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Database: UniProt
Entry: F9P7I3_STRCV
LinkDB: F9P7I3_STRCV
Original site: F9P7I3_STRCV 
ID   F9P7I3_STRCV            Unreviewed;       400 AA.
AC   F9P7I3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=CTP synthase (glutamine hydrolyzing) {ECO:0000256|ARBA:ARBA00012291};
DE            EC=6.3.4.2 {ECO:0000256|ARBA:ARBA00012291};
GN   Name=pyrG {ECO:0000313|EMBL:EGV08572.1};
GN   ORFNames=HMPREF1042_1845 {ECO:0000313|EMBL:EGV08572.1};
OS   Streptococcus constellatus subsp. pharyngis SK1060 = CCUG 46377.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus; Streptococcus anginosus group.
OX   NCBI_TaxID=1035184 {ECO:0000313|EMBL:EGV08572.1, ECO:0000313|Proteomes:UP000003287};
RN   [1] {ECO:0000313|EMBL:EGV08572.1, ECO:0000313|Proteomes:UP000003287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK1060 {ECO:0000313|EMBL:EGV08572.1,
RC   ECO:0000313|Proteomes:UP000003287};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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; AFUP01000004; EGV08572.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9P7I3; -.
DR   eggNOG; COG0504; Bacteria.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000003287; Unassembled WGS sequence.
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; 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; 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}.
FT   DOMAIN          1..131
FT                   /note="CTP synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06418"
FT   DOMAIN          166..390
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        245
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        372
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        374
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   400 AA;  44567 MW;  46A81DEBA50E0FE5 CRC64;
     MIITEVGGTV GDIESLPFLE ALRQMKADVG ADNVMYIHTT LLPYLKAAGE MKTKPTQHSV
     KELRGLGIQP NMLVIRTEKP AGQNIKNKLA QFCDVAPEAV IESLDVEHLY QIPLNLQAQN
     MDQIVCDHLK LDVPEADMTD WSAMVDKVMN LKKQVKIALV GKYVELPDAY ISVVEALKHS
     GYANDAEIKL SWINANDVTT ENVAELLNDA DGIIVPGGFG HRGTEGKIAT IQYARENDVP
     MLGICLGMQL TCVEFARHVL GFNDANSSEL NPDTQHPVID LMRDQIDVED MGGTLRLGLY
     PSKLKRGSKA AAAYDNQEVV QRRHRHRYEF NNEFRQQFED AGFVFSGVSP DNRLVEIVEI
     PENKFFVACQ YHPELSSRPN RPEGLYTAFV TAAVENSENK
//
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