ID K1R3V0_CRAGI Unreviewed; 2195 AA.
AC K1R3V0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=CAD protein {ECO:0000313|EMBL:EKC28536.1};
GN ORFNames=CGI_10010911 {ECO:0000313|EMBL:EKC28536.1};
OS Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC28536.1};
RN [1] {ECO:0000313|EMBL:EKC28536.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC28536.1};
RX PubMed=22992520; DOI=10.1038/nature11413;
RA Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L.,
RA Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W., Paps J., Zhu Y.,
RA Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., Wen B.,
RA Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., Xu Z., Liu Y.,
RA Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., Cheng P., Jiang X.,
RA Li J., Fan D., Wang W., Fu W., Wang T., Wang B., Zhang J., Peng Z., Li Y.,
RA Li N., Wang J., Chen M., He Y., Tan F., Song X., Zheng Q., Huang R.,
RA Yang H., Du X., Chen L., Yang M., Gaffney P.M., Wang S., Luo L., She Z.,
RA Ming Y., Huang W., Zhang S., Huang B., Zhang Y., Qu T., Ni P., Miao G.,
RA Wang J., Wang Q., Steinberg C.E., Wang H., Li N., Qian L., Zhang G., Li Y.,
RA Yang H., Liu X., Wang J., Yin Y., Wang J.;
RT "The oyster genome reveals stress adaptation and complexity of shell
RT formation.";
RL Nature 490:49-54(2012).
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 EMBL; JH818799; EKC28536.1; -; Genomic_DNA.
DR HOGENOM; CLU_000513_2_1_1; -.
DR InParanoid; K1R3V0; -.
DR OMA; WSPFNGK; -.
DR UniPathway; UPA00070; UER00115.
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; 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; 3.30.470.20; 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; 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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT ACT_SITE 256
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 340
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 342
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2195 AA; 242864 MW; 9BB8AF11FD7F76A4 CRC64;
MEATNGWLEL EDGTRFPGFI FGAKTSVPGE VVFQTGMVGY PESLTDPSYS KQILILTYPL
IGNYGIPAEE KDEFGLTEWF ESAKIHVAGL IVGDVTEKYS HWSAVKSLSK WLSEFNVPGL
YGLDTRSLTK KIREKGTMLG KIVVEGMKSS DVPLIDPNKI NLVSEVSLKE PVVYNPKGEL
TIVAVDCGIK YNQIRCLCQR GAKVKVVPWD YKISSDEYDG LFISNGPGDP QMCKATIESL
RRVVKEEKYK PIFGICLGHQ LLSLAIGAKT FKMRYGNRGH NLPCTYDDTI RCYITTQNHG
FAVDGGTLPE GWSSLFINAN DKTNEGIVHD TKPFFSTQFH PEHMGGPRDL ECLFDVFLNQ
VILHKRGQNS PTVKEKLYMT LQTPVHVPPV SSDRPRKVLI LGSGGLSIGQ AGEFDYSGSQ
AVKALKEEGI QTILINPNIA TVQTSKGLAD KVYFLPITTE YVTQVIKNER PDGVLLTFGG
QTALNCGVQL TKTGVLEKYA VKVLGTQVAS IEWTEDREVF ANKMAEIGES VAPSEAAYTV
EQVVQAAERL GYPVLVRAAF ALGGLGSGFA DNKEQLLTLA SAAFAHTSQV LVDKSLKGWK
EVEYEVVRDA FDNCITVCNM ENVDPLGIHT GESIVVAPSQ TLTNIEYNML RTTAIKVIRH
LGVVGECNIQ YALNPESKEY FIIEVNARLS RSSALASKAT GYPLAYVAAK LSLGIPLPVL
RNSVTNSEEN STTACFEPSL DYCVVKVPRW DLKKFSRVST KIGSSMKSVG EVMAIGRRFE
EAVQKALRMM DPSAMGFDPY FTKVSEGELR EPTDERIFVL AGALKQGYSV DKLYELTKID
RWFLHKFKNI TDCMSGLERY RDKMGSIPRA VLLEAKKLGF CDEQIAKSVE STELMVRKKR
SELKICPCVK QIDTVAAEWP AQTNYLYLTY NGSENDVSFP GGYIMVIGSG VYRIGSSVEF
DWCAVNCIRS LREMGYKTIM VNYNPETVST DYDMCDRLYF DEISFETVMD IYNLENPEGI
ILSVGGQLPN NIAMPLHRQQ AAKDFCKEVG YPCLVRPSYV LSGAAMNVAH SDKDLEDYLG
QASAVSKEHP VVISKFILEA KEIDVDAVAA DGEVICMAVS EHVENAGVHS GDATLVTPPQ
DLNEETLAKI RVICCAIGRA LEVTGPFNLQ LIAKDNQLKV IECNVRVSRS LPFVSKTLDH
DFIATATRVI MGEVVEPINV LYGCGRVGVK VPVFSFSRLQ GADVLLGVEM ASTGEVACFG
ENRYEAYLKA IISTGFKIPK KNILLSIGSF KDKKELLPSV KSLQTMGYSL YASMGTADFY
NEHGLKVNPV DWPYEDTGDH KNGGEQATIA DYLSDNMFDL VINLPLRNSG SYRASSFVTQ
GYKTRRMAVD YSVPLITDIK CSKLLIESIR RLNGMAPPLK THIDCISSSR VMRLPGLIDV
HVHVREPGAT HKEDWSSATS AALAGGITMI LAMPNTNPPT VDEAALTLTQ KARKLLANFS
SSLARLGARC DYGIFLGASS DNYTTLPLIS PKACALKMYL NETFTTLKLN DLSVWMKHFE
HWPKQLPICA HAEGTHTAAV ILLSELYKRS VHICHVARKE EILVIKAAKE RGLAVTCEVA
PHHLFLTSDD LDRIGQSRGQ VRPCLVTTED QETLWENIDI IDCFATDHAP HAVEEKNSAK
PPPGFPGLET MLPLLLTAVH DGRLTIEDLV AKLHTNPKKI FSLPDQPDTY IEVDLEHHWT
IPDHMTYSKS KWTPFAGMKV VGKVMRTVLR GEVAYIENEI LVPKGFGSDI KSYVLQTAAP
LGSGDQLHVQ IPPISFTGSS QPSSEPSSPR KLIHTHLSDR SRPRLVDQSY EYRERDLSAG
DYGRRDPAFL PPVPHGIPQP PGMPYYTQGV TGHHILSVKS FTKDQLHSLF NLAHQFRVAV
LRDRPLDYIL KGKVMASMFF EVSTRTSCSF SAