ID A0A1J4T8N1_9BACT Unreviewed; 555 AA.
AC A0A1J4T8N1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE RecName: Full=CTP synthase (glutamine hydrolyzing) {ECO:0000256|ARBA:ARBA00012291};
DE EC=6.3.4.2 {ECO:0000256|ARBA:ARBA00012291};
GN ORFNames=AUJ35_01425 {ECO:0000313|EMBL:OIO07856.1};
OS Candidatus Falkowbacteria bacterium CG1_02_41_21.
OC Bacteria; Candidatus Falkowbacteria.
OX NCBI_TaxID=1805147 {ECO:0000313|EMBL:OIO07856.1, ECO:0000313|Proteomes:UP000182860};
RN [1] {ECO:0000313|EMBL:OIO07856.1, ECO:0000313|Proteomes:UP000182860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_41_21 {ECO:0000313|EMBL:OIO07856.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(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}.
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:OIO07856.1}.
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DR EMBL; MNUV01000024; OIO07856.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4T8N1; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000182860; 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 8..271
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 314..544
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 392
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 525
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 527
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 555 AA; 62490 MW; 8C9380DFAA530C4F CRC64;
MAKKIPTKYI FVVGGVMSGV GKGITTASIG EILQTKGYSV SAIKMDPYIN IDAGTMNPIE
HGEVFVTEDG DETDQDIGNY ERFLNKNIYK ENYMTTGRIY QTVINKERNL EYKGKCVQVV
PHIPMEIRDR INQAVKKTGA EIMIIEIGGT VGEYENLLFL EAARIMKLYS PKDVVFVMVS
YLPVPNMIGE MKTKPTQHAV RNLNSAGIQP DFIVARSEVA IDQHRREKIA VNCNIHPENV
IAAPDADSIY DIPLNFEKDK LGDRILKQLD LKARDKKPDN NSAWEQMVKN TKIKSPEVAI
GIVGKYFATG DFSLTDSYIS VIEAVKHAAA YNHCRVKLEW INAEDVEKQG TQILKKLVGI
IVPQGWGSRG AEGKIATIKY CRTNNIPYFG LCYGMQMAVI EFARDACDLK GANSEEVDEE
TLYSVIHIMP GQEKLIKEKG YGGTIRLGGW PCKIMPQTRL AKAYARFSEQ KVVSERHRHR
YEFNNDYRTV FEKNGLTIAG TSPDGLIVEA IEITKHPFFI GTQFHPEYIS RPLAPHPLFV
EFVKVCKELK PKKKK
//
