ID F8KSF8_HELBC Unreviewed; 543 AA.
AC F8KSF8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=CTP synthase (glutamine hydrolyzing) {ECO:0000256|ARBA:ARBA00012291};
DE EC=6.3.4.2 {ECO:0000256|ARBA:ARBA00012291};
GN OrderedLocusNames=HBZC1_07410 {ECO:0000313|EMBL:CCB79727.1};
OS Helicobacter bizzozeronii (strain CIII-1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1002804 {ECO:0000313|EMBL:CCB79727.1, ECO:0000313|Proteomes:UP000008387};
RN [1] {ECO:0000313|EMBL:CCB79727.1, ECO:0000313|Proteomes:UP000008387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIII-1 {ECO:0000313|EMBL:CCB79727.1,
RC ECO:0000313|Proteomes:UP000008387};
RX PubMed=21705603; DOI=10.1128/JB.05439-11;
RA Schott T., Rossi M., Hanninen M.L.;
RT "Genome sequence of Helicobacter bizzozeronii strain CIII-1, an isolate
RT from human gastric mucosa.";
RL J. Bacteriol. 193:4565-4566(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}.
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DR EMBL; FR871757; CCB79727.1; -; Genomic_DNA.
DR RefSeq; WP_013890191.1; NC_015674.1.
DR AlphaFoldDB; F8KSF8; -.
DR STRING; 1002804.HBZC1_07410; -.
DR KEGG; hbi:HBZC1_07410; -.
DR eggNOG; COG0504; Bacteria.
DR HOGENOM; CLU_011675_5_0_7; -.
DR OMA; EFNNAYR; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000008387; Chromosome.
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, ECO:0000313|EMBL:CCB79727.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000008387}.
FT DOMAIN 4..266
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 305..540
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 521
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 523
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 543 AA; 60555 MW; FBE7C544B64A586D CRC64;
MQTRFVFITG GVLSSLGKGV ASSSLAHLLK LCAFKVDILK IDPYINVDPG TLSPFEHGEV
FVTADGSETD LDIGHYERFL NKDFSKANNF TTGQIYLSVI EKEREGKYLG KTIQVIPHIV
EEIKERILKL GEGKDFLIVE VGGTVGDIEG MVYLEAIREL RSALGSKQVA NIHVTLVPLI
ATSHELKTKP TQHSIIELRR LGVSANIILA RCSQDLSPEI KTKIASSCDV CVENVIQAKD
APTIYACPTH YLQEGLLDAL FRHFNLQASL DQHALQQWED LVYHILNPKR TIKIGFVGKY
VHLGESYKSY LESMVCVGAH LKVKVDVVFI NSEDLQNQEG ESDTQLKQRI ARTLQDLQGI
LIPGGFGHRG IEGMINAITY ARENHVPLFG VCLGAQLMVV EFARHVLGLS GAHSSEFDKN
APHKVVDLLH SQTNTTHKGS SMRLGTHAIT LKKDSQIAQI YHAENILERH RHRYTINPAY
LEDYAKHGLE VIATSLDDNQ QSIIEALTLK NRYFFLGVQY HPEFTSRLIA PNPLFKAFVQ
ACM
//