(data stored in ACNUC7421 zone)

SWISSPROT: PYRG_RHOOB

ID   PYRG_RHOOB              Reviewed;         589 AA.
AC   C1ASX9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=CTP synthase {ECO:0000255|HAMAP-Rule:MF_01227};
DE            EC=6.3.4.2 {ECO:0000255|HAMAP-Rule:MF_01227};
DE   AltName: Full=Cytidine 5'-triphosphate synthase {ECO:0000255|HAMAP-Rule:MF_01227};
DE   AltName: Full=Cytidine triphosphate synthetase {ECO:0000255|HAMAP-Rule:MF_01227};
DE            Short=CTP synthetase {ECO:0000255|HAMAP-Rule:MF_01227};
DE            Short=CTPS {ECO:0000255|HAMAP-Rule:MF_01227};
DE   AltName: Full=UTP--ammonia ligase {ECO:0000255|HAMAP-Rule:MF_01227};
GN   Name=pyrG {ECO:0000255|HAMAP-Rule:MF_01227};
GN   OrderedLocusNames=ROP_06640;
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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:0000255|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:0000255|HAMAP-Rule:MF_01227};
CC   -!- ACTIVITY REGULATION: Allosterically activated by GTP, when
CC       glutamine is the substrate; GTP has no effect on the reaction when
CC       ammonia is the substrate. The allosteric effector GTP functions by
CC       stabilizing the protein conformation that binds the tetrahedral
CC       intermediate(s) formed during glutamine hydrolysis. Inhibited by
CC       the product CTP, via allosteric rather than competitive
CC       inhibition. {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo
CC       pathway; CTP from UDP: step 2/2. {ECO:0000255|HAMAP-
CC       Rule:MF_01227}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- MISCELLANEOUS: CTPSs have evolved a hybrid strategy for
CC       distinguishing between UTP and CTP. The overlapping regions of the
CC       product feedback inhibitory and substrate sites recognize a common
CC       feature in both compounds, the triphosphate moiety. To
CC       differentiate isosteric substrate and product pyrimidine rings, an
CC       additional pocket far from the expected kinase/ligase catalytic
CC       site, specifically recognizes the cytosine and ribose portions of
CC       the product inhibitor. {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- SIMILARITY: Belongs to the CTP synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01227}.
DR   EMBL; AP011115; BAH48911.1; -; Genomic_DNA.
DR   RefSeq; WP_012687914.1; NC_012522.1.
DR   SMR; C1ASX9; -.
DR   MEROPS; C26.964; -.
DR   PRIDE; C1ASX9; -.
DR   EnsemblBacteria; BAH48911; BAH48911; ROP_06640.
DR   KEGG; rop:ROP_06640; -.
DR   PATRIC; fig|632772.20.peg.724; -.
DR   eggNOG; ENOG4105C8D; Bacteria.
DR   eggNOG; COG0504; LUCA.
DR   HOGENOM; HOG000077515; -.
DR   KO; K01937; -.
DR   OMA; EFNNAYR; -.
DR   OrthoDB; 783657at2; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000002212; 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-KW.
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; C1ASX9.
DR   SWISS-2DPAGE; C1ASX9.
KW   ATP-binding; Complete proteome; Glutamine amidotransferase; Ligase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Pyrimidine biosynthesis.
FT   CHAIN         1    589       CTP synthase.
FT                                /FTId=PRO_1000164956.
FT   DOMAIN      306    554       Glutamine amidotransferase type-1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   NP_BIND      24     29       ATP. {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   NP_BIND     162    164       Allosteric inhibitor CTP.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   NP_BIND     202    207       Allosteric inhibitor CTP; alternate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   NP_BIND     202    207       UTP; alternate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   REGION        1    281       Amidoligase domain. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   REGION      397    400       L-glutamine binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   ACT_SITE    396    396       Nucleophile; for glutamine hydrolysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   ACT_SITE    527    527       {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   ACT_SITE    529    529       {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   METAL        81     81       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   METAL       155    155       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   BINDING      23     23       Allosteric inhibitor CTP; alternate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   BINDING      23     23       UTP; alternate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   BINDING      81     81       ATP. {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   BINDING     238    238       Allosteric inhibitor CTP; alternate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   BINDING     238    238       UTP; alternate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   BINDING     369    369       L-glutamine; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   BINDING     419    419       L-glutamine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   BINDING     480    480       L-glutamine; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
SQ   SEQUENCE   589 AA;  63924 MW;  E32980040E717982 CRC64;
     MPQSRTHSRT ATKHIFVSGG VASSLGKGLT ASSLGQLLTA RGMRVTMQKL DPYLNVDPGT
     MNPFQHGEVF VTEDGAETDL DVGHYERFLD RDLSGQANVT TGQVYSTVIA KERRGEYLGD
     TVQVIPHITD EIKSRILAMS GPDLQGHRPD VVITEIGGTV GDIESQPFLE AARQVRHDVG
     RDNVFFLHVS LVPYLAPSGE LKTKPTQHSV AALRNIGIQP DALILRCDRE VPPALKNKIA
     LMCDVDVDGC ISTPDAPSIY DIPKVLHSEG LDAYVVRQLG LPFRDVDWTV WGNLLERVHQ
     PRETVRIALV GKYVDLPDAY LSVTEALRAG GFANRSKVEI SWVPSDACET EAGAQAALGD
     VDGVLIPGGF GIRGIEGKLG AIRYARHRKT PLLGLCLGLQ CVVIEAARSV GLDDANSAEF
     EPETTHPVIS TMADQEDVIA GEADLGGTMR LGAYPAVLAK GSVVARAYGS EEVSERHRHR
     YEVNNAYRDR IAKSGLRFSG TSPDGHLVEF VEYPADQHPF FVATQAHPEL KSRPTRPHPL
     FAAFVDAALR HKLEERLPVD VHGEERAAAD DEIAESADRD EVASVDSAG
//

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