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Database: UniProt
Entry: A0A0E0A334_9ORYZ
LinkDB: A0A0E0A334_9ORYZ
Original site: A0A0E0A334_9ORYZ 
ID   A0A0E0A334_9ORYZ        Unreviewed;       624 AA.
AC   A0A0E0A334;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
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   Oryza glumipatula.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM05G28180.4};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM05G28180.4}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A., Panaud O., Oliveira A.C.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OGLUM05G28180.4}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) 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   AlphaFoldDB; A0A0E0A334; -.
DR   EnsemblPlants; OGLUM05G28180.4; OGLUM05G28180.4; OGLUM05G28180.
DR   Gramene; OGLUM05G28180.4; OGLUM05G28180.4; OGLUM05G28180.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
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:SF25; CTP SYNTHASE; 1.
DR   Pfam; PF06418; CTP_synth_N; 2.
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:UP000026961}.
FT   DOMAIN          2..154
FT                   /note="CTP synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06418"
FT   DOMAIN          168..288
FT                   /note="CTP synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06418"
FT   DOMAIN          329..562
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        544
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        546
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   624 AA;  68376 MW;  B34CD01B56C623F3 CRC64;
     MKYVLVTGGV VSGLGKGVTA SSIGVVLKDC GLRVTSIKID PYLNTDAGTM SPFEHGEVFV
     LDDGGEVDLD LGNYERFLDI KLTRDNNITT GKIYQAVIDK ERRGDYLGKT VQVVPHITDE
     IQEWIERVAM NPVDGTDEPA DVCVIELGGT IGDKIFSPHN DSGILDAGDI ESMPFIEALG
     QFSYRVGAGN FCLVHVSLVP VLNVVGEQKT KPTQHSVRGL RGLGLIPDIL ACRSTQPLEE
     NVKVKLAQFC HVPISNIVNL HDVTNIWHIP LLLRDQKAHE SILKVLDLQC VGKVPRAPKL
     TEWTERASKF DKLKTPVRIA MVGKYTGLSD SYLSVLKALL HASVALDRKL VVDWVPSCDL
     EDSAATETPD AYEKAWDLLK GAHGVLVPGG FGDRGVQGKI LAAKYARENN VPYLGICLGM
     QIAVIEFARS VMKLRGANST EFDPATTTPC VIFMPEGSKT HMGATMRLGS RRTFFQANTC
     KSAKLYGNAS YVDERHRHRY EVNPEMVPEF EKAGLSFVGR DESGTRMEII ELPTHRFFVG
     AQFHPEFKSR PGKPSPLFMG LIAASSGQLD HLLQQSCGVV SSPVRRGNYC NGATKQQKLY
     QNGHVKNGLV NGCYYANGNS ILHT
//
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