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Q83GR0 (GLMU_TROWT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. 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:TWT_188
OrganismTropheryma whipplei (strain Twist) (Whipple's bacillus) [Complete proteome] [HAMAP]
Taxonomic identifier203267 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeTropheryma

Protein attributes

Sequence length595 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 caution

The sequence AAO44285.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 595595Bifunctional protein GlmU HAMAP-Rule MF_01631
PRO_0000244320

Regions

Region1 – 369369Pyrophosphorylase By similarity
Region10 – 134UDP-GlcNAc binding By similarity
Region81 – 822UDP-GlcNAc binding By similarity
Region370 – 39021Linker By similarity
Region391 – 595205N-acetyltransferase By similarity
Region525 – 5262Acetyl-CoA binding By similarity

Sites

Active site5021Proton acceptor By similarity
Metal binding1651Magnesium By similarity
Metal binding3671Magnesium By similarity
Binding site241UDP-GlcNAc By similarity
Binding site751UDP-GlcNAc By similarity
Binding site2011UDP-GlcNAc; via amide nitrogen By similarity
Binding site2161UDP-GlcNAc By similarity
Binding site2301UDP-GlcNAc By similarity
Binding site3671UDP-GlcNAc By similarity
Binding site4721Acetyl-CoA; amide nitrogen By similarity
Binding site4901Acetyl-CoA By similarity
Binding site5051Acetyl-CoA By similarity
Binding site5161Acetyl-CoA By similarity
Binding site5621Acetyl-CoA; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q83GR0 [UniParc].

Last modified June 27, 2006. Version 2.
Checksum: 6F145B2ED00519E7

FASTA59565,166
        10         20         30         40         50         60 
MKSDLAIVIL AAGRGTRMRS STPKVLHNIA GLPMVAHVLR GAQLLKPCKT IVVFRDVRVE 

        70         80         90        100        110        120 
QYIRNTFPDV LTVAQSDALY GTGFGVFSAI PWIRSESYGN TYPNTRHESH AEYELDACDL 

       130        140        150        160        170        180 
DTCNPASDRL NDQESLKGGR HIHTKSGDVT NNKPFPSRVL ILYADVPLVP FQLLEELVRK 

       190        200        210        220        230        240 
PLKQAVGAIV TTHLDNPKGY GRVMRDNLGS IAKIIEDSNI LPEQSINEVN TGVGIFDTEY 

       250        260        270        280        290        300 
LQDALNKLLK CHIAHSPNQD CVTNQDCVTN QDCVTNQDCV TNQDCVPAAH TEAHVLSPKV 

       310        320        330        340        350        360 
IVTEQIHKKA ESEHQHAGQW MCRQDTVGAQ NTKEEMRLTD IVEYFYNNGL RVNSITTSDS 

       370        380        390        400        410        420 
ELLLGVNNRV QLAKTEKILN DQIIKRWQLY GVTIKSPETT WIDSTVQLSE DVLILPGCIL 

       430        440        450        460        470        480 
SGRTRIEEGA VIGPFATISD SFIGKNTIVK RAEIIDARIE EGAVIGPFAF IRPGTVIGKD 

       490        500        510        520        530        540 
SKVGTFVEIK QSNIGPESKV PHLSYIGDAN IGSHVNIGAG NIFANYDGKL KHETCIDDGV 

       550        560        570        580        590 
KTGAGNVFVA PVKVGRGAYT GAGSVIRDDI EEGALSLTEL KQKTIPKWAE NRGDG 

« Hide

References

[1]"Tropheryma whipplei twist: a human pathogenic Actinobacteria with a reduced genome."
Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M., Claverie J.-M.
Genome Res. 13:1800-1809(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Twist.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014184 Genomic DNA. Translation: AAO44285.1. Different initiation.
RefSeqNP_787316.1. NC_004572.3.

3D structure databases

ProteinModelPortalQ83GR0.
SMRQ83GR0. Positions 5-45.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203267.TWT188.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO44285; AAO44285; TWT_188.
GeneID1482456.
KEGGtwh:TWT188.
PATRIC23996739. VBITroWhi72342_0255.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1207.
KOK04042.
OMANKHKTII.
OrthoDBEOG6Z6FQZ.
ProtClustDBCLSK230032.

Enzyme and pathway databases

BioCycTWHI203267:GJDK-201-MONOMER.
UniPathwayUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Family and domain databases

HAMAPMF_01631. GlmU.
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR025877. MobA-like_NTP_Trfase_dom.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamPF00132. Hexapep. 3 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMSSF51161. SSF51161. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLMU_TROWT
AccessionPrimary (citable) accession number: Q83GR0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 27, 2006
Last modified: February 19, 2014
This is version 71 of the entry and version 2 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