PYRG2_HUMAN
ID PYRG2_HUMAN Reviewed; 586 AA.
AC Q9NRF8; B3KWM2; Q9BRI0; Q9H809; Q9H8K9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=CTP synthase 2;
DE EC=6.3.4.2;
DE AltName: Full=CTP synthetase 2;
DE AltName: Full=UTP--ammonia ligase 2;
GN Name=CTPS2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=10899599; DOI=10.1016/s0167-4781(00)00141-x;
RA van Kuilenburg A.B.P., Meinsma R., Vreken P., Waterham H.R.,
RA van Gennip A.H.;
RT "Identification of a cDNA encoding an isoform of human CTP synthetase.";
RL Biochim. Biophys. Acta 1492:548-552(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Retinoblastoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION.
RX PubMed=16179339; DOI=10.1074/jbc.m509622200;
RA Han G.-S., Sreenivas A., Choi M.-G., Chang Y.-F., Martin S.S.,
RA Baldwin E.P., Carman G.M.;
RT "Expression of human CTP synthetase in Saccharomyces cerevisiae reveals
RT phosphorylation by protein kinase A.";
RL J. Biol. Chem. 280:38328-38336(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571 AND SER-574, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571 AND SER-574, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568 AND SER-571, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571 AND SER-574, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571 AND SER-574, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC either L-glutamine or ammonia as the source of nitrogen. Constitutes
CC the rate-limiting enzyme in the synthesis of cytosine nucleotides.
CC {ECO:0000269|PubMed:10899599, ECO:0000269|PubMed:16179339}.
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 -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC CTP from UDP: step 2/2.
CC -!- INTERACTION:
CC Q9NRF8; P17812: CTPS1; NbExp=4; IntAct=EBI-740874, EBI-1042983;
CC Q9NRF8; Q9NRF8: CTPS2; NbExp=5; IntAct=EBI-740874, EBI-740874;
CC Q9NRF8; Q9NZD8: SPG21; NbExp=4; IntAct=EBI-740874, EBI-742688;
CC -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000305}.
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DR EMBL; AF226667; AAF91241.1; -; mRNA.
DR EMBL; AK023549; BAB14607.1; -; mRNA.
DR EMBL; AK024070; BAB14814.1; -; mRNA.
DR EMBL; AK125332; BAG54184.1; -; mRNA.
DR EMBL; AK125348; BAG54188.1; -; mRNA.
DR EMBL; AC073909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471074; EAW98912.1; -; Genomic_DNA.
DR EMBL; BC006256; AAH06256.2; -; mRNA.
DR EMBL; BC034986; AAH34986.1; -; mRNA.
DR CCDS; CCDS14175.1; -.
DR RefSeq; NP_001137474.1; NM_001144002.1.
DR RefSeq; NP_062831.3; NM_019857.4.
DR RefSeq; NP_787055.1; NM_175859.2.
DR RefSeq; XP_005274619.1; XM_005274562.3.
DR RefSeq; XP_006724566.1; XM_006724503.3.
DR PDB; 2V4U; X-ray; 2.30 A; A=297-562.
DR PDB; 2VKT; X-ray; 2.50 A; A=297-562.
DR PDB; 3IHL; X-ray; 2.80 A; A/B=1-275.
DR PDB; 6PK4; EM; 3.50 A; A/B/C/D=1-586.
DR PDB; 6PK7; EM; 3.10 A; A/D/E/F=1-586.
DR PDB; 7MH1; EM; 2.80 A; H/J/K/L=1-586.
DR PDB; 7MIH; EM; 2.80 A; A/B/C/E=1-586.
DR PDB; 7MII; EM; 2.70 A; A/B/C/E=1-586.
DR PDBsum; 2V4U; -.
DR PDBsum; 2VKT; -.
DR PDBsum; 3IHL; -.
DR PDBsum; 6PK4; -.
DR PDBsum; 6PK7; -.
DR PDBsum; 7MH1; -.
DR PDBsum; 7MIH; -.
DR PDBsum; 7MII; -.
DR AlphaFoldDB; Q9NRF8; -.
DR SMR; Q9NRF8; -.
DR BioGRID; 121144; 139.
DR IntAct; Q9NRF8; 15.
DR STRING; 9606.ENSP00000401264; -.
DR MEROPS; C26.966; -.
DR GlyGen; Q9NRF8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NRF8; -.
