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A2RMV7

- GLMU_LACLM

UniProt

A2RMV7 - GLMU_LACLM

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Protein
Bifunctional protein GlmU
Gene
glmU, llmg_2076
Organism
Lactococcus lactis subsp. cremoris (strain MG1363)
Status
Reviewed - 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 By similarity.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

Binds 1 magnesium ion per subunit By similarity.UniRule annotation

Pathwayi

Sites

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

GO - Molecular functioni

  1. UDP-N-acetylglucosamine diphosphorylase activity Source: UniProtKB-HAMAP
  2. glucosamine-1-phosphate N-acetyltransferase activity Source: UniProtKB-HAMAP
  3. magnesium ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. UDP-N-acetylglucosamine biosynthetic process Source: UniProtKB-UniPathway
  2. cell morphogenesis Source: UniProtKB-HAMAP
  3. lipid A biosynthetic process Source: UniProtKB-UniPathway
  4. lipopolysaccharide biosynthetic process Source: InterPro
  5. peptidoglycan biosynthetic process Source: UniProtKB-HAMAP
  6. regulation of cell shape Source: UniProtKB-KW
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 GlmU
Including the following 2 domains:
UDP-N-acetylglucosamine pyrophosphorylase (EC:2.7.7.23)
Alternative name(s):
N-acetylglucosamine-1-phosphate uridyltransferase
Glucosamine-1-phosphate N-acetyltransferase (EC:2.3.1.157)
Gene namesi
Name:glmU
Ordered Locus Names:llmg_2076
OrganismiLactococcus lactis subsp. cremoris (strain MG1363)
Taxonomic identifieri416870 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus
ProteomesiUP000000364: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 458458Bifunctional protein GlmUUniRule annotation
PRO_1000056169Add
BLAST

Interactioni

Subunit structurei

Homotrimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi416870.llmg_2076.

Structurei

3D structure databases

ProteinModelPortaliA2RMV7.
SMRiA2RMV7. Positions 2-452.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 229229Pyrophosphorylase By similarity
Add
BLAST
Regioni8 – 114UDP-GlcNAc binding By similarity
Regioni77 – 782UDP-GlcNAc binding By similarity
Regioni230 – 25021Linker By similarity
Add
BLAST
Regioni251 – 458208N-acetyltransferase By similarity
Add
BLAST

Sequence similaritiesi

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.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1207.
HOGENOMiHOG000283476.
KOiK04042.
OMAiDCVTNQD.
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

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MNKFAIVLAA GKGTRMKSAL PKVLHQVAGK SMLAHVLKSV SEVEIAKNVV    50
IVGHEADRVI ATLPKGTQFV KQVEQLGTGH AVRIAADLLA NEEGATLVIA 100
GDTPLITGET LGALFDYHFA QKATATILTA IAPNPTGYGR IIRDEKDSVE 150
KIVEQKDANA FEKSITEINT GTYIFDNKSL FKALTEITTD NAQGEYYLTD 200
VIEIFKKVGQ TIAAHILDDF DESLGVNDRV ALSQAEATMR KRINHEHMVN 250
GVTLIDPATT YIDSEVTIGA ETVIEANVTI KGNTFIGKNV LITNGSRIEN 300
SEIHSNCEVR NSTVEESRMS VGSNVGPYAH LRPGTVLSEE VHVGNFVEIK 350
GSTLGKGTKA GHLTYIGNAT VGEKVNFGAG TITANFDGKN KFNTEIDDFA 400
FIGSNSTIIA PLHIGKNALT AAGSVVTEDV PDEAVEIGRG KQVNKLGRAK 450
KMPHYRGQ 458
Length:458
Mass (Da):49,122
Last modified:March 6, 2007 - v1
Checksum:i316B0BCDDC8F6546
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
GeneIDi4797872.
KEGGillm:llmg_2076.
PATRICi22285342. VBILacLac4574_2123.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM406671 Genomic DNA. Translation: CAL98643.1 .
RefSeqi WP_011835789.1. NC_009004.1.
YP_001033331.1. NC_009004.1.

3D structure databases

ProteinModelPortali A2RMV7.
SMRi A2RMV7. Positions 2-452.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 416870.llmg_2076.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAL98643 ; CAL98643 ; llmg_2076 .
GeneIDi 4797872.
KEGGi llm:llmg_2076.
PATRICi 22285342. VBILacLac4574_2123.

Phylogenomic databases

eggNOGi COG1207.
HOGENOMi HOG000283476.
KOi K04042.
OMAi DCVTNQD.
OrthoDBi EOG6Z6FQZ.

Enzyme and pathway databases

UniPathwayi UPA00113 ; UER00532 .
UPA00113 ; UER00533 .
UPA00973 .
BioCyci LLAC416870:GCDT-2078-MONOMER.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
HAMAPi MF_01631. GlmU.
InterProi IPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR005835. NTP_transferase.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view ]
Pfami PF00132. Hexapep. 2 hits.
PF00483. NTP_transferase. 1 hit.
[Graphical view ]
SUPFAMi SSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsi TIGR01173. glmU. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 57 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

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