ID A0A158P5V0_ANGCA Unreviewed; 606 AA.
AC A0A158P5V0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 Angiostrongylus cantonensis (Rat lungworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0000023101-mRNA-1};
RN [1] {ECO:0000313|Proteomes:UP000035642}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:ACAC_0000023101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) 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 AlphaFoldDB; A0A158P5V0; -.
DR STRING; 6313.A0A158P5V0; -.
DR WBParaSite; ACAC_0000023101-mRNA-1; ACAC_0000023101-mRNA-1; ACAC_0000023101.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000035642; 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; 2.
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; 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; 2.
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:UP000035642}.
FT DOMAIN 2..204
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 295..473
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 378
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 558
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 560
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 606 AA; 67746 MW; C2F4B7D0C130B6E4 CRC64;
MKYILVTGGV ISGVGKGIIS SSIGVLLKNN GYKVSVIKID PYLNIDAGTF SPYEHGEVFV
LDDGAEVDLD LGNYERFLSV RLTRDNNITT GKMFQHVTER ERRGDYCGQT VQLIPHFTDA
VIQWIERVAR IPVDGTIECP DVCIIELGGT VGDIEGMTYL AAFERFQRPA LKDCMMNVHV
SLVVHPYATG EPKTKPMQNS VSFLELRAGY PFNFKLIFVV GIHDVSNIYK VPLLLQEQHV
LDIIIHRLHL KPINKVVQRN LKFNMCHWRQ LSELCDSFNE EVVIALVGKY VKIDDAYASV
NKALKHAAIH SKRALVDAEL LESGKPLELK ARCDSAWEIV RSSHGIIVPG GFDKRGVEGM
IKTCQYAREN GVPFLGVCLG MQCAAIEVAR NILGISNANS TEFNKDLHEN EQIIIDMPEH
NVESRGLGGT MRLGRRTSVF LTEQCKLRRL YGKDEIEERH RHRYEVNPRL VPDLSSKGLL
FVGMGVDETT CTTLTNHCRT QSSAALMKMA KDYRTNEDLL STITDLCHQG GDGVIRPAVR
MEICEMKGHP YFVGTQFHPE YLSHPLQPSP PFLGLLLAAS GQLDVSYLQG VRTPSPMFSL
MEQCST
//
