ID   PYRG_ALCBS              Reviewed;         545 AA.
AC   Q0VQD8;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=CTP synthase;
DE            EC=6.3.4.2;
DE   AltName: Full=UTP--ammonia ligase;
DE   AltName: Full=CTP synthetase;
GN   Name=pyrG; OrderedLocusNames=ABO_1162;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(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   -!- 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; AM286690; CAL16610.1; -; Genomic_DNA.
DR   RefSeq; YP_692882.1; -.
DR   GeneID; 4211642; -.
DR   GenomeReviews; AM286690_GR; ABO_1162.
DR   KEGG; abo:ABO_1162; -.
DR   NMPDR; fig|393595.12.peg.1173; -.
DR   HOGENOM; Q0VQD8; -.
DR   OMA; Q0VQD8; EFNNAYR.
DR   BioCyc; ABOR393595:ABO_1162-MON; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; IEA:HAMAP.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01227; -; 1.
DR   InterPro; IPR004468; CTP_synthase.
DR   InterPro; IPR017456; CTP_synthase_N.
DR   InterPro; IPR017926; GATASE_1.
DR   InterPro; IPR000991; GATase_class1_C.
DR   PANTHER; PTHR11550; PyrG_synth; 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    545       CTP synthase.
FT                                /FTId=PRO_0000266050.
FT   DOMAIN      290    541       Glutamine amidotransferase type-1.
FT   REGION        1    252       Aminator domain.
FT   ACT_SITE    378    378       Nucleophile (By similarity).
FT   ACT_SITE    514    514       By similarity.
FT   ACT_SITE    516    516       By similarity.
SQ   SEQUENCE   545 AA;  59687 MW;  8FA206D99BCCA6D8 CRC64;
     MSRFIFVTGG VVSSLGKGIT SASLATLLEA RGLNVTLIKM DPYINVDPGT MSPYQHGEVF
     VTEDGAETDL DLGHYERFIR TRLNRRNSFT TGRVYQHVLD KERRGEYLGA TVQVIPHITD
     EIKLKIREGA GDADVAIVEI GGTAGDIESL PFLEAARQMR VELGSSQSLL VHLTLVPYIA
     TAGEIKTKPT QHSVKELRSI GLQPDILVCR ADDPIPQSAR EKIALFTNVE ARAVISSPDC
     KTIYQVPRGM HEQGLDAIVV EKFGLDLPEP DLGEWDRVVE AQLNPEHEVT VGMVGKYIEL
     VDAYKSLNEA LIHAGISNRA KVNILYLDAE DIERDGTGVL ESLDAILVPG GFGDRGTEGK
     IAAIRYAREN KVPYLGICLG MQLAVIEYAR HVAGIEKAHS SELNPNTPDP VVGLITEWIT
     EDGQKELRSA DSDLGGTMRL GGQECVLEAD SRAAECYGST HIVERHRHRY EVNNNYLPQL
     EAAGLKIVGR SADGELVEVI EVGDHPWFVA CQFHPEFTST PRDGHGLFKG YVAAALAEQK
     AHKET
//