GenomeNet

Database: UniProt
Entry: B1X4F7_PAUCH
LinkDB: B1X4F7_PAUCH
Original site: B1X4F7_PAUCH 
ID   B1X4F7_PAUCH            Unreviewed;       531 AA.
AC   B1X4F7;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=CTP synthase {ECO:0000256|RuleBase:RU810713};
DE            EC=6.3.4.2 {ECO:0000256|RuleBase:RU810713};
DE   AltName: Full=UTP--ammonia ligase {ECO:0000256|RuleBase:RU810713};
GN   Name=pyrG {ECO:0000313|EMBL:ACB42826.1};
GN   OrderedLocusNames=PCC_0386 {ECO:0000313|EMBL:ACB42826.1};
OS   Paulinella chromatophora.
OG   Plastid; Organellar chromatophore {ECO:0000313|EMBL:ACB42826.1}.
OC   Eukaryota; Sar; Rhizaria; Cercozoa; Imbricatea; Silicofilosea; Euglyphida;
OC   Paulinellidae; Paulinella.
OX   NCBI_TaxID=39717 {ECO:0000313|EMBL:ACB42826.1};
RN   [1] {ECO:0000313|EMBL:ACB42826.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Gloeckner G., Nowack E., Melkonian M.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACB42826.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18356055; DOI=10.1016/j.cub.2008.02.051;
RA   Nowack E.C.M., Melkonian M., Gloeckner G.;
RT   "Chromatophore genome sequence of Paulinella sheds light on acquisition of
RT   photosynthesis by eukaryotes.";
RL   Curr. Biol. 18:410-418(2008).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC       either L-glutamine or ammonia as the source of nitrogen.
CC       {ECO:0000256|RuleBase:RU810713}.
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         ECO:0000256|RuleBase:RU810713};
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC       CTP from UDP: step 2/2. {ECO:0000256|ARBA:ARBA00005171,
CC       ECO:0000256|RuleBase:RU810713}.
CC   -!- SIMILARITY: Belongs to the CTP synthase family.
CC       {ECO:0000256|ARBA:ARBA00007533, ECO:0000256|RuleBase:RU810713}.
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; CP000815; ACB42826.1; -; Genomic_DNA.
DR   RefSeq; YP_002049036.1; NC_011087.1.
DR   AlphaFoldDB; B1X4F7; -.
DR   MEROPS; C26.964; -.
DR   GeneID; 6481348; -.
DR   UniPathway; UPA00159; UER00277.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniRule.
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   HAMAP; MF_01227; PyrG; 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, ECO:0000256|RuleBase:RU810713};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU810713};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU810713}; Plastid {ECO:0000313|EMBL:ACB42826.1};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975,
KW   ECO:0000256|RuleBase:RU810713}.
FT   DOMAIN          3..267
FT                   /note="CTP synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06418"
FT   DOMAIN          303..526
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        381
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        507
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        509
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   531 AA;  58726 MW;  565C1185A0581B55 CRC64;
     MAKFVFVTGG VVSSIGKGIV AASLGRLLKS RSYNVSILKL DPYLNVDPGT MSPYQHGEVF
     VTEDGAETDL DLGHYERFTD TPMSKLNSVT TGSIYQSVIS KERRGGYNGG TVQVIPHITK
     EIRERIHLVA SSSRADIVIT EIGGTVGDIE SLPFLEAIRE FRGDVGQHDV AYVHVTLLPY
     IGTSGEIKTK PTQHSVKELR SIGIQPDLLV CRCDREITEE LRGKIGGFCG VSKHAVIPAI
     DADSIYAVPL TLEEHGLCRE ILKVLNLINY KSDMENWEQL VYRLRHPGPS VKIALVGKYI
     QLNDAYLSVV ESLRHACLHQ DASLNLQWIC AEQIEQQGAE SLLKGIDALV VPGGFGNRGV
     DGKIAAIQWA REQRIPFLGL CLGMQCAVIE WARNIAGLIN ATSTELESET EHPVIHLLPE
     QQNIIDRGGT MRLGISPCKI KVGTMAARLY GKKVVYERHR HRYEFNNAYR NLFIESGYVI
     SGTSPDGRLV ELIELPGHPF FTACQYHPEF LSRLGVPHPL FRGLIEAAQQ N
//
DBGET integrated database retrieval system