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Database: UniProt
Entry: H2TJ57_TAKRU
LinkDB: H2TJ57_TAKRU
Original site: H2TJ57_TAKRU 
ID   H2TJ57_TAKRU            Unreviewed;       592 AA.
AC   H2TJ57;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   24-JAN-2024, entry version 66.
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=ctps1 {ECO:0000313|Ensembl:ENSTRUP00000024711.2};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000024711.2, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000024711.2, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000024711.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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   RefSeq; XP_003969120.1; XM_003969071.2.
DR   AlphaFoldDB; H2TJ57; -.
DR   STRING; 31033.ENSTRUP00000024711; -.
DR   Ensembl; ENSTRUT00000024812.3; ENSTRUP00000024711.2; ENSTRUG00000009834.3.
DR   GeneID; 101070525; -.
DR   KEGG; tru:101070525; -.
DR   CTD; 322089; -.
DR   eggNOG; KOG2387; Eukaryota.
DR   GeneTree; ENSGT00910000144179; -.
DR   InParanoid; H2TJ57; -.
DR   OMA; EFNNAYR; -.
DR   OrthoDB; 166427at2759; -.
DR   TreeFam; TF300379; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000005226; Chromosome 12.
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:UP000005226}.
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          562..592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..592
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   592 AA;  66308 MW;  BB7924E941684B17 CRC64;
     MMKYILVTGG VISGIGKGII ASSVGTILKS CGLHVTAIKI DPYINIDAGT FSPYEHGEVF
     VLDDGGEVDL DLGNYERFLD IRLTRDNNLT TGKIYQSVIN KERRGDYLGK TVQVVPHITD
     AIQEWVVKQA KVSVDDDDVE PQVCVIELGG TVGDIESMPF IEAFRQFQFK VKRENFCNIH
     VSLIPQPGTT GEQKTKPTQN SVRELRGLGL SPDLIMCRCT TALETSVKEK ISMFCHVEPE
     QVICVHDVSS IYRVPLLLES QGVVSYLSRR LNMPIETRPR KMLTKWKEMS DRSDRLLEQC
     SIALVGKYTK FSDSYASVIK ALEHSALAIS HKLEVKYIDS ACLEPSTLQE EPVKYHEAWQ
     KLCSSGGVLV PGGFGVRGTE GKIHAISWAR KQKKPFLGVC LGMQLAVCEF ARNELGWEDA
     NSTEFDPETK HPVVIDMPEH NPGQMGGTMR LGKRRTLFKS PSSILRKLYG DAEYVEERHR
     HRFEVNPELK SHFEDKGFRF VGQDIEGERM EVIELDDHPY FVGVQYHPEF TSRPIKPSPP
     YLGLLLASAG KLQSYLQKGC RLSPRDTYSD QSGSSTPDSE ISELKLPSIS SE
//
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