GCDPH_CAMJE
ID GCDPH_CAMJE Reviewed; 200 AA.
AC Q0P8J7;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Gamma-glutamyl-CDP-amidate hydrolase {ECO:0000303|PubMed:29023101};
DE EC=3.5.1.129 {ECO:0000269|PubMed:29023101};
GN OrderedLocusNames=Cj1417c {ECO:0000312|EMBL:CAL35526.1};
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).
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 hydrolysis of CDP-L-glutamine to L-
CC glutamate and cytidine diphosphoramidate (PubMed:29023101).
CC {ECO:0000269|PubMed:17675288, ECO:0000269|PubMed:29023101}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(5)-(cytidine 5'-diphosphoramidyl)-L-glutamine =
CC cytidine 5'-diphosphoramidate + H(+) + L-glutamate;
CC Xref=Rhea:RHEA:57312, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:141582, ChEBI:CHEBI:141583;
CC EC=3.5.1.129; Evidence={ECO:0000269|PubMed:29023101};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=28 uM for CDP-L-glutamine {ECO:0000269|PubMed:29023101};
CC Note=kcat is 34 min(-1). {ECO:0000269|PubMed:29023101};
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}.
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DR EMBL; AL111168; CAL35526.1; -; Genomic_DNA.
DR PIR; A81287; A81287.
DR RefSeq; WP_002858074.1; NC_002163.1.
DR RefSeq; YP_002344800.1; NC_002163.1.
DR AlphaFoldDB; Q0P8J7; -.
DR SMR; Q0P8J7; -.
DR IntAct; Q0P8J7; 15.
DR STRING; 192222.Cj1417c; -.
DR PaxDb; Q0P8J7; -.
DR PRIDE; Q0P8J7; -.
DR DNASU; 905706; -.
DR EnsemblBacteria; CAL35526; CAL35526; Cj1417c.
DR GeneID; 905706; -.
DR KEGG; cje:Cj1417c; -.
DR PATRIC; fig|192222.6.peg.1398; -.
DR eggNOG; COG2071; Bacteria.
DR HOGENOM; CLU_030756_5_0_7; -.
DR OMA; LGIMWHP; -.
DR BRENDA; 3.5.1.129; 16305.
DR SABIO-RK; Q0P8J7; -.
DR UniPathway; UPA00934; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR011697; Peptidase_C26.
DR InterPro; IPR044668; PuuD-like.
DR PANTHER; PTHR43235; PTHR43235; 2.
DR Pfam; PF07722; Peptidase_C26; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Capsule biogenesis/degradation; Hydrolase; Reference proteome.
FT CHAIN 1..200
FT /note="Gamma-glutamyl-CDP-amidate hydrolase"
FT /id="PRO_0000445430"
FT DOMAIN 20..200
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 101
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 200 AA; 23500 MW; 3B8FF69042AB3EF7 CRC64;
MFIGITQRLI CNDSYHEKRE CLALDWGKLF NKDLFKNFTP LPLSYEIDFS YYKHLIKAVI
LSGGNDLSFY SPNVLSKKRD LYEKQVIEIC LEEKIPLLGI CRGAQMIAHY FNSHISPCEN
HIGKHEVFFS KEKFISNSFH NFAIEKLGED LVELCLAKDN TIEAFKHKYE NIFGIMWHIE
RENGLNNIQI LKEWFSLIKE
