Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q13T65 (GLMU_BURXL)

Last modified February 9, 2010. Version 27. 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: Bxeno_A4186
ORF Names: Bxe_A0207
OrganismBurkholderia xenovorans (strain LB400) [Complete proteome] [HAMAP]
Taxonomic identifier266265 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

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_0000263121

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
Q13T65-1 [UniParc].

Last modified December 12, 2006. Version 2.
Checksum: 27A72EF1A44189AB

FASTA45347,936
        10         20         30         40         50         60 
MNIVILAAGT GKRMRSALPK VLHPLAGRPL LAHVIDTART LKPTHLVVVI GHGAEAVRKA 

        70         80         90        100        110        120 
VAAPDVQFAV QEQQLGTGHA VQQALPLLDP SAPTLVLYGD VPLTRAGTLQ ALTDRAGQGG 

       130        140        150        160        170        180 
YGVLTVTLAD PSGYGRIVRD AHGKVARIVE QKDATPEQLA IAEINTGIIV APTERLGDWL 

       190        200        210        220        230        240 
AALKNDNAQG EFYLTDAVEM AIEAGLEVVT TQPDHEWETL GVNSKQQLAE LERIHQRNVA 

       250        260        270        280        290        300 
DALLVAGVTL ADPARLDVRG TLECGRDVSI DVNCVFEGRV TLADNVTVGP NCVIRNANIG 

       310        320        330        340        350        360 
AGTRVDAFTH IEGAEVGANV VLGPYARLRP GASLHDESHV GNFVEVKNAV LGHGSKANHL 

       370        380        390        400        410        420 
TYIGDADIGA RVNIGAGTIT CNYDGANKFR TIIEDDVFVG SDTQLVAPVR VKRGATIAAG 

       430        440        450 
TTVWKDVEAD ALVLNDKTQT SRTGYVRPTK KKS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000270 Genomic DNA. Translation: ABE32724.1. Different initiation.
RefSeqYP_560776.1.

3D structure databases

SMRQ13T65. Positions 1-447.
ModBaseSearch...

Genome annotation databases

GeneID4006220.
GenomeReviewsGene locus Bxeno_A4186 in contig CP000270_GR.
KEGGbxe:Bxe_A0207.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG688195.
OMAAIVEERD.

Family and domain databases

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

Entry information

Entry nameGLMU_BURXL
AccessionPrimary (citable) accession number: Q13T65
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 12, 2006
Last modified: February 9, 2010
This is version 27 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