ID G7YP97_CLOSI Unreviewed; 3016 AA. AC G7YP97; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 28-JUN-2023, entry version 51. 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, ECO:0000313|Proteomes:UP000008909}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DF143923; GAA54778.1; -; Genomic_DNA. 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:UniProtKB-UniRule. DR CDD; cd01744; GATase1_CPSase; 1. DR Gene3D; 3.40.50.20; -; 2. DR Gene3D; 3.40.50.880; -; 1. DR Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2. 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; 3.20.20.140; Metal-dependent hydrolases; 1. DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1. DR HAMAP; MF_01209; CPSase_S_chain; 1. 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 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 Pfam; PF02142; MGS; 1. DR Pfam; PF00185; OTCace; 1. DR Pfam; PF02729; OTCace_N; 1. DR PRINTS; PR00100; AOTCASE. DR PRINTS; PR00101; ATCASE. DR PRINTS; PR00098; CPSASE. DR PRINTS; PR00099; CPSGATASE. DR SMART; SM01096; CPSase_L_D3; 1. DR SMART; SM01097; CPSase_sm_chain; 1. DR SMART; SM00851; MGS; 1. DR SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 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; SSF51338; Composite domain of metallo-dependent hydrolases; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1. DR SUPFAM; SSF52440; PreATP-grasp domain; 2. 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; PS51273; GATASE_TYPE_1; 1. DR PROSITE; PS51855; MGS; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU00409}; KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605}; KW 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 Reference proteome {ECO:0000313|Proteomes:UP000008909}; 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" FT ACT_SITE 845 FT /note="Nucleophile" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605" FT ACT_SITE 929 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605" FT ACT_SITE 931 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605" 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 //