PYRG_GIBZE
ID PYRG_GIBZE Reviewed; 580 AA.
AC O74638; A0A098DSG1; A0A0E0SCX1; A0A1I9FMD5; I1RUK1; Q4I4G1; Q7LWD4;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 2.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=CTP synthase;
DE EC=6.3.4.2;
DE AltName: Full=CTP synthetase;
DE AltName: Full=UTP--ammonia ligase;
GN Name=URA7; ORFNames=FGRAMPH1_01T25925, FGRRES_07897_M, FGSG_07897;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=F15;
RX PubMed=9762900; DOI=10.1016/s0014-5793(98)01061-8;
RA Kimura M., Matsumoto G., Shingu Y., Yoneyama K., Yamaguchi I.;
RT "The mystery of the trichothecene 3-O-acetyltransferase gene. Analysis of
RT the region around Tri101 and characterization of its homologue from
RT Fusarium sporotrichioides.";
RL FEBS Lett. 435:163-168(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 498-580.
RX PubMed=9648241; DOI=10.1271/bbb.62.1033;
RA Kimura M., Shingu Y., Yoneyama K., Yamaguchi I.;
RT "Features of Tri101, the trichothecene 3-O-acetyltransferase gene, related
RT to the self-defense mechanism in Fusarium graminearum.";
RL Biosci. Biotechnol. Biochem. 62:1033-1036(1998).
CC -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC either L-glutamine or ammonia as the source of nitrogen.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-
CC glutamate + phosphate; Xref=Rhea:RHEA:26426, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.4.2;
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC CTP from UDP: step 2/2.
CC -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CEF84284.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ESU14222.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB011417; BAA33767.1; -; Genomic_DNA.
DR EMBL; DS231666; ESU14222.1; ALT_SEQ; Genomic_DNA.
DR EMBL; HG970335; CEF84284.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB009607; BAA29036.1; -; Genomic_DNA.
DR PIR; JW0086; JW0086.
DR PIR; T43732; T43732.
DR RefSeq; XP_011327729.1; XM_011329427.1.
DR AlphaFoldDB; O74638; -.
DR SMR; O74638; -.
DR STRING; 5518.FGSG_07897P0; -.
DR PRIDE; O74638; -.
DR EnsemblFungi; ESU14222; ESU14222; FGSG_07897.
DR GeneID; 23554944; -.
DR KEGG; fgr:FGSG_07897; -.
DR eggNOG; KOG2387; Eukaryota.
DR HOGENOM; CLU_011675_5_0_1; -.
DR InParanoid; O74638; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000070720; Chromosome 4.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd03113; CTPS_N; 1.
DR CDD; cd01746; GATase1_CTP_Synthase; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR004468; CTP_synthase.
DR InterPro; IPR017456; CTP_synthase_N.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR033828; GATase1_CTP_Synthase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11550; PTHR11550; 1.
DR Pfam; PF06418; CTP_synth_N; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00337; PyrG; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..580
FT /note="CTP synthase"
FT /id="PRO_0000138280"
FT DOMAIN 304..559
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 403
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 532
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 534
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT CONFLICT 239
FT /note="V -> A (in Ref. 1; BAA33767)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 580 AA; 63866 MW; 3854C7AE01C67E5F CRC64;
MKVVLVSGGV ISGVGKGIIA SSAGLLLKTL GLRVTAIKTD PYINTDAGLL NPLEHGECFV
LDDGGETDLD LGNYERYLGI QLSRDSNITT GKIYKQVIEK ERRGDYLGKT VQVVPHITDA
IQDWIERVAK IPVDASGEAP DVCIIELGGT IGDLESGPFV EALSQLRHRL GRDNFLSISV
SYVPIINGEE KTKPTQHAIR QVRSAGLIPD VIACRCEREL DQATITKIAR SCQVEDEQVI
GVRNMDTIYQ VPLLLEQEGL LKLLQKGLAL DKCQVTPPMA QKGQALWDLW KKTVVPDRHL
EPVNIILVGK YVSLDDSYLS VHKALEHSAM RCNRKLNLVS VDSEHLEPEM QEKDPRKFHE
AWAHVVRAQG IIVPGGFGTR GIQGMVDVAK WARERKLPYL GICLGMQTAV IEYARNVMGL
KGATSEEFSA TAEHRVVIFM PEGSKEQMGG TMRLGSRTSH FKPGTEWSKL RGLYGGVDVV
EERHRHRYEV NPDYIEDLEK AGLSLTSMDD QGVRVETIEL KDHPFFVGLQ AHPEYKSKTL
APAPSLLGLV AASSGCLDEI IEAAHKKQSS SNGVSDVTNF
