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Q494C1 (GLMU_BLOPB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 65. 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:BPEN_010
OrganismBlochmannia pennsylvanicus (strain BPEN) [Complete proteome] [HAMAP]
Taxonomic identifier291272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeant endosymbiontsCandidatus Blochmannia

Protein attributes

Sequence length462 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 – 462462Bifunctional protein GlmU HAMAP-Rule MF_01631
PRO_0000233739

Regions

Region1 – 235235Pyrophosphorylase By similarity
Region11 – 144UDP-GlcNAc binding By similarity
Region85 – 862UDP-GlcNAc binding By similarity
Region107 – 1093UDP-GlcNAc binding By similarity
Region236 – 25621Linker By similarity
Region257 – 462206N-acetyltransferase By similarity
Region392 – 3932Acetyl-CoA binding By similarity

Sites

Active site3691Proton acceptor By similarity
Metal binding1091Magnesium By similarity
Metal binding2331Magnesium By similarity
Binding site251UDP-GlcNAc By similarity
Binding site801UDP-GlcNAc By similarity
Binding site1441UDP-GlcNAc; via amide nitrogen By similarity
Binding site1591UDP-GlcNAc By similarity
Binding site2331UDP-GlcNAc By similarity
Binding site3391Acetyl-CoA; amide nitrogen By similarity
Binding site3571Acetyl-CoA By similarity
Binding site3721Acetyl-CoA By similarity
Binding site3831Acetyl-CoA By similarity
Binding site4291Acetyl-CoA; via amide nitrogen By similarity
Binding site4461Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q494C1 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 9E857B19A26FCFD2

FASTA46251,550
        10         20         30         40         50         60 
MSYINFSAII LAAGRGNRML SDTPKVLYQI GGKFMLQHLI DSVMQVGVSS IYVVHGYKGE 

        70         80         90        100        110        120 
MIIKEINTNQ YKIPVYWILQ HDLTGTGDAV QRVLPFISDD EEVLVLYGDV PFVSYKTLQR 

       130        140        150        160        170        180 
LHVIKSQCDI SMLTATLPNP KGYGRIVRNQ EGSVVSIIEH DDIINDDQKK IKEVSTGIFI 

       190        200        210        220        230        240 
AISNHLKCWL STLTTHKSKN EFYLTDIIQI AHQSGYSIHT MCPDDTFEIM GVNSKSDFVD 

       250        260        270        280        290        300 
LDKQYQQRKV QCLLSSGLMI IDPNRFDLRG TLVHGKDVYI DINVIIEGHV SLGNRVKIGA 

       310        320        330        340        350        360 
SCILKDTIVA DDVEIYPFSI IENTTIGFQS KVGPFVRLRP GTELKEKSHV GNFVEIKNTR 

       370        380        390        400        410        420 
LGEQSKVKHL SYLGDAEIGN QVNIGAGTII CNYDGMMKHQ TIIGDDVFIG ADSQLVAPIT 

       430        440        450        460 
IGKNVTIGAG TTVTRDVAAN ETIISRIRQF SILNWKRLKN KK 

« Hide

References

[1]"Genome sequence of Blochmannia pennsylvanicus indicates parallel evolutionary trends among bacterial mutualists of insects."
Degnan P.H., Lazarus A.B., Wernegreen J.J.
Genome Res. 15:1023-1033(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BPEN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000016 Genomic DNA. Translation: AAZ40660.1.
RefSeqYP_277532.1. NC_007292.1.

3D structure databases

ProteinModelPortalQ494C1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING291272.BPEN_010.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ40660; AAZ40660; BPEN_010.
GeneID3562625.
KEGGbpn:BPEN_010.
PATRIC31964906. VBICanBlo110049_0010.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHOG000283476.
KOK04042.
OMADCVTNQD.
OrthoDBEOG6Z6FQZ.

Enzyme and pathway databases

BioCycBPEN291272:GJ9N-16-MONOMER.
UniPathwayUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
HAMAPMF_01631. GlmU.
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR025877. MobA-like_NTP_Trfase_dom.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamPF00132. Hexapep. 3 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMSSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsTIGR01173. glmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_BLOPB
AccessionPrimary (citable) accession number: Q494C1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: September 13, 2005
Last modified: June 11, 2014
This is version 65 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