ID A0AAE1LQH4_9NEOP Unreviewed; 2323 AA. AC A0AAE1LQH4; DT 29-MAY-2024, integrated into UniProtKB/TrEMBL. DT 29-MAY-2024, sequence version 1. DT 27-NOV-2024, entry version 4. DE SubName: Full=CAD protein {ECO:0000313|EMBL:KAK3928308.1}; GN ORFNames=KUF71_016555 {ECO:0000313|EMBL:KAK3928308.1}; OS Frankliniella fusca. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Paraneoptera; Thysanoptera; Terebrantia; Thripoidea; Thripidae; OC Frankliniella. OX NCBI_TaxID=407009 {ECO:0000313|EMBL:KAK3928308.1, ECO:0000313|Proteomes:UP001219518}; RN [1] {ECO:0000313|EMBL:KAK3928308.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PL_HMW_Pooled {ECO:0000313|EMBL:KAK3928308.1}; RC TISSUE=Head {ECO:0000313|EMBL:KAK3928308.1}; RA Catto M.A., Jacobson A., Kennedy G., Labadie P., Hunt B.G., Srinivasan R.; RL Submitted (JUL-2021) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KAK3928308.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PL_HMW_Pooled {ECO:0000313|EMBL:KAK3928308.1}; RX PubMed=37344773; RA Catto M.A., Labadie P.E., Jacobson A.L., Kennedy G.G., Srinivasan R., RA Hunt B.G.; RT "Pest status, molecular evolution, and epigenetic factors derived from the RT genome assembly of Frankliniella fusca, a thysanopteran phytovirus RT vector."; RL BMC Genomics 24:0-0(2023). CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate + H(+); 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=hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl CC phosphate + L-glutamate + 2 ADP + phosphate + 2 H(+); 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=hydrogencarbonate + NH4(+) + 2 ATP = carbamoyl phosphate + 2 CC ADP + phosphate + 2 H(+); Xref=Rhea:RHEA:18029, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:456216; CC EC=6.3.4.16; Evidence={ECO:0000256|ARBA:ARBA00043687}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutamine + H2O = L-glutamate + NH4(+); CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2; CC Evidence={ECO:0000256|ARBA:ARBA00001062}; CC -!- CATALYTIC ACTIVITY: CC Reaction=carbamoyl phosphate + L-aspartate = N-carbamoyl-L-aspartate + CC phosphate + H(+); 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 2nd section; belongs to the CarB family. CC {ECO:0000256|ARBA:ARBA00043998}. CC -!- SIMILARITY: In the 3rd section; belongs to the metallo-dependent CC hydrolases superfamily. DHOase family. CAD subfamily. CC {ECO:0000256|ARBA:ARBA00043968}. CC -!- SIMILARITY: In the C-terminal section; belongs to the CC aspartate/ornithine carbamoyltransferase superfamily. ATCase family. CC {ECO:0000256|ARBA:ARBA00043979}. CC -!- SIMILARITY: In the N-terminal section; belongs to the CarA family. CC {ECO:0000256|ARBA:ARBA00043984}. 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:KAK3928308.1}. 