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C4KN38 (C4KN38_BURPE) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Bifunctional protein GlmU HAMAP-Rule MF_01631
Gene names
Name:glmU HAMAP-Rule MF_01631 EMBL ACQ97373.1
ORF Names:GBP346_A0244 EMBL ACQ97373.1
OrganismBurkholderia pseudomallei MSHR346 EMBL ACQ97373.1
Taxonomic identifier536230 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group ›

Protein attributes

Sequence length453 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 SAAS SAAS005882

Catalytic activity

Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate. HAMAP-Rule MF_01631 SAAS SAAS005882

UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine. HAMAP-Rule MF_01631 SAAS SAAS005882

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01631 SAAS SAAS005882

Pathway

Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. HAMAP-Rule MF_01631 SAAS SAAS005882

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 SAAS SAAS005882

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. HAMAP-Rule MF_01631 SAAS SAAS005882

Subunit structure

Homotrimer By similarity. HAMAP-Rule MF_01631 SAAS SAAS005882

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01631 SAAS SAAS005882.

Sequence similarities

In the C-terminal section; belongs to the transferase hexapeptide repeat family. HAMAP-Rule MF_01631

In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family. HAMAP-Rule MF_01631

Ontologies

Keywords
   Biological processCell shape
Cell wall biogenesis/degradation HAMAP-Rule MF_01631 SAAS SAAS005882
Peptidoglycan synthesis HAMAP-Rule MF_01631 SAAS SAAS005882
   Cellular componentCytoplasm HAMAP-Rule MF_01631 SAAS SAAS005882
   DomainRepeat HAMAP-Rule MF_01631 SAAS SAAS005882
   LigandMagnesium HAMAP-Rule MF_01631 SAAS SAAS005882
Metal-binding HAMAP-Rule MF_01631 SAAS SAAS005882
   Molecular functionAcyltransferase HAMAP-Rule MF_01631 SAAS SAAS005882 EMBL ACQ97373.1
Nucleotidyltransferase HAMAP-Rule MF_01631 SAAS SAAS005882 EMBL ACQ97373.1
Transferase
   Technical termMultifunctional enzyme HAMAP-Rule MF_01631 SAAS SAAS005882
Gene Ontology (GO)
   Biological_processUDP-N-acetylglucosamine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

cell morphogenesis

Inferred from electronic annotation. Source: HAMAP

lipid A biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

lipopolysaccharide biosynthetic process

Inferred from electronic annotation. Source: InterPro

peptidoglycan biosynthetic process

Inferred from electronic annotation. Source: HAMAP

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionUDP-N-acetylglucosamine diphosphorylase activity

Inferred from electronic annotation. Source: HAMAP

glucosamine-1-phosphate N-acetyltransferase activity

Inferred from electronic annotation. Source: HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region1 – 225225Pyrophosphorylase By similarity HAMAP-Rule MF_01631
Region6 – 94UDP-GlcNAc binding By similarity HAMAP-Rule MF_01631
Region76 – 772UDP-GlcNAc binding By similarity HAMAP-Rule MF_01631
Region98 – 1003UDP-GlcNAc binding By similarity HAMAP-Rule MF_01631
Region226 – 24621Linker By similarity HAMAP-Rule MF_01631
Region247 – 453207N-acetyltransferase By similarity HAMAP-Rule MF_01631
Region382 – 3832Acetyl-CoA binding By similarity HAMAP-Rule MF_01631

