CTDTR_CAMJE
ID CTDTR_CAMJE Reviewed; 253 AA.
AC Q0P8J8;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=CTP:phosphoglutamine cytidylyltransferase {ECO:0000303|PubMed:29023101, ECO:0000303|PubMed:30929435};
DE EC=2.7.7.103 {ECO:0000269|PubMed:29023101, ECO:0000269|PubMed:30929435};
GN OrderedLocusNames=Cj1416c {ECO:0000312|EMBL:CAL35525.1};
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 IN CAPSULE BIOSYNTHESIS, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=17675288; DOI=10.1074/jbc.m704413200;
RA McNally D.J., Lamoureux M.P., Karlyshev A.V., Fiori L.M., Li J.,
RA Thacker G., Coleman R.A., Khieu N.H., Wren B.W., Brisson J.R.,
RA Jarrell H.C., Szymanski C.M.;
RT "Commonality and biosynthesis of the O-methyl phosphoramidate capsule
RT modification in Campylobacter jejuni.";
RL J. Biol. Chem. 282:28566-28576(2007).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=29023101; DOI=10.1021/acs.biochem.7b00905;
RA Taylor Z.W., Brown H.A., Holden H.M., Raushel F.M.;
RT "Biosynthesis of nucleoside diphosphoramidates in Campylobacter jejuni.";
RL Biochemistry 56:6079-6082(2017).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000303|PubMed:30929435};
RX PubMed=30929435; DOI=10.1021/acs.biochem.9b00189;
RA Taylor Z.W., Raushel F.M.;
RT "Manganese-Induced Substrate Promiscuity in the Reaction Catalyzed by
RT Phosphoglutamine Cytidylyltransferase from Campylobacter jejuni.";
RL Biochemistry 58:2144-2151(2019).
CC -!- FUNCTION: Involved in the biosynthesis of the O-methyl phosphoramidate
CC (MeOPN) group found on the capsular polysaccharide (CPS) of C.jejuni
CC (PubMed:17675288). Catalyzes the formation of CDP-L-glutamine from CTP
CC and L-glutamine phosphate (PubMed:29023101, PubMed:30929435). In the
CC presence of MnCTP, catalyzes the displacement of pyrophosphate from CTP
CC using phosphoramidate, methyl phosphate, methyl phosphonate, phosphate,
CC arsenate, ethanolamine phosphate, (R/S)-glycerol-1-phosphate, glycerol-
CC 2-phosphate, serinol phosphate, L-serine phosphate and 3-phospho-D-
CC glycerate as substrate in addition to L-glutamine phosphate
CC (PubMed:30929435). {ECO:0000269|PubMed:17675288,
CC ECO:0000269|PubMed:29023101, ECO:0000269|PubMed:30929435}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + H(+) + N(5)-phospho-L-glutamine = diphosphate + N(5)-
CC (cytidine 5'-diphosphoramidyl)-L-glutamine; Xref=Rhea:RHEA:57308,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:139073, ChEBI:CHEBI:141583; EC=2.7.7.103;
CC Evidence={ECO:0000269|PubMed:29023101, ECO:0000269|PubMed:30929435};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=120 uM for L-glutamine phosphate {ECO:0000269|PubMed:29023101};
CC KM=170 uM for MgCTP {ECO:0000269|PubMed:29023101};
CC Note=kcat is 57 min(-1) with L-glutamine phosphate as substrate (in
CC the presence of MgCTP) (PubMed:29023101). kcat is 0.35 min(-1) with
CC L-glutamine phosphate as substrate (in the presence of MnCTP). kcat
CC is 0.6 min(-1) with phosphoramidate as substrate (in the presence of
CC MnCTP). kcat is 3.7 min(-1) with 3-phospho-D-glycerate as substrate
CC (in the presence of MnCTP). kcat is 0.18 min(-1) with phosphate as
CC substrate (in the presence of MnCTP). kcat is 0.07 min(-1) with
CC methyl phosphate as substrate (in the presence of MnCTP). kcat is
CC 0.15 min(-1) with methyl phosphonate as substrate (in the presence of
CC MnCTP). kcat is 0.18 min(-1) with arsenate as substrate (in the
CC presence of MnCTP). kcat is 0.017 min(-1) with ethanolamine phosphate
CC as substrate (in the presence of MnCTP). kcat is 0.07 min(-1) with
CC (R/S)-glycerol-1-phosphate as substrate (in the presence of MnCTP).
