ID A0A1J0FA14_9PHYC Unreviewed; 540 AA.
AC A0A1J0FA14;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=CTP synthase (glutamine hydrolyzing) {ECO:0000256|ARBA:ARBA00012291};
DE EC=6.3.4.2 {ECO:0000256|ARBA:ARBA00012291};
GN Name=OS5_333R {ECO:0000313|EMBL:APC25846.1};
OS Only Syngen Nebraska virus 5.
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Algavirales; Phycodnaviridae; Chlorovirus.
OX NCBI_TaxID=1917232 {ECO:0000313|EMBL:APC25846.1};
RN [1] {ECO:0000313|EMBL:APC25846.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OSyNE-5 {ECO:0000313|EMBL:APC25846.1};
RX PubMed=27816636; DOI=10.1016/j.virol.2016.10.013;
RA Quispe C.F., Esmael A., Sonderman O., McQuinn M., Agarkova I., Battah M.,
RA Duncan G.A., Dunigan D.D., Smith T.P., De Castro C., Speciale I., Ma F.,
RA Van Etten J.L.;
RT "Characterization of a new chlorovirus type with permissive and non-
RT permissive features on phylogenetically related algal strains.";
RL Virology 500:103-113(2016).
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 -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC CTP from UDP: step 2/2. {ECO:0000256|ARBA:ARBA00005171}.
CC -!- SIMILARITY: Belongs to the CTP synthase family.
CC {ECO:0000256|ARBA:ARBA00007533}.
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DR EMBL; KX857749; APC25846.1; -; Genomic_DNA.
DR RefSeq; YP_009325851.1; NC_032001.1.
DR GeneID; 30344147; -.
DR KEGG; vg:30344147; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000204497; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
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};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000204497}.
FT DOMAIN 9..269
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 306..530
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 386
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 511
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 513
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 540 AA; 60780 MW; 169413432C5DC78B CRC64;
MTENKKHKKF MFITGGVSSS LGKGLAAASI ASLLERRCLK IAMLKMDPYI NVDPGTMSPT
QHGEVFVTDD GAETDLDLGH YERFTSLTLK RESNFTTGQV YLKVIENERE GSYLGKTVQV
VPHITDEIKR RIHIAAEKSD ILIGEIGGTV GDIESLPFIE AIRQLSHDEG TANVLFIHLV
LLPYIATAGE LKSKPAQHSV KELMSQGLLP HIIISRSDRP VDEDTLDKIS RFCNISRKNV
FQSIDMDSIY KVPLEFHKQG LDERISELLG FRVPDAKIED LEKVVYNFTH PLREVKIGIV
GKYTDLIESY KSLVEALHHG AIANRLKFKP IYIDSEQLES GERLDELLSH VQGILVPGGF
GVRGTKGIIK AIEYARTKKI PFFGICLGMQ LAVIEYARHV AGITDATSEE FQSGGTHLIH
YMKGQKKEGT KGGTMRLGSY DCSLEEGTLG RKIYQTDTIH ERHRHRLEVN NMYIDALTEA
HMTFSGFNKE LNLVEVIELK DHPFFIACQY HPEFKSKPFS PHPLFKTFIE EADRKNLNTK
//
