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Q04DS4

- GLMU_OENOB

UniProt

Q04DS4 - GLMU_OENOB

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Protein
Bifunctional protein GlmU
Gene
glmU, OEOE_1542
Organism
Oenococcus oeni (strain ATCC BAA-331 / PSU-1)
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 sitei23 – 231UDP-GlcNAc By similarity
Binding sitei69 – 691UDP-GlcNAc By similarity
Metal bindingi97 – 971Magnesium By similarity
Binding sitei132 – 1321UDP-GlcNAc; via amide nitrogen By similarity
Binding sitei148 – 1481UDP-GlcNAc By similarity
Binding sitei163 – 1631UDP-GlcNAc By similarity
Metal bindingi214 – 2141Magnesium By similarity
Binding sitei214 – 2141UDP-GlcNAc By similarity
Binding sitei286 – 2861Acetyl-CoA; amide nitrogen By similarity
Binding sitei304 – 3041Acetyl-CoA By similarity
Active sitei316 – 3161Proton acceptor By similarity
Binding sitei319 – 3191Acetyl-CoA By similarity
Binding sitei330 – 3301Acetyl-CoA By similarity
Binding sitei358 – 3581Acetyl-CoA By similarity
Binding sitei376 – 3761Acetyl-CoA; via amide nitrogen By similarity
Binding sitei393 – 3931Acetyl-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

BioCyciOOEN203123:GHNL-1542-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:OEOE_1542
OrganismiOenococcus oeni (strain ATCC BAA-331 / PSU-1)
Taxonomic identifieri203123 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLeuconostocaceaeOenococcus
ProteomesiUP000000774: 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 – 426426Bifunctional protein GlmUUniRule annotation
PRO_1000069734Add
BLAST

Interactioni

Subunit structurei

Homotrimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi203123.OEOE_1542.

Structurei

3D structure databases

ProteinModelPortaliQ04DS4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 216216Pyrophosphorylase By similarity
Add
BLAST
Regioni9 – 124UDP-GlcNAc binding By similarity
Regioni217 – 23721Linker By similarity
Add
BLAST
Regioni238 – 426189N-acetyltransferase By similarity
Add
BLAST
Regioni339 – 3402Acetyl-CoA binding By similarity

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.
OMAiCNIAAGT.
OrthoDBiEOG6Z6FQZ.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU.
InterProiIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR025877. MobA-like_NTP_Trfase_dom.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 3 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

Q04DS4-1 [UniParc]FASTAAdd to Basket

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MSEVDVVILA AGKGSRMKDD LSKPLHKVAG LPMLEWICRA VRKFNPKNII    50
AVQGADEDFS SYVDETVVQK EQLGSADALR CAFPKIDAEK LIVINADMPL 100
MTENDLVDLV EKGEGFDAAL LTADLKKPFG YGRVIPVGER NVVEQIVEER 150
DATADQKKLH LVNAGVYLFR ADYIKRAINN VTTDNSQSEY YLTDALPGAK 200
IVQVADWHDI LGVNTQQQLA AVSKIARKRI NDQIMANGVT MIDPLTTYID 250
ANVLVGTGTI IKPGTVIEHD SVIGAENEIG PYAHLREKTV TGIDVHIGNF 300
VETKNAKIGD HTHIGHLTYV GDAEVGQAVN IGAGTIFVNY DGKNKHMTKV 350
GDRAFIGSNS KLVAPVEIAS EAITAAGSTI TDNVDQHAMG IARQRQTNKS 400
DFWQRMPHED FATEYDAKHD QRDDQP 426
Length:426
Mass (Da):46,641
Last modified:November 14, 2006 - v1
Checksum:iCCDF7323AEBC1E01
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000411 Genomic DNA. Translation: ABJ57398.1.
RefSeqiWP_011677759.1. NC_008528.1.
YP_811063.1. NC_008528.1.

Genome annotation databases

EnsemblBacteriaiABJ57398; ABJ57398; OEOE_1542.
GeneIDi4415811.
KEGGiooe:OEOE_1542.
PATRICi22801324. VBIOenOen113004_1568.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000411 Genomic DNA. Translation: ABJ57398.1 .
RefSeqi WP_011677759.1. NC_008528.1.
YP_811063.1. NC_008528.1.

3D structure databases

ProteinModelPortali Q04DS4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 203123.OEOE_1542.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABJ57398 ; ABJ57398 ; OEOE_1542 .
GeneIDi 4415811.
KEGGi ooe:OEOE_1542.
PATRICi 22801324. VBIOenOen113004_1568.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00113 ; UER00532 .
UPA00113 ; UER00533 .
UPA00973 .
BioCyci OOEN203123:GHNL-1542-MONOMER.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
HAMAPi MF_01631. GlmU.
InterProi IPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR025877. MobA-like_NTP_Trfase_dom.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view ]
Pfami PF00132. Hexapep. 3 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view ]
SUPFAMi SSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-331 / PSU-1.

Entry informationi

Entry nameiGLMU_OENOB
AccessioniPrimary (citable) accession number: Q04DS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 14, 2006
Last modified: September 3, 2014
This is version 65 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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