PYRG_DICDI
ID PYRG_DICDI Reviewed; 569 AA.
AC Q54V77;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=CTP synthase;
DE EC=6.3.4.2;
DE AltName: Full=CTP synthetase;
DE AltName: Full=UTP--ammonia ligase;
GN Name=ctps; ORFNames=DDB_G0280567;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC either L-glutamine or ammonia as the source of nitrogen. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-
CC glutamate + phosphate; Xref=Rhea:RHEA:26426, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.4.2;
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC CTP from UDP: step 2/2.
CC -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000305}.
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DR EMBL; AAFI02000037; EAL67085.1; -; Genomic_DNA.
DR RefSeq; XP_641054.1; XM_635962.1.
DR AlphaFoldDB; Q54V77; -.
DR SMR; Q54V77; -.
DR STRING; 44689.DDB0230162; -.
DR MEROPS; C26.A36; -.
DR PaxDb; Q54V77; -.
DR EnsemblProtists; EAL67085; EAL67085; DDB_G0280567.
DR GeneID; 8622612; -.
DR KEGG; ddi:DDB_G0280567; -.
DR dictyBase; DDB_G0280567; ctps.
DR eggNOG; KOG2387; Eukaryota.
DR HOGENOM; CLU_011675_5_0_1; -.
DR InParanoid; Q54V77; -.
DR OMA; EFNNAYR; -.
DR PhylomeDB; Q54V77; -.
DR Reactome; R-DDI-499943; Interconversion of nucleotide di- and triphosphates.
DR UniPathway; UPA00159; UER00277.
DR PRO; PR:Q54V77; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0097268; C:cytoophidium; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003883; F:CTP synthase activity; ISS:dictyBase.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006241; P:CTP biosynthetic process; ISS:dictyBase.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0008654; P:phospholipid biosynthetic process; ISS:dictyBase.
DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; ISS:dictyBase.
DR CDD; cd03113; CTPS_N; 1.
DR CDD; cd01746; GATase1_CTP_Synthase; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR004468; CTP_synthase.
DR InterPro; IPR017456; CTP_synthase_N.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR033828; GATase1_CTP_Synthase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11550; PTHR11550; 1.
DR Pfam; PF06418; CTP_synth_N; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00337; PyrG; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..569
FT /note="CTP synthase"
FT /id="PRO_0000327649"
FT DOMAIN 313..569
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 410
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 541
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 543
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 569 AA; 63238 MW; 37103FA6B757CE81 CRC64;
MKYIVVTGGV LSGIGKGIIA SSTAMILKSM GLRVTSIKID PYLNIDAGTM SPFEHGEVFV
LDDGGEVDLD LGNYERFLDV NLGKDNNITT GKIYNLVIEK ERKGQYLGKT VQVVPHITEE
IQNWIERVAH LPVDGDKGTP DVCVIELGGT VGDIESMPFT EALRQFQFRV GVENFCLMHV
SLVPVLGVVG EQKTKPSQQS IRELRSLGLS PDFCLCRSTQ PLTEETKKKI SLFCHVAPDN
VIGVHDVSNI YRVPILLNQQ NLPNLVLRRL QLNPKVDLSK TSPSESTPYW MASWKGLADR
MDKITNESLN PIRIAMVGKY TGLTDAYLSV IKALDHASMA IERKMVIDWV EASNLETQNS
STAEYKKSWE MLRGAHGILV PGGFGDRGIE GMILTANYAR TSGKPFLGIC LGLQIAVIEY
ARNVMGWENA NSEEFSASGS GKNVVVFMPE VSKTHMGGTM RLGSRDTIFT DVDNKISKLY
NVDKVGQAVE ERHRHRYEVN PEVVDEIHAK GLHFVGKDTT GVRMEIVELK DHDYYVACQF
HPEFKSRPQR PSPPFIGLLN ASLERLKKM
