ID E6ZLJ3_SPORE Unreviewed; 686 AA.
AC E6ZLJ3;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=CTP synthase {ECO:0000256|RuleBase:RU810713};
DE EC=6.3.4.2 {ECO:0000256|RuleBase:RU810713};
DE AltName: Full=UTP--ammonia ligase {ECO:0000256|RuleBase:RU810713};
GN ORFNames=sr12062 {ECO:0000313|EMBL:CBQ68196.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ68196.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ68196.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
CC -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC either L-glutamine or ammonia as the source of nitrogen.
CC {ECO:0000256|RuleBase:RU810713}.
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 Evidence={ECO:0000256|ARBA:ARBA00000314,
CC ECO:0000256|RuleBase:RU810713};
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC CTP from UDP: step 2/2. {ECO:0000256|ARBA:ARBA00005171,
CC ECO:0000256|RuleBase:RU810713}.
CC -!- SIMILARITY: Belongs to the CTP synthase family.
CC {ECO:0000256|ARBA:ARBA00007533, ECO:0000256|RuleBase:RU810713}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQ311430; CBQ68196.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZLJ3; -.
DR EnsemblFungi; CBQ68196; CBQ68196; sr12062.
DR VEuPathDB; FungiDB:sr12062; -.
DR eggNOG; KOG2387; Eukaryota.
DR HOGENOM; CLU_011675_5_0_1; -.
DR OrthoDB; 166427at2759; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000008867; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd03113; CTPS_N; 1.
DR CDD; cd01746; GATase1_CTP_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00337; PyrG; 1.
DR PANTHER; PTHR11550; CTP SYNTHASE; 1.
DR PANTHER; PTHR11550:SF0; CTP SYNTHASE-RELATED; 1.
DR Pfam; PF06418; CTP_synth_N; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU810713};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU810713};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU810713};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975,
KW ECO:0000256|RuleBase:RU810713}.
FT DOMAIN 2..270
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 316..505
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT REGION 636..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 405
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 578
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 580
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 686 AA; 75412 MW; 1A5D635B70AFB01F CRC64;
MKYIVVSGGV ISGIGKGVIA SSTGLLLKTL GLRVTAIKVD PYMNIDAGTM SPTEHGEVYV
LDDGGEADLD LGNYERYLDV TLSRDNNITT GKIYRQVIEK ERKGDYLGKT VQIVPHLTNA
IQDWIERVAQ RPVDGSGESP EVCIIELGGT VGDIESAPFV EAMRQFQFRV GHDNFALIHV
SLVPVIGGEQ KTKPTQAAIR DLRGLGLVPD MIAARCPVPL ERAVINKLSM FCHVGPEQVM
AVHDVSSTYH VPLLLEEQGM VRFFQKRLGL DVNGSIPRPM KEQGNELRRR WRDLTVGHDR
MIDKVEIVLI GKYTSLHDSY MSVVKSLEHA ALRCHRKLEL KWVESSDLEP AAESDNSVKY
HQAWQALCSA KGILVPGGFG TRGTEGMISA ARWAREKRVP YLGICLGFQI AVIEYVRNVL
GIDTAGSAEL DANCKDPVII YMPEISKTHL GGTMRLGLRP SIFQKGTHEW SKIHQLYGGQ
PVVWERHRHR YEVNPEYVER IESAAANPSA KATPQKIPSD IPAASPPFTS PRLGSFAEVA
EVFTGVDELK FVGRDEKGER MQIAELRHHP YFVGMQAHPE FCSRPLNPSP PFLGFIAASA
GLLEEQLAMQ KNYVPPHPKS HMISESEMVK RREAGEVDVD DKPATTPPGA ATPTRSLSVN
KGPKADLAVA ARIAAAEKAN GSAADR
//
