ID PYRG_METST Reviewed; 534 AA.
AC Q2NH50;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 01-MAY-2013, entry version 54.
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; OrderedLocusNames=Msp_0453;
OS Methanosphaera stadtmanae (strain DSM 3091).
OC Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3091;
RX PubMed=16385054; DOI=10.1128/JB.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H.,
RA Hedderich R., Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this
RT human intestinal archaeon is restricted to methanol and H2 for methane
RT formation and ATP synthesis.";
RL J. Bacteriol. 188:642-658(2006).
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 -!- SIMILARITY: Belongs to the CTP synthase family.
CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
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DR EMBL; CP000102; ABC56853.1; -; Genomic_DNA.
DR RefSeq; YP_447496.1; NC_007681.1.
DR HSSP; P17812; 2C5M.
DR ProteinModelPortal; Q2NH50; -.
DR SMR; Q2NH50; 2-530.
DR STRING; 339860.Msp_0453; -.
DR EnsemblBacteria; ABC56853; ABC56853; Msp_0453.
DR GeneID; 3855104; -.
DR KEGG; mst:Msp_0453; -.
DR eggNOG; COG0504; -.
DR HOGENOM; HOG000077515; -.
DR KO; K01937; -.
DR OMA; TNEIKDR; -.
DR ProtClustDB; PRK05380; -.
DR BioCyc; MSTA339860:GJEZ-453-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 1 534 CTP synthase.
FT /FTId=PRO_0000266276.
FT DOMAIN 294 532 Glutamine amidotransferase type-1.
FT REGION 1 254 Aminator domain.
FT ACT_SITE 380 380 Nucleophile (By similarity).
FT ACT_SITE 505 505 By similarity.
FT ACT_SITE 507 507 By similarity.
SQ SEQUENCE 534 AA; 59678 MW; EA4DF9FCC2996E12 CRC64;
MSKYIVVTGG VVSSIGKGIT SASIGRILRS YGVNVTAIKI DPYLNWDSGT LNPYQHGEVY
VTDDGMECDL DLGHYERFLD VELSGKANIT TGKVYSSVIE KERKGEYLGS CVQIIPHITD
EIKLMIRNVA EKTKAEVVMV EVGGTVGDIE SQPFIEAVRQ LKNEEGHDNC MFVHVTYVPY
LKAAKEFKTK PTQHSTKELR GLGINPDMIV CRSELSLDAN LKEKIAHFCD VPIEAVINTP
DAHSIYEVPL IMYSANVGSY ILNRLNIDTA TNKADLYEWS QIVEDLKIET PKVKIAVVGK
YIELEDAYIS IRESLKHAGA ANKVHVDIDW IKADNDFNID ILKQYDGLLI PGGFGERGIN
GKIEAVKYAI KNNVPIFGIC LGLHAMSIAI AQLNGYPDAN STEFDENSTC PVIDMMEEQK
KINNMGGTMR LGAYPCKIKE GTLAYEAYKD TNISERHRHR YEVNNEYRDI LTSAGAIISG
TSPDDFLVEM IELENHPWFL GCQFHPEFKS RPNKAHPLFK SFIKAAKNKK QNQK
//