DR PhosphoSitePlus; Q9NRF8; -.
DR BioMuta; CTPS2; -.
DR DMDM; 74752919; -.
DR EPD; Q9NRF8; -.
DR jPOST; Q9NRF8; -.
DR MassIVE; Q9NRF8; -.
DR MaxQB; Q9NRF8; -.
DR PaxDb; Q9NRF8; -.
DR PeptideAtlas; Q9NRF8; -.
DR PRIDE; Q9NRF8; -.
DR ProteomicsDB; 82349; -.
DR Antibodypedia; 337; 209 antibodies from 27 providers.
DR DNASU; 56474; -.
DR Ensembl; ENST00000359276.9; ENSP00000352222.4; ENSG00000047230.15.
DR Ensembl; ENST00000380241.7; ENSP00000369590.3; ENSG00000047230.15.
DR Ensembl; ENST00000443824.5; ENSP00000401264.1; ENSG00000047230.15.
DR GeneID; 56474; -.
DR KEGG; hsa:56474; -.
DR MANE-Select; ENST00000359276.9; ENSP00000352222.4; NM_175859.3; NP_787055.1.
DR UCSC; uc004cxk.4; human.
DR CTD; 56474; -.
DR DisGeNET; 56474; -.
DR GeneCards; CTPS2; -.
DR HGNC; HGNC:2520; CTPS2.
DR HPA; ENSG00000047230; Low tissue specificity.
DR MIM; 300380; gene.
DR neXtProt; NX_Q9NRF8; -.
DR OpenTargets; ENSG00000047230; -.
DR PharmGKB; PA27021; -.
DR VEuPathDB; HostDB:ENSG00000047230; -.
DR eggNOG; KOG2387; Eukaryota.
DR GeneTree; ENSGT00910000144179; -.
DR HOGENOM; CLU_011675_5_0_1; -.
DR InParanoid; Q9NRF8; -.
DR OMA; FKPGTEW; -.
DR OrthoDB; 810128at2759; -.
DR PhylomeDB; Q9NRF8; -.
DR TreeFam; TF300379; -.
DR BioCyc; MetaCyc:HS00585-MON; -.
DR BRENDA; 6.3.4.2; 2681.
DR PathwayCommons; Q9NRF8; -.
DR Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates.
DR SignaLink; Q9NRF8; -.
DR SIGNOR; Q9NRF8; -.
DR UniPathway; UPA00159; UER00277.
DR BioGRID-ORCS; 56474; 14 hits in 703 CRISPR screens.
DR ChiTaRS; CTPS2; human.
DR EvolutionaryTrace; Q9NRF8; -.
DR GeneWiki; CTPS2; -.
DR GenomeRNAi; 56474; -.
DR Pharos; Q9NRF8; Tbio.
DR PRO; PR:Q9NRF8; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9NRF8; protein.
DR Bgee; ENSG00000047230; Expressed in jejunal mucosa and 162 other tissues.
DR ExpressionAtlas; Q9NRF8; baseline and differential.
DR Genevisible; Q9NRF8; HS.
DR GO; GO:0097268; C:cytoophidium; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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; IPI:IntAct.
DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006241; P:CTP biosynthetic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; TAS:ProtInc.
DR CDD; cd03113; CTPS_N; 1.
DR CDD; cd01746; GATase1_CTP_Synthase; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 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 PANTHER; PTHR11550; PTHR11550; 1.
DR Pfam; PF06418; CTP_synth_N; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00337; PyrG; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Glutamine amidotransferase; Ligase;
KW Nucleotide-binding; Phosphoprotein; Pyrimidine biosynthesis;
KW Reference proteome.
