ID J4C447_THEOR Unreviewed; 1671 AA.
AC J4C447;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Carbamoyl phosphate synthase II {ECO:0000313|EMBL:BAM41556.1};
GN ORFNames=TOT_030000951 {ECO:0000313|EMBL:BAM41556.1};
OS Theileria orientalis strain Shintoku.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM41556.1, ECO:0000313|Proteomes:UP000003786};
RN [1] {ECO:0000313|EMBL:BAM41556.1, ECO:0000313|Proteomes:UP000003786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shintoku {ECO:0000313|EMBL:BAM41556.1,
RC ECO:0000313|Proteomes:UP000003786};
RX PubMed=22951932;
RA Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT "Comparative genome analysis of three eukaryotic parasites with differing
RT abilities to transform leukocytes reveals key mediators of Theileria-
RT induced leukocyte transformation.";
RL MBio 3:e00204-e00212(2012).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00043737};
CC -!- SUBUNIT: Heterodimer composed of 2 chains; the small (or glutamine)
CC chain promotes the hydrolysis of glutamine to ammonia, which is used by
CC the large (or ammonia) chain to synthesize carbamoyl phosphate.
CC {ECO:0000256|ARBA:ARBA00044031}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
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DR EMBL; AP011948; BAM41556.1; -; Genomic_DNA.
DR RefSeq; XP_009691857.1; XM_009693562.1.
DR STRING; 869250.J4C447; -.
DR EnsemblProtists; BAM41556; BAM41556; TOT_030000951.
DR GeneID; 20716088; -.
DR KEGG; tot:TOT_030000951; -.
DR VEuPathDB; PiroplasmaDB:TOT_030000951; -.
DR eggNOG; KOG0370; Eukaryota.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000003786; Chromosome 3.
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:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR PANTHER; PTHR11405:SF4; CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC SMALL CHAIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00098; CPSASE.
DR PRINTS; PR00099; CPSGATASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 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}; Reference proteome {ECO:0000313|Proteomes:UP000003786};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 609..816
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1224..1415
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1481..1671
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 1068..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1089
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1671 AA; 186815 MW; 289FAF88768D64C9 CRC64;
MEDGRVFHGY SFGYDGGSSP NVATNATTSP NGNLETSGEV VFSTSMLGYA ESVTDANYAG
QILVLTYPEI GNIGVPSHML DEYGLLKFFE SNHTYLRGLV VCNYTFKPSH WLAVETFSTF
LKTKKVLAMA CVDTRALTKH LTTYGTTLGK IILHKTPLYQ RPNGVDGHNS PSLRDLMSPG
TFFDPSTKKL DELLPTLPTH YYSFFPHAST ANTFSRVVVR YKFDLNDLTK VAGDLKKVDF
HKLYLNNVDF TNHTTALVGL SDSLNGLRLL VVVNFGLKNS ILRSLLNNCP NNVRVLVVPY
NCDFSVFDYD GLFLGNGPGN PNNYTEVVKV VRKVLAKGKP IFGVCLGNLL LGLAGGYKCV
KMHKGNYGAN QPCIDLRTYK CYATSQSHRY MLVKDPNQGA SRWCTLFENA NDNSLEGLVN
LDFPYFSVQF HPLSNPLHFR HPDGNWRTYD LDTSFLYRDF FTCLMKKTLI PIHIRVMSSH
IRCKRILLLS SGGLSIGQAG EFDYSGYQAI KALKESDAKI ILVNPNIATV QTSKGMAHVT
YFLPITFEYV KQIIEKEKPD GIMCAFGGQT GLNVGIELYE KKVLEDNNCE ILGTSIKTII
DTEDRFLFNK KMAEIGERCA PSKECKSVEE CVETAKKLGY PVLVRGNFEL GGFGSGFADN
ETELLSIVNR MFGSNRGKTS TKVCLLVVTD VCVHVDKSLK GWKEIEFEVL RDGNDNCVCA
ASMENFDPLG VHTGDSIVVA PAQTLNAGEC SHLRQVAFNV VRHLDLVGEC NIQFAVNPHK
FEYFIVELNA RLSRSSALAS KATGYPLAYM AAKIALGYDL VQMRNSITLI TTACFEPSLD
YLVVKMPRWD LRKFENADNR IGSSMKSVGE VMAIGRTFEE VIQKSLRMVS ESKLGFDAGR
CSKLGLVEIK NLLENPTPDR MHAIYRAFEL GLTVEEVNTL TWIDNWFLHR LYNIYDWSNK
LRGRRLSEMT YDEMHHYKVL GFSDKQIAKP DLTNSTEPVN RVDAAVDDEE SCETEDNVRR
HRLNLGVSAK VKIIDTLAAE YPVVTNYCYL TYNSVENDIL PLNYKLQSGP TSPGSNRTSV
STKFDDGTPH SKSPLSVKML KYCTGSIVVL GCGAYRIGSS IEFDWSAVGC IKTLRKLGHS
AIIVNCNPET VSTDFDVSDR LYFEELSVEM VNEIYRFESP NGIILSVGGQ TANNLALKLD
ELGLNILGTP VSSIDKCECR NKFSNICDLL GIDQPSWEEF TCVNAAKRFC DKVGFPVLAR
PSYVLSGASM KVILSHKELE TYLGTSAVVN RKHPVVISKF IQNAKEIEMD CVAKDGDIIN
YAISEHVENA GVHSGDATLI LPAQNIFVDT HRRIKNITQK LAKHLKISGP FNVQFMCKKN
RIKVIECNLR ASRTFPFISS TFNVDFIELS TKVMVGVPVR RENIQLMDLD YVAVKMPLFS
FDRLYPSDPL LGVEMKSTGE IAAFGETKYE AFLKAMTACG MKIPENGVLL SLGSRVNKFI
FSRKIKGLLS LGLDVYATEG TYDYIKQMWE SEHQFFVSNT NDEFYKGLQG LTEFNDDEFD
FEVKKLGQFR KVHKPPTPRP NCAGASAENE EVFRLISEKK VDMFINVSDS VNSMFTTSGY
VMRRAFVDSK LGLITSSKLA ILLIDALMYR RSRLDKGKEF ISVKSHQDYL S
//
