ID A0A1D3CTZ8_9EIME Unreviewed; 473 AA.
AC A0A1D3CTZ8;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Carbamoyl phosphate synthetase {ECO:0000313|EMBL:OEH74658.1};
GN ORFNames=cyc_04629 {ECO:0000313|EMBL:OEH74658.1};
OS Cyclospora cayetanensis.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Cyclospora.
OX NCBI_TaxID=88456 {ECO:0000313|EMBL:OEH74658.1, ECO:0000313|Proteomes:UP000095192};
RN [1] {ECO:0000313|EMBL:OEH74658.1, ECO:0000313|Proteomes:UP000095192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHN_HEN01 {ECO:0000313|EMBL:OEH74658.1,
RC ECO:0000313|Proteomes:UP000095192};
RX PubMed=27129308; DOI=10.1186/s12864-016-2632-3;
RA Liu S., Wang L., Zheng H., Xu Z., Roellig D.M., Li N., Frace M.A., Tang K.,
RA Arrowood M.J., Moss D.M., Zhang L., Feng Y., Xiao L.;
RT "Comparative genomics reveals Cyclospora cayetanensis possesses coccidia-
RT like metabolism and invasion components but unique surface antigens.";
RL BMC Genomics 17:316-316(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC ChEBI:CHEBI:456216; EC=6.3.4.16;
CC Evidence={ECO:0000256|ARBA:ARBA00043687};
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:OEH74658.1}.
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DR EMBL; JROU02001976; OEH74658.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D3CTZ8; -.
DR VEuPathDB; ToxoDB:cyc_04629; -.
DR VEuPathDB; ToxoDB:LOC34621136; -.
DR InParanoid; A0A1D3CTZ8; -.
DR Proteomes; UP000095192; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 2.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR PRINTS; PR00098; CPSASE.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 2.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS51855; MGS; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000095192}.
FT DOMAIN 18..209
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 275..473
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 473 AA; 51883 MW; 8C213D3D746BC093 CRC64;
MGTSVSSIDC CEDRHKFSKL CDELRLDQPA WSEFTSFDAA QEFSNKVGFP VLVRPSYVLS
GAAMRVVTND EQLREFLQVA AVVSGDSPVV ISKFVSNAKE VEFDSVASRG EILNYAISEH
VENAGTHSGD ATLILPAQKL YVETIRRVKK IAQKLARALN VSGPFNIQFI CKNNEVKIIE
CNLRASRTFP FISKCFGVDF IEQATKVMVG APVSAESIHL MDLEFVCVKA PVFSFNRLRG
CDPLLGVEMR STGEVACFGT DKHEAFLKAL VSTGLRLPLK KRSILLVTGP LWSKVEFFPF
AIKLMKLGFT IYATEGTYEF LHKGAQDADS GPACVVGEDF EADEPWGYLP SRVEDGKGGA
AACATGLAPS FDLDKQLIPV SKEETPSGSD RQSAKSIIAG GMVELVINTP GRTSTEAITT
GYLIRRAAID AGVPLMTDLK VAAFFVESIS RKIAREREGK RFWEVRAWDE YQP
//
