ID F5HPC6_BORGR Unreviewed; 201 AA.
AC F5HPC6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=CTP synthase (glutamine hydrolyzing) {ECO:0000256|ARBA:ARBA00012291};
DE EC=6.3.4.2 {ECO:0000256|ARBA:ARBA00012291};
DE Flags: Fragment;
GN Name=pyrG {ECO:0000313|EMBL:BAK23830.1};
OS Borreliella garinii (Borrelia garinii).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borreliella.
OX NCBI_TaxID=29519 {ECO:0000313|EMBL:BAK23830.1};
RN [1] {ECO:0000313|EMBL:BAK23830.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=J-15 {ECO:0000313|EMBL:BAK23830.1};
RX PubMed=21411595; DOI=10.1128/JCM.02544-10;
RA Takano A., Nakao M., Masuzawa T., Takada N., Yano Y., Ishiguro F.,
RA Fujita H., Ito T., Ma X., Oikawa Y., Kawamori F., Kumagai K., Mikami T.,
RA Hanaoka N., Ando S., Honda N., Taylor K., Tsubota T., Konnai S.,
RA Watanabe H., Ohnishi M., Kawabata H.;
RT "Multilocus Sequence Typing Implicates Rodents as the Main Reservoir Host
RT of Human-Pathogenic Borrelia garinii in Japan.";
RL J. Clin. Microbiol. 49:2035-2039(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB556298; BAK23830.1; -; Genomic_DNA.
DR AlphaFoldDB; F5HPC6; -.
DR UniPathway; UPA00159; UER00277.
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-KW.
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; IPR027417; P-loop_NTPase.
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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT DOMAIN 2..102
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 141..199
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAK23830.1"
FT NON_TER 201
FT /evidence="ECO:0000313|EMBL:BAK23830.1"
SQ SEQUENCE 201 AA; 21987 MW; 3FCA53FFE003F972 CRC64;
GSGNIAFIHL TYVPSPAGIN EQKSKPTQQS VKTLNKAGIF PDLIIARSSQ VLTDQIRKKV
AMFCNVESTS IIDNIDVSTI YEIPISFYKQ GVHEILSSKL NIKVDPKIEE LSKLVGIIKS
NFFVPKKIIN IAICGKYAEL DDSYASIRES LVHVGANLDL LIKSTLIDSN DLNESYLKEF
DGIIVPGGFG GKGYEGKIIA I
//