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-MAY-2013, entry version 76.
DE RecName: Full=CTP synthase;
DE EC=6.3.4.2;
DE AltName: Full=CTP synthetase;
DE AltName: Full=UTP--ammonia ligase;
GN Name=pyrG; Synonyms=ctrA; 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 (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: ATP + UTP + NH(3) = ADP + phosphate + CTP.
CC -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine
CC is the substrate. Inhibited by CTP (By similarity).
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo
CC pathway; CTP from UDP: step 2/2.
CC -!- SUBUNIT: Homotetramer (By similarity).
CC -!- SIMILARITY: Belongs to the CTP synthase family.
CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
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DR EMBL; BA000004; BAB07511.1; -; Genomic_DNA.
DR PIR; H84123; H84123.
DR RefSeq; NP_244659.1; 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; TNEIKDR; -.
DR ProtClustDB; PRK05380; -.
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:HAMAP.
DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:HAMAP.
DR HAMAP; MF_01227; PyrG; 1; -.
DR InterPro; IPR004468; CTP_synthase.
DR InterPro; IPR017456; CTP_synthase_N.
DR InterPro; IPR017926; GATASE_1.
DR PANTHER; PTHR11550; PTHR11550; 1.
DR Pfam; PF06418; CTP_synth_N; 1.
DR Pfam; PF00117; GATase; 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.
FT CHAIN 1 532 CTP synthase.
FT /FTId=PRO_0000138164.
FT DOMAIN 293 532 Glutamine amidotransferase type-1.
FT REGION 1 255 Aminator domain.
FT ACT_SITE 382 382 Nucleophile (By similarity).
FT ACT_SITE 508 508 By similarity.
FT ACT_SITE 510 510 By similarity.
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
//
