ID A0A087XGQ9_POEFO Unreviewed; 588 AA.
AC A0A087XGQ9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=CTP synthase {ECO:0000256|RuleBase:RU810713};
DE EC=6.3.4.2 {ECO:0000256|RuleBase:RU810713};
DE AltName: Full=UTP--ammonia ligase {ECO:0000256|RuleBase:RU810713};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000004962.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000004962.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC either L-glutamine or ammonia as the source of nitrogen.
CC {ECO:0000256|RuleBase:RU810713}.
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:0000256|ARBA:ARBA00000314,
CC ECO:0000256|RuleBase:RU810713};
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC CTP from UDP: step 2/2. {ECO:0000256|ARBA:ARBA00005171,
CC ECO:0000256|RuleBase:RU810713}.
CC -!- SIMILARITY: Belongs to the CTP synthase family.
CC {ECO:0000256|ARBA:ARBA00007533, ECO:0000256|RuleBase:RU810713}.
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DR EMBL; AYCK01007349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01007350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007558471.1; XM_007558409.2.
DR RefSeq; XP_016529977.1; XM_016674491.1.
DR RefSeq; XP_016529978.1; XM_016674492.1.
DR RefSeq; XP_016529979.1; XM_016674493.1.
DR AlphaFoldDB; A0A087XGQ9; -.
DR STRING; 48698.ENSPFOP00000004962; -.
DR Ensembl; ENSPFOT00000004971.2; ENSPFOP00000004962.2; ENSPFOG00000004872.2.
DR GeneID; 103142373; -.
DR KEGG; pfor:103142373; -.
DR CTD; 322089; -.
DR eggNOG; KOG2387; Eukaryota.
DR GeneTree; ENSGT00910000144179; -.
DR OrthoDB; 166427at2759; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd03113; CTPS_N; 1.
DR CDD; cd01746; GATase1_CTP_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00337; PyrG; 1.
DR PANTHER; PTHR11550; CTP SYNTHASE; 1.
DR PANTHER; PTHR11550:SF0; CTP SYNTHASE-RELATED; 1.
DR Pfam; PF06418; CTP_synth_N; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU810713};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU810713};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU810713};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975,
KW ECO:0000256|RuleBase:RU810713};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760}.
FT DOMAIN 3..273
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 312..540
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT REGION 565..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 400
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 527
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 529
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 588 AA; 65837 MW; 13590F0F919A3599 CRC64;
MMKYILVTGG VISGIGKGII ASSVGTILKS CGLHVTAIKI DPYINIDAGT FSPYEHGEVF
VLDDGGEVDL DLGNYERFLD IRLTKDNNLT TGKIYQSVIN KERRGDYLGK TVQVVPHITD
AIQEWVMKQA KVPVDGDETE PQVCVIELGG TVGDIESMPF IEAFRQFQFK VKRENFCNIH
VSLIPQPSAT GEQKTKPTQN SVRELRGLGL SPDLIMCRCT TALENSVKEK ISMFCHVEPQ
QVICVHDVSS IYRVPLLLED QGVVGYLSSR LNMPIETKSR TMLTKWKEMS DRSDRLLEQC
SIALVGKYTK FSDSYASVIK ALEHSALAIS HRLEVKYIDS ASLEPTTLQE EPVKYHDAWQ
KLCSADGVLV PGGFGVRGTE GKIHAINWAR KQRKPFLGVC LGMQLAVCEY ARNVLGWPDA
NSTEFDPESK HPVVIDMPEH NPGQMGGTMR LGKRRTIFKT SNSIMRKLYG DAEYVEERHR
HRFEVNPELK SHFEDKGFHF VGQDVEGERM EIIELDDHPY FVGVQYHPEF TSRPIKPSPP
YLGLLLAAAG KLQGYLQKGC RLSPRDVYSD RSGSSTPDSE ISEIPTCY
//
