ID A2QFZ4_ASPNC Unreviewed; 579 AA.
AC A2QFZ4;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
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=An03g01310 {ECO:0000313|EMBL:CAK38104.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK38104.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK38104.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270045; CAK38104.1; -; Genomic_DNA.
DR RefSeq; XP_001390033.1; XM_001389996.2.
DR AlphaFoldDB; A2QFZ4; -.
DR EnsemblFungi; CAK38104; CAK38104; An03g01310.
DR GeneID; 4980119; -.
DR KEGG; ang:An03g01310; -.
DR VEuPathDB; FungiDB:An03g01310; -.
DR HOGENOM; CLU_011675_5_0_1; -.
DR OrthoDB; 166427at2759; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000006706; Chromosome 6R.
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:UP000006706}.
FT DOMAIN 2..274
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 319..552
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 406
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 579 AA; 64028 MW; C2AB7ACCCD439190 CRC64;
MKYVLVSGGV ISGVGKGIIA SSTGLLLKTT GLAVTSIKID PYINIDAGTM APTEHGEVYV
TDDGGEMDLD LGNYERYLLS SLSRDHNITT GKVYQHVINR ERIGHYLGKT VQVVPHVTDA
IQEWIQRVAK IPVDESKAEP DVCIIELGGT VGDIESAPFI HALSQLQRKA GKGNFVQIHV
SYVPVIPPGP GGEQKTKPTQ RAISDVRSAG LNPDLIACRC EQPLEDSTIQ KIANMCSVEQ
HQVIAVHNVT TTYHVPMLLE KQKLISTITD MLDLKSIPQT PERKEQGSRM WNDWCDLARG
QDFLHDSVSI ALVGKYTSLH DAYISVSKAL EHAAMYCHKK VQIIWVDSSH LEDDTASPAD
YHKAWHAVCT ADGVLVPGGF GNRGTEGMMK VITWARTNNK PFLGVCLGMQ LAVLEFCRNV
ANVKDVGSEE LHPKAENHAI VYMPEVDKGK LGGTMRLGRH PCVFQENTEW SRLRSLYGPS
VSQIEERHRH RYEVNPEMIE QIEKAGLSFI GKDIKGERME IVEIKDHPWF VGVQFHPEYL
SRVLSPSRAF LGFFAAAAGC LDEVSKAVVQ GQRSIGRKQ
//