Sites

Active site3591Proton acceptor By similarity HAMAP-Rule MF_01631
Metal binding1001Magnesium By similarity HAMAP-Rule MF_01631
Metal binding2231Magnesium By similarity HAMAP-Rule MF_01631
Binding site201UDP-GlcNAc By similarity HAMAP-Rule MF_01631
Binding site711UDP-GlcNAc By similarity HAMAP-Rule MF_01631
Binding site1351UDP-GlcNAc; via amide nitrogen By similarity HAMAP-Rule MF_01631
Binding site1501UDP-GlcNAc By similarity HAMAP-Rule MF_01631
Binding site1651UDP-GlcNAc By similarity HAMAP-Rule MF_01631
Binding site2231UDP-GlcNAc By similarity HAMAP-Rule MF_01631
Binding site3291Acetyl-CoA; amide nitrogen By similarity HAMAP-Rule MF_01631
Binding site3471Acetyl-CoA By similarity HAMAP-Rule MF_01631
Binding site3621Acetyl-CoA By similarity HAMAP-Rule MF_01631
Binding site3731Acetyl-CoA By similarity HAMAP-Rule MF_01631
Binding site4011Acetyl-CoA By similarity HAMAP-Rule MF_01631
Binding site4191Acetyl-CoA; via amide nitrogen By similarity HAMAP-Rule MF_01631

Sequences

Sequence LengthMass (Da)Tools
C4KN38 [UniParc].

Last modified July 7, 2009. Version 1.
Checksum: DD66245B6F0CA1AB

FASTA45347,610
        10         20         30         40         50         60 
MNIVILAAGT GKRMRSALPK VLHPLAGRPL LSHVIDTARA LAPSRLVVVI GHGAEQVRAA 

        70         80         90        100        110        120 
VAAPDVQFAV QEQQLGTGHA VRQALPLLDP SQPTLVLYGD VPLTRTATLK RLADAATDAR 

       130        140        150        160        170        180 
YGVLTVTLDD PTGYGRIVRD QAGCVTRIVE QKDASPDELR IDEINTGIVV APTAQLSMWL 

       190        200        210        220        230        240 
GALGNDNAQG EYYLTDVVEQ AIEAGFEIVT TQPDDEWETL GVNSKAQLAE LERIHQRNLA 

       250        260        270        280        290        300 
DALLAAGVTL ADPARIDVRG TLTCGRDVSI DVNCVFEGDV TLADGVTIGA NCVIRHAAIA 

       310        320        330        340        350        360 
AGARVDAFSH LDGATVGANA VVGPYARLRP GAVLAADAHV GNFVEVKNAT LGQGSKANHL 

       370        380        390        400        410        420 
TYLGDADIGA RVNVGAGTIT CNYDGANKFR TVIEDDVFVG SDTQFVAPVR VGRGVTVAAG 

       430        440        450 
TTVWKDVAAD MLVLNDKTQT AKSGYVRPVK KKS

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References

[1]Harkins D.M., Brinkac L.M., Rogers Y.C., Detter J.C., Munk A.C., Bruce D.C., Keim P., Sims D.R., Brettin T.S.
Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: MSHR346 EMBL ACQ97373.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001408 Genomic DNA. Translation: ACQ97373.1.
RefSeqYP_002894971.1. NC_012695.1.

3D structure databases

ProteinModelPortalC4KN38.
SMRC4KN38. Positions 1-447.
ModBaseSearch...

Protein-protein interaction databases

STRING536230.GBP346_A0244.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACQ97373; ACQ97373; GBP346_A0244.
GeneID7890883.
KEGGbpr:GBP346_A0244.
PATRIC32569753. VBIBurPse130472_0219.

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHOG000283476.
KOK04042.
ProtClustDBCLSK930247.

Enzyme and pathway databases

BioCycBPSE536230:GHVQ-307-MONOMER.
UniPathwayUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Family and domain databases

HAMAPMF_01631. GlmU.
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR025877. MobA-like_NTP_Trfase_dom.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PANTHERPTHR22572:SF17. PTHR22572:SF17. 1 hit.
PfamPF00132. Hexapep. 4 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMSSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMsTIGR01173. glmU. 1 hit.
ProtoNetSearch...

Entry information

Entry nameC4KN38_BURPE
AccessionPrimary (citable) accession number: C4KN38
Entry history
Integrated into UniProtKB/TrEMBL: July 7, 2009
Last sequence update: July 7, 2009
Last modified: April 3, 2013
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info