ID   PYRG_SCHPO              Reviewed;         600 AA.
AC   O42644;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=CTP synthase;
DE            EC=6.3.4.2;
DE   AltName: Full=CTP synthetase;
DE   AltName: Full=UTP--ammonia ligase;
GN   Name=ura7; ORFNames=SPAC10F6.03c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC       either L-glutamine or ammonia as the source of nitrogen.
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; CU329670; CAA15716.1; -; Genomic_DNA.
DR   PIR; T37497; T37497.
DR   RefSeq; NP_593254.1; NM_001018651.2.
DR   AlphaFoldDB; O42644; -.
DR   SMR; O42644; -.
DR   BioGRID; 279378; 5.
DR   STRING; 4896.SPAC10F6.03c.1; -.
DR   iPTMnet; O42644; -.
DR   MaxQB; O42644; -.
DR   PaxDb; O42644; -.
DR   PRIDE; O42644; -.
DR   EnsemblFungi; SPAC10F6.03c.1; SPAC10F6.03c.1:pep; SPAC10F6.03c.
DR   GeneID; 2542937; -.
DR   KEGG; spo:SPAC10F6.03c; -.
DR   PomBase; SPAC10F6.03c; -.
DR   VEuPathDB; FungiDB:SPAC10F6.03c; -.
DR   eggNOG; KOG2387; Eukaryota.
DR   HOGENOM; CLU_011675_5_0_1; -.
DR   InParanoid; O42644; -.
DR   OMA; EFNNAYR; -.
DR   PhylomeDB; O42644; -.
DR   Reactome; R-SPO-499943; Interconversion of nucleotide di- and triphosphates.
DR   UniPathway; UPA00159; UER00277.
DR   PRO; PR:O42644; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0097268; C:cytoophidium; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; ISO:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; ISO:PomBase.
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:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; ISO:PomBase.
DR   GO; GO:0006241; P:CTP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
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..600
FT                   /note="CTP synthase"
FT                   /id="PRO_0000138282"
FT   DOMAIN          304..570
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        403
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        532
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        534
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   600 AA;  66867 MW;  72D7EE95B678E4EC CRC64;
     MKYVLVSGGV ISGIGKGVIA SSTGLLLKTL GLKVTSIKID PYMNIDAGTM SPLEHGEVFV
     LNDGGEVDLD LGNYERYLNV TLTHDNNITT GKVYSNVIQK ERRGDYLGKT VQIVPHVTNE
     IQDWVERVAR IPVDQSGEEP DVCIVELGGT VGDIESAAFV EAMRQFQFRV GHENFVSIHV
     SLVPVINGEQ KTKPTQQAIR DLRSLGITPD LIACRCKQPL EKSVIDKISL FCHVGPEQVL
     AVHDVSSTYH VPQLLEDKLL EYLKIRFALD KISVSRELAL AGENMWSSWK HLTQGYDHLF
     KKVTIVLVGK YTHLQDSYIS VIKALEHSAM RCGRKLDLQW VEASHLEAST NTSDPLSYHK
     AWHLVCSANG ILVPGGFGSR GVEGMIAAAK WARENNTPYL GICLGMQVAV IEFARSVCGI
     EGAFSEEFDK ECENNVVVYM PEIDKDKLGG TMRLGLRPTF FQPNSEWSKL RKLHKMVDEV
     LERHRHRYEI NPAFVSRLEQ GGISFIGKDE RGERMEIIEK RDHPYFVGVQ YHPEYLSKPL
     KPSPPIFGLV AASAGLLDEF IQSGEEVEWS NFSHFNAESA LADMNDSVEV TEEATVVTIS