ID A0A1B8GJN5_9PEZI Unreviewed; 586 AA.
AC A0A1B8GJN5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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 Name=URA7_2 {ECO:0000313|EMBL:OBT96035.1};
GN ORFNames=VE01_06697 {ECO:0000313|EMBL:OBT96035.1};
OS Pseudogymnoascus verrucosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=342668 {ECO:0000313|EMBL:OBT96035.1, ECO:0000313|Proteomes:UP000091956};
RN [1] {ECO:0000313|EMBL:OBT96035.1, ECO:0000313|Proteomes:UP000091956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10579 {ECO:0000313|EMBL:OBT96035.1,
RC ECO:0000313|Proteomes:UP000091956};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000091956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10579 {ECO:0000313|Proteomes:UP000091956};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
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}.
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DR EMBL; KV460231; OBT96035.1; -; Genomic_DNA.
DR RefSeq; XP_018129768.1; XM_018276137.1.
DR AlphaFoldDB; A0A1B8GJN5; -.
DR STRING; 342668.A0A1B8GJN5; -.
DR GeneID; 28840083; -.
DR OrthoDB; 166427at2759; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000091956; Unassembled WGS sequence.
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; -; 1.
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; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000091956}.
FT DOMAIN 2..270
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 315..540
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 404
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 533
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 535
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 586 AA; 64671 MW; 0FFF689341314BC4 CRC64;
MKYVLVSGGV ISGIGKGVIA SSTGLLLKTI GLKVTSIKID PYMNVDAGTM APTEHGEVFV
LDDGGEVDLD LGNYERYLNI TLTRENNITT GKIYQHVIER ERRGDYLGRT VQVVPHLTDA
IQDWIERVAR VPVDDTNEAP DVCIIELGGT VGDIESAPFI EAMRQLRRRA GKDNFLQIHV
SLVPVIQGEQ KTKPTQAAIK DARSAGLSPD LIACRCDVPL EKATTNKIAM FCQVEPEQVI
AVHNVASTYH VPLLLEKQGL ITTVRDILKL DAVTKSEHLI SRGQRTWAEW KTLTTSQDRL
FETVTIALVG KYTNLHDSYL SVIKSLEHSA MRCHKKLELQ WVDASDLEDD AKTARPAGFH
AAWHQVCTAD GILVPGGFGI RGTEGMIKAA QWARTQKVPY LGICLGMQLA VIEFARHVCG
LEGASSTELS EQCAEPIVLF MPEVDRSAMG GTMRLGIRPT IFQPGSEWSR LRKLYGDRTE
IHERHRHRYE VNPEYVERLA AGGLTFVGKD DKGERMEVVE IKDHPWFVGV QYHPEYLSRV
LSPSRPYLGF VAAASGCLDK ITGEIADLDA QAQALGLGER SEGVAT
//
