Skip Header

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

Reviewed, UniProtKB/Swiss-Prot Q9A5Z3 (GLMU_CAUCR)

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: CC_2304
OrganismCaulobacter crescentus (Caulobacter vibrioides) [Complete proteome] [HAMAP]
Taxonomic identifier155892 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter

Protein attributes

Sequence length462 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 – 462462Bifunctional protein glmU HAMAP MF_01631
PRO_0000233754

Regions

Region1 – 239239Pyrophosphorylase By similarity
Region17 – 204Substrate binding By similarity
Region89 – 902Substrate binding By similarity
Region240 – 26021Linker By similarity
Region261 – 462202N-acetyltransferase By similarity

Sites

Active site3561Proton acceptor By similarity
Metal binding1141Magnesium By similarity
Metal binding2371Magnesium By similarity
Binding site841Substrate By similarity
Binding site1501Substrate By similarity
Binding site1651Substrate By similarity
Binding site1801Substrate By similarity
Binding site3801Acetyl-CoA By similarity
Binding site3981Acetyl-CoA By similarity
Binding site4331Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9A5Z3-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 84FCE7C136972D3B

FASTA46248,191
        10         20         30         40         50         60 
MTESVSKPVR PRAAVILAAG QGTRMKSPTP KVLHRLAGRT LLDHAIDAAE GLGCERIIVV 

        70         80         90        100        110        120 
VGAHSPQVGE SARKRLGPDA TVIQDPPLGT GHAVLAAKDA LADFHGDVVV TYADCPLTTA 

       130        140        150        160        170        180 
PVIAPLFDLI THVAHVAVLG FEAQNPTGYG RLILAPGHVL LRIVEEKEAD LATKQVKHCN 

       190        200        210        220        230        240 
SGVLAADRAV LFDLLANVRN DNAKGEYYLT DVVGLAHERH LSTRTAFAPE ASVQGVNAQA 

       250        260        270        280        290        300 
ELAAAEAVWQ QNRRKALMVD GVTMPAPDTV HLAWDTQIAG GAVVEQFVVF GPGVSVASGA 

       310        320        330        340        350        360 
VIKAFSHLEG AVVGEGALIG PYARLRPGAE IGPDAHIGNF VEVKKVKVGA GAKANHLSYL 

       370        380        390        400        410        420 
GDGSVGEKAN IGAGTIFCNY DGFEKFETHV GKGAFIGSNS ALVAPVRVGD GAMTGSGSVI 

       430        440        450        460 
TKDVEDGALA LSRADQTSKA GWATKFRAIK QAQKDKKKDK KA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005673 Genomic DNA. Translation: AAK24275.1.
PIRG87534.
RefSeqNP_421107.1.

3D structure databases

SMRQ9A5Z3. Positions 10-444.
ModBaseSearch...

Genome annotation databases

GeneID941054.
GenomeReviewsGene locus CC_2304 in contig AE005673_GR.
KEGGccr:CC_2304.
NMPDRfig|190650.1.peg.2287.
TIGRCC_2304.

Phylogenomic databases

HOGENOMHBG688195.
OMAGSKVNHL.

Enzyme and pathway databases

BRENDA2.3.1.157. 2191.
2.7.7.23. 2191.

Family and domain databases

HAMAPMF_01631. GlmU.
[Tree]
InterProIPR005882. Bifunctional_GlmU.
IPR001228. ISPD_synthase.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamPF01128. IspD. 1 hit.
[Graphical view]
TIGRFAMsTIGR01173. glmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_CAUCR
AccessionPrimary (citable) accession number: Q9A5Z3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: June 1, 2001
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