ID   G7YP97_CLOSI            Unreviewed;      3016 AA.
AC   G7YP97;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=CAD protein {ECO:0000256|ARBA:ARBA00017075};
DE            EC=2.1.3.2 {ECO:0000256|ARBA:ARBA00013008};
DE            EC=3.5.2.3 {ECO:0000256|ARBA:ARBA00012860};
DE            EC=6.3.5.5 {ECO:0000256|ARBA:ARBA00012738};
GN   ORFNames=CLF_105410 {ECO:0000313|EMBL:GAA54778.1};
OS   Clonorchis sinensis (Chinese liver fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Clonorchis.
OX   NCBI_TaxID=79923 {ECO:0000313|EMBL:GAA54778.1};
RN   [1] {ECO:0000313|EMBL:GAA54778.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Henan {ECO:0000313|EMBL:GAA54778.1};
RX   PubMed=22023798; DOI=10.1186/gb-2011-12-10-r107;
RA   Wang X., Chen W., Huang Y., Sun J., Men J., Liu H., Luo F., Guo L., Lv X.,
RA   Deng C., Zhou C., Fan Y., Li X., Huang L., Hu Y., Liang C., Hu X., Xu J.,
RA   Yu X.;
RT   "The draft genome of the carcinogenic human liver fluke Clonorchis
RT   sinensis.";
RL   Genome Biol. 12:R107-R107(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Henan;
RA   Wang X., Huang Y., Chen W., Liu H., Guo L., Chen Y., Luo F., Zhou W.,
RA   Sun J., Mao Q., Liang P., Zhou C., Tian Y., Men J., Lv X., Huang L.,
RA   Zhou J., Hu Y., Li R., Zhang F., Lei H., Li X., Hu X., Liang C., Xu J.,
RA   Wu Z., Yu X.;
RT   "The genome and transcriptome sequence of Clonorchis sinensis provide
RT   insights into the carcinogenic liver fluke.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate;
CC         Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00000462};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC         carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:456216; EC=6.3.5.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00001777};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-
CC         aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58228; EC=2.1.3.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001363};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00004812}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 2/3.
CC       {ECO:0000256|ARBA:ARBA00004852}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 3/3.
CC       {ECO:0000256|ARBA:ARBA00004880}.
CC   -!- SIMILARITY: In the central section; belongs to the metallo-dependent
CC       hydrolases superfamily. DHOase family. CAD subfamily.
CC       {ECO:0000256|ARBA:ARBA00008454}.
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DR   EMBL; DF143923; GAA54778.1; -; Genomic_DNA.
DR   InParanoid; G7YP97; -.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000008909; Unassembled WGS sequence.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR   CDD; cd01744; GATase1_CPSase; 1.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.1370; -; 2.
DR   Gene3D; 3.40.50.1380; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.50.30.20; -; 1.
DR   HAMAP; MF_01209; CPSase_S_chain; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR   InterPro; IPR002082; Asp_carbamoyltransf.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR006275; CarbamoylP_synth_lsu.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR   InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR   InterPro; IPR006274; CarbamoylP_synth_ssu.
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; IPR035686; CPSase_GATase1.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR036914; MGS-like_dom_sf.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   Pfam; PF01979; Amidohydro_1; 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   Pfam; PF02142; MGS; 1.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00098; CPSASE.
DR   SMART; SM01096; CPSase_L_D3; 1.
DR   SMART; SM01097; CPSase_sm_chain; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF48108; SSF48108; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   SUPFAM; SSF52021; SSF52021; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF52335; SSF52335; 1.
DR   SUPFAM; SSF52440; SSF52440; 2.
DR   SUPFAM; SSF53671; SSF53671; 1.
DR   TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR   TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR   TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
