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Q8Y304 (GLMU_RALSO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 77. 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:
Bifunctional protein GlmU

Including the following 2 domains:

  1. UDP-N-acetylglucosamine pyrophosphorylase
    EC=2.7.7.23
    Alternative name(s):
    N-acetylglucosamine-1-phosphate uridyltransferase
  2. Glucosamine-1-phosphate N-acetyltransferase
    EC=2.3.1.157
Gene names
Name:glmU
Ordered Locus Names:RSc0177
ORF Names:RS01048
OrganismRalstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum) [Complete proteome] [HAMAP]
Taxonomic identifier267608 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia

Protein attributes

Sequence length455 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

Catalytic activity

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

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

Cofactor

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

Pathway

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

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.

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

Subunit structure

Homotrimer By similarity. HAMAP-Rule MF_01631

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01631.

Sequence similarities

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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 455455Bifunctional protein GlmU HAMAP-Rule MF_01631
PRO_0000233830

Regions

Region1 – 225225Pyrophosphorylase By similarity
Region6 – 94UDP-GlcNAc binding By similarity
Region76 – 772UDP-GlcNAc binding By similarity
Region98 – 1003UDP-GlcNAc binding By similarity
Region226 – 24621Linker By similarity
Region247 – 455209N-acetyltransferase By similarity
Region382 – 3832Acetyl-CoA binding By similarity

Sites

Active site3591Proton acceptor By similarity
Metal binding1001Magnesium By similarity
Metal binding2231Magnesium By similarity
Binding site201UDP-GlcNAc By similarity
Binding site711UDP-GlcNAc By similarity
Binding site1351UDP-GlcNAc; via amide nitrogen By similarity
Binding site1501UDP-GlcNAc By similarity
Binding site1651UDP-GlcNAc By similarity
Binding site2231UDP-GlcNAc By similarity
Binding site3291Acetyl-CoA; amide nitrogen By similarity
Binding site3471Acetyl-CoA By similarity
Binding site3621Acetyl-CoA By similarity
Binding site3731Acetyl-CoA By similarity
Binding site4011Acetyl-CoA By similarity
Binding site4191Acetyl-CoA; via amide nitrogen By similarity
Binding site4361Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8Y304 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: D7A3647EA8320BD4

FASTA45548,670
        10         20         30         40         50         60 
MNIVILAAGL GKRMRSALPK VLHPLAGKPL LAHVIETARS LSPTRLVVVV GHGGDRVRDM 

        70         80         90        100        110        120 
VGAPDVTFAT QDQQLGTGHA VMQALDQLDD TVPTLVLYGD VPLTRAETLN ALVGAAGQDH 

       130        140        150        160        170        180 
LGVLTVHLDD PTGYGRIVRD ATGRITRIVE QKDANETQLA IHEVNTGILV CPTARLKTWL 

       190        200        210        220        230        240 
ATLRNDNAQG EYYLTDVIER AASEGLPITS AHPLAEWETL GVNSKVQLAE LERIHQRNLA 

       250        260        270        280        290        300 
QQLLEDGVTL IDPARIDIRG RLTCGRDVVI DIDCIFEGNV TLGDGVRIGA HAVIRDAAIQ 

       310        320        330        340        350        360 
AGAEILPFCH IEQATVGAQS RIGPYARLRP GTELAEDVHI GNFVEVKNSQ IAAHSKANHL 

       370        380        390        400        410        420 
AYVGDATVGS RVNIGAGTIT CNYDGANKFR TIIEDDAFIG SDTQLVAPVR VGRGATLGAG 

       430        440        450 
TTLTKDAPEG QLTVSRARQT TVNGWQRPVK QKKDA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL646052 Genomic DNA. Translation: CAD13705.1.
RefSeqNP_518298.1. NC_003295.1.

3D structure databases

ProteinModelPortalQ8Y304.
SMRQ8Y304. Positions 1-447.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING267608.RSc0177.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD13705; CAD13705; RSc0177.
GeneID1218980.
KEGGrso:RSc0177.
PATRIC20258893. VBIRalSol70888_0181.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHOG000283476.
KOK04042.
OMADCVTNQD.
OrthoDBEOG6Z6FQZ.

Enzyme and pathway databases

BioCycRSOL267608:GCVU-178-MONOMER.
UniPathwayUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
HAMAPMF_01631. GlmU.
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR025877. MobA-like_NTP_Trfase_dom.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamPF00132. Hexapep. 3 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMSSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsTIGR01173. glmU. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLMU_RALSO
AccessionPrimary (citable) accession number: Q8Y304
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: March 1, 2002
Last modified: June 11, 2014
This is version 77 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

PATHWAY comments

Index of metabolic and biosynthesis pathways