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Q8KA74 (GLMU_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. 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:BUsg_028
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length461 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 – 461461Bifunctional protein GlmU HAMAP MF_01631
PRO_0000068699

Regions

Region1 – 229229Pyrophosphorylase By similarity
Region11 – 144Substrate binding By similarity
Region81 – 822Substrate binding By similarity
Region230 – 25021Linker By similarity
Region251 – 461211N-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 site4231Acetyl-CoA; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8KA74 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 6D38A10B70780C10

FASTA46151,735
        10         20         30         40         50         60 
MLKKEINVVI LAAGKGTRMQ SSYPKVLHKL GGKTILEHVI NIAKSVKPKK IILVYNNKEK 

        70         80         90        100        110        120 
EIKSKISDTS IDWVIQKEQK GTGDAILKAS KKFSDKDDIV VLYGDMPYIS IESIKKLFTS 

       130        140        150        160        170        180 
KKQSDISLLT AYVKNPDGYG RVFKKNGKVI KIIEEQDANF HEKKIKEVYS GTFIANGKDL 

       190        200        210        220        230        240 
KRWLNQINNK NIKKEFYATD IVHFANLENS TIKTVQVLNC KEILGVNNKL QLSILEKIFR 

       250        260        270        280        290        300 
KKQVNDLLLS GVTLKDPNHF ILRGILKHGK NIEIDTGVIL EGNIILGNNI KIGVGSVIKN 

       310        320        330        340        350        360 
SFIDDQTEIK EYTIIENVKI GKKCIIGPFA HLRPKTVLDD QIHVGNFVEI KDSIIKKESK 

       370        380        390        400        410        420 
IKHLSYFGNS EIGSQVNIGA GSITCNYDGV NKFKTIIGDN VLIGANTKLI APIKITKNAT 

       430        440        450        460 
IAAGTTLTQD VNTPCLIYNN KEQKQKKNWK RPQKIIKKTD Q

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE013218 Genomic DNA. Translation: AAM67599.1.
RefSeqNP_660388.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8KA74.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBUCT00000000480; EBBUCP00000000480; EBBUCG00000000480.
GeneID1005844.
GenomeReviewsGene locus BUsg_028 in contig AE013218_GR.
KEGGbas:BUsg028.
PATRIC21246813. VBIBucAph100086_0028.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000008186.
HOGENOMHBG688195.
OMAGSKVNHL.
ProtClustDBCLSK493047.

Enzyme and pathway databases

BioCycBAPH198804:BUSG028-MONOMER.

Family and domain databases

HAMAPMF_01631. GlmU.
[Tree]
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR011004. Trimer_LpxA-like.
[Graphical view]
KOK04042.
PANTHERPTHR22572:SF17. PTHR22572:SF17. 1 hit.
PfamPF00132. Hexapep. 2 hits.
[Graphical view]
SUPFAMSSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMsTIGR01173. GlmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_BUCAP
AccessionPrimary (citable) accession number: Q8KA74
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 67 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. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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