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Reviewed, UniProtKB/Swiss-Prot Q1LTV6 (GLMU_BAUCH)

Last modified June 16, 2009. Version 26. 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: BCI_0139
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

Pathway

Nucleotide-sugar biosynthesis; UDP-N-acetyl-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from D-glucosamine 6-phosphate (route II): step 2/2. HAMAP MF_01631

Nucleotide-sugar biosynthesis; UDP-N-acetyl-D-glucosamine biosynthesis; UDP-N-acetyl-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.

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 – 469469Bifunctional protein glmU HAMAP MF_01631
PRO_0000263119

Regions

Region1 – 236236Pyrophosphorylase By similarity
Region11 – 144Substrate binding By similarity
Region88 – 892Substrate binding By similarity
Region237 – 25721Linker By similarity
Region258 – 469212N-acetyltransferase By similarity

Sites

Active site3701Proton acceptor By similarity
Metal binding1121Magnesium By similarity
Metal binding2341Magnesium By similarity
Binding site831Substrate By similarity
Binding site1471Substrate; via amide nitrogen By similarity
Binding site1611Substrate By similarity
Binding site1761Substrate By similarity
Binding site3941Acetyl-CoA By similarity
Binding site4121Acetyl-CoA By similarity
Binding site4301Acetyl-CoA; via amide nitrogen By similarity
Binding site4471Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1LTV6-1 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 40B1DF6A5C2902E1

FASTA46951,774
        10         20         30         40         50         60 
MLNIKLNIVI LAAGKSTRMN SDIPKVLHLL AGKPILQYVI DTAIKLKAKC KSTNIYIVYG 

        70         80         90        100        110        120 
YKGELLQQKL AHKQKTFLHW IKQVEQSGTG HAVQQVLPFL GKDEEVLILY GDVPLISFQT 

       130        140        150        160        170        180 
LIHLLTTRSK QGLSLLTANL TNPDGYGRIL YKEQEVVGII EHQEANAQQK LISEINTGIL 

       190        200        210        220        230        240 
AVSSNELKIW ITKLTNNNSM NEFYLTDIIA LAWQEGKKIH TIHPEKISEI NGINDCAQLA 

       250        260        270        280        290        300 
NLERLYQKEQ AESLLRIGVI IADPNRFDLR GELKHGDNIF FDTNVLIEGQ VSLGNQVTIG 

       310        320        330        340        350        360 
TGCIIKNTVI GDNVIIKPYS IIEEAHLANG SIVGPFAHLR PGSKIEENAY VGNFVEIKKS 

       370        380        390        400        410        420 
TLGKKSKVAH LSYIGDANIG KDVNIGAGTI TCNYDGANKH QTIIGDNVFI GSDSQLIAPL 

       430        440        450        460 
TIGDGATIGA GTTVTSNVTS NEVIISRIRQ FPIINWQRPK KKIRYNIIY 

« Hide

References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000238 Genomic DNA. Translation: ABF13975.1.
RefSeqYP_588608.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4056403.
GenomeReviewsGene locus BCI_0139 in contig CP000238_GR.
KEGGbci:BCI_0139.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1LTV6.
OMAQ1LTV6. TRMKSKL.

Family and domain databases

HAMAPMF_01631.
[Tree]
InterProIPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR005882. UDP_GlcNAc_PyrPase.
[Graphical view]
PfamPF00132. Hexapep. 6 hits.
[Graphical view]
TIGRFAMsTIGR01173. glmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_BAUCH
AccessionPrimary (citable) accession number: Q1LTV6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: May 30, 2006
Last modified: June 16, 2009
This is version 26 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