PGLD_CAMJE
ID PGLD_CAMJE Reviewed; 195 AA.
AC Q0P9D1;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=UDP-N-acetylbacillosamine N-acetyltransferase;
DE EC=2.3.1.203;
DE AltName: Full=Protein glycosylation D;
DE AltName: Full=UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine N-acetyltransferase;
GN Name=pglD; OrderedLocusNames=Cj1123c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=17087520; DOI=10.1021/bi061456h;
RA Olivier N.B., Chen M.M., Behr J.R., Imperiali B.;
RT "In vitro biosynthesis of UDP-N,N'-diacetylbacillosamine by enzymes of the
RT Campylobacter jejuni general protein glycosylation system.";
RL Biochemistry 45:13659-13669(2006).
RN [3]
RP FUNCTION.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=19448740; DOI=10.1139/o09-002;
RA Demendi M., Creuzenet C.;
RT "Cj1123c (PglD), a multifaceted acetyltransferase from Campylobacter
RT jejuni.";
RL Biochem. Cell Biol. 87:469-483(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-195.
RA Jin X., Bera A., Wasserman S., Smith D., Sauder J.M., Burley S.K.,
RA Shapiro L.;
RT "Crystal structure of putative transferase from Campylobacter jejuni subsp.
RT jejuni NCTC 11168.";
RL Submitted (OCT-2006) to the PDB data bank.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 2-195 IN COMPLEX WITH COENZYME A,
RP SUBUNIT, AND MUTAGENESIS OF ASN-118; GLU-124; HIS-125 AND HIS-134.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=18198901; DOI=10.1021/bi702032r;
RA Rangarajan E.S., Ruane K.M., Sulea T., Watson D.C., Proteau A., Leclerc S.,
RA Cygler M., Matte A., Young N.M.;
RT "Structure and active site residues of PglD, an N-acetyltransferase from
RT the bacillosamine synthetic pathway required for N-glycan synthesis in
RT Campylobacter jejuni.";
RL Biochemistry 47:1827-1836(2008).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) IN COMPLEX WITH UDP-4-AMINO-SUGAR
RP AND ACETYL-COA, SUBUNIT, MUTAGENESIS OF HIS-15; HIS-125 AND HIS-134,
RP REACTION MECHANISM, ACTIVE SITE, AND SITE.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=18667421; DOI=10.1074/jbc.m801207200;
RA Olivier N.B., Imperiali B.;
RT "Crystal structure and catalytic mechanism of PglD from Campylobacter
RT jejuni.";
RL J. Biol. Chem. 283:27937-27946(2008).
CC -!- FUNCTION: Acetyltransferase that modifies the UDP-4-amino-sugar to form
CC UDP-N,N'-diacetylbacillosamine in the N-linked protein glycosylation
CC pathway. {ECO:0000269|PubMed:17087520, ECO:0000269|PubMed:19448740}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + UDP-N-acetylbacillosamine = CoA + H(+) + UDP-
CC N,N'-diacetylbacillosamine; Xref=Rhea:RHEA:34159, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:63277,
CC ChEBI:CHEBI:67134; EC=2.3.1.203;
CC Evidence={ECO:0000269|PubMed:17087520};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 mM for UDP-N-acetylbacillosamine {ECO:0000269|PubMed:17087520,
CC ECO:0000269|PubMed:18667421};
CC KM=0.41 mM for UDP-N-acetylbacillosamine
CC {ECO:0000269|PubMed:17087520};
CC Vmax=14700 nmol/sec/mg enzyme {ECO:0000269|PubMed:17087520,
CC ECO:0000269|PubMed:18667421};
CC Note=kcat is 483000 min(-1) (PubMed:17087520). kcat is 314 sec(-1)
CC (PubMed:18667421). {ECO:0000269|PubMed:17087520,
CC ECO:0000269|PubMed:18667421};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:17087520}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:18198901,
CC ECO:0000269|PubMed:18667421}.
CC -!- MISCELLANEOUS: N-linked protein glycosylation in C.jejuni consists in
CC the transfer of a heptasaccharide (GalNAc-alpha1,4-GalNAc-alpha1,4-
CC (Glcbeta1,3)-GalNAc-alpha1,4-GalNAc-alpha1,4-GalNAc-alpha1,3-
CC bacillosamine) from a membrane-anchored undecaprenylpyrophosphate (Und-
CC PP)-linked donor to the Asn side chain of proteins at the Asn-X-Ser/Thr
CC motif. {ECO:0000305|PubMed:17087520}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL111168; CAL35240.1; -; Genomic_DNA.
DR PIR; F81316; F81316.
DR RefSeq; WP_002852865.1; NC_002163.1.
