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A8EWU5 (GLMU_ARCB4) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. 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:Abu_2204
OrganismArcobacter butzleri (strain RM4018) [Complete proteome] [HAMAP]
Taxonomic identifier367737 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Arcobacter

Protein attributes

Sequence length432 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 – 432432Bifunctional protein GlmU HAMAP MF_01631
PRO_0000337706

Regions

Region1 – 223223Pyrophosphorylase By similarity
Region9 – 124Substrate binding By similarity
Region82 – 832Substrate binding By similarity
Region224 – 24421Linker By similarity
Region245 – 432188N-acetyltransferase By similarity

Sites

Active site3361Proton acceptor By similarity
Metal binding1031Magnesium By similarity
Metal binding2211Magnesium By similarity
Binding site751Substrate By similarity
Binding site1351Substrate; via amide nitrogen By similarity
Binding site1491Substrate By similarity
Binding site1641Substrate By similarity
Binding site3601Acetyl-CoA By similarity
Binding site3781Acetyl-CoA By similarity
Binding site3961Acetyl-CoA; via amide nitrogen By similarity
Binding site4131Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
A8EWU5 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: E2C3DCF7F321890E

FASTA43247,487
        10         20         30         40         50         60 
MGKKSIIILA AGAGTRMKSD TPKVLHKISG KPMLYYSIKE ALKLSDDITV VLYHQFEKVK 

        70         80         90        100        110        120 
AEIEKYFSNI NFVIQDHKNY PGTGGAVMGI TPKYEKVLVL NGDMPLIQAN ELEKFEINAT 

       130        140        150        160        170        180 
IVMSVLELES ADGYGRVIIE NGNVKKIVEQ KDASEDELKI TTANAGIYQF ETKFLLENLP 

       190        200        210        220        230        240 
KLDNNNAQKE YYITDLVEMA ISQGKVLKPL VVNEENFKGV NSKVELADAE VIHQNRIKKE 

       250        260        270        280        290        300 
FMKAGVIMRL PDTIYIEEGV EIEGESIIEN GVSLLGNAKI INSHIKTNSV VEDSIVKDSD 

       310        320        330        340        350        360 
VGPMGRVRPG SELTNTHIGN FVETKKAKLT GVKAGHLSYL GDCSIDEGTN IGCGTITCNY 

       370        380        390        400        410        420 
DGVNKHQTII GKNVFVGSDT QFVAPVNIED DVLIGAGSTV TGNVKKGELY LTRAKAKTID 

       430 
GFFYKHFSSK KK

« Hide

References

[1]"The complete genome sequence and analysis of the Epsilonproteobacterium Arcobacter butzleri."
Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M., Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A., Rogosin A., Stanker L.H., Mandrell R.E.
PLoS ONE 2:E1358-E1358(2007) [PubMed: 18159241] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RM4018.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000361 Genomic DNA. Translation: ABV68418.1.
RefSeqYP_001491088.1. NC_009850.1.

3D structure databases

ProteinModelPortalA8EWU5.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8EWU5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5625281.
GenomeReviewsGene locus Abu_2204 in contig CP000361_GR.
KEGGabu:Abu_2204.
PATRIC20965772. VBIArcBut20197_2147.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHBG688195.
OMAGSKVNHL.
ProtClustDBPRK14359.

Enzyme and pathway databases

BioCycABUT367737:ABU_2204-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. 1 hit.
[Graphical view]
SUPFAMSSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMsTIGR01173. GlmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_ARCB4
AccessionPrimary (citable) accession number: A8EWU5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 13, 2007
Last modified: January 25, 2012
This is version 35 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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