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Database: UniProt
Entry: Q9K6D7
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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   01-OCT-2014, entry version 86.
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=CTP synthetase {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.
CC       {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. Inhibited by CTP. {ECO:0000255|HAMAP-
CC       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   -!- 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}.
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DR   EMBL; BA000004; BAB07511.1; -; Genomic_DNA.
DR   PIR; H84123; H84123.
DR   RefSeq; NP_244659.1; NC_002570.2.
DR   RefSeq; WP_010899917.1; NC_002570.2.
DR   ProteinModelPortal; Q9K6D7; -.
DR   SMR; Q9K6D7; 2-531.
DR   STRING; 272558.BH3792; -.
DR   EnsemblBacteria; BAB07511; BAB07511; BAB07511.
DR   GeneID; 890528; -.
DR   KEGG; bha:BH3792; -.
DR   PATRIC; 18944898; VBIBacHal18977_3947.
DR   eggNOG; COG0504; -.
DR   HOGENOM; HOG000077515; -.
DR   KO; K01937; -.
DR   OMA; SVNIKYI; -.
DR   OrthoDB; EOG6RC3NR; -.
DR   BioCyc; BHAL272558:GJC5-3895-MONOMER; -.
DR   UniPathway; UPA00159; UER00277.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-HAMAP.
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   Nucleotide-binding; Pyrimidine biosynthesis; 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   REGION        1    255       Aminator domain.
FT   ACT_SITE    382    382       Nucleophile. {ECO:0000255|HAMAP-
FT                                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}.
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
//
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