GenomeNet

Database: UniProt
Entry: F8KSF8_HELBC
LinkDB: F8KSF8_HELBC
Original site: F8KSF8_HELBC 
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}.
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; 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
//
DBGET integrated database retrieval system