ID A0A1V8V8D9_9PEZI Unreviewed; 594 AA.
AC A0A1V8V8D9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=B0A51_00567 {ECO:0000313|EMBL:OQO32198.1};
OS Rachicladosporium sp. CCFEE 5018.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO32198.1, ECO:0000313|Proteomes:UP000192386};
RN [1] {ECO:0000313|EMBL:OQO32198.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCFEE 5018 {ECO:0000313|EMBL:OQO32198.1};
RX PubMed=28684563;
RA Coleine C., Masonjones S., Selbmann L., Zucconi L., Onofri S., Pacelli C.,
RA Stajich J.E.;
RT "Draft Genome Sequences of the Antarctic Endolithic Fungi Rachicladosporium
RT antarcticum CCFEE 5527 and Rachicladosporium sp. CCFEE 5018.";
RL Genome Announc. 5:e00397-17(2017).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQO32198.1}.
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DR EMBL; NAEU01000008; OQO32198.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8V8D9; -.
DR STRING; 1974281.A0A1V8V8D9; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000192386; 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:UP000192386}.
FT DOMAIN 2..270
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 316..548
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 536
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 538
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 594 AA; 66062 MW; 0A2126A38C733F1A CRC64;
MKYVLVSGGV ISGVGKGIIA SSAGLLLKTM GLKVSSIKID PYINTDAGTM NPKEHGEVYV
LDDGGEVDLD LGNYERYLNV TLTKDNNITL GKIYSQVIER ERRGDYLGKT VQVVPHVTGA
IEEWIQRVAK VPVDDTGLEP DVCIIELGGT VGDIESMAFV EALCELRRNC GRDDFMQIHV
SYVPLVHGEQ KTKPTQMAIR SVRSAGLVPD LIACRCEKPL ETAAVEKIAR FCQVQVPHVL
NVRDMPSTYQ VPILLYEQDL IALMTTTLRL DEISIPQAMK QKGDHIWSTW KDLCLGLEHL
RDNLDIVLVG KYLECPDSYL SVIKSLEHAA MRCRRKLNLI MIDAEHLEPH TNKSDPASFH
KAWHAVSTAA GILVPGGFGA RGTEGMIAAA EWARESKTPY LGICLGMQLA VVEFARSVCE
IPIPQATSYE FDANSEDRVI ISMPEHHPGK LGGTMRLGLR PTLWQPDTQW SKLRALYGLN
NESINERHRH RYEVNPSYID QLQDKGLTFI GKDETGVRQE IIELRDHPWF VGVQFHPEYL
SRVLEPSKPY LGFIAAAAKI LDEITAEGQR VWSNGGQVNG LTNGHAALYR LPVL
//
