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Database: UniProt
Entry: H9GNR8_ANOCA
LinkDB: H9GNR8_ANOCA
Original site: H9GNR8_ANOCA 
ID   H9GNR8_ANOCA            Unreviewed;       591 AA.
AC   H9GNR8;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 70.
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=CTPS1 {ECO:0000313|Ensembl:ENSACAP00000016678.1};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000016678.1, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000016678.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000016678.1};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000016678.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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   RefSeq; XP_003226945.1; XM_003226897.3.
DR   AlphaFoldDB; H9GNR8; -.
DR   STRING; 28377.ENSACAP00000016678; -.
DR   Ensembl; ENSACAT00000017008.3; ENSACAP00000016678.1; ENSACAG00000016935.3.
DR   GeneID; 100553732; -.
DR   KEGG; acs:100553732; -.
DR   CTD; 1503; -.
DR   eggNOG; KOG2387; Eukaryota.
DR   GeneTree; ENSGT00910000144179; -.
DR   HOGENOM; CLU_011675_5_0_1; -.
DR   InParanoid; H9GNR8; -.
DR   OMA; EFNNAYR; -.
DR   OrthoDB; 166427at2759; -.
DR   TreeFam; TF300379; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000001646; Unplaced.
DR   Bgee; ENSACAG00000016935; Expressed in forelimb bud and 13 other cell types or tissues.
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-UniRule.
DR   GO; GO:0042100; P:B cell proliferation; IEA:Ensembl.
DR   GO; GO:0006241; P:CTP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR   GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
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   HAMAP; MF_01227; PyrG; 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:SF8; CTP SYNTHASE 1; 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:UP000001646}.
FT   DOMAIN          2..272
FT                   /note="CTP synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06418"
FT   DOMAIN          311..539
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   REGION          563..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..580
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        399
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        526
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        528
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   591 AA;  66829 MW;  031BF63AF72B5AF7 CRC64;
     MKYILVTGGV ISGIGKGIIA SSVGTILKSC GLHVTSIKID PYINIDAGTF SPYEHGEVFV
     LDDGGEVDLD LGNYERFLDI RLTKDNNLTT GKIYQYVINK ERKGDYLGKT VQVVPHITDA
     IQEWVLRQAR IPVDEDGVEP QVCVIELGGT VGDIESMPFI EAFRQFQFKV KRENFCNIHV
     SLVPQPSSTG EQKTKPTQNS VRELRGLGIS PDLIVCRCST PLDTSVKEKI SMFCHVEPEQ
     VICVHDVSSI YRVPLLLEEQ GVVDYFRHRL NLPIEKQPRR MLMKWKEMSD RYDRLLETCS
     IALVGKYTKF SDSYASVIKA LEHSSLAINH KLEIKYIDSA DLEPITLQEE PVRYHEAWQK
     LCSSDGVLVP GGFGVRGTEG KIQAISWARK QKKPFLGVCL GMQLAVVEFA RNILNWKDAN
     STEFDPKTAH PVVIDMPEHN PGQMGGTMRL GKRRTVFQTD NSVMRKLYGD CDHIEERHRH
     RFEVNPELRN ALEEKGMKFV GQDVEGERME IVELEEHPFF VGVQYHPEFL SRPIKPSPPY
     FGFLLASAGR LAHYLQKGCR LSPRDTYSDR SGSSSPDSEM TELKFPAVNH E
//
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