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Reviewed, UniProtKB/Swiss-Prot Q2T1V2 (GLMU_BURTA)

Last modified June 16, 2009. Version 28. 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

Names and origin

Protein namesRecommended name:
    Bifunctional protein glmU
Including the following 2 domains:
    1- Recommended name:
            UDP-N-acetylglucosamine pyrophosphorylase
              EC=2.7.7.23
        Alternative name(s):
            N-acetylglucosamine-1-phosphate uridyltransferase
    2- Recommended name:
            Glucosamine-1-phosphate N-acetyltransferase
              EC=2.3.1.157
Gene names
Name: glmU
Ordered Locus Names: BTH_I0289
OrganismBurkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]
Taxonomic identifier271848 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length453 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-GlcNAc. Responsible for the acetylation of Glc-N-1-P to give GlcNAc-1-P and for the uridyl transfer from UTP to GlcNAc-1-P which produces UDP-GlcNAc By similarity.

Catalytic activity

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

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

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Pathway

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

Nucleotide-sugar biosynthesis; UDP-N-acetyl-D-glucosamine biosynthesis; UDP-N-acetyl-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.

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

Subcellular location

Cytoplasm By similarity.

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 – 453453Bifunctional protein glmU HAMAP MF_01631
PRO_0000244291

Regions

Region1 – 225225Pyrophosphorylase By similarity
Region6 – 94Substrate binding By similarity
Region76 – 772Substrate binding By similarity
Region226 – 24621Linker By similarity
Region247 – 453207N-acetyltransferase By similarity

Sites

Active site3591Proton acceptor By similarity
Metal binding1001Magnesium By similarity
Metal binding2231Magnesium By similarity
Binding site711Substrate By similarity
Binding site1351Substrate; via amide nitrogen By similarity
Binding site1501Substrate By similarity
Binding site1651Substrate By similarity
Binding site3831Acetyl-CoA By similarity
Binding site4011Acetyl-CoA By similarity
Binding site4191Acetyl-CoA; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2T1V2-1 [UniParc].

Last modified June 27, 2006. Version 2.
Checksum: 8B35CB83975886C0

FASTA45347,711
        10         20         30         40         50         60 
MNIVILAAGT GKRMRSALPK VLHPLAGRPL LSHVIDTARA LAPSRLVVVI GHGAERVRAA 

        70         80         90        100        110        120 
VAAPDVQFAV QEQQLGTGHA VRQALPLLDP SQPTLVLYGD VPLTRAATLR RLADAATDAR 

       130        140        150        160        170        180 
YGVLTVTLDD PTGYGRIVRD QAGCVTRIVE QKDASADELK IAEINTGIVV APTAQLSMWL 

       190        200        210        220        230        240 
GALGNDNAQG EYYLTDVVEQ AIEAGFEIVT TQPDDEWETL GVNSKAQLAE LERIHQRKLA 

       250        260        270        280        290        300 
EALLADGVTL ADPARIDVRG KLTCGRDVSI DVNCVFEGDV TLADGVTIGA NCVIRNAAIA 

       310        320        330        340        350        360 
AGARVDAFSH LDGATLGANT VVGPYARLRP GAVLADDAHV GNFVEVKNAT LGHGSKANHL 

       370        380        390        400        410        420 
TYLGDADIGA RVNVGAGTIT CNYDGANKFR TVIEDDVFVG SDTQFVAPVR VGRGVTVAAG 

       430        440        450 
TTVWKDVAEG MLVLNDKTQT AKSGYVRPVK KKS 

« Hide

Cross-references

Sequence databases

CP000086 Genomic DNA. Translation: ABC38024.1. Different initiation.
RefSeqYP_440847.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3849694.
GenomeReviewsGene locus BTH_I0289 in contig CP000086_GR.
KEGGbte:BTH_I0289.
TIGRBTH_I0289.

Phylogenomic databases

HOGENOMQ2T1V2.

Enzyme and pathway databases

BioCycBTHA271848:BTH_I0289-MON.

Family and domain databases

HAMAPMF_01631.
[Tree]
InterProIPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR001228. ISPD_synthase.
IPR005882. UDP_GlcNAc_PyrPase.
[Graphical view]
PfamPF00132. Hexapep. 6 hits.
PF01128. IspD. 1 hit.
[Graphical view]
TIGRFAMsTIGR01173. glmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_BURTA
AccessionPrimary (citable) accession number: Q2T1V2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 27, 2006
Last modified: June 16, 2009
This is version 28 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)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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