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A2RMV7 (GLMU_LACLM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:llmg_2076
OrganismLactococcus lactis subsp. cremoris (strain MG1363) [Complete proteome] [HAMAP]
Taxonomic identifier416870 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length458 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 – 458458Bifunctional protein GlmU HAMAP-Rule MF_01631
PRO_1000056169

Regions

Region1 – 229229Pyrophosphorylase By similarity
Region8 – 114UDP-GlcNAc binding By similarity
Region77 – 782UDP-GlcNAc binding By similarity
Region230 – 25021Linker By similarity
Region251 – 458208N-acetyltransferase By similarity

Sites

Active site3621Proton acceptor By similarity
Metal binding1021Magnesium By similarity
Metal binding2271Magnesium By similarity
Binding site221UDP-GlcNAc By similarity
Binding site721UDP-GlcNAc By similarity
Binding site1391UDP-GlcNAc; via amide nitrogen By similarity
Binding site1541UDP-GlcNAc By similarity
Binding site1691UDP-GlcNAc By similarity
Binding site2271UDP-GlcNAc By similarity
Binding site3321Acetyl-CoA; amide nitrogen By similarity
Binding site3501Acetyl-CoA By similarity
Binding site3651Acetyl-CoA By similarity
Binding site3761Acetyl-CoA By similarity
Binding site4041Acetyl-CoA By similarity
Binding site4221Acetyl-CoA; via amide nitrogen By similarity
Binding site4391Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
A2RMV7 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: 316B0BCDDC8F6546

FASTA45849,122
        10         20         30         40         50         60 
MNKFAIVLAA GKGTRMKSAL PKVLHQVAGK SMLAHVLKSV SEVEIAKNVV IVGHEADRVI 

        70         80         90        100        110        120 
ATLPKGTQFV KQVEQLGTGH AVRIAADLLA NEEGATLVIA GDTPLITGET LGALFDYHFA 

       130        140        150        160        170        180 
QKATATILTA IAPNPTGYGR IIRDEKDSVE KIVEQKDANA FEKSITEINT GTYIFDNKSL 

       190        200        210        220        230        240 
FKALTEITTD NAQGEYYLTD VIEIFKKVGQ TIAAHILDDF DESLGVNDRV ALSQAEATMR 

       250        260        270        280        290        300 
KRINHEHMVN GVTLIDPATT YIDSEVTIGA ETVIEANVTI KGNTFIGKNV LITNGSRIEN 

       310        320        330        340        350        360 
SEIHSNCEVR NSTVEESRMS VGSNVGPYAH LRPGTVLSEE VHVGNFVEIK GSTLGKGTKA 

       370        380        390        400        410        420 
GHLTYIGNAT VGEKVNFGAG TITANFDGKN KFNTEIDDFA FIGSNSTIIA PLHIGKNALT 

       430        440        450 
AAGSVVTEDV PDEAVEIGRG KQVNKLGRAK KMPHYRGQ 

« Hide

References

[1]"The complete genome sequence of the lactic acid bacterial paradigm Lactococcus lactis subsp. cremoris MG1363."
Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C., Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P., van Sinderen D., Kok J.
J. Bacteriol. 189:3256-3270(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MG1363.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM406671 Genomic DNA. Translation: CAL98643.1.
RefSeqYP_001033331.1. NC_009004.1.

3D structure databases

ProteinModelPortalA2RMV7.
SMRA2RMV7. Positions 2-452.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING416870.llmg_2076.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL98643; CAL98643; llmg_2076.
GeneID4797872.
KEGGllm:llmg_2076.
PATRIC22285342. VBILacLac4574_2123.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHOG000283476.
KOK04042.
OMANKHKTII.
OrthoDBEOG6Z6FQZ.
ProtClustDBPRK14354.

Enzyme and pathway databases

BioCycLLAC416870:GCDT-2078-MONOMER.
UniPathwayUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Family and domain databases

HAMAPMF_01631. GlmU.
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR005835. NTP_transferase.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamPF00132. Hexapep. 2 hits.
PF00483. NTP_transferase. 1 hit.
[Graphical view]
SUPFAMSSF51161. SSF51161. 1 hit.
TIGRFAMsTIGR01173. glmU. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLMU_LACLM
AccessionPrimary (citable) accession number: A2RMV7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 6, 2007
Last modified: February 19, 2014
This is version 54 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