Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

  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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei56 – 561Substrate; via amide nitrogen
Active sitei125 – 1251Proton acceptor1 Publication
Sitei126 – 1261Increases basicity of active site His
Binding sitei134 – 1341Acetyl-CoA1 Publication
Binding sitei155 – 1551Acetyl-CoA; via amide nitrogen1 Publication
Binding sitei173 – 1731Acetyl-CoA; via amide nitrogen and carbonyl oxygen1 Publication

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-1096-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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi15 – 151H → A: Induces a higher KM and approximate 3-fold decrease in the turnover number. 1 Publication
Mutagenesisi118 – 1181N → A: Reduction in catalytic activity. 1 Publication
Mutagenesisi124 – 1241E → A: Reduction in catalytic activity. 1 Publication
Mutagenesisi125 – 1251H → A: Strong reduction in catalytic activity. 2 Publications
Mutagenesisi134 – 1341H → A: Slight reduction in catalytic activity. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 195195UDP-N-acetylbacillosamine N-acetyltransferasePRO_0000422585Add
BLAST

Proteomic databases

PaxDbiQ0P9D1.

Interactioni

Subunit structurei

Homotrimer.2 Publications

Protein-protein interaction databases

IntActiQ0P9D1. 3 interactions.
STRINGi192222.Cj1123c.

Structurei

Secondary structure

1
195
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Helixi15 – 2612Combined sources
Beta strandi29 – 346Combined sources
Turni36 – 383Combined sources
Helixi40 – 456Combined sources
Beta strandi50 – 534Combined sources
Helixi58 – 6912Combined sources
Turni70 – 723Combined sources
Beta strandi89 – 913Combined sources
Beta strandi181 – 1833Combined sources
Beta strandi186 – 1883Combined sources
Turni189 – 1924Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-195.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ0P9D1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni13 – 153Substrate binding
Regioni35 – 362Substrate binding

Sequence similaritiesi

Phylogenomic databases

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

Family and domain databases

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
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. Positions 2-195.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ0P9D1. 3 interactions.
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-1096-MONOMER.
MetaCyc:MONOMER-17320.
BRENDAi2.3.1.203. 1087.

Miscellaneous databases

EvolutionaryTraceiQ0P9D1.

Family and domain databases

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: September 7, 2016
This is version 61 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.