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UDP-N-acetylbacillosamine N-acetyltransferase (EC 2.3.1.203) (Protein glycosylation D) (UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine N-acetyltransferase)

 PGLD_CAMJE              Reviewed;         195 AA.
Q0P9D1;
29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
19-SEP-2006, sequence version 1.
05-JUL-2017, entry version 66.
RecName: Full=UDP-N-acetylbacillosamine N-acetyltransferase;
EC=2.3.1.203;
AltName: Full=Protein glycosylation D;
AltName: Full=UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine N-acetyltransferase;
Name=pglD; OrderedLocusNames=Cj1123c;
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 /
NCTC 11168).
Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
Campylobacteraceae; Campylobacter.
NCBI_TaxID=192222;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700819 / NCTC 11168;
PubMed=10688204; DOI=10.1038/35001088;
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W.,
Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M.,
Whitehead S., Barrell B.G.;
"The genome sequence of the food-borne pathogen Campylobacter jejuni
reveals hypervariable sequences.";
Nature 403:665-668(2000).
[2]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
PATHWAY.
STRAIN=ATCC 700819 / NCTC 11168;
PubMed=17087520; DOI=10.1021/bi061456h;
Olivier N.B., Chen M.M., Behr J.R., Imperiali B.;
"In vitro biosynthesis of UDP-N,N'-diacetylbacillosamine by enzymes of
the Campylobacter jejuni general protein glycosylation system.";
Biochemistry 45:13659-13669(2006).
[3]
FUNCTION.
STRAIN=ATCC 700819 / NCTC 11168;
PubMed=19448740; DOI=10.1139/o09-002;
Demendi M., Creuzenet C.;
"Cj1123c (PglD), a multifaceted acetyltransferase from Campylobacter
jejuni.";
Biochem. Cell Biol. 87:469-483(2009).
[4]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-195.
Jin X., Bera A., Wasserman S., Smith D., Sauder J.M., Burley S.K.,
Shapiro L.;
"Crystal structure of putative transferase from Campylobacter jejuni
subsp. jejuni NCTC 11168.";
Submitted (OCT-2006) to the PDB data bank.
[5]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 2-195 IN COMPLEX WITH
COENZYME A, SUBUNIT, AND MUTAGENESIS OF ASN-118; GLU-124; HIS-125 AND
HIS-134.
STRAIN=ATCC 700819 / NCTC 11168;
PubMed=18198901; DOI=10.1021/bi702032r;
Rangarajan E.S., Ruane K.M., Sulea T., Watson D.C., Proteau A.,
Leclerc S., Cygler M., Matte A., Young N.M.;
"Structure and active site residues of PglD, an N-acetyltransferase
from the bacillosamine synthetic pathway required for N-glycan
synthesis in Campylobacter jejuni.";
Biochemistry 47:1827-1836(2008).
[6]
X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) IN COMPLEX WITH
UDP-4-AMINO-SUGAR AND ACETYL-COA, SUBUNIT, MUTAGENESIS OF HIS-15;
HIS-125 AND HIS-134, REACTION MECHANISM, ACTIVE SITE, AND SITE.
STRAIN=ATCC 700819 / NCTC 11168;
PubMed=18667421; DOI=10.1074/jbc.M801207200;
Olivier N.B., Imperiali B.;
"Crystal structure and catalytic mechanism of PglD from Campylobacter
jejuni.";
J. Biol. Chem. 283:27937-27946(2008).
-!- FUNCTION: Acetyltransferase that modifies the UDP-4-amino-sugar to
form UDP-N,N'-diacetylbacillosamine in the N-linked protein
glycosylation pathway. {ECO:0000269|PubMed:17087520,
ECO:0000269|PubMed:19448740}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + UDP-N-acetylbacillosamine = CoA +
UDP-N,N'-diacetylbacillosamine. {ECO:0000269|PubMed:17087520}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.0 mM for UDP-N-acetylbacillosamine
{ECO:0000269|PubMed:17087520, ECO:0000269|PubMed:18667421};
KM=0.41 mM for UDP-N-acetylbacillosamine
{ECO:0000269|PubMed:17087520};
Vmax=14700 nmol/sec/mg enzyme {ECO:0000269|PubMed:17087520,
ECO:0000269|PubMed:18667421};
Note=kcat is 483000 min(-1) (PubMed:17087520). Kcat is 314 sec(-
1) (PubMed:18667421). {ECO:0000269|PubMed:17087520,
ECO:0000269|PubMed:18667421};
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000269|PubMed:17087520}.
-!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:18198901,
ECO:0000269|PubMed:18667421}.
-!- 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.
{ECO:0000305|PubMed:17087520}.
-!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
{ECO:0000305}.
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EMBL; AL111168; CAL35240.1; -; Genomic_DNA.
PIR; F81316; F81316.
RefSeq; WP_002852865.1; NC_002163.1.
