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Q7VT27 (GLMU_BORPE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:BP3730
OrganismBordetella pertussis
Taxonomic identifier520 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length457 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 – 457457Bifunctional protein GlmU HAMAP MF_01631
PRO_0000233742

Regions

Region1 – 230230Pyrophosphorylase By similarity
Region7 – 104Substrate binding By similarity
Region78 – 792Substrate binding By similarity
Region231 – 25121Linker By similarity
Region252 – 457206N-acetyltransferase By similarity

Sites

Active site3641Proton acceptor By similarity
Metal binding1061Magnesium By similarity
Metal binding2281Magnesium By similarity
Binding site731Substrate By similarity
Binding site1401Substrate; via amide nitrogen By similarity
Binding site1551Substrate By similarity
Binding site1701Substrate By similarity
Binding site3881Acetyl-CoA By similarity
Binding site4061Acetyl-CoA By similarity
Binding site4241Acetyl-CoA; via amide nitrogen By similarity
Binding site4411Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VT27 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: FD2B6BECD5A7C66D

FASTA45748,400
        10         20         30         40         50         60 
MLNVVILAAG LGKRMQSDLP KVLHTLAGRP MLDHVIGSAR QLQPARIIVV VGHGADRVKA 

        70         80         90        100        110        120 
AFEGQPGLQF ALQQPQHGTG HAVQQAVPQL LEGDGEDDVT LVLYGDVPLV QPATLQNLLQ 

       130        140        150        160        170        180 
ARGRGVAVLT EVLADSTGYG RIVRDAQGQV CRIVEHKDAS EAERAIKEVN TGILAAPTAR 

       190        200        210        220        230        240 
LKDWLGRITN DNAQGEYYLT DVIGLAVGDG VPVGAAQPGA SWETLGVNSR VQQAQLERAW 

       250        260        270        280        290        300 
QSELARRQLE AGVTLADPAR FDVRGTLSCG RDVFIDVGCV FEGTVTLGDG VRVGPHCVLR 

       310        320        330        340        350        360 
DVAVQAGARI EAYSHLQQAK VGQEAVVGPY ARLRPGADLG ERSHVGNFVE IKNSVLQADS 

       370        380        390        400        410        420 
KANHLAYIGD ADIGARVNVG AGTITCNYDG VNKHRTVIED DAFIGSDTQL VAPVRVGKGA 

       430        440        450 
TLGAGTTLTK DAPAGQLTIS RARQSTIEGW KRPVKKS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX640422 Genomic DNA. Translation: CAE43987.1.
RefSeqNP_882233.1. NC_002929.2.

3D structure databases

ProteinModelPortalQ7VT27.
SMRQ7VT27. Positions 2-452.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2665001.
GenomeReviewsGene locus BP3730 in contig BX470248_GR.
KEGGbpe:BP3730.
NMPDRfig|257313.1.peg.3303.
PATRIC21161138. VBIBorPer7866_4033.

Phylogenomic databases

HOGENOMHBG688195.
OMAGSKVNHL.
PhylomeDBQ7VT27.
ProtClustDBCLSK921175.

Enzyme and pathway databases

BioCycBPER257313:BP3730-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. 3 hits.
[Graphical view]
SUPFAMSSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMsTIGR01173. GlmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_BORPE
AccessionPrimary (citable) accession number: Q7VT27
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 54 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