ID A0A0S7X3D3_9BACT Unreviewed; 543 AA.
AC A0A0S7X3D3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 13-SEP-2023, entry version 28.
DE RecName: Full=CTP synthase (glutamine hydrolyzing) {ECO:0000256|ARBA:ARBA00012291};
DE EC=6.3.4.2 {ECO:0000256|ARBA:ARBA00012291};
GN ORFNames=AMJ49_03210 {ECO:0000313|EMBL:KPJ56902.1};
OS Parcubacteria bacterium DG_74_2.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1703766 {ECO:0000313|EMBL:KPJ56902.1, ECO:0000313|Proteomes:UP000051668};
RN [1] {ECO:0000313|EMBL:KPJ56902.1, ECO:0000313|Proteomes:UP000051668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_74_2 {ECO:0000313|EMBL:KPJ56902.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPJ56902.1}.
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DR EMBL; LJNF01000007; KPJ56902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7X3D3; -.
DR PATRIC; fig|1703766.3.peg.1259; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000051668; 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; 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; 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 3..266
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 306..536
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 517
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 519
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 543 AA; 61624 MW; 1D78D9DF7ACCBD46 CRC64;
MSKYIFIAGG VMSGIGKGVA TASIGRILKS KGFEVTAIKI DPYINVDAGT MNPIEHGEIF
VTKDGVECDQ DVGNYERFLD ENLTTENYIT TGRVYKAVIN RERNLEYQGR CVEVVPDIPN
EVIFRIKKAA KITKADFVLI EIGGTVGEYQ NLLFLEAARM MKLNNPKGVI FILVSYLPIP
KMIGEMKTKP TQTAVRLLNE AGIQPDIILA RARVPLDEPR KRKISIFCNV KPEDVISAPD
AKIIYEIPLN FEKENLGNRI LRKFNLKAKK NKLTDWEDLI KKIKSAKKIV KIGIVGKYFE
TGKFTLMDSY ISVIEAVKHA AWFFKRKPAI HWLSAGKYER NPKSVKELKN FDGIIVPGGF
GSRGIEGKIK AIEFCRRKKI PYLGLCLGMQ LAVVEFARNV CKIKNAHSTE FASGNKYQGV
IDVLPEQKAL LKDKRYGGTM RLGDYKCELK KGTKSWLAFE KVKNVLERHR HRYELNNEFR
KVLQKKGLDF AGINPKRDLV EIIELKNHPF FVASQFHPEF KSKPLKPHPL FREFIKTAIK
NAG
//
