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Reviewed, UniProtKB/Swiss-Prot A5G0T8 (GLMU_ACICJ)

Last modified November 3, 2009. Version 21. 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: Acry_2275
OrganismAcidiphilium cryptum (strain JF-5) [Complete proteome] [HAMAP]
Taxonomic identifier349163 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcidiphilium

Protein attributes

Sequence length437 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-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.

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 – 437437Bifunctional protein glmU HAMAP MF_01631
PRO_1000056132

Regions

Region1 – 223223Pyrophosphorylase By similarity
Region8 – 114Substrate binding By similarity
Region75 – 762Substrate binding By similarity
Region224 – 24421Linker By similarity
Region245 – 437193N-acetyltransferase By similarity

Sites

Active site3401Proton acceptor By similarity
Metal binding981Magnesium By similarity
Metal binding2211Magnesium By similarity
Binding site701Substrate By similarity
Binding site1351Substrate; via amide nitrogen By similarity
Binding site1491Substrate By similarity
Binding site1641Substrate By similarity
Binding site3641Acetyl-CoA By similarity
Binding site3821Acetyl-CoA By similarity
Binding site4001Acetyl-CoA; via amide nitrogen By similarity
Binding site4171Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
A5G0T8-1 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: FF36514EF776428C

FASTA43744,474
        10         20         30         40         50         60 
MHNTAVILAA GLGTRMKSSR PKVLHHIAGR PMLAHLLAAC KTAFAATVVV TGPDMDEVAR 

        70         80         90        100        110        120 
AAAPHPTVIQ RERLGTAHAA LAAADHFGAG AVTLVYGDNP LVTGPTLQRL GARLGAGDAA 

       130        140        150        160        170        180 
LVLLGTRPPE PGAFGRIIGP AGFAERIVEF ADATEAERAV GLCNVGGFSA AAADMRRWLG 

       190        200        210        220        230        240 
NIGNDNAKGE YYLTDLVAVA RAEGASVAVV EAPWDECRGV NSRAELAAAE AAMQSRLRAA 

       250        260        270        280        290        300 
ALAAGVTMTA PETVFLAADT ALAADVTIEP HVVFGPGVTV GPDVTIRAFS HLEGCAISAG 

       310        320        330        340        350        360 
AIIGPYARLR PGSDIGAGAH VGNFVELKAA RLGAGAKANH LTYLGDAEIG PRANIGAGTI 

       370        380        390        400        410        420 
TCNYDGFAKH RTTIGADAFI GSDVALVAPV SVGDRAIIAA GSVITDPVAA DALALARGRQ 

       430 
VEKPGRAAEL RMTKGKR 

« Hide

References

[1]"Complete sequence of chromosome of Acidiphilium cryptum JF-5."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000697 Genomic DNA. Translation: ABQ31470.1.
RefSeqYP_001235389.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA5G0T8.

Genome annotation databases

GeneID5160736.
GenomeReviewsGene locus Acry_2275 in contig CP000697_GR.
KEGGacr:Acry_2275.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAMERTCLA.

Family and domain databases

HAMAPMF_01631.
[Tree]
InterProIPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR001228. ISPD_synthase.
IPR005882. UDP_GlcNAc_PyrPase.
[Graphical view]
PfamPF00132. Hexapep. 7 hits.
PF01128. IspD. 1 hit.
[Graphical view]
TIGRFAMsTIGR01173. glmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_ACICJ
AccessionPrimary (citable) accession number: A5G0T8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: November 3, 2009
This is version 21 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