(data stored in SCRATCH zone)

SWISSPROT: D1YVU7_METPS

ID   D1YVU7_METPS            Unreviewed;       545 AA.
AC   D1YVU7;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 63.
DE   RecName: Full=CTP synthase {ECO:0000256|HAMAP-Rule:MF_01227};
DE            EC=6.3.4.2 {ECO:0000256|HAMAP-Rule:MF_01227};
DE   AltName: Full=Cytidine 5'-triphosphate synthase {ECO:0000256|HAMAP-Rule:MF_01227};
DE   AltName: Full=Cytidine triphosphate synthetase {ECO:0000256|HAMAP-Rule:MF_01227};
DE            Short=CTP synthetase {ECO:0000256|HAMAP-Rule:MF_01227};
DE            Short=CTPS {ECO:0000256|HAMAP-Rule:MF_01227};
DE   AltName: Full=UTP--ammonia ligase {ECO:0000256|HAMAP-Rule:MF_01227};
GN   Name=pyrG {ECO:0000256|HAMAP-Rule:MF_01227,
GN   ECO:0000313|EMBL:BAI60569.1};
GN   OrderedLocusNames=MCP_0497 {ECO:0000313|EMBL:BAI60569.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60569.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC       either L-glutamine or ammonia as the source of nitrogen. Regulates
CC       intracellular CTP levels through interactions with the four
CC       ribonucleotide triphosphates. {ECO:0000256|HAMAP-Rule:MF_01227}.
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|HAMAP-Rule:MF_01227};
CC   -!- ACTIVITY REGULATION: Allosterically activated by GTP, when glutamine is
CC       the substrate; GTP has no effect on the reaction when ammonia is the
CC       substrate. The allosteric effector GTP functions by stabilizing the
CC       protein conformation that binds the tetrahedral intermediate(s) formed
CC       during glutamine hydrolysis. Inhibited by the product CTP, via
CC       allosteric rather than competitive inhibition. {ECO:0000256|HAMAP-
CC       Rule:MF_01227}.
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC       CTP from UDP: step 2/2. {ECO:0000256|HAMAP-Rule:MF_01227}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01227}.
CC   -!- MISCELLANEOUS: CTPSs have evolved a hybrid strategy for distinguishing
CC       between UTP and CTP. The overlapping regions of the product feedback
CC       inhibitory and substrate sites recognize a common feature in both
CC       compounds, the triphosphate moiety. To differentiate isosteric
CC       substrate and product pyrimidine rings, an additional pocket far from
CC       the expected kinase/ligase catalytic site, specifically recognizes the
CC       cytosine and ribose portions of the product inhibitor.
CC       {ECO:0000256|HAMAP-Rule:MF_01227}.
CC   -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01227}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01227}.
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DR   EMBL; AP011532; BAI60569.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0497; -.
DR   MEROPS; C26.964; -.
DR   EnsemblBacteria; BAI60569; BAI60569; MCP_0497.
DR   KEGG; mpd:MCP_0497; -.
DR   PATRIC; fig|304371.9.peg.511; -.
DR   eggNOG; arCOG00063; Archaea.
DR   eggNOG; COG0504; LUCA.
DR   HOGENOM; HOG000077514; -.
DR   KO; K01937; -.
DR   OMA; EFNNAYR; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000001882; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   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   PANTHER; PTHR11550; PTHR11550; 1.
DR   Pfam; PF06418; CTP_synth_N; 1.
DR   Pfam; PF00117; GATase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00337; PyrG; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1YVU7.
DR   SWISS-2DPAGE; D1YVU7.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01227};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01227};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01227};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01227};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01227};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01227};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882}.
FT   DOMAIN          290..528
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51273"
FT   NP_BIND         13..18
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   NP_BIND         147..149
FT                   /note="Allosteric inhibitor CTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   NP_BIND         186..191
FT                   /note="Allosteric inhibitor CTP; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   NP_BIND         186..191
FT                   /note="UTP; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   REGION          1..265
FT                   /note="Amidoligase domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   REGION          379..382
FT                   /note="L-glutamine binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   ACT_SITE        378
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        378
FT                   /note="Nucleophile; for glutamine hydrolysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   ACT_SITE        501
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        503
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   METAL           70
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   METAL           140
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         12
FT                   /note="Allosteric inhibitor CTP; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         12
FT                   /note="UTP; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         70
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         222
FT                   /note="Allosteric inhibitor CTP; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         222
FT                   /note="UTP; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         351
FT                   /note="L-glutamine; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         402
FT                   /note="L-glutamine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         458
FT                   /note="L-glutamine; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
SQ   SEQUENCE   545 AA;  61015 MW;  46DF04710B60FF81 CRC64;
     MKYVVVTGGV MSGLGKGITA ASTGRILKNK GYKVTAIKID PYINIDAGTM SPFQHGEVYV
     LKDGGEADID LGHYERFMDI NLTSEHNITT GKIYKTVIEK ERRGDYLGKT VQIIPHITNE
     IKERIRHIAK KSGADICLVE VGGTVGDIES MPFLEAVRQM RAEEAEEDLT LIHVTLVPID
     TMDEQKTKPT QHSVKELREL GIQPDIIVAR CKKPLARSTK QKIALFTDVR EEAVISCHDS
     DDIYKVPIQL EHEGMPNVLM RHMNLPPLDD SKSWNEMVGR LVAADKSLTV AILSKYGIED
     VYLSVKEALK HAGIATGAKI KIKWVESEEL EKADDLSKFF TDVDGILVPG GFGTRGIEGN
     IKGIQYAREH NIPYLGLCLG FQLATIEFTR NVVGYKDATS SEFSTTGTHV IDFLPEQKDV
     KNMGGTMRLG EHKLWIKDNT LAHRLYGATK ISERHRHRYE VNPDLIDEIE SHGLVYSAKN
     DNRMEILELP SHRFFMGTQF HPEFKSRPER PSPPFLGFVQ AMLDAKKPEA GKIVARNSRE
     PLTSN
//

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