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; JAHWGI010001326; KAK3928308.1; -; Genomic_DNA. DR Proteomes; UP001219518; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:InterPro. DR GO; GO:0004151; F:dihydroorotase activity; IEA:TreeGrafter. 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:0019240; P:citrulline biosynthetic process; IEA:TreeGrafter. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0006228; P:UTP biosynthetic process; IEA:TreeGrafter. DR CDD; cd01316; CAD_DHOase; 1. DR CDD; cd01744; GATase1_CPSase; 1. DR CDD; cd01423; MGS_CPS_I_III; 1. DR FunFam; 3.40.50.1370:FF:000002; Aspartate carbamoyltransferase 2; 1. DR FunFam; 3.40.50.1370:FF:000005; CAD protein-like isoform X1; 1. DR FunFam; 3.40.50.1380:FF:000005; CAD protein-like isoform X1; 1. DR FunFam; 3.30.470.20:FF:000004; Carbamoyl-phosphate synthase (glutamine-hydrolyzing); 1. DR FunFam; 3.40.50.880:FF:000006; Carbamoyl-phosphate synthase 1, mitochondrial; 1. DR FunFam; 3.50.30.20:FF:000002; Carbamoyl-phosphate synthase 1, mitochondrial; 1. DR FunFam; 1.10.1030.10:FF:000001; Carbamoyl-phosphate synthase large chain; 1. DR FunFam; 3.20.20.140:FF:000036; Carbamoyl-phosphate synthase large chain; 1. DR FunFam; 3.30.1490.20:FF:000001; Carbamoyl-phosphate synthase large chain; 1. DR FunFam; 3.30.470.20:FF:000001; Carbamoyl-phosphate synthase large chain; 1. DR FunFam; 3.40.50.20:FF:000001; Carbamoyl-phosphate synthase large chain; 1. DR FunFam; 3.40.50.20:FF:000002; Carbamoyl-phosphate synthase large chain; 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; 2. DR HAMAP; MF_00001; Asp_carb_tr; 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 NCBIfam; TIGR00670; asp_carb_tr; 1. DR NCBIfam; TIGR01369; CPSaseII_lrg; 1. DR NCBIfam; TIGR01368; CPSaseIIsmall; 1. DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1. DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1. 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; 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 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; 2. DR SUPFAM; SSF52440; PreATP-grasp domain; 2. DR PROSITE; PS50975; ATP_GRASP; 2. DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1. DR PROSITE; PS00866; CPSASE_1; 1. DR PROSITE; PS00867; CPSASE_2; 2. DR PROSITE; PS00482; DIHYDROOROTASE_1; 1. 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:UP001219518}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 553..745 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT DOMAIN 1087..1278 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT DOMAIN 1343..1561 FT /note="MGS-like" FT /evidence="ECO:0000259|PROSITE:PS51855" FT ACT_SITE 282 FT /note="Nucleophile" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605" FT