Skip Header

Contribute Send feedback
Read comments (?) or add your own

P57139 (GLMU_BUCAI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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)
Taxonomic identifier107806 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

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

Subunit structure

Homotrimer By similarity. 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_0000068698

Regions

Region1 – 229229Pyrophosphorylase By similarity
Region11 – 144Substrate binding By similarity
Region81 – 822Substrate binding By similarity
Region230 – 25021Linker By similarity
Region251 – 459209N-acetyltransferase By similarity

Sites

Active site3631Proton acceptor By similarity
Metal binding1051Magnesium By similarity
Metal binding2271Magnesium By similarity
Binding site761Substrate By similarity
Binding site1401Substrate; via amide nitrogen By similarity
Binding site1541Substrate By similarity
Binding site3871Acetyl-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: 10993077] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: APS.
+Additional computationally mapped references.

Cross-references

Sequence databases

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

3D structure databases

ProteinModelPortalP57139.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBUCT00000002855; EBBUCP00000002631; EBBUCG00000002855.
GeneID1109535.
GenomeReviewsGene locus BU027 in contig BA000003_GR.
KEGGbuc:BU027.
PATRIC21243558. VBIBucAph127364_0039.

Phylogenomic databases

GeneTreeEBGT00050000008186.
HOGENOMHBG688195.
OMAGSKVNHL.
PhylomeDBP57139.
ProtClustDBCLSK493047.

Enzyme and pathway databases

BioCycBSP107806:BU027-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_BUCAI
AccessionPrimary (citable) accession number: P57139
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: January 25, 2012
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Buchnera aphidicola (subsp. Acyrthosiphon pisum)

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents