ID   PYRG_FIBSU              Reviewed;         133 AA.
AC   Q939R0;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   15-JAN-2008, entry version 28.
DE   CTP synthase (EC 6.3.4.2) (UTP--ammonia ligase) (CTP synthetase)
DE   (Fragment).
GN   Name=pyrG;
OS   Fibrobacter succinogenes (Bacteroides succinogenes).
OC   Bacteria; Fibrobacteres; Fibrobacterales; Fibrobacteraceae;
OC   Fibrobacter.
OX   NCBI_TaxID=833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S85 / ATCC 19169;
RX   MEDLINE=21427455; PubMed=11535801;
RA   Griffiths E., Gupta R.S.;
RT   "The use of signature sequences in different proteins to determine the
RT   relative branching order of bacterial divisions: evidence that
RT   Fibrobacter diverged at a similar time to Chlamydia and the Cytophaga-
RT   Flavobacterium-Bacteroides division.";
RL   Microbiology 147:2611-2622(2001).
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; AY017383; AAK13023.1; -; Genomic_DNA.
DR   GO; GO:0003883; F:CTP synthase activity; IEA:HAMAP.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01227; -; 1.
DR   InterPro; IPR000991; GATase_1.
DR   InterPro; IPR012998; GATase_1_AS.
DR   InterPro; IPR004468; PyrG_synth.
DR   PANTHER; PTHR11550; PyrG_synth; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Glutamine amidotransferase; Ligase; Pyrimidine biosynthesis.
FT   CHAIN        <1   >133       CTP synthase.
FT                                /FTId=PRO_0000138186.
FT   DOMAIN       <1   >133       Glutamine amidotransferase type-1.
FT   ACT_SITE      3      3       Nucleophile (By similarity).
FT   ACT_SITE    131    131       By similarity.
FT   ACT_SITE    133    133       By similarity.
FT   NON_TER       1      1
FT   NON_TER     133    133
SQ   SEQUENCE   133 AA;  15322 MW;  40554D2944D78123 CRC64;
     GICLGMQMLA IEFARNVLGL KVANSTEFDE NTTPRFIRDL EEQKDGHDKG GTMRLGLYPC
     KLAKDSNAAN VYKREKITER HRHRYEFNYN SEFRKELEKA GLKIAGTSPD GKLVEMVELK
     NHPYFEACQF HPE
//