ID PYRG_FIBSS Reviewed; 563 AA.
AC Q939R0; C9RS78; D9S4K4;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 31-MAY-2011, entry version 48.
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=Fisuc_1822, FSU_2325;
OS Fibrobacter succinogenes (strain ATCC 19169 / S85).
OC Bacteria; Fibrobacteres; Fibrobacterales; Fibrobacteraceae;
OC Fibrobacter.
OX NCBI_TaxID=59374;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19169 / S85;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Weimer P.J., Stevenson D.M., Boyum J., Brumm P.I., Mead D.;
RT "Complete sequence of Fibrobacter succinogenes subsp. succinogenes
RT S85.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19169 / S85;
RA Durkin A.S., Nelson K.E., Morrison M., Forsberg C.W., Wilson D.B.,
RA Russell J.B., Cann I.K.O., Mackie R.I., White B.A.;
RT "Complete sequence of Fibrobacter succinogenes subsp. succinogenes
RT S85.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 388-520.
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; CP001792; ACX75414.1; -; Genomic_DNA.
DR EMBL; CP002158; ADL27373.1; -; Genomic_DNA.
DR EMBL; AY017383; AAK13023.1; -; Genomic_DNA.
DR RefSeq; YP_003249896.1; NC_013410.1.
DR ProteinModelPortal; Q939R0; -.
DR GeneID; 8522434; -.
DR GenomeReviews; CP001792_GR; Fisuc_1822.
DR GenomeReviews; CP002158_GR; FSU_2325.
DR KEGG; fsu:Fisuc_1822; -.
DR OMA; RVTMQKL; -.
DR ProtClustDB; PRK05380; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003883; F:CTP synthase activity; IEA:EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR HAMAP; MF_01227; PyrG; 1; -.
DR InterPro; IPR004468; CTP_synthase.
DR InterPro; IPR017456; CTP_synthase_N.
DR InterPro; IPR017926; GATASE_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 1 563 CTP synthase.
FT /FTId=PRO_0000138186.
FT DOMAIN 303 545 Glutamine amidotransferase type-1.
FT REGION 12 265 Aminator domain (By similarity).
FT ACT_SITE 390 390 Nucleophile (By similarity).
FT ACT_SITE 518 518 By similarity.
FT ACT_SITE 520 520 By similarity.
FT CONFLICT 395 397 CCV -> MLA (in Ref. 3; AAK13023).
FT CONFLICT 403 403 D -> N (in Ref. 3; AAK13023).
FT CONFLICT 407 409 WKD -> LKV (in Ref. 3; AAK13023).
FT CONFLICT 421 428 HPVIDLMD -> PRFIRDLE (in Ref. 3;
FT AAK13023).
FT CONFLICT 432 435 NVTE -> DGHD (in Ref. 3; AAK13023).
FT CONFLICT 444 444 A -> L (in Ref. 3; AAK13023).
FT CONFLICT 457 458 KL -> NV (in Ref. 3; AAK13023).
FT CONFLICT 461 461 S -> R (in Ref. 3; AAK13023).
FT CONFLICT 465 465 S -> T (in Ref. 3; AAK13023).
SQ SEQUENCE 563 AA; 62460 MW; 768352B39EE391D6 CRC64;
MAKATAKNSA KQPKYIFITG GVVSSLGKGI TSASLALLLK SRGYKVFMQK LDPYLNVDPG
TMSPYQHGEV FVTDDGYETD LDLGHYERFA GVQCSKASSY TSGRIYSSVL SKERAGHYLG
GTVQVIPHIT NEIKDAFRSA AESGADIILC EIGGVAGDIE SLPFLEAARQ FRFEVGVENT
CFIHLTLVPY LKAAGELKTK PSQHSVAELR NIGIFPDILV CRTEMHIPQE HLDKLALFCN
VKPECVIEEK DVKDSVYAVP RELSKQELDL RVLEQLHLSV HPIVHSEWDS LVKKATQPKY
ECTIALVGKY IAIRDAYKSV HEALQHAGMA NNAKVNVECI EAEELEKNPK LIKKADGILI
PGGFGSRGVN GKCAAIRYAR ENKVPLLGIC LGMQCCVIEF ARDVLGWKDA NSTEFDENTT
HPVIDLMDEQ KNVTEKGGTM RLGAYPCKLA KDSNAAKLYK SEKISERHRH RYEFNYNSEF
RKELEKAGLK IAGTSPDGKL VEMVELKNHP YFEACQFHPE FKSRPTDPHP LFTGLVKAAL
EQKKANGKKP TAPSEKTKKT KTK
//