ID   PYG1B_XENLA             Reviewed;         591 AA.
AC   Q7ZXP9;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=CTP synthase 1-B {ECO:0000305};
DE            EC=6.3.4.2 {ECO:0000250|UniProtKB:P17812};
DE   AltName: Full=CTP synthetase 1-B;
DE   AltName: Full=UTP--ammonia ligase 1-B;
GN   Name=ctps1-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This enzyme is involved in the de novo synthesis of CTP, a
CC       precursor of DNA, RNA and phospholipids. Catalyzes the ATP-dependent
CC       amination of UTP to CTP with either L-glutamine or ammonia as a source
CC       of nitrogen. {ECO:0000250|UniProtKB:P17812}.
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         Evidence={ECO:0000250|UniProtKB:P17812};
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC       CTP from UDP: step 2/2. {ECO:0000250|UniProtKB:P17812}.
CC   -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000305}.
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DR   EMBL; BC044325; AAH44325.1; -; mRNA.
DR   RefSeq; NP_001080188.1; NM_001086719.1.
DR   RefSeq; XP_018100292.1; XM_018244803.1.
DR   AlphaFoldDB; Q7ZXP9; -.
DR   SMR; Q7ZXP9; -.
DR   DNASU; 379880; -.
DR   GeneID; 379880; -.
DR   KEGG; xla:379880; -.
DR   CTD; 379880; -.
DR   Xenbase; XB-GENE-957436; ctps1.L.
DR   OMA; TVHQNGH; -.
DR   OrthoDB; 810128at2759; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 379880; Expressed in neurula embryo and 19 other tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; ISS:UniProtKB.
DR   GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006241; P:CTP biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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   HAMAP; MF_01227; PyrG; 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   2: Evidence at transcript level;
KW   ATP-binding; Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW   Pyrimidine biosynthesis; Reference proteome.
FT   CHAIN           1..591
FT                   /note="CTP synthase 1-B"
FT                   /id="PRO_0000247031"
FT   DOMAIN          300..554
FT                   /note="Glutamine amidotransferase type-1"
FT   REGION          562..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        399
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        526
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        528
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   591 AA;  66887 MW;  85F5026B818DC071 CRC64;
     MKYILVTGGV ISGIGKGVIA SSVGTILKSS NLHVTSIKID PYINIDAGTF SPYEHGEVFV
     LDDGGEVDLD LGNYERFLDI RLTKDNNLTT GKIYQSVINK ERKGDYLGKT VQVVPHITEA
     IQEWVMRQAL IPVDEDGIEP EVCVIELGGT VGDIESMPFV EAFRQFQFKA RRENFCNIHV
     SLVPQPSATG EQKTKPTQNS VRELRGLGLS PDLVVCRCST PLDTSVKEKI SMFCHVEPQQ
     VICVHDVSSI YRVPLLLEEQ GVVDYFRQRL DLPIGRQPRR LLMKWKEMAD RYERLLESCS
     IALVGKYTKF SDSYASVIKA LEHSALAINH RLEIKYIDSA DLEQETLQEE PVRYHEAWQK
     LCSSDGILVP GGFGVRGTEG KIQAIAWARK QKKPFLGVCL GMQLAVVEFA RDVLDWKDAN
     STEFNPKTSH PVVIDMPEHN PGQMGGTMRL GKRRTIFHSQ NSVMKKLYGG HEYVEERHRH
     RYEVNPELRR ELEARGLKFV GQDTEGERME IVELEDHPYF VGVQYHPEFL SRPIKPSPPY
     FGLLLASVGR LSQYIERGCR LSPRDTYSDR SENSSPDAEI AELKLPMIDH E