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Reviewed, UniProtKB/Swiss-Prot Q8UEH0 (GLMU_AGRT5)

Last modified February 9, 2010. Version 51. 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: Atu1787
ORF Names: AGR_C_3287
OrganismAgrobacterium tumefaciens (strain C58 / ATCC 33970) [Complete proteome] [HAMAP]
Taxonomic identifier176299 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacterium

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_0000233721

Regions

Region1 – 231231Pyrophosphorylase By similarity
Region10 – 134Substrate binding By similarity
Region82 – 832Substrate binding By similarity
Region232 – 25221Linker By similarity
Region253 – 453201N-acetyltransferase By similarity

Sites

Active site3481Proton acceptor By similarity
Metal binding1071Magnesium By similarity
Metal binding2291Magnesium By similarity
Binding site771Substrate By similarity
Binding site1431Substrate By similarity
Binding site1571Substrate By similarity
Binding site1721Substrate By similarity
Binding site3721Acetyl-CoA By similarity
Binding site3901Acetyl-CoA By similarity
Binding site4251Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8UEH0-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 9F1826910319BD1C

FASTA45347,877
        10         20         30         40         50         60 
MERSSLAVIL AAGDSTRMKS SKSKVLHPVA GRPMIGHVVE AVAGAGVGAV ALVVGRDADN 

        70         80         90        100        110        120 
VAAAASLKGL QVEAFLQKER KGTGHAVLAA REAIKRGFDD VIVAYGDVPL ITSATLDRAR 

       130        140        150        160        170        180 
EAIAAGADVA VIGFHTDRPT GYGRLLVENG ELVAIREEKD ATDEERKVTW CNSGLMAING 

       190        200        210        220        230        240 
RNALDLLDRI GNSNVKGEYY LTDVVEIARS LGRRAIAIDA PEKELTGCNN RAELAFIERL 

       250        260        270        280        290        300 
WQERRRHELM VDGVSMIAPE TVFLSFDTKI GQDVLIEPNV VFGPGVTIEP GAIVHAFSHL 

       310        320        330        340        350        360 
EGAHLAEGAV VGPFARLRPG ANLHANAKVG NFCEVKKAEI GEGAKVNHLT YIGDAFVGAG 

       370        380        390        400        410        420 
SNIGAGAITC NYDGYNKSET RIGANSFIGS NSSLVAPVTI GERAYIASGS VITDDVPADA 

       430        440        450 
LAFGRARQEV KPGRAVALRE RAKAQKEAKK KSS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE007869 Genomic DNA. Translation: AAK87557.1.
PIRAD2796.
D97575.
RefSeqNP_354772.1.

3D structure databases

SMRQ8UEH0. Positions 3-433.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8UEH0.

Genome annotation databases

GeneID1133825.
GenomeReviewsGene locus Atu1787 in contig AE007869_GR.
KEGGatc:AGR_C_3287.
atu:Atu1787.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHBG688195.
OMAMERTCLA.
PhylomeDBQ8UEH0.

Enzyme and pathway databases

BioCycATUM176299-1:ATU1787-MONOMER.

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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_AGRT5
AccessionPrimary (citable) accession number: Q8UEH0
Secondary accession number(s): Q7CYJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: June 1, 2002
Last modified: February 9, 2010
This is version 51 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