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P57139 (GLMU_BUCAI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 90. 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:BU027
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) [Reference proteome] [HAMAP]
Taxonomic identifier107806 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

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-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 – 459459Bifunctional protein GlmU HAMAP-Rule MF_01631
PRO_0000068698

Regions

Region1 – 229229Pyrophosphorylase By similarity
Region11 – 144UDP-GlcNAc binding By similarity
Region81 – 822UDP-GlcNAc binding By similarity
Region103 – 1053UDP-GlcNAc binding By similarity
Region230 – 25021Linker By similarity
Region251 – 459209N-acetyltransferase By similarity
Region386 – 3872Acetyl-CoA binding By similarity

Sites

Active site3631Proton acceptor By similarity
Metal binding1051Magnesium By similarity
Metal binding2271Magnesium By similarity
Binding site251UDP-GlcNAc By similarity
Binding site761UDP-GlcNAc By similarity
Binding site1401UDP-GlcNAc; via amide nitrogen By similarity
Binding site1541UDP-GlcNAc By similarity
Binding site2271UDP-GlcNAc By similarity
Binding site3331Acetyl-CoA; amide nitrogen By similarity
Binding site3511Acetyl-CoA By similarity
Binding site3661Acetyl-CoA By similarity
Binding site3771Acetyl-CoA By similarity
Binding site4051Acetyl-CoA By similarity
Binding site4231Acetyl-CoA; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
P57139 [UniParc].

Last modified December 1, 2000. Version 1.
Checksum: C26CAFBD3852AAF4

FASTA45951,182
        10         20         30         40         50         60 
MLTQEIIIVI LAAGKGTRMK SNHPKVLHFL GGKTILEHVI ETAQSIKPKK IILVYSDQKK 

        70         80         90        100        110        120 
PVLSNIYNIP IQWIIQKKPQ GTGHAILLAI KKISDNTEIL VLYGDVPFIS PVSIKKLQKS 

       130        140        150        160        170        180 
KKQSKISLLT AKVKNPNGYG RILRKKGKVI SIIEDQDASN EQKNIKEIYS GIFIAQSKDL 

       190        200        210        220        230        240 
TRWLKKIDKK NEKQEFYATD IIALAHLEGS FIKTIEPLNY EEILGINNKL QLSNLEKIFQ 

       250        260        270        280        290        300 
KKQINKLLIN GVTIKDPSHF IFRGTLQHGQ NVEIDTGVIL ENNVILGDDV KIGPGCIIRN 

       310        320        330        340        350        360 
SSIDSNTNIQ AYTIIENSKI GKGCIIGPFA HLRSNTLLDR NVHIGNFVET KDTFIKNESK 

       370        380        390        400        410        420 
VKHLSYLGNS EIGSKVNIGA GSITCNYDGA NKFKTIIGDN VLVGSNTQLI APIKIAKNTT 

       430        440        450 
IAAGTTVTKD VNTPCLVYNT KEQKYKKNWM RSKKIIKKN 

« Hide

References

[1]"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS."
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.
Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: APS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000003 Genomic DNA. Translation: BAB12754.1.
RefSeqNP_239868.1. NC_002528.1.

3D structure databases

ProteinModelPortalP57139.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB12754; BAB12754; BAB12754.
GeneID1109535.
KEGGbuc:BU027.
PATRIC21243558. VBIBucAph127364_0039.

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHOG000283476.
KOK04042.
OMANKHKTII.
OrthoDBEOG6Z6FQZ.
ProtClustDBCLSK493047.

Enzyme and pathway databases

BioCycBAPH107806:GBZJ-27-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. 3 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_BUCAI
AccessionPrimary (citable) accession number: P57139
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: February 19, 2014
This is version 90 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

Buchnera aphidicola (subsp. Acyrthosiphon pisum)

Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names