Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q0BB89 (GLMU_BURCM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Bamb_3028
OrganismBurkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD)) [Complete proteome] [HAMAP]
Taxonomic identifier339670 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia 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_1000056141

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
Q0BB89 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: EF884BDB497CB18D

FASTA45347,927
        10         20         30         40         50         60 
MNIVILAAGT GKRMRSALPK VLHPLAGRPL LSHVIATART LQPSRLVVVV GHGAEQVQAA 

        70         80         90        100        110        120 
VAAPDVQFAV QAEQLGTGHA VRQALPLLDP AQPTLVLYGD VPLTRASTLR RLVDAARDGS 

       130        140        150        160        170        180 
YGILTVTLDD PTGYGRIVRD AAGFVTRIVE QKDASPEQLK IAEINTGIII TPTGQLAMWL 

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

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

       310        320        330        340        350        360 
TGTRIDAFTH 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 cepacia AMMD."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K., Ramette A., Tiedje J., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-244 / AMMD.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000440 Genomic DNA. Translation: ABI88584.1.
RefSeqYP_774918.1. NC_008390.1.

3D structure databases

ProteinModelPortalQ0BB89.
SMRQ0BB89. Positions 1-447.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0BB89.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4310510.
GenomeReviewsGene locus Bamb_3028 in contig CP000440_GR.
KEGGbam:Bamb_3028.
NMPDRfig|339670.3.peg.136.
PATRIC19021824. VBIBurAmb61564_3173.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHBG688195.
OMAGSKVNHL.
PhylomeDBQ0BB89.
ProtClustDBCLSK930247.

Enzyme and pathway databases

BioCycBAMB339670:BAMB_3028-MONOMER.

Family and domain databases

HAMAPMF_01631. GlmU.
[Tree]
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR011004. Trimer_LpxA-like.
[Graphical view]
KOK04042.
PANTHERPTHR22572:SF17. PTHR22572:SF17. 1 hit.
PfamPF00132. Hexapep. 4 hits.
[Graphical view]
SUPFAMSSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMsTIGR01173. GlmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_BURCM
AccessionPrimary (citable) accession number: Q0BB89
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 17, 2006
Last modified: January 25, 2012
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents