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Reviewed, UniProtKB/Swiss-Prot A1V7Z3 (GLMU_BURMS)

Last modified November 3, 2009. Version 22. 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: BMASAVP1_A3051
OrganismBurkholderia mallei (strain SAVP1) [Complete proteome] [HAMAP]
Taxonomic identifier320388 [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-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. HAMAP 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 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_1000056143

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
A1V7Z3-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: D10729361F10D8CE

FASTA45347,580
        10         20         30         40         50         60 
MNIVILAAGT GKRMRSALPK VLHPLAGRPL LSHVIDTARA LAPSRLVVVI GHGAEQVRAA 

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

       130        140        150        160        170        180 
YGVLTVTLDD PTGYGRIVRD QAGCVTRIVE QKDASPDELR IDEINTGIVV APTAQLSMWL 

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

       250        260        270        280        290        300 
DALLAAGVTL ADPARIDVRG TLACGRDVSI DVNCVFEGDV TLADGVTIGA NCVIRHAAIA 

       310        320        330        340        350        360 
AGARVDAFSH LDGATVGANA VVGPYARLRP GAVLAADAHV GNFVEVKNAT LGQGSKANHL 

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

       430        440        450 
TTVWKDVAAD MLVLNDKTQT AKSGYVRPVK KKS 

« Hide

References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000526 Genomic DNA. Translation: ABM52634.1.
RefSeqYP_994346.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4681393.
GenomeReviewsGene locus BMASAVP1_A3051 in contig CP000526_GR.
KEGGbmv:BMASAVP1_A3051.
TIGRBMASAVP1_A3051.

Phylogenomic databases

OMATRMKSKL.

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_BURMS
AccessionPrimary (citable) accession number: A1V7Z3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: November 3, 2009
This is version 22 of the entry and version 1 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