DR   PROSITE; PS00866; CPSASE_1; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1.
DR   PROSITE; PS51855; MGS; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:GAA54778.1}.
FT   DOMAIN          1131..1323
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1717..1908
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          2004..2175
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
FT   REGION          172..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          232..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3016 AA;  333210 MW;  4620F7501D4BD25A CRC64;
     MMSPRIATKR LQANCRARRT DQQPSDQQPI GVQTSAIDIR IIYVYIMRPR ASSSNPQLAP
     GCTLGRILFL LCINDVYGAI SHDERPVFSS SVVYGVARYK TQLRRAQHQQ QQTEVSGTTL
     KGCGRDFEEN SCGSVITLGM TVPCHHCTDM LRFMDSPVTV VKGAAIGEGI RSSVGAGSGK
     YGSESLPKRG NPHRSRSINT SESTPSISRY EQKNYTVTGL WVTWKIQKSN DDQRINGSRG
     RIPRNTRPLN QPIKETNPDL KATRKRPNNN RTITHKTVEL NTPNEENQTK ILRPATRCCF
     RSFISSDRSG GFHPLNPALT MSPRLVKKRL QFNCQAQRTD QQSISAPELP IFHDTARQIH
     ILQTHASFDC IQVDGIGQSS LQLNSNALYG QILIHKESGK ITPSNRRDRG NETNEKTRVI
     TPDATQSEVT QKASAGDQAF AQEREETAAD ETRLLSKLSP ERLVGDVPLH GEHTSLFGYR
     DRHGSMASVF NTDASLPRNR DLFETLIMKE KSRMDLVLPY YNHSKGCDIR KCLPPPNLTH
     WIITFQLWST FDFSCFAVKK LLLLFRNRNF RKSMNQCDVK QAEERSFGDS RPLGRLELHD
     GTVYDGFLYG SCGEAAGEVV FQTGMVGYIE SLTDPSYHSQ LLVLTYPSIG NYGVPSSQEA
     DEFGLPKWFE SNTIYARALI VSELCCDYSH FAAKRSLHEW LAENRVTCLS NIDTRELTLK
     LRQHGTVLGR IYPLPRGEPV PDWFDPASHN LVSHVSCRQE KIFNANGDVH VAVVDCGVKF
     NQIRCFCRKG AKVTLLPSSS DLSTRINEFD ALFISNGPGD PSHCTHLVDQ IRQWMKSNKP
     LFGICLGHQL VARAVGLETY KMKYGNRGHN QPCIHLETKR CFITSQNHGY SVDVSNLPEG
     WYELFRNVND HSNEGLAHRQ KPWMTVQFHP EHMAGPQDLE FLFDVFLDQV RSPSDMTLSE
     RLTKTITYDQ LRFEQLLAVR PNRPQKILLL GSGGLSIGQA GEFDYSGSQA LKALREEGVQ
     TLLINPNVAT VQTTSGMADK IFLLPVTPDC VARIIEAERP DGILIGFGGQ TGLTCGLALA
     YPDLNNKTDE TLTAPDDNDA PPLSILEQYD CRILGTPAAT IEITENRQMF ADAMHSIGEK
     VAPAAAATTV PATVDVANRL GFPVLIRAAF ALGGMGSGFA ENVEELEQLA TRALSQTPQI
     FIDKSLKGWK EVEYEVVRDA YNNCITVCNM ENIDPVGIHT GESIVVAPSQ TLSNVEYNML
     RSVAIKVACH LHIVGECNIQ FALDPNSLTY YIIEVNARLS RSSALASKAT GYPLAYIAAK
     LCLGRSLPEL SNVVTGGRTT ACFEPSLDYC VVKVPRWDLS KFTRVSRNIG SSMKSVGEVM
     AISRCFEEAI QKALRMSKPS VLGFTSGDHQ ADADILADPT DQRIFVLAAA LKDGWSVDKI
     HTLTQIDKWF LYRFAAIAEC EKELKTLRDG VLTKIVRLFE DPVTQSVSSS VLPSLHTLIR
     AKRLGFSDQQ IGEALHSSAL SVRETREKIY LGPLVRRVDT VAGEWPATTN YLYLSYADIP
     LAGVLQLGHS NELDRFPNKL QCRLNPSGKH DVSFEPQTQI MVLGSGVYRI GSSVEFDWCA
     VGCVRELRRL GWSSIMLNCN PETVSTDFDM CDRLYFDELS LERVLDIYKL ESAVGVIVSM
     GGQTPNNIAM PMHRLGVPIL GTSAESIDSA ENRFKFSRLL DCMGISQPRW RELTDVESAK
     SFCQQVGYPV LVRPSYVLSG AAMNVAYDPQ DLATYLSAAQ AISPEHPVVI SQFILDAKEI
     DVDAIAQAGR VVAIAVSEHV ENAGVHSGDA TLVTPPQDLN AETLDRIKQI VHSLADELQV
     SGPFNLQVIA KDNRLQIIEA NLRVSRSFPF VSKTLKYDFV AAATRCILGS ARDSICPPVT
     GSRTEAAYRH SSSRGFLEPT VDVLNGVPGY VGVKVPVFSF SRLLGADVLL GVEMVSTGEV
     ACFGRDRYEA YLLAQEAALF NTNGRLPRPK ESIFLSIGSY RHKKELLTSV SQLSRLGYKL
     YGSTGTADYY QTQGVPVIPV EWPYEDSDVA KQMYVHFGGA QNSDTDVRDR TVQEYLAEKQ
     FGLIVSLTMR KTGYRRPSAF VTRGYMTRRL AVETNVPLIT DVKLFKLLAE ALYRHYRGRT
     LPGKSKDSLL PLRRPDQPGV ECRLLPLHCI SSSQILYLPG LIDIHVHTRD PGHEYKEDWC
     TATVAALAGG IVAVLAMPNT NPAVVDEASL QFAMERAASR AYCDYGLFVG ATADNAGSVG
     QLGGHVVGLK MYLNETFSTL SLSGKLNIWK KHFETWPISK PICCHAEGET MAAVLLLAEL
     TGRSVHICHV ARKAEIELIR DAKARGLKVT CEVSPHHLFL TEDDLPDCGG WREVRPRLGT
     REDVQALWAN LDSIDCFATD HAPHLASEKA TSNAPPGFPG LESMLPLFLT AMCEGRLTLT
     DLIERLHVNP RRIFNLASDT NLLNAGDTLD RCMFDDTWVE VDMGAEWSLP GSYRVNSPYA
     EPPVTAPTLY TRAGWSPFAG RRVRGRVRRV VLRGELAFVD GRLLVKPGFG INLASQMTTV
     IASKAVLQEL PRVEVAEHAM ISSPVSPVPR TRFESYSERV QDDSVCIGGP SALVDVRSFG
     PSVPPTSGAP PSVNVSSWIE GISGHHLLSC EGFPKNALHR LFNLAHSFRQ AVLKNKPLDD
     ICRGKVMACL FFEPSTRTAN SFSVAMQRLG GSVIHFNESV SSLSKGETLS DTLRILASYC
     DCLVIRHPGK GEVQLAANSV LNRPIINAGD GVGEHPTQAM LDVFTIREEI GTVNGLTVTM
     VGDLANGRTV HSLARLLCLY NVRLRYVTHC EQLRMPEEVK QYVAARGIPQ EEMSSLEEAL
     PDTDVLYMTR VQAERIQSTD SMAVGQFVVT PELMTLAKKS GMIVMHPLPR VGEISPSFDS
     DPRAAYFRQA EYGITGLGEN SSAGQTVFWH AEYVPTSAAF EALGQPSSIP TLVLPVGGMA
     AWYRKGVTAE RLYGTT
//