GenomeNet

Database: UniProt
Entry: F1KXY5_ASCSU
LinkDB: F1KXY5_ASCSU
Original site: F1KXY5_ASCSU 
ID   F1KXY5_ASCSU            Unreviewed;       712 AA.
AC   F1KXY5;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 38.
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   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY42739.1};
RN   [1] {ECO:0000313|EMBL:ADY42739.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21685128; DOI=10.1101/gr.121426.111;
RA   Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA   Davis R.E.;
RT   "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT   functional diversification, and novel developmental profiles.";
RL   Genome Res. 21:1462-1477(2011).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JI167766; ADY42739.1; -; mRNA.
DR   AlphaFoldDB; F1KXY5; -.
DR   UniPathway; UPA00159; UER00277.
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   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; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   2: Evidence at transcript level;
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          15..285
FT                   /note="CTP synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06418"
FT   DOMAIN          328..512
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        417
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        612
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        614
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   712 AA;  78474 MW;  85BFF0111060E037 CRC64;
     MGNTKELAMN VPPVKMVLVT GGVISGVGKG IISSSLGVLL KAHGYRVSAI KIDPYINIDA
     GTFSPFEHGE VFVLDDGGEV DLDLGNYERF LNVRLTRDNN ITTGKIYQHV IERERRGDYL
     GKTVQTIPHV TGAIVDWVER VAAIPVDGTN QRPDVCIIEL GGTIGDIEGM PFVAAFEKFQ
     RPAYRDLLMT VHVSLILDPK TTGEPKTKPM QNSVRNLRAS GLIPDLLMCR SEKPLSKALR
     EKIAAFGMVE PEQVIGVHDV ANIYKVPLLL HQQNVLEMIV ERLKLPHVDS LGAISLTPNM
     FQWTHLSNLC DSFAEEVRIA LVGKYVRITD AYASVNKALK HAAIHAKRKL IIEYVDAEYL
     EETTDPERIA DYNRAWQAVR NSHGILVPGG FGDRGIEGKI AACGYARRNE IPFLGICLGM
     QCAAIEFARN VLGIKRANST EFDKEITGDE QVVIDMPEHD AVNKGAGGTM RLGLRETVFL
     TDNCKLRKLY GTRRVNERHR HRFEVNPEVV SRLSRSGLLF VGMGTDEKPT SNMAERRTAS
     SAVLMQLAEV ETRSNSSQED LSEPIPNAVD NNLLAKIDEL CKRGGDGKEK AAVRMEMLEL
     QGHPYFVGVQ YHPEYLSHPL QPSPPFFGLV CAASGQLESF LRGSKIPSPM SILKSAENYS
     NGLTNDTLRA THSFVNKMGS LNEQVNGGFE EGGAGDSENT KRIVFEVTQT TG
//
DBGET integrated database retrieval system