CDK_CAMJE
ID CDK_CAMJE Reviewed; 170 AA.
AC Q0P8J9;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Cytidine diphosphoramidate kinase {ECO:0000303|PubMed:29578334};
DE Short=CDK {ECO:0000303|PubMed:29578334};
DE EC=2.7.1.224 {ECO:0000269|PubMed:29578334};
GN OrderedLocusNames=Cj1415c {ECO:0000312|EMBL:CAL35524.1};
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, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF SER-85.
RX PubMed=29578334; DOI=10.1021/acs.biochem.8b00279;
RA Taylor Z.W., Raushel F.M.;
RT "Cytidine diphosphoramidate kinase: an enzyme required for the biosynthesis
RT of the O-methyl phosphoramidate modification in the capsular
RT polysaccharides of Campylobacter jejuni.";
RL Biochemistry 57:2238-2244(2018).
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 ATP-dependent phosphorylation of
CC cytidine diphosphoramidate (CDP-NH(2)) to form cytidine 3'-phosphate
CC 5'-diphosphoramidate (PubMed:29578334). Can also use other substrates
CC such as the corresponding adenine and uridine diphosphoramidate
CC derivatives or cytidine diphosphoramidate analogs, with lower
CC efficiency (PubMed:29578334). {ECO:0000269|PubMed:17675288,
CC ECO:0000269|PubMed:29578334}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cytidine 5'-diphosphoramidate = ADP + cytidine 3'-
CC phospho-5'-diphosphoramidate + H(+); Xref=Rhea:RHEA:57316,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:141582,
CC ChEBI:CHEBI:141584, ChEBI:CHEBI:456216; EC=2.7.1.224;
CC Evidence={ECO:0000269|PubMed:29578334};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.11 mM for cytidine diphosphoramidate
CC {ECO:0000269|PubMed:29578334};
CC KM=1.5 mM for ATP {ECO:0000269|PubMed:29578334};
CC KM=0.39 mM for 2'-deoxycytidine diphosphoramidate
CC {ECO:0000269|PubMed:29578334};
CC KM=4.2 mM for CDP {ECO:0000269|PubMed:29578334};
CC KM=1.4 mM for CDP-methyl phosphate {ECO:0000269|PubMed:29578334};
CC KM=0.8 mM for CDP-methyl phosphonate {ECO:0000269|PubMed:29578334};
CC KM=21 mM for uridine diphosphoramidate {ECO:0000269|PubMed:29578334};
CC KM=5.6 mM for adenosine diphosphoramidate
CC {ECO:0000269|PubMed:29578334};
CC Note=kcat is 2.2 sec(-1) with cytidine diphosphoramidate as
CC substrate. kcat is 2.2 sec(-1) with 2'-deoxycytidine
CC diphosphoramidate as substrate. kcat is 0.64 sec(-1) with CDP as
CC substrate. kcat is 0.65 sec(-1) with CDP-methyl phosphate as
CC substrate. kcat is 1.4 sec(-1) with CDP-methyl phosphonate as
CC substrate. kcat is 0.023 sec(-1) with uridine diphosphoramidate as
CC substrate. kcat is 0.08 sec(-1) with adenosine diphosphoramidate as
CC substrate. {ECO:0000269|PubMed:29578334};
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 -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000305}.
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DR EMBL; AL111168; CAL35524.1; -; Genomic_DNA.
DR PIR; G81286; G81286.
DR RefSeq; WP_002858462.1; NC_002163.1.
DR RefSeq; YP_002344798.1; NC_002163.1.
DR AlphaFoldDB; Q0P8J9; -.
DR SMR; Q0P8J9; -.
DR STRING; 192222.Cj1415c; -.
DR PaxDb; Q0P8J9; -.
DR PRIDE; Q0P8J9; -.
DR EnsemblBacteria; CAL35524; CAL35524; Cj1415c.
DR GeneID; 905704; -.
DR KEGG; cje:Cj1415c; -.
DR PATRIC; fig|192222.6.peg.1396; -.
DR eggNOG; COG0529; Bacteria.
DR HOGENOM; CLU_046932_2_3_7; -.
DR OMA; DIVWHEA; -.
DR BRENDA; 2.7.1.224; 16305.
DR UniPathway; UPA00934; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0000103; P:sulfate assimilation; IEA:InterPro.
DR CDD; cd02027; APSK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Capsule biogenesis/degradation; Kinase; Reference proteome; Transferase.
FT CHAIN 1..170
FT /note="Cytidine diphosphoramidate kinase"
FT /id="PRO_0000445427"
FT MUTAGEN 85
FT /note="S->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:29578334"
SQ SEQUENCE 170 AA; 19884 MW; E3C9478521DC100E CRC64;
MKNNPYIIWL TGLAGSGKTT IGQALYEKLK LKYKNLIYLD GDELREILGH YAYDRQGRID
MALKRAKFAK FLNDQGMMVI VTTISMFNEI YDYNRKQLKN YYEIYIECDM HELIQRDQKG
LYTKALNKEI DNVVGVDIEF DKPEADLVIN NSCRNNLEEK VELIIKKLAL