CC kcat is 0.08 min(-1) with glycerol-2-phosphate as substrate (in the
CC presence of MnCTP). kcat is 0.017 min(-1) with serinol phosphate as
CC substrate (in the presence of MnCTP). kcat is 0.18 min(-1) with L-
CC serine phosphate as substrate (in the presence of MnCTP)
CC (PubMed:30929435). {ECO:0000269|PubMed:29023101,
CC ECO:0000269|PubMed:30929435};
CC -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC {ECO:0000269|PubMed:17675288}.
CC -!- DISRUPTION PHENOTYPE: Mutant does not express the MeOPN CPS
CC modification. {ECO:0000269|PubMed:17675288}.
CC -!- BIOTECHNOLOGY: This enzyme is able to catalyze reactions that produce
CC natural compounds CDP-ethanolamine, CDP-1-glycerol and CDP-2-glycerol,
CC two of which are not available commercially. It can also produce CDP-
CC serine, CDP-serinol and CDP-3-D-glycerate which may be potential
CC inhibitors or mechanistic probes for enzymes that use CDP-glycerol. The
CC labeled nucleotides, such as beta-[(18)O4]-CDP, generated with this
CC enzyme can be used to probe the details of enzyme-catalyzed reactions
CC using positional isotope exchange (PIX) and molecular isotope exchange
CC (MIX) techniques. {ECO:0000269|PubMed:30929435}.
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DR EMBL; AL111168; CAL35525.1; -; Genomic_DNA.
DR PIR; H81286; H81286.
DR RefSeq; WP_002858404.1; NC_002163.1.
DR RefSeq; YP_002344799.1; NC_002163.1.
DR AlphaFoldDB; Q0P8J8; -.
DR SMR; Q0P8J8; -.
DR IntAct; Q0P8J8; 14.
DR STRING; 192222.Cj1416c; -.
DR PaxDb; Q0P8J8; -.
DR PRIDE; Q0P8J8; -.
DR DNASU; 905705; -.
DR EnsemblBacteria; CAL35525; CAL35525; Cj1416c.
DR GeneID; 905705; -.
DR KEGG; cje:Cj1416c; -.
DR PATRIC; fig|192222.6.peg.1397; -.
DR eggNOG; COG1213; Bacteria.
DR HOGENOM; CLU_029499_5_1_7; -.
DR OMA; QYMGLLK; -.
DR BRENDA; 2.7.7.103; 13746.
DR SABIO-RK; Q0P8J8; -.
DR UniPathway; UPA00934; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0070567; F:cytidylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Capsule biogenesis/degradation; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..253
FT /note="CTP:phosphoglutamine cytidylyltransferase"
FT /id="PRO_0000445429"
SQ SEQUENCE 253 AA; 29533 MW; 781769F9833B0FCC CRC64;
MNAIILAAGF GSRLMPLTKD QPKCMVEYKN KKIIDYEIEA LKSAGINEIA VVGGYLNDVL
KNYLNKYDIE HFFINSKYDK TNMVHTFFCA KDFMLKCIEE KQDLIISYAD IVYFQDCVQK
LINAKEELAI VVDKSWCKLW SKRFANPLED AETLKMTNGY IIELGKKANA YDEIEAQYIG
LFKFSYQFLS EVIAFYEMLD RDILYDNKNF ENMYMTSFLQ ALIEKYNNAK AVEIDGNWCE
IDFMSDLEVQ IEK
