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A9MBM3 (GLMU_BRUC2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Bifunctional protein GlmU

Including the following 2 domains:

  1. UDP-N-acetylglucosamine pyrophosphorylase
    EC=2.7.7.23
    Alternative name(s):
    N-acetylglucosamine-1-phosphate uridyltransferase
  2. Glucosamine-1-phosphate N-acetyltransferase
    EC=2.3.1.157
Gene names
Name:glmU
Ordered Locus Names:BCAN_B0583
OrganismBrucella canis (strain ATCC 23365 / NCTC 10854) [Complete proteome] [HAMAP]
Taxonomic identifier483179 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length454 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 – 454454Bifunctional protein GlmU HAMAP MF_01631
PRO_1000088124

Regions

Region1 – 232232Pyrophosphorylase By similarity
Region11 – 144Substrate binding By similarity
Region83 – 842Substrate binding By similarity
Region233 – 25321Linker By similarity
Region254 – 454201N-acetyltransferase By similarity

Sites

Active site3491Proton acceptor By similarity
Metal binding1081Magnesium By similarity
Metal binding2301Magnesium By similarity
Binding site781Substrate By similarity
Binding site1441Substrate; via amide nitrogen By similarity
Binding site1581Substrate By similarity
Binding site1731Substrate By similarity
Binding site3731Acetyl-CoA By similarity
Binding site3911Acetyl-CoA By similarity
Binding site4091Acetyl-CoA; via amide nitrogen By similarity
Binding site4261Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
A9MBM3 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: EC9A7E45C23F3B18

FASTA45447,935
        10         20         30         40         50         60 
MTDRTCLSIV LAAGEGTRMK SNLPKVLHRV AGLPLVCHVV NAVRGTGKSD VALVVGRGAE 

        70         80         90        100        110        120 
DVRSAVEKIA GPVSAFEQKE RLGTAHAVLA AREAIARGYD DLLIVFGDTP LIEAQSLLAA 

       130        140        150        160        170        180 
RERLAQGADL VVIGFRPASP HGYGRLIEEG GQLVAIIEEK EATDEQKKIG FCNGGLMALR 

       190        200        210        220        230        240 
GQHALALLDA VGNDNAKGEY YLTDIVAIAH GKGLNVTAIE VPVDNVIGIN NRAELAEAET 

       250        260        270        280        290        300 
IWQNRKRREL MLSGVTLIAP ETVFFSYDTV IEPDVVIEPN VFFGPSVHVA SGALIHSFSH 

       310        320        330        340        350        360 
LEGAQVGEKA EIGPFARLRP GADLAEKSKV GNFCEVKNAK VGKGAKINHL TYIGDAVIGA 

       370        380        390        400        410        420 
SSNIGAGTIT CNYDGYNKFK TIIGDNAFIG SNSSLVAPVE IGDNAYIASG SVITADVPAD 

       430        440        450 
ALALGRARQE TKEGRAKILR EKYAAIKAAK SVSK

« Hide

References

[1]"Brucella canis ATCC 23365 whole genome shotgun sequencing project."
Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M., Snyder E.E. expand/collapse author list , Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C., Munk C., Brettin T.S.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 23365 / NCTC 10854.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000873 Genomic DNA. Translation: ABX63760.1.
RefSeqYP_001594531.1. NC_010104.1.

3D structure databases

ProteinModelPortalA9MBM3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9MBM3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5786727.
GenomeReviewsGene locus BCAN_B0583 in contig CP000873_GR.
KEGGbcs:BCAN_B0583.
PATRIC17834362. VBIBruCan25663_2802.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG688195.
OMAMERTCLA.
ProtClustDBPRK14353.

Enzyme and pathway databases

BioCycBCAN483179:BCAN_B0583-MONOMER.

Family and domain databases

HAMAPMF_01631. GlmU.
[Tree]
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR011004. Trimer_LpxA-like.
[Graphical view]
KOK04042.
PANTHERPTHR22572:SF17. PTHR22572:SF17. 1 hit.
PfamPF00132. Hexapep. 4 hits.
[Graphical view]
SUPFAMSSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMsTIGR01173. GlmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_BRUC2
AccessionPrimary (citable) accession number: A9MBM3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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