ACT_SITE 366 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605" FT ACT_SITE 368 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605" SQ SEQUENCE 2323 AA; 256574 MW; C08895CBD2AFBEAB CRC64; MWKLERTRAD RLADKMCLTV AEQQPCALVL EDGTVLQGRS FGAPVATHGE VVFQTGMVGY PESLTDPSYH AQILVLTYPL VGNYGVPNEE LDEHGLPRYF ESRRIWAAGL VVGEICDTPS HWAMARTLSQ WLGTHGIPGI CGIDTRALTQ RLRERGSILG HIVMGPNPAP SQSLSFLDPN TRNLVAEVSI KAPITYNPSG SPRICAVDCG LKYNQLRCLL KRGVRVDMVP WNHPLDPSQF DGLFLSNGPG DPAMCSVTVE NIKKLLAAKP GTPQLKPIFG ICLGHQLLST AAGCRTYKMI YGNRGHNQPV THHGTERCFM TSQNHGFAVD AKNLPSGWNA LFTNTNDKSN EGIVHDSMPF FSVQFHPEHT PGPEDLECLF DVFLDEVKAH AQSWGRGSGV KMADRIHDRL VYRPAPGVIP PCPEKPPRKV LILGSGGLSI GQAGEFDYSG SQALKALREQ NIHTVLINPN IATVQTSKGL ADKVYFLPLI PEYVEQVICH ERPDGVLLTF GGQTALNCGV SLNEAGVFEK YNVKILGTPI QAIIDTEDRK VFAERVNEIG EKVAPSCAVN SVQEALDAAE KLGYPVLARA AFSLGGLGSG FANTAEELRV LATQALAHSS QLIVDKSLKG WKEVEYEVVR DAYDNCITVC NMENVDPLGI HTGESIVVAP SQTLSNLEYN KLRSTALKVI RHLGIVGECN IQYAVSPTSN EFYIIEVNAR LSRSSALASK ATGYPLAYVA AKLSLGLRLP DIRNSVTGST TACFEPSLDY CVVKIPRWDL AKFARVCSKI GSSMKSVGEV MSIGRCFEEA FQKALRMVDE NIKGFDPSIR PVDDAELEAP TDKRTFVLAA AFSAGYTIDR LYELTKIDRW FLHKMRNIIE FQSILESLNQ GTLSRDLLLQ AKQLGFCDTQ IATFVKSTEL AVRKFREEVK VLPFVKQIDT VAAEWPAMTN YLYLTYNGSA HDIAFNRGST MVIGSGVYRI GSSVEFDWCA VGCLRELRRL GRKTIMVNYN PETVSTDYDM VDRLYFEEIS FEVVMDIYNA ENPEGIILSM GGQLPNNIAM DLHRQQARIF GTSPDSVDSA ENRFKFSRML DRNGIGQPRW KELTNLESAK SFCNEVGYPC LVRPSYVLSG AAMNVAHTPQ DLETYLNTAS NVSKEHPVVI SKFILEAKEI DVDAVACDGA ILCMAVSEHV ENAGVHSGDA TLITPPQDIN EQTLCRITAI AKAIAGHLEV TGPFNMQLIA KDNDIKVIEC NVRVSRSFPF VSKTLDHDFV AMATRVIVGE KVEPVNVMAG CGKVGCKVPQ FSFSRLAGAD VMLGVEMAST GEVACFGENR YEAYLKAMMS TGFTIPKHSI LLSVGSFKHK MELLPSMQAL SKMGYKLYAS MGTADFYTEH GVDFFDPSPI AWSESKRQFF SRHRAAAVTH LHVDRRALAV PHEEGPDEGL VDAGHGAQHG HEAEVEPVQW TFENLEATDK EEKGELKHLA DFLAKKQFEL VINLPMRNGG ARRVSSFVTH GYRTRRLAVD YSVPLVTDVK CAKLLVEAML RIGGAPPMKT HTDCASSSTM VRLPGLIDVH VHVREPGATH KEDYSTCTSA ALAGGVTIIC AMPNTKPTIT DPSAFQLVKE LAAAKARCDY AVFVGASSEN YSTIRELAPL AAGLKMYLNE TFSTLRLKDL TVWRKHMDAW PHNSPLCVHA EGQTTAAVLL LATFQNRPIH VCHVARKEEI QIIRAAKEKG LPVTCEVCPH HLFLTEKDVK HLGEKKSRVK PNLVTEEDQQ ALWENLDIID CFATDHAPHT VEEKDSENAP PGFPGLETML PLLLTAVHEG RLTLEDIKDK LYRNPRRIFN LPEQPNTYVE VNMDAEWTIP DTLQFSKARW TPFAGRKVRG CVQRVVLRGE VAYVDGQVLV PPGFGQDVRE LQSRRQPLLN AFSSPSPAVN NCADPTFNGS RPSSAMEFDR PHVLREVDET HRYENGLDGS HERLHHLTPD PQSINRSSSP LLSHTHTRIR YNSESNLYPG AGGQPNSLIG AHVLSVKMFT KDHLNEIFNL AQTMRAFVLK ERNLDHILKG KIMASIFYEV STRTSCSFSA AMLRLGGQVI HMDETSSSVK KGETLEDSVA VMAGYSDVVV LRHPEPGAVN KASAHCRKPL INAGDGIGEH PTQALLDIFT IREEIGTVNG LTITMVGDLR HGRTVHSLAR LLTLYNIQLR YVAPPGLGMP QHVVDFVNSK GIPQENYSSL DNALPETDVL YVTRIQKERF ASQEEYEKVK GSYVVTPKLM TRAKRKMIVM HPLPRVDEIS AEFDSDPRAS YFRQAESGMY VRMALLAMVM GRC //