DR RefSeq; YP_002344516.1; NC_002163.1.
DR PDB; 2NPO; X-ray; 2.20 A; A=2-195.
DR PDB; 2VHE; X-ray; 1.80 A; A/B=2-195.
DR PDB; 3BFP; X-ray; 1.75 A; A=2-195.
DR PDB; 3BSS; X-ray; 2.30 A; A=1-195.
DR PDB; 3BSW; X-ray; 1.77 A; A=1-195.
DR PDB; 3BSY; X-ray; 1.80 A; A/B/C=1-195.
DR PDB; 5T2Y; X-ray; 1.94 A; A/B=1-195.
DR PDB; 5TYH; X-ray; 2.10 A; A=1-195.
DR PDBsum; 2NPO; -.
DR PDBsum; 2VHE; -.
DR PDBsum; 3BFP; -.
DR PDBsum; 3BSS; -.
DR PDBsum; 3BSW; -.
DR PDBsum; 3BSY; -.
DR PDBsum; 5T2Y; -.
DR PDBsum; 5TYH; -.
DR AlphaFoldDB; Q0P9D1; -.
DR SMR; Q0P9D1; -.
DR IntAct; Q0P9D1; 3.
DR STRING; 192222.Cj1123c; -.
DR BindingDB; Q0P9D1; -.
DR ChEMBL; CHEMBL4105798; -.
DR PaxDb; Q0P9D1; -.
DR PRIDE; Q0P9D1; -.
DR EnsemblBacteria; CAL35240; CAL35240; Cj1123c.
DR GeneID; 905414; -.
DR KEGG; cje:Cj1123c; -.
DR PATRIC; fig|192222.6.peg.1105; -.
DR eggNOG; COG0110; Bacteria.
DR HOGENOM; CLU_081811_2_3_7; -.
DR OMA; GAHCIIN; -.
DR BioCyc; MetaCyc:MON-17320; -.
DR BRENDA; 2.3.1.203; 1087.
DR UniPathway; UPA00378; -.
DR EvolutionaryTrace; Q0P9D1; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:UniProtKB.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IDA:UniProtKB.
DR CDD; cd03360; LbH_AT_putative; 1.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR041561; PglD_N.
DR InterPro; IPR020019; Sia_OAcTrfase_NeuD-like.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF17836; PglD_N; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR TIGRFAMs; TIGR03570; NeuD_NnaD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..195
FT /note="UDP-N-acetylbacillosamine N-acetyltransferase"
FT /id="PRO_0000422585"
FT ACT_SITE 125
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:18667421"
FT BINDING 13..15
FT /ligand="substrate"
FT BINDING 35..36
FT /ligand="substrate"
FT BINDING 56
FT /ligand="substrate"
FT BINDING 134
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:18667421"
FT BINDING 155
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:18667421"
FT BINDING 173
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:18667421"
FT SITE 126
FT /note="Increases basicity of active site His"
FT MUTAGEN 15
FT /note="H->A: Induces a higher KM and approximate 3-fold
FT decrease in the turnover number."
FT /evidence="ECO:0000269|PubMed:18667421"
FT MUTAGEN 118
FT /note="N->A: Reduction in catalytic activity."
FT /evidence="ECO:0000269|PubMed:18198901"
FT MUTAGEN 124
FT /note="E->A: Reduction in catalytic activity."
FT /evidence="ECO:0000269|PubMed:18198901"
FT MUTAGEN 125
FT /note="H->A: Strong reduction in catalytic activity."
FT /evidence="ECO:0000269|PubMed:18198901,
FT ECO:0000269|PubMed:18667421"
FT MUTAGEN 134
FT /note="H->A: Slight reduction in catalytic activity."
FT /evidence="ECO:0000269|PubMed:18198901,
FT ECO:0000269|PubMed:18667421"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:3BFP"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:3BFP"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:3BFP"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:2VHE"
FT HELIX 40..45
FT /evidence="ECO:0007829|PDB:3BSW"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:3BFP"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:3BFP"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:3BFP"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:3BSW"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:3BSS"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2VHE"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:2VHE"
SQ SEQUENCE 195 AA; 21148 MW; 8C6312D439AE90E2 CRC64;
MARTEKIYIY GASGHGLVCE DVAKNMGYKE CIFLDDFKGM KFESTLPKYD FFIAIGNNEI
RKKIYQKISE NGFKIVNLIH KSALISPSAI VEENAGILIM PYVVINAKAK IEKGVILNTS
SVIEHECVIG EFSHVSVGAK CAGNVKIGKN CFLGINSCVL PNLSLADDSI LGGGATLVKN
QDEKGVFVGV PAKRM
