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Q577Y2 (GLMU_BRUAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BruAb2_0641
OrganismBrucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]
Taxonomic identifier262698 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

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-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain By similarity. HAMAP-Rule MF_01631

Catalytic activity

Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate. HAMAP-Rule MF_01631

UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine. HAMAP-Rule MF_01631

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule 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-Rule 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-Rule MF_01631

Subunit structure

Homotrimer By similarity. HAMAP-Rule MF_01631

Subcellular location

Cytoplasm By similarity HAMAP-Rule 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-Rule MF_01631
PRO_0000233744

Regions

Region1 – 232232Pyrophosphorylase By similarity
Region11 – 144UDP-GlcNAc binding By similarity
Region83 – 842UDP-GlcNAc binding By similarity
Region233 – 25321Linker By similarity
Region254 – 454201N-acetyltransferase By similarity
Region372 – 3732Acetyl-CoA binding By similarity

Sites

Active site3491Proton acceptor By similarity
Metal binding1081Magnesium By similarity
Metal binding2301Magnesium By similarity
Binding site251UDP-GlcNAc By similarity
Binding site781UDP-GlcNAc By similarity
Binding site1441UDP-GlcNAc; via amide nitrogen By similarity
Binding site1581UDP-GlcNAc By similarity
Binding site1731UDP-GlcNAc By similarity
Binding site2301UDP-GlcNAc By similarity
Binding site3191Acetyl-CoA; amide nitrogen By similarity
Binding site3371Acetyl-CoA By similarity
Binding site3521Acetyl-CoA By similarity
Binding site3631Acetyl-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
Q577Y2 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: 98D0D7E9AA0EAF2C

FASTA45447,886
        10         20         30         40         50         60 
MTDRTCLSIV LAAGEGTRMK SNLPKVLHRV AGLPLVCHVV NAVRGTGKSD VALVVGRGAE 

        70         80         90        100        110        120 
DVRSAVEKIA GPVSAFEQKE RLGTAHAVLA AHEAIARGYD 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 AYIGDAVIGA 

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

       430        440        450 
ALALGRARQE TKEGRAKILR EKYAAIKAAK SVSK 

« Hide

References

[1]"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis."
Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.
J. Bacteriol. 187:2715-2726(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9-941.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017224 Genomic DNA. Translation: AAX76052.1.
RefSeqYP_223413.1. NC_006933.1.

3D structure databases

ProteinModelPortalQ577Y2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262698.BruAb2_0641.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAX76052; AAX76052; BruAb2_0641.
GeneID3342275.
KEGGbmb:BruAb2_0641.
PATRIC17827563. VBIBruAbo15061_2955.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHOG000283476.
KOK04042.
OMAANAGIMV.
OrthoDBEOG6Z6FQZ.
ProtClustDBPRK14353.

Enzyme and pathway databases

BioCycBABO262698:GJC2-2856-MONOMER.
UniPathwayUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Family and domain databases

HAMAPMF_01631. GlmU.
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR025877. MobA-like_NTP_Trfase_dom.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamPF00132. Hexapep. 4 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMSSF51161. SSF51161. 1 hit.
TIGRFAMsTIGR01173. glmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_BRUAB
AccessionPrimary (citable) accession number: Q577Y2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 10, 2005
Last modified: February 19, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Brucella abortus strain 9-941

Brucella abortus (strain 9-941): entries and gene names