ID A0A2C9JR43_BIOGL Unreviewed; 715 AA.
AC A0A2C9JR43;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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};
GN Name=106064479 {ECO:0000313|EnsemblMetazoa:BGLB006657-PB};
OS Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Planorbidae; Biomphalaria.
OX NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB006657-PB, ECO:0000313|Proteomes:UP000076420};
RN [1] {ECO:0000313|EnsemblMetazoa:BGLB006657-PB}
RP IDENTIFICATION.
RC STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB006657-PB};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 RefSeq; XP_013078497.1; XM_013223043.1.
DR AlphaFoldDB; A0A2C9JR43; -.
DR STRING; 6526.A0A2C9JR43; -.
DR EnsemblMetazoa; BGLB006657-RB; BGLB006657-PB; BGLB006657.
DR VEuPathDB; VectorBase:BGLB006657; -.
DR OrthoDB; 166427at2759; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000076420; Unassembled WGS sequence.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01746; GATase1_CTP_Synthase; 1.
DR CDD; cd00947; TBP_aldolase_IIB; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR004468; CTP_synthase.
DR InterPro; IPR017456; CTP_synthase_N.
DR InterPro; IPR000771; FBA_II.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR033828; GATase1_CTP_Synthase.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00167; cbbA; 1.
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; PF01116; F_bP_aldolase; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF51569; Aldolase; 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}.
FT DOMAIN 1..217
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 253..472
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 331
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 457
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 459
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 715 AA; 79891 MW; 856A1E1ED4D2501C CRC64;
MNPYQHGEVF VTKDGGETDL DLGHYERFTS VELTKNSNIT AGRIYYDVLI KERKGTFLGK
TIQVVPHITD EIKNNIYRTA EESKSEVLIV EFGGTVGDIE IYPFVEVARQ IYLEKGRENV
MFIFVTLVPK IRVNNEIKTK PTQFAVKELG RIGIQPDILV LRCEEDLENE VLEKISMFCN
VQTNCVMKAI DVDNIYKIPI YLHNQEFDQR VIERLGLLNN PIKLDNWYSL INKIENLNKE
ITIGLVGKYI ELEDAYKSVI ESAKIAGFHN LAKVKIKMIN ARKLNNSNIQ EQFRNVDGVI
IPGGFGYEGV EGKILAIKYT RENNVPMLGI CLGMQLALVE FARNILNYET ANSTEFDPET
DHPIVHIIRG KSEQDEKGGT LRLGNYNCEL KNNSLAYECY GQKIIQERHR HRYEVNSKYI
KEFEKHGMIF SGINPDNHLC EIVELENHPF FIASQYHPEF KNNLTNPNPL FIGVSEGAAK
YFGGYNTVVG IVTNLMIDLN ITVPVAVHLD HGSSIESAKK AVDAGFSSIM IDGSHFSIDE
NIRITKEVVA MCKPKGISVE GEVGLVAGEE DGVHGGSAAT YADENECIRM AKEGGIDFLA
ATLGSVHGHY NGAPKLGFEQ MVTISSKADI PLVLHGGSGI PDADIVKAIK SGQSKINVNT
ECQDAFAHAL NKYFANKMDQ ADKGYDPRKI IGFGIKETKR VIIEKIKLFG SDNKA
//
