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Protein

UDP-N-acetylbacillosamine N-acetyltransferase

Gene

pglD

Organism
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acetyltransferase that modifies the UDP-4-amino-sugar to form UDP-N,N'-diacetylbacillosamine in the N-linked protein glycosylation pathway.2 Publications

Catalytic activityi

Acetyl-CoA + UDP-N-acetylbacillosamine = CoA + UDP-N,N'-diacetylbacillosamine.1 Publication

Kineticsi

kcat is 483000 min(-1) (PubMed:17087520). Kcat is 314 sec(-1) (PubMed:18667421).2 Publications

Manual assertion based on experiment ini

  1. KM=1.0 mM for UDP-N-acetylbacillosamine2 Publications
  2. KM=0.41 mM for UDP-N-acetylbacillosamine1 Publication
  1. Vmax=14700 nmol/sec/mg enzyme2 Publications

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.1 Publication
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei56Substrate; via amide nitrogen1
Active sitei125Proton acceptor1 Publication1
Sitei126Increases basicity of active site His1
Binding sitei134Acetyl-CoA1 Publication1
Binding sitei155Acetyl-CoA; via amide nitrogen1 Publication1
Binding sitei173Acetyl-CoA; via amide nitrogen and carbonyl oxygen1 Publication1

GO - Molecular functioni

GO - Biological processi

  • protein N-linked glycosylation via asparagine Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciCJEJ192222:GJTS-1052-MONOMER.
MetaCyc:MONOMER-17320.
BRENDAi2.3.1.203. 1087.
UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-N-acetylbacillosamine N-acetyltransferase (EC:2.3.1.203)
Alternative name(s):
Protein glycosylation D
UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine N-acetyltransferase
Gene namesi
Name:pglD
Ordered Locus Names:Cj1123c
OrganismiCampylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Taxonomic identifieri192222 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
Proteomesi
  • UP000000799 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi15H → A: Induces a higher KM and approximate 3-fold decrease in the turnover number. 1 Publication1
Mutagenesisi118N → A: Reduction in catalytic activity. 1 Publication1
Mutagenesisi124E → A: Reduction in catalytic activity. 1 Publication1
Mutagenesisi125H → A: Strong reduction in catalytic activity. 2 Publications1
Mutagenesisi134H → A: Slight reduction in catalytic activity. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004225851 – 195UDP-N-acetylbacillosamine N-acetyltransferaseAdd BLAST195

Proteomic databases

PaxDbiQ0P9D1.

Interactioni

Subunit structurei

Homotrimer.2 Publications

Protein-protein interaction databases

IntActiQ0P9D1. 3 interactors.
STRINGi192222.Cj1123c.

Structurei

Secondary structure

1195
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 10Combined sources6
Helixi15 – 26Combined sources12
Beta strandi29 – 34Combined sources6
Turni36 – 38Combined sources3
Helixi40 – 45Combined sources6
Beta strandi50 – 53Combined sources4
Helixi58 – 69Combined sources12
Turni70 – 72Combined sources3
Beta strandi89 – 91Combined sources3
Beta strandi181 – 183Combined sources3
Beta strandi186 – 188Combined sources3
Turni189 – 192Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NPOX-ray2.20A2-195[»]
2VHEX-ray1.80A/B2-195[»]
3BFPX-ray1.75A2-195[»]
3BSSX-ray2.30A1-195[»]
3BSWX-ray1.77A1-195[»]
3BSYX-ray1.80A/B/C1-195[»]
ProteinModelPortaliQ0P9D1.
SMRiQ0P9D1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ0P9D1.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni13 – 15Substrate binding3
Regioni35 – 36Substrate binding2

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105MME. Bacteria.
COG0110. LUCA.
HOGENOMiHOG000253005.
KOiK15913.
OMAiTVIMAGA.

Family and domain databases

CDDicd03360. LbH_AT_putative. 1 hit.
Gene3Di3.40.50.20. 1 hit.
InterProiIPR001451. Hexapep.
IPR016185. PreATP-grasp_dom.
IPR020019. Sia_OAcTrfase_NeuD-like.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 1 hit.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
TIGRFAMsiTIGR03570. NeuD_NnaD. 1 hit.

Sequencei

Sequence statusi: Complete.

Q0P9D1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARTEKIYIY GASGHGLVCE DVAKNMGYKE CIFLDDFKGM KFESTLPKYD
60 70 80 90 100
FFIAIGNNEI RKKIYQKISE NGFKIVNLIH KSALISPSAI VEENAGILIM
110 120 130 140 150
PYVVINAKAK IEKGVILNTS SVIEHECVIG EFSHVSVGAK CAGNVKIGKN
160 170 180 190
CFLGINSCVL PNLSLADDSI LGGGATLVKN QDEKGVFVGV PAKRM
Length:195
Mass (Da):21,148
Last modified:September 19, 2006 - v1
Checksum:i8C6312D439AE90E2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL111168 Genomic DNA. Translation: CAL35240.1.
PIRiF81316.
RefSeqiWP_002852865.1. NC_002163.1.
YP_002344516.1. NC_002163.1.

Genome annotation databases

EnsemblBacteriaiCAL35240; CAL35240; Cj1123c.
GeneIDi905414.
KEGGicje:Cj1123c.
PATRICi20059204. VBICamJej33762_1105.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL111168 Genomic DNA. Translation: CAL35240.1.
PIRiF81316.
RefSeqiWP_002852865.1. NC_002163.1.
YP_002344516.1. NC_002163.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NPOX-ray2.20A2-195[»]
2VHEX-ray1.80A/B2-195[»]
3BFPX-ray1.75A2-195[»]
3BSSX-ray2.30A1-195[»]
3BSWX-ray1.77A1-195[»]
3BSYX-ray1.80A/B/C1-195[»]
ProteinModelPortaliQ0P9D1.
SMRiQ0P9D1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ0P9D1. 3 interactors.
STRINGi192222.Cj1123c.

Proteomic databases

PaxDbiQ0P9D1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAL35240; CAL35240; Cj1123c.
GeneIDi905414.
KEGGicje:Cj1123c.
PATRICi20059204. VBICamJej33762_1105.

Phylogenomic databases

eggNOGiENOG4105MME. Bacteria.
COG0110. LUCA.
HOGENOMiHOG000253005.
KOiK15913.
OMAiTVIMAGA.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciCJEJ192222:GJTS-1052-MONOMER.
MetaCyc:MONOMER-17320.
BRENDAi2.3.1.203. 1087.

Miscellaneous databases

EvolutionaryTraceiQ0P9D1.

Family and domain databases

CDDicd03360. LbH_AT_putative. 1 hit.
Gene3Di3.40.50.20. 1 hit.
InterProiIPR001451. Hexapep.
IPR016185. PreATP-grasp_dom.
IPR020019. Sia_OAcTrfase_NeuD-like.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 1 hit.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
TIGRFAMsiTIGR03570. NeuD_NnaD. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPGLD_CAMJE
AccessioniPrimary (citable) accession number: Q0P9D1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2013
Last sequence update: September 19, 2006
Last modified: November 2, 2016
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

N-linked protein glycosylation in C.jejuni consists in the transfer of a heptasaccharide (GalNAc-alpha1,4-GalNAc-alpha1,4-(Glcbeta1,3)-GalNAc-alpha1,4-GalNAc-alpha1,4-GalNAc-alpha1,3-bacillosamine) from a membrane-anchored undecaprenylpyrophosphate (Und-PP)-linked donor to the Asn side chain of proteins at the Asn-X-Ser/Thr motif.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.