GenomeNet

Database: UniProt
Entry: Q9K6D7
LinkDB: Q9K6D7
Original site: Q9K6D7 
ID   PYRG_BACHD              Reviewed;         532 AA.
AC   Q9K6D7;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   07-SEP-2016, entry version 101.
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}; Synonyms=ctrA;
GN   OrderedLocusNames=BH3792;
OS   Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM
OS   9153 / C-125).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N.,
RA   Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S.,
RA   Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus
RT   halodurans and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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: ATP + UTP + L-glutamine = ADP + phosphate +
CC       CTP + L-glutamate. {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine
CC       is the substrate; GTP has no effect on the reaction when ammonia
CC       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}.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC       {ECO:0000255|HAMAP-Rule:MF_01227}.
DR   EMBL; BA000004; BAB07511.1; -; Genomic_DNA.
DR   PIR; H84123; H84123.
DR   RefSeq; WP_010899917.1; NC_002570.2.
DR   ProteinModelPortal; Q9K6D7; -.
DR   SMR; Q9K6D7; 2-531.
DR   STRING; 272558.BH3792; -.
DR   MEROPS; C26.964; -.
DR   EnsemblBacteria; BAB07511; BAB07511; BAB07511.
DR   KEGG; bha:BH3792; -.
DR   PATRIC; 18944898; VBIBacHal18977_3947.
DR   eggNOG; ENOG4105C8D; Bacteria.
DR   eggNOG; COG0504; LUCA.
DR   HOGENOM; HOG000077515; -.
DR   KO; K01937; -.
DR   OMA; TMRLGEY; -.
DR   OrthoDB; POG091H02IX; -.
DR   BioCyc; BHAL272558:GJC5-3895-MONOMER; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000001258; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-HAMAP.
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-HAMAP.
DR   Gene3D; 3.40.50.300; -; 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; 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;
KW   ATP-binding; Complete proteome; Glutamine amidotransferase; Ligase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Pyrimidine biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    532       CTP synthase.
FT                                /FTId=PRO_0000138164.
FT   DOMAIN      293    532       Glutamine amidotransferase type-1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   NP_BIND      15     20       ATP. {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   NP_BIND     149    151       Allosteric inhibitor CTP.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   NP_BIND     189    194       Allosteric inhibitor CTP; alternate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   NP_BIND     189    194       UTP; alternate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   NP_BIND     241    243       ATP. {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   REGION        1    268       Amidoligase domain. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   REGION      383    386       L-glutamine binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   ACT_SITE    382    382       Nucleophile; for glutamine hydrolysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   ACT_SITE    508    508       {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   ACT_SITE    510    510       {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   METAL        72     72       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   METAL       142    142       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   BINDING      14     14       Allosteric inhibitor CTP; alternate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   BINDING      14     14       UTP; alternate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   BINDING      55     55       L-glutamine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   BINDING      72     72       ATP. {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   BINDING     225    225       Allosteric inhibitor CTP; alternate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   BINDING     225    225       UTP; alternate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   BINDING     355    355       L-glutamine; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   BINDING     406    406       L-glutamine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   BINDING     463    463       L-glutamine; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
SQ   SEQUENCE   532 AA;  59255 MW;  FDBCE953D4F8218D CRC64;
     MTTKYIFVTG GVVSSLGKGI TAASLGRLLK NRGMKVTIQK FDPYINVDPG TMSPYQHGEV
     FVTDDGAETD LDLGHYERFI DINLNKNSNV TTGKIYSSVL KKERRGDYLG GTVQVIPHVT
     NEIKERVFRA GRETNADVVI TEIGGTVGDI ESLPFLEAIR QIKSDIGVDN VMYIHCTLIP
     YLAAAGEMKS KPTQHSVKEL RSLGIQPNVI VVRTEKPVPE EMKEKIALFC DIRKDSVIEA
     RDADTLYEVP LDLQAQNLDE IVCDHLNLSC QEADMTEWKS LVEKVKNLSG LVKIALVGKY
     VALPDAYLSV AEALRHAGYA FDADINIKWV DSEDVTAENV AEQLQGVDGI LVPGGFGDRG
     IEGKIEAIRY AREQKIPFLG ICLGMQLASI EFARNVLGLE GAHSAEINPD TPHPIIDLLP
     EQKDVEDMGG TLRLGLYPCK LKNGTLAQSA YNDQVIYERH RHRYEFNNQY REQMEAKGFM
     FSGTSPDGRL VEIVELGDHP FFIASQFHPE FVSRPTRPQP LFREFIQASL RK
//
DBGET integrated database retrieval system