FT CHAIN 1..586
FT /note="CTP synthase 2"
FT /id="PRO_0000247033"
FT DOMAIN 300..554
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT REGION 563..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 399
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 526
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 528
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CONFLICT 220
FT /note="T -> S (in Ref. 2; BAB14814)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="F -> L (in Ref. 2; BAB14607)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="V -> A (in Ref. 2; BAB14607)"
FT /evidence="ECO:0000305"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:7MII"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:7MII"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:7MII"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:7MII"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:7MII"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:7MII"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:7MII"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:6PK4"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:7MII"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:7MII"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:7MII"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:7MII"
FT HELIX 90..102
FT /evidence="ECO:0007829|PDB:7MII"
FT TURN 103..108
FT /evidence="ECO:0007829|PDB:7MII"
FT HELIX 113..129
FT /evidence="ECO:0007829|PDB:7MII"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:7MII"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:7MII"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:6PK7"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:7MII"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:7MII"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:7MII"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:7MII"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:7MII"
FT HELIX 195..206
FT /evidence="ECO:0007829|PDB:7MII"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:7MII"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:7MII"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:7MII"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:7MII"
FT HELIX 252..258
FT /evidence="ECO:0007829|PDB:7MII"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:7MII"
FT HELIX 262..270
FT /evidence="ECO:0007829|PDB:7MII"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:6PK7"
FT HELIX 284..292
FT /evidence="ECO:0007829|PDB:7MII"
FT STRAND 297..306
FT /evidence="ECO:0007829|PDB:2V4U"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:2V4U"
FT HELIX 315..327
FT /evidence="ECO:0007829|PDB:2V4U"
FT STRAND 330..338
FT /evidence="ECO:0007829|PDB:2V4U"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:2V4U"
FT HELIX 344..349
FT /evidence="ECO:0007829|PDB:2V4U"
FT HELIX 351..363
FT /evidence="ECO:0007829|PDB:2V4U"
FT STRAND 365..369
FT /evidence="ECO:0007829|PDB:2V4U"
FT HELIX 378..390
FT /evidence="ECO:0007829|PDB:2V4U"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:2V4U"
FT HELIX 400..413
FT /evidence="ECO:0007829|PDB:2V4U"
FT STRAND 419..422
FT /evidence="ECO:0007829|PDB:2V4U"
FT STRAND 429..435
FT /evidence="ECO:0007829|PDB:2V4U"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:6PK4"
FT STRAND 443..447
FT /evidence="ECO:0007829|PDB:6PK4"
FT STRAND 449..458
FT /evidence="ECO:0007829|PDB:2V4U"
FT HELIX 463..467
FT /evidence="ECO:0007829|PDB:2V4U"
FT STRAND 472..480
FT /evidence="ECO:0007829|PDB:2V4U"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:2V4U"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:2V4U"
FT HELIX 490..492
FT /evidence="ECO:0007829|PDB:2V4U"
FT STRAND 495..503
FT /evidence="ECO:0007829|PDB:2V4U"
FT STRAND 508..518
FT /evidence="ECO:0007829|PDB:2V4U"
FT STRAND 520..526
FT /evidence="ECO:0007829|PDB:2V4U"
FT HELIX 527..530
FT /evidence="ECO:0007829|PDB:2V4U"
FT STRAND 533..535
FT /evidence="ECO:0007829|PDB:6PK7"
FT HELIX 538..548
FT /evidence="ECO:0007829|PDB:2V4U"
FT HELIX 551..556
FT /evidence="ECO:0007829|PDB:2V4U"
SQ SEQUENCE 586 AA; 65678 MW; AC1CF2E67D89741B CRC64;
MKYILVTGGV ISGIGKGIIA SSIGTILKSC GLRVTAIKID PYINIDAGTF SPYEHGEVFV
LNDGGEVDLD LGNYERFLDI NLYKDNNITT GKIYQHVINK ERRGDYLGKT VQVVPHITDA
VQEWVMNQAK VPVDGNKEEP QICVIELGGT IGDIEGMPFV EAFRQFQFKA KRENFCNIHV
SLVPQLSATG EQKTKPTQNS VRALRGLGLS PDLIVCRSST PIEMAVKEKI SMFCHVNPEQ
VICIHDVSST YRVPVLLEEQ SIVKYFKERL HLPIGDSASN LLFKWRNMAD RYERLQKICS
IALVGKYTKL RDCYASVFKA LEHSALAINH KLNLMYIDSI DLEKITETED PVKFHEAWQK
LCKADGILVP GGFGIRGTLG KLQAISWART KKIPFLGVCL GMQLAVIEFA RNCLNLKDAD
STEFRPNAPV PLVIDMPEHN PGNLGGTMRL GIRRTVFKTE NSILRKLYGD VPFIEERHRH
RFEVNPNLIK QFEQNDLSFV GQDVDGDRME IIELANHPYF VGVQFHPEFS SRPMKPSPPY
LGLLLAATGN LNAYLQQGCK LSSSDRYSDA SDDSFSEPRI AELEIS
