PYRG2_CHICK
ID PYRG2_CHICK Reviewed; 586 AA.
AC Q5F3Z1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=CTP synthase 2;
DE EC=6.3.4.2;
DE AltName: Full=CTP synthetase 2;
DE AltName: Full=UTP--ammonia ligase 2;
GN Name=CTPS2; ORFNames=RCJMB04_4c5;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC either L-glutamine or ammonia as the source of nitrogen. Constitutes
CC the rate-limiting enzyme in the synthesis of cytosine nucleotides (By
CC similarity). {ECO:0000250}.
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 -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC CTP from UDP: step 2/2.
CC -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000305}.
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DR EMBL; AJ851509; CAH65143.1; -; mRNA.
DR RefSeq; NP_001025978.1; NM_001030807.1.
DR AlphaFoldDB; Q5F3Z1; -.
DR SMR; Q5F3Z1; -.
DR STRING; 9031.ENSGALP00000026650; -.
DR MEROPS; C26.A36; -.
DR PaxDb; Q5F3Z1; -.
DR Ensembl; ENSGALT00000026701; ENSGALP00000026650; ENSGALG00000016549.
DR GeneID; 418620; -.
DR KEGG; gga:418620; -.
DR CTD; 56474; -.
DR VEuPathDB; HostDB:geneid_418620; -.
DR eggNOG; KOG2387; Eukaryota.
DR GeneTree; ENSGT00910000144179; -.
DR HOGENOM; CLU_011675_5_0_1; -.
DR InParanoid; Q5F3Z1; -.
DR OMA; FKPGTEW; -.
DR OrthoDB; 810128at2759; -.
DR PhylomeDB; Q5F3Z1; -.
DR Reactome; R-GGA-499943; Interconversion of nucleotide di- and triphosphates.
DR UniPathway; UPA00159; UER00277.
DR PRO; PR:Q5F3Z1; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000016549; Expressed in spermatid and 12 other 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-UniPathway.
DR GO; GO:0006241; P:CTP biosynthetic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR CDD; cd03113; CTPS_N; 1.
DR CDD; cd01746; GATase1_CTP_Synthase; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 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 PANTHER; PTHR11550; PTHR11550; 1.
DR Pfam; PF06418; CTP_synth_N; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00337; PyrG; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..586
FT /note="CTP synthase 2"
FT /id="PRO_0000247036"
FT DOMAIN 300..554
FT /note="Glutamine amidotransferase type-1"
FT REGION 562..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 399
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 526
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 528
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 586 AA; 66069 MW; 1530ADBF5B108FE3 CRC64;
MKYILVTGGV ISGIGKGIIA SSIGTILKSC GLRVTAIKID PYINIDAGTF SPYEHGEVFV
LNDGGEVDLD LGNYERFLDI NLYKDNNITT GKIYQHVINK ERHGDYLGKT VQVVPHITDA
VQEWVMNQAK VPVDDDRKEP QICVIELGGT IGDIEGMPFV EAFRQFQFKA KRENFCNIHV
SLVPQPNATG EQKTKPTQNS VRALRGLGLS PDLIVCRSAK PIEMAVKEKI SMFCHVEPEQ
VIFIHDVSST YRVPILLEEQ GIIKYFKQRL NLPIDDQPSD LLMKWKKMAD RYERLLKVCS
IALVGKYTKL SDCYASVFKA LEHSALAINH KLDLMYIDST ELERSTEVEN SVKYHQAWHK
LCKADGILVP GGFGIRGTEG KLQAISWART KKKPFLGVCL GMQLAVVEFA RNCLNWKDAN
STEFDPDTKS PVVIDMPEHN PGDMGGTMRL GKRRTVFKTQ NSILRKLYGD EMFVEERHRH
RYEVNPELTH CFEEKGLKFV GHDTEGNRME MIELENHPYF VGVQFHPEFS SRPMKPSPPY
LGLLLAATGT LNAYLQRGCK LSPSESYSDL SDDSSPEKEF PKSETS
