ID A0A3B4Z724_9TELE Unreviewed; 2234 AA.
AC A0A3B4Z724;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=CAD protein {ECO:0000313|RefSeq:XP_008279845.1};
DE SubName: Full=Carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase {ECO:0000313|Ensembl:ENSSPAP00000004573.1};
GN Name=cad {ECO:0000313|RefSeq:XP_008279845.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000004573.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000004573.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_008279845.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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=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; EC=3.5.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001062};
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 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}.
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DR RefSeq; XP_008279845.1; XM_008281623.1.
DR STRING; 144197.ENSSPAP00000004573; -.
DR Ensembl; ENSSPAT00000004665.1; ENSSPAP00000004573.1; ENSSPAG00000003422.1.
DR GeneID; 103357188; -.
DR CTD; 790; -.
DR GeneTree; ENSGT00940000157241; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000261400; Unplaced.
DR Proteomes; UP000694891; Unplaced.
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:Ensembl.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0021610; P:facial nerve morphogenesis; IEA:Ensembl.
DR GO; GO:0021615; P:glossopharyngeal nerve morphogenesis; IEA:Ensembl.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0001946; P:lymphangiogenesis; IEA:Ensembl.
DR GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0030947; P:regulation of vascular endothelial growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:1900746; P:regulation of vascular endothelial growth factor signaling pathway; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0021636; P:trigeminal nerve morphogenesis; IEA:Ensembl.
DR GO; GO:0021644; P:vagus nerve morphogenesis; IEA:Ensembl.
DR CDD; cd01316; CAD_DHOase; 1.
DR CDD; cd01744; GATase1_CPSase; 1.
DR CDD; cd01423; MGS_CPS_I_III; 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_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; 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 PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
DR PROSITE; PS00866; CPSASE_1; 2.
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:UP000694891};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 520..712
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1056..1247
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1312..1468
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 1816..1862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 255
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 339
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 341
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2234 AA; 247279 MW; CFA885DA95C3605D CRC64;
MAEMASLILE DGTTFRGRLF GANVSVSGEV VFQTGMVGYP EALTDPSYRC QLLTLTYPLV
GNYGVPKDEE GEFGLSKWFE SSKIHAAALI IGELAESPSH WSSVKSLDQW LKEQGIPGLQ
GVDTRRLTKK IREKGTMLGK LVVDGTRENN IPFDNPDQRN LVQEVSMKEP QVFNPSGSLR
ITVVDCGIKY NQIRCLAQRG ACVTVVPWDH PLDSSDFDGL FISNGPGDPQ LCQATINNVR
RVVCVDQPKP VFGICLGHQL LSLVIGAKTY KMKYGNRGHN QPCIHNGTDR CFITSQNHGF
AVDPDTLPKD WDVLFTNAND HTNEGIVHNT KPLFSVQFHP EHMAGPTDLV GLFDVFLNTV
KDHKEGKAAK SVKQRLMDHL TFPGSPKAEE VCRPRKVLIL GSGGLSIGQA GEFDYSGSQA
IKALKEENIQ TVLINPNIAT VQTSKGLADK VYFLPITPEY VTQVIKNERP DGVLLTFGGQ
TALNCGVELT KLGVLEKYKV KVLGTPVASI EMTEDRKIFV EKMEEINEHV APSEAALSVE
QAVAAAERLG YPVLVRSAFA LGGLGSGFAN NRDELTSLVT AAFAHTSQVL VDKSLKGWKE
IEYEVVRDAY DNCVTVCNME NIDPLGIHTG ESIVVAPSQT LNDHEYNMLR NTAIKVIRHL
GIVGECNIQY ALNPESEQYY IIEVNARLSR SSALASKATG YPLAYVAAKL GLGIPLPQLK
NSVTNQTTAN FEPSLDYCVV KVPRWDLSKF LRVSTKIGSS MKSVGEVMAI GRSFEEAFQK
ALRMVDENCV GFDHTIKPVS EKELQTPTDK RIFVLAAAFR AGYTVDQLYE LTKIDRWFLH
KMKNIADHER LLETYNQDES TMPPEVMRKA KQLGFSDKQI ALAVQSTELA VRKLRHDWSI
LPVVKQIDTV AAEWPAHTNY LYLTYHGTEN DLSFHDQHVM VIGSGVYRIG SSVEFDWCAV
GCITELRKMG YKTIMVNYNP ETVSTDYDMC DRLYFDEISF EVVMDIYERE NPEGVILSMG
GQLPNNIAMS LHRQQCRILG TSPEFIDCAE NRFKFSRMLD TIGISQPQWK ELSETESAVK
FCEKVGYPCL VRPSYVLSGA AMNVAYSDSD LEKYLSNAVA VSKEHPVVIS KFIQEAKEID
VDAVACDGVV MAIAVSEHVE NAGVHSGDAT LVTPPQDLNQ KTIERIKMIV HAIGQELQVT
GPFNLQLIAK DDQLKVIECN VRVSRSFPFV SKTLGVDLVA LATQAIMGEN EEPVGLMRGK
GIVGVKVPQF SFSRLAGADV VLGVEMTSTG EVACFGENRY EAYLKAMLST GFKIPKKNIL
LSIGSYKNKS ELLPTVQALE SLGYDLYASL GTADFYTEHG VKVTAVDWPF EEDDSECATK
EKQRSIMNYL EENHFDLVIN LSMRNSGGRR LSSFVTKGYR TRRMAIDYSV PLIIDIKCTK
LFVQALRQIG RTPPVKTHID SMASQTLVRL PGLIDVHVHL REPGATHKED FSSGTAAALA
GGVTLVCAMP NTAPAITDSS TLALVQKLAK AGCRCDYALY LGAASDNAAV LPSIASQAAG
LKMYLNDTYS TLKMDNVSLW MEHFEKWPKQ MPIVAHAERQ TVAAILMVAQ LYQRPVHICH
VARKEEILII RAAKQKGIHV TCEVAPHHLF LCEDNVPDIG DGRAQVRPML ATREDMEALW
ENLDIIDCFA TDHAPHSVEE KNSERPPPGY PGLETMLPLL LTAVSDGRLT LDDIVRRLYD
NPRRIFNLPV QENTYVEVDL EQEWVIPQAM QFTKSKWTPF QGLKVKGKVR RVVLRGEVAY
IDGQVLVPPG YGEDVKTWPT ASAQPSEPVK EGPQTPERTR PTPPRDGLVR TRAQSPRRAA
REAGYLLPPR IHRSSDPGLP PEMVALPAAS AGDGYSHPPP LSRLLSPQSG PGQIPPGQVS
HFQTSPLLHP LVGQHILSVR QFSKEQISHL FNVAHTLRLM VQKERSVDIL KGKVMASMFY
EVSTRTSSSF AAAMQRLGGS VVHFSESTSS TQKGESLADS VQTMSCYADV LVLRHPTPGA
VENASRHCRK PVINAGDGVG EHPTQALLDV FTIREELGTV NGMTITMVGD LKHGRTVHSL
AKLLTQYRIT LRYVAPKNLH MPAEIISYVA SKGIKQEEFE SIEEALPETD VLYMTRIQKE
RFASEEEYKA CFGQFILTPH IMTVAKKKMV VMHPLPRVNE ISAEVDTDPR AAYFRQAENG
MYIRMALLAT VMGR
//
