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Database: UniProt
Entry: F6V5U6_CIOIN
LinkDB: F6V5U6_CIOIN
Original site: F6V5U6_CIOIN 
ID   F6V5U6_CIOIN            Unreviewed;       673 AA.
AC   F6V5U6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 2.
DT   24-JAN-2024, entry version 71.
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   Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC   Cionidae; Ciona.
OX   NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000012365.3, ECO:0000313|Proteomes:UP000008144};
RN   [1] {ECO:0000313|Proteomes:UP000008144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12481130; DOI=10.1126/science.1080049;
RA   Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA   Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA   Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA   Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA   Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA   Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA   Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA   Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA   Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA   Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA   Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA   Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA   Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA   Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA   Satoh N., Rokhsar D.S.;
RT   "The draft genome of Ciona intestinalis: insights into chordate and
RT   vertebrate origins.";
RL   Science 298:2157-2167(2002).
RN   [2] {ECO:0000313|Ensembl:ENSCINP00000012365.3}
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   EMBL; EAAA01000920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F6V5U6; -.
DR   STRING; 7719.ENSCINP00000012365; -.
DR   Ensembl; ENSCINT00000012365.3; ENSCINP00000012365.3; ENSCING00000005983.3.
DR   GeneTree; ENSGT00910000144179; -.
DR   HOGENOM; CLU_011675_5_0_1; -.
DR   InParanoid; F6V5U6; -.
DR   OMA; FKPGTEW; -.
DR   TreeFam; TF300379; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000008144; Unassembled WGS sequence.
DR   GO; GO:0097268; C:cytoophidium; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR   GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006241; P:CTP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
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   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:UP000008144}.
FT   DOMAIN          8..282
FT                   /note="CTP synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06418"
FT   DOMAIN          320..531
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   REGION          649..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        654..673
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        408
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        601
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        603
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   673 AA;  75766 MW;  D65E1F01A15E1EE2 CRC64;
     ISQIKKMKYI LVSGGVISGI GKGVISSSIG TILKSYGHRV TAIKIDPYLN IDAGTFSPYE
     HGEVFVLDDG GEVDLDLGNY ERFLNVKLHK DNNITTGKIY QHVISKERRG DYLGKTVQDK
     VVPHVTDAIM EWVERVAKIP VNGDSAEPEV CIIEDQLGGT IGDIEGMPFV EAFRQFQFRV
     KPENFCNIHV SLLPQPSTTG EQKTKPTQHS VRALRGLGLS PDLICCRSQS PIEMSVKEKI
     SNFCHVAPEQ VITVHDVSSL YHVPMLLEKQ NLSAYFNKRL GLTKRPKKSM LSQWQNLAEK
     YDRIQSSCNI ALVGKYTRLE DSYASVIKAL RHAALAINRK LVLTIIDSTE LEEETLKEKP
     VVYHDAWKQL CLADGVLVPG GFGPRGVEGK VAAVKWARLN KKPYLGVCLG LQVAAIEFAR
     TVLNMEDANS SELNPNTSHP VVIDMPEHNK GDMGGTMRLG QRRTVFQTED SILRKLYNQP
     HNFVDERHRH RYEINPTYIH LYEEKGFMFV GHDVEGLRME IMELKGKLSS VCWLWLCEQL
     GIVTRTSVNM ENNSHSIVKK TNLIGLPRGI CADQPDNTKH CKHVCRLNYS NHPYFVGVQF
     HPEFLSRPIQ PSPPYLGLLL ASCNKLESYI QRGNRLSPRE RIYITDEESS ENELEVFSQL
     TGDSNSLSSI ESK
//
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