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Q7VQV4 (GLMU_BLOFL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Bfl010
OrganismBlochmannia floridanus [Complete proteome] [HAMAP]
Taxonomic identifier203907 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › ant endosymbionts › Candidatus Blochmannia

Protein attributes

Sequence length465 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

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 – 465465Bifunctional protein GlmU HAMAP MF_01631
PRO_0000233738

Regions

Region1 – 237237Pyrophosphorylase By similarity
Region11 – 144Substrate binding By similarity
Region85 – 862Substrate binding By similarity
Region238 – 25821Linker By similarity
Region259 – 465207N-acetyltransferase By similarity

Sites

Active site3711Proton acceptor By similarity
Metal binding1101Magnesium By similarity
Metal binding2351Magnesium By similarity
Binding site801Substrate By similarity
Binding site1451Substrate; via amide nitrogen By similarity
Binding site1601Substrate By similarity
Binding site3951Acetyl-CoA By similarity
Binding site4311Acetyl-CoA; via amide nitrogen By similarity
Binding site4481Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VQV4 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: F651C7E6DEF99D8D

FASTA46551,831
        10         20         30         40         50         60 
MLRKKYSVII LAAGQGKRML SSIPKVMHKI AGRSMLQHLI DSVSKINIQS IYIVYNESLR 

        70         80         90        100        110        120 
EFIPTIYSNK CTISIYWVLQ ESVRGTGYAV QQVLSMIHDD NEDILILYGD VPLISDKTLN 

       130        140        150        160        170        180 
NLCLMKSKCD IGLLTAYVKN PQGYGRIIRN QYGDVVSIIE DIDIVNQNDR IIKEIHSGIF 

       190        200        210        220        230        240 
ISVSGYLKSW LNYLIENNLW CNELYLTAII DIAYKNNFVI NAIHPVDVCE VIGINNKSDL 

       250        260        270        280        290        300 
VKAERVYQIK EAQKLLELGV MISDLNRFDL RGKLVCGEDV CIDVNVIIEG CVSLGNRVKI 

       310        320        330        340        350        360 
GASCILKDVE IGDDVIIYPF SFIENSKIHC KSKIGPFARL RPGTCLQEQV HIGNFVELKN 

       370        380        390        400        410        420 
IKLGNNSKVG HLSYLGDADV GNYVNIGAGT IICNYNGKTK NYTCIEDNVF VGADSQLVAP 

       430        440        450        460 
ITIGKNAVIG AGTTVTQNVD KDDVIISRVR QFSIVNDKVD KNKKN

« Hide

References

[1]"The genome sequence of Blochmannia floridanus: comparative analysis of reduced genomes."
Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F., Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B., van Ham R.C.H.J., Gross R., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003) [PubMed: 12886019] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX248583 Genomic DNA. Translation: CAD83538.1.
RefSeqNP_878325.1. NC_005061.1.

3D structure databases

ProteinModelPortalQ7VQV4.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7VQV4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1499210.
GenomeReviewsGene locus Bfl010 in contig BX248583_GR.
KEGGbfl:Bfl010.
PATRIC31963605. VBICanBlo38691_0010.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHBG688195.
OMAGSKVNHL.
PhylomeDBQ7VQV4.
ProtClustDBCLSK492480.

Enzyme and pathway databases

BioCycCBLO203907:BFL010-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_BLOFL
AccessionPrimary (citable) accession number: Q7VQV4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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