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Protein

Bifunctional protein GlmU

Gene

glmU

Organism
Lactococcus lactis subsp. cremoris (strain MG1363)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate.UniRule annotation
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Pathway: UDP-N-acetyl-alpha-D-glucosamine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Bifunctional protein GlmU (glmU)
This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II), the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.

Pathway: UDP-N-acetyl-alpha-D-glucosamine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional protein GlmU (glmU)
This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate, the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.

Pathway: LPS lipid A biosynthesis

This protein is involved in the pathway LPS lipid A biosynthesis, which is part of Bacterial outer membrane biogenesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway LPS lipid A biosynthesis and in Bacterial outer membrane biogenesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei22 – 221UDP-GlcNAcUniRule annotation
Binding sitei72 – 721UDP-GlcNAcUniRule annotation
Metal bindingi102 – 1021MagnesiumUniRule annotation
Binding sitei139 – 1391UDP-GlcNAc; via amide nitrogenUniRule annotation
Binding sitei154 – 1541UDP-GlcNAcUniRule annotation
Binding sitei169 – 1691UDP-GlcNAcUniRule annotation
Metal bindingi227 – 2271MagnesiumUniRule annotation
Binding sitei227 – 2271UDP-GlcNAcUniRule annotation
Binding sitei332 – 3321Acetyl-CoA; amide nitrogenUniRule annotation
Binding sitei350 – 3501Acetyl-CoAUniRule annotation
Active sitei362 – 3621Proton acceptorUniRule annotation
Binding sitei365 – 3651Acetyl-CoAUniRule annotation
Binding sitei376 – 3761Acetyl-CoAUniRule annotation
Binding sitei404 – 4041Acetyl-CoAUniRule annotation
Binding sitei422 – 4221Acetyl-CoA; via amide nitrogenUniRule annotation
Binding sitei439 – 4391Acetyl-CoAUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciLLAC416870:GCDT-2078-MONOMER.
UniPathwayiUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional protein GlmUUniRule annotation
Including the following 2 domains:
UDP-N-acetylglucosamine pyrophosphorylaseUniRule annotation (EC:2.7.7.23UniRule annotation)
Alternative name(s):
N-acetylglucosamine-1-phosphate uridyltransferaseUniRule annotation
Glucosamine-1-phosphate N-acetyltransferaseUniRule annotation (EC:2.3.1.157UniRule annotation)
Gene namesi
Name:glmUUniRule annotation
Ordered Locus Names:llmg_2076
OrganismiLactococcus lactis subsp. cremoris (strain MG1363)
Taxonomic identifieri416870 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus
ProteomesiUP000000364 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 458458Bifunctional protein GlmUPRO_1000056169Add
BLAST

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Protein-protein interaction databases

STRINGi416870.llmg_2076.

Structurei

3D structure databases

ProteinModelPortaliA2RMV7.
SMRiA2RMV7. Positions 2-452.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 229229PyrophosphorylaseUniRule annotationAdd
BLAST
Regioni8 – 114UDP-GlcNAc bindingUniRule annotation
Regioni77 – 782UDP-GlcNAc bindingUniRule annotation
Regioni230 – 25021LinkerUniRule annotationAdd
BLAST
Regioni251 – 458208N-acetyltransferaseUniRule annotationAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.UniRule annotation
In the C-terminal section; belongs to the transferase hexapeptide repeat family.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1207.
HOGENOMiHOG000283476.
KOiK04042.
OMAiFAHARPK.
OrthoDBiEOG6Z6FQZ.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU.
InterProiIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR005835. NTP_transferase.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 2 hits.
PF00483. NTP_transferase. 1 hit.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR01173. glmU. 1 hit.

Sequencei

Sequence statusi: Complete.

A2RMV7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKFAIVLAA GKGTRMKSAL PKVLHQVAGK SMLAHVLKSV SEVEIAKNVV
60 70 80 90 100
IVGHEADRVI ATLPKGTQFV KQVEQLGTGH AVRIAADLLA NEEGATLVIA
110 120 130 140 150
GDTPLITGET LGALFDYHFA QKATATILTA IAPNPTGYGR IIRDEKDSVE
160 170 180 190 200
KIVEQKDANA FEKSITEINT GTYIFDNKSL FKALTEITTD NAQGEYYLTD
210 220 230 240 250
VIEIFKKVGQ TIAAHILDDF DESLGVNDRV ALSQAEATMR KRINHEHMVN
260 270 280 290 300
GVTLIDPATT YIDSEVTIGA ETVIEANVTI KGNTFIGKNV LITNGSRIEN
310 320 330 340 350
SEIHSNCEVR NSTVEESRMS VGSNVGPYAH LRPGTVLSEE VHVGNFVEIK
360 370 380 390 400
GSTLGKGTKA GHLTYIGNAT VGEKVNFGAG TITANFDGKN KFNTEIDDFA
410 420 430 440 450
FIGSNSTIIA PLHIGKNALT AAGSVVTEDV PDEAVEIGRG KQVNKLGRAK

KMPHYRGQ
Length:458
Mass (Da):49,122
Last modified:March 6, 2007 - v1
Checksum:i316B0BCDDC8F6546
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM406671 Genomic DNA. Translation: CAL98643.1.
RefSeqiWP_011835789.1. NC_009004.1.
YP_001033331.1. NC_009004.1.

Genome annotation databases

EnsemblBacteriaiCAL98643; CAL98643; llmg_2076.
KEGGillm:llmg_2076.
PATRICi22285342. VBILacLac4574_2123.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM406671 Genomic DNA. Translation: CAL98643.1.
RefSeqiWP_011835789.1. NC_009004.1.
YP_001033331.1. NC_009004.1.

3D structure databases

ProteinModelPortaliA2RMV7.
SMRiA2RMV7. Positions 2-452.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi416870.llmg_2076.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAL98643; CAL98643; llmg_2076.
KEGGillm:llmg_2076.
PATRICi22285342. VBILacLac4574_2123.

Phylogenomic databases

eggNOGiCOG1207.
HOGENOMiHOG000283476.
KOiK04042.
OMAiFAHARPK.
OrthoDBiEOG6Z6FQZ.

Enzyme and pathway databases

UniPathwayiUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.
BioCyciLLAC416870:GCDT-2078-MONOMER.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU.
InterProiIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR005835. NTP_transferase.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 2 hits.
PF00483. NTP_transferase. 1 hit.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR01173. glmU. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiGLMU_LACLM
AccessioniPrimary (citable) accession number: A2RMV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 6, 2007
Last modified: May 27, 2015
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.