RefSeq; YP_002344516.1; NC_002163.1.
PDB; 2NPO; X-ray; 2.20 A; A=2-195.
PDB; 2VHE; X-ray; 1.80 A; A/B=2-195.
PDB; 3BFP; X-ray; 1.75 A; A=2-195.
PDB; 3BSS; X-ray; 2.30 A; A=1-195.
PDB; 3BSW; X-ray; 1.77 A; A=1-195.
PDB; 3BSY; X-ray; 1.80 A; A/B/C=1-195.
PDB; 5T2Y; X-ray; 1.94 A; A/B=1-195.
PDB; 5TYH; X-ray; 2.10 A; A=1-195.
PDBsum; 2NPO; -.
PDBsum; 2VHE; -.
PDBsum; 3BFP; -.
PDBsum; 3BSS; -.
PDBsum; 3BSW; -.
PDBsum; 3BSY; -.
PDBsum; 5T2Y; -.
PDBsum; 5TYH; -.
ProteinModelPortal; Q0P9D1; -.
SMR; Q0P9D1; -.
IntAct; Q0P9D1; 3.
STRING; 192222.Cj1123c; -.
PaxDb; Q0P9D1; -.
EnsemblBacteria; CAL35240; CAL35240; Cj1123c.
GeneID; 905414; -.
KEGG; cje:Cj1123c; -.
PATRIC; fig|192222.6.peg.1105; -.
eggNOG; ENOG4105MME; Bacteria.
eggNOG; COG0110; LUCA.
HOGENOM; HOG000253005; -.
KO; K15913; -.
OMA; SIIEHDC; -.
BioCyc; CJEJ192222:GJTS-1052-MONOMER; -.
BioCyc; MetaCyc:MONOMER-17320; -.
BRENDA; 2.3.1.203; 1087.
UniPathway; UPA00378; -.
EvolutionaryTrace; Q0P9D1; -.
Proteomes; UP000000799; Chromosome.
GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IDA:UniProtKB.
GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IDA:UniProtKB.
CDD; cd03360; LbH_AT_putative; 1.
InterPro; IPR001451; Hexapep.
InterPro; IPR020019; Sia_OAcTrfase_NeuD-like.
InterPro; IPR011004; Trimer_LpxA-like.
Pfam; PF00132; Hexapep; 1.
SUPFAM; SSF51161; SSF51161; 1.
TIGRFAMs; TIGR03570; NeuD_NnaD; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Complete proteome; Reference proteome;
Transferase.
CHAIN 1 195 UDP-N-acetylbacillosamine N-
acetyltransferase.
/FTId=PRO_0000422585.
REGION 13 15 Substrate binding.
REGION 35 36 Substrate binding.
ACT_SITE 125 125 Proton acceptor.
{ECO:0000269|PubMed:18667421}.
BINDING 56 56 Substrate; via amide nitrogen.
BINDING 134 134 Acetyl-CoA.
{ECO:0000269|PubMed:18667421}.
BINDING 155 155 Acetyl-CoA; via amide nitrogen.
{ECO:0000269|PubMed:18667421}.
BINDING 173 173 Acetyl-CoA; via amide nitrogen and
carbonyl oxygen.
{ECO:0000269|PubMed:18667421}.
SITE 126 126 Increases basicity of active site His.
MUTAGEN 15 15 H->A: Induces a higher KM and approximate
3-fold decrease in the turnover number.
{ECO:0000269|PubMed:18667421}.
MUTAGEN 118 118 N->A: Reduction in catalytic activity.
{ECO:0000269|PubMed:18198901}.
MUTAGEN 124 124 E->A: Reduction in catalytic activity.
{ECO:0000269|PubMed:18198901}.
MUTAGEN 125 125 H->A: Strong reduction in catalytic
activity. {ECO:0000269|PubMed:18198901,
ECO:0000269|PubMed:18667421}.
MUTAGEN 134 134 H->A: Slight reduction in catalytic
activity. {ECO:0000269|PubMed:18198901,
ECO:0000269|PubMed:18667421}.
STRAND 5 10 {ECO:0000244|PDB:3BFP}.
HELIX 15 26 {ECO:0000244|PDB:3BFP}.
STRAND 29 34 {ECO:0000244|PDB:3BFP}.
TURN 36 38 {ECO:0000244|PDB:2VHE}.
HELIX 40 45 {ECO:0000244|PDB:3BSW}.
STRAND 50 53 {ECO:0000244|PDB:3BFP}.
HELIX 58 69 {ECO:0000244|PDB:3BFP}.
TURN 70 72 {ECO:0000244|PDB:3BFP}.
STRAND 89 91 {ECO:0000244|PDB:3BSW}.
STRAND 181 183 {ECO:0000244|PDB:3BSS}.
STRAND 186 188 {ECO:0000244|PDB:2VHE}.
TURN 189 192 {ECO:0000244|PDB:2VHE}.
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


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