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Reviewed, UniProtKB/Swiss-Prot A0R8C1 (GLMU_BACAH)

Last modified February 9, 2010. Version 30. 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: BALH_0044
OrganismBacillus thuringiensis (strain Al Hakam) [Complete proteome] [HAMAP]
Taxonomic identifier412694 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length459 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 – 459459Bifunctional protein glmU HAMAP MF_01631
PRO_0000337708

Regions

Region1 – 230230Pyrophosphorylase By similarity
Region9 – 124Substrate binding By similarity
Region78 – 792Substrate binding By similarity
Region231 – 25121Linker By similarity
Region252 – 459208N-acetyltransferase By similarity

Sites

Active site3631Proton acceptor By similarity
Metal binding1031Magnesium 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 site3871Acetyl-CoA By similarity
Binding site4231Acetyl-CoA; via amide nitrogen By similarity
Binding site4401Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
A0R8C1-1 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: 438E43713A39DA05

FASTA45949,423
        10         20         30         40         50         60 
MSNRFAVILA AGKGTRMKSK LYKVLHPVCG KPMVQHVVDQ VSQLGLQKLV TVVGHGAEMV 

        70         80         90        100        110        120 
QEQLGNVSEF ALQAEQLGTA HAVDQAAGVL ANEEGTTLVI CGDTPLITAE TMEALLQQHK 

       130        140        150        160        170        180 
EAGAMATVLT AYIEEPAGYG RIVRNENGHV EKIVEHKDAN EKELAIKEIN TGTYCFDNKA 

       190        200        210        220        230        240 
LFASLSKVSN DNVQGEYYLP DVIEILKNEG HIVSAYQTEH FDETLGVNDR VALSQAEIIM 

       250        260        270        280        290        300 
KNRINRKNMV NGVTIIDPSN TYISADAIIG SDTVLHPGTI IEGNTVIGSD CEIGPHTVIR 

       310        320        330        340        350        360 
DSEIGDRTTI RQSTVHDSKL GTEVSVGPFA HIRPDSVIGD EVRVGNFVEI KKTVFGNRSK 

       370        380        390        400        410        420 
ASHLSYIGDA QVGEDVNLGC GSITVNYDGK NKFKTVIGNG VFIGCNSNLV APVTVEDGAY 

       430        440        450 
VAAGSTITEN VPSKALSVAR ARQVNKEDYV DQLLNKKKS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000485 Genomic DNA. Translation: ABK83464.1. Different initiation.
RefSeqYP_892971.1.

3D structure databases

SMRA0R8C1. Positions 3-453.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0R8C1.

Genome annotation databases

GeneID4545824.
GenomeReviewsGene locus BALH_0044 in contig CP000485_GR.
KEGGbtl:BALH_0044.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHBG688195.

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_BACAH
AccessionPrimary (citable) accession number: A0R8C1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: February 9, 2010
This is version 30 of the entry and version 2 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