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Q04DS4 (GLMU_OENOB) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 64. 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:OEOE_1542
OrganismOenococcus oeni (strain ATCC BAA-331 / PSU-1) [Complete proteome] [HAMAP]
Taxonomic identifier203123 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLeuconostocaceaeOenococcus

Protein attributes

Sequence length426 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 – 426426Bifunctional protein GlmU HAMAP-Rule MF_01631
PRO_1000069734

Regions

Region1 – 216216Pyrophosphorylase By similarity
Region9 – 124UDP-GlcNAc binding By similarity
Region217 – 23721Linker By similarity
Region238 – 426189N-acetyltransferase By similarity
Region339 – 3402Acetyl-CoA binding By similarity

Sites

Active site3161Proton acceptor By similarity
Metal binding971Magnesium By similarity
Metal binding2141Magnesium By similarity
Binding site231UDP-GlcNAc By similarity
Binding site691UDP-GlcNAc By similarity
Binding site1321UDP-GlcNAc; via amide nitrogen By similarity
Binding site1481UDP-GlcNAc By similarity
Binding site1631UDP-GlcNAc By similarity
Binding site2141UDP-GlcNAc By similarity
Binding site2861Acetyl-CoA; amide nitrogen By similarity
Binding site3041Acetyl-CoA By similarity
Binding site3191Acetyl-CoA By similarity
Binding site3301Acetyl-CoA By similarity
Binding site3581Acetyl-CoA By similarity
Binding site3761Acetyl-CoA; via amide nitrogen By similarity
Binding site3931Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q04DS4 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: CCDF7323AEBC1E01

FASTA42646,641
        10         20         30         40         50         60 
MSEVDVVILA AGKGSRMKDD LSKPLHKVAG LPMLEWICRA VRKFNPKNII AVQGADEDFS 

        70         80         90        100        110        120 
SYVDETVVQK EQLGSADALR CAFPKIDAEK LIVINADMPL MTENDLVDLV EKGEGFDAAL 

       130        140        150        160        170        180 
LTADLKKPFG YGRVIPVGER NVVEQIVEER DATADQKKLH LVNAGVYLFR ADYIKRAINN 

       190        200        210        220        230        240 
VTTDNSQSEY YLTDALPGAK IVQVADWHDI LGVNTQQQLA AVSKIARKRI NDQIMANGVT 

       250        260        270        280        290        300 
MIDPLTTYID ANVLVGTGTI IKPGTVIEHD SVIGAENEIG PYAHLREKTV TGIDVHIGNF 

       310        320        330        340        350        360 
VETKNAKIGD HTHIGHLTYV GDAEVGQAVN IGAGTIFVNY DGKNKHMTKV GDRAFIGSNS 

       370        380        390        400        410        420 
KLVAPVEIAS EAITAAGSTI TDNVDQHAMG IARQRQTNKS DFWQRMPHED FATEYDAKHD 


QRDDQP 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000411 Genomic DNA. Translation: ABJ57398.1.
RefSeqYP_811063.1. NC_008528.1.

3D structure databases

ProteinModelPortalQ04DS4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203123.OEOE_1542.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ57398; ABJ57398; OEOE_1542.
GeneID4415811.
KEGGooe:OEOE_1542.
PATRIC22801324. VBIOenOen113004_1568.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHOG000283476.
KOK04042.
OMACNIAAGT.
OrthoDBEOG6Z6FQZ.

Enzyme and pathway databases

BioCycOOEN203123:GHNL-1542-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.
ProtoNetSearch...

Entry information

Entry nameGLMU_OENOB
AccessionPrimary (citable) accession number: Q04DS4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 14, 2006
Last modified: July 9, 2014
This is version 64 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