PYRG_NEUCR
ID PYRG_NEUCR Reviewed; 579 AA.
AC Q7RZV2;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 2.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=CTP synthase;
DE EC=6.3.4.2;
DE AltName: Full=CTP synthetase;
DE AltName: Full=UTP--ammonia ligase;
GN Name=pyr-7; Synonyms=ura7; ORFNames=NCU00261;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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=EAA28496.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CM002238; EAA28496.2; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_957732.2; XM_952639.2.
DR AlphaFoldDB; Q7RZV2; -.
DR SMR; Q7RZV2; -.
DR STRING; 5141.EFNCRP00000000004; -.
DR PRIDE; Q7RZV2; -.
DR EnsemblFungi; EAA28496; EAA28496; NCU00261.
DR GeneID; 3873894; -.
DR KEGG; ncr:NCU00261; -.
DR HOGENOM; CLU_011675_5_0_1; -.
DR InParanoid; Q7RZV2; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0097268; C:cytoophidium; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003883; F:CTP synthase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006241; P:CTP biosynthetic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
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..579
FT /note="CTP synthase"
FT /id="PRO_0000138281"
FT DOMAIN 310..558
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 402
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 531
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 533
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 579 AA; 64142 MW; 9A5D3FC01F9DD319 CRC64;
MKFVLVSGGV VSGVGKGIIA SSCGLLLKTL GLKVTAIKID PYINVDAGTM NPKEHGECFV
LHDGGETDLD LGNYERYLGV DLARDNNITT GKVYQQVIEN ERKGKYLGRT VQVVPHVIDA
IIDTINRVSR VPVDKSGEEP DVCIIELGGT VGDIESMPFV EALTQLRHRA GKNNFINIHV
SYVPVVNGEQ KTKPTQHAVK SVRSAGLIPD LIACRCEKPL EQGTINKVAS SCQVEVNQVL
AVRDMPTIYQ VPLLLEEQGL LRELKETLKL DDVKLSPARV SQGQEVWAKW QKIVPLGYAE
TVDIVLVGKY VELHDAYLSV IKALEHSAMR CGRKLNLIWV DSEHLEEKTQ KEDPTKYHKA
WHDVCVAKGI LVPGGFGHRG TEGMIRAAQW AREQKTPFLG VCLGMQVAVI EAARNLCELK
DATSEEFDAN AEHRVIIFMP EGSKEKLGGT MRLGTRSTHF QPGSEFSKLR ALYGEATTIE
ERHRHRYEVN PDYIEKLEQS GLIFIGKDDS GERMEVVEIK DHPYYVGVQY HPEYTSRVLD
PSRPFLGFVA AAIGCLDQIT KEILQDAGFA NGSINGAHF
