_01631 SAAS SAAS005882

Subunit structure

Homotrimer By similarity. HAMAP-Rule MF_01631 SAAS SAAS005882

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01631 SAAS SAAS005882.

Sequence similarities

In the C-terminal section; belongs to the transferase hexapeptide repeat family. HAMAP-Rule MF_01631

In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family. HAMAP-Rule MF_01631

Ontologies

Keywords
   Biological processCell shape
Cell wall biogenesis/degradation HAMAP-Rule MF_01631 SAAS SAAS005882
Peptidoglycan synthesis HAMAP-Rule MF_01631 SAAS SAAS005882
   Cellular componentCytoplasm HAMAP-Rule MF_01631 SAAS SAAS005882
   DomainRepeat HAMAP-Rule MF_01631 SAAS SAAS005882
   LigandMagnesium HAMAP-Rule MF_01631 SAAS SAAS005882
Metal-binding HAMAP-Rule MF_01631 SAAS SAAS005882
   Molecular functionAcyltransferase HAMAP-Rule MF_01631 SAAS SAAS005882
Nucleotidyltransferase HAMAP-Rule MF_01631 SAAS SAAS005882
Transferase
   Technical termComplete proteome
Multifunctional enzyme HAMAP-Rule MF_01631 SAAS SAAS005882
Gene Ontology (GO)
   Biological_processUDP-N-acetylglucosamine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

cell morphogenesis

Inferred from electronic annotation. Source: HAMAP

lipid A biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

lipopolysaccharide biosynthetic process

Inferred from electronic annotation. Source: InterPro

peptidoglycan biosynthetic process

Inferred from electronic annotation. Source: HAMAP

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionUDP-N-acetylglucosamine diphosphorylase activity

Inferred from electronic annotation. Source: HAMAP

glucosamine-1-phosphate N-acetyltransferase activity

Inferred from electronic annotation. Source: HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region1 – 236236Pyrophosphorylase By similarity HAMAP-Rule MF_01631
Region17 – 204UDP-GlcNAc binding By similarity HAMAP-Rule MF_01631
Region90 – 912UDP-GlcNAc binding By similarity HAMAP-Rule MF_01631
Region237 – 25721Linker By similarity HAMAP-Rule MF_01631
Region258 – 443186N-acetyltransferase By similarity HAMAP-Rule MF_01631
Region372 – 3732Acetyl-CoA binding By similarity HAMAP-Rule MF_01631

Sites

Active site3491Proton acceptor By similarity HAMAP-Rule MF_01631
Metal binding1161Magnesium By similarity HAMAP-Rule MF_01631
Metal binding2341Magnesium By similarity HAMAP-Rule MF_01631
Binding site311UDP-GlcNAc By similarity HAMAP-Rule MF_01631
Binding site1481UDP-GlcNAc; via amide nitrogen By similarity HAMAP-Rule MF_01631
Binding site1621UDP-GlcNAc By similarity HAMAP-Rule MF_01631
Binding site1771UDP-GlcNAc By similarity HAMAP-Rule MF_01631
Binding site2341UDP-GlcNAc By similarity HAMAP-Rule MF_01631
Binding site3211Acetyl-CoA; amide nitrogen By similarity HAMAP-Rule MF_01631
Binding site3381Acetyl-CoA By similarity HAMAP-Rule MF_01631
Binding site3521Acetyl-CoA By similarity HAMAP-Rule MF_01631
Binding site3631Acetyl-CoA By similarity HAMAP-Rule MF_01631
Binding site3911Acetyl-CoA By similarity HAMAP-Rule MF_01631
Binding site4091Acetyl-CoA; via amide nitrogen By similarity HAMAP-Rule MF_01631
Binding site4261Acetyl-CoA By similarity HAMAP-Rule MF_01631

Sequences

Sequence LengthMass (Da)Tools
B5Z751 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: 31C009BEBD36E708

FASTA44349,224
        10         20         30         40         50         60 
MLKFPKKRIL MLSVIILAAG KGTRMRSGLP KTLHTICGEP MLFYILETAF SISNDVHLVL 

        70         80         90        100        110        120 
HHQQERIKEA VLERFKGVIF HTQIVEKYSG TGGAIMQEDK TPIPTKHERV LILNADMPLI 

       130        140        150        160        170        180 
TKDALTPLLE SKNNAIGLLH LADPKGYGRV VLENHQVKKI VEEKDANDEE KTIKSVNAGV 

       190        200        210        220        230        240 
YFFERKFLEK YLPKLNDQNA QKEYYLTDLI ALGINENETI DAIFLEEECF LGVNRQTERA 

       250        260        270        280        290        300 
KAEEIMLERL RKNAMDLGVV MQLPKSIYLE KGVSFKGECV LEQGVRLIGN CLIENARIKA 

       310        320        330        340        350        360 
YSVIEESQII NSSVGPFAHA RPKSVICDSH VGNFVETKNA KLQGTKAGHL SYLGDCEIGK 

       370        380        390        400        410        420 
NTNVGAGVIT CNYDGKKKHQ TIIGENVFIG SDSQLVAPIT IGSNVLIGSG TTITKDIPSG 

       430        440 
SLSLSRAPQI NIENGYFKFF KKP

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References

[1]"The complete genome sequence of Helicobacter pylori strain G27."
Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S., Ottemann K.M., Stein M., Salama N.R., Guillemin K.
J. Bacteriol. 191:447-448(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: G27 EMBL ACI27400.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001173 Genomic DNA. Translation: ACI27400.1.
RefSeqYP_002266266.1. NC_011333.1.

3D structure databases

ProteinModelPortalB5Z751.
ModBaseSearch...

Protein-protein interaction databases

STRING563041.HPG27_641.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI27400; ACI27400; HPG27_641.
GeneID6963530.
KEGGhpg:HPG27_641.
PATRIC20599261. VBIHelPyl113476_0686.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHOG000283476.
KOK04042.
OMAEPQTHLR.
ProtClustDBPRK14359.

Enzyme and pathway databases

UniPathwayUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Family and domain databases

HAMAPMF_01631. GlmU.
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR025877. MobA-like_NTP_Trfase_dom.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PANTHERPTHR22572:SF17. PTHR22572:SF17. 1 hit.
PfamPF00132. Hexapep. 1 hit.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMSSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMsTIGR01173. glmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB5Z751_HELPG
AccessionPrimary (citable) accession number: B5Z751
Entry history
Integrated into UniProtKB/TrEMBL: November 25, 2008
Last sequence update: November 25, 2008
Last modified: May 1, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info