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Reviewed, UniProtKB/Swiss-Prot A0KB52 (GLMU_BURCH)

Last modified February 9, 2010. 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: Bcen2424_2981
OrganismBurkholderia cenocepacia (strain HI2424) [Complete proteome] [HAMAP]
Taxonomic identifier331272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length453 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-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. HAMAP MF_01631

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. HAMAP 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 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 HAMAP 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 – 453453Bifunctional protein glmU HAMAP MF_01631
PRO_1000056140

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
A0KB52-1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: C7E28C14DF2CD9A7

FASTA45348,003
        10         20         30         40         50         60 
MNIVILAAGT GKRMRSALPK VLHPLAGRPL LSHVIDTART LQPSRLVVVV GHGAEQVKAA 

        70         80         90        100        110        120 
VAAPDVQFAV QAEQLGTGHA VRQALPLLDP AQPTLVLYGD VPLTRASTLQ RLVDAARDGR 

       130        140        150        160        170        180 
YGILTVTLDD PTGYGRIVRD ASGFVTRIVE QKDASPEELK IAEINTGIIV TPTAQLSMWL 

       190        200        210        220        230        240 
GALKNENAQG EYYLTDVVEL AIEAGFEVVT SQPDDEWETL GVNSKAQLAE LERIHQRNVA 

       250        260        270        280        290        300 
DALLVDGVTL ADPARVDVRG TLRCGRDVSI DVNCVFEGNV TIADNVTIGA NCVIRNASVG 

       310        320        330        340        350        360 
AGTRIDAFTH IDGAELGANT VIGPYARLRP GAQLADEAHV GNFVEVKNAV IGHGSKANHL 

       370        380        390        400        410        420 
TYIGDADIGA RVNIGAGTIT CNYDGANKFR TVIEDDVFVG SDTQLVAPVR VGRGVTIAAG 

       430        440        450 
TTIWKDVAEG VLALNEKTQT AKSGYVRPVK KKS 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia cenocepacia HI2424."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., LiPuma J.J., Gonzalez C.F., Konstantinidis K., Tiedje J.M., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000458 Genomic DNA. Translation: ABK09729.1.
RefSeqYP_836622.1.

3D structure databases

SMRA0KB52. Positions 1-447.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0KB52.

Genome annotation databases

GeneID4449715.
GenomeReviewsGene locus Bcen2424_2981 in contig CP000458_GR.
KEGGbch:Bcen2424_2981.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHBG688195.
OMAGSKVNHL.

Family and domain databases

HAMAPMF_01631. GlmU.
[Tree]
InterProIPR005882. Bifunctional_GlmU.
IPR018357. Hexapep_transf_CS.
IPR005835. NTP_transferase.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamPF00483. NTP_transferase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01173. glmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_BURCH
AccessionPrimary (citable) accession number: A0KB52
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 12, 2006
Last modified: February 9, 2010
This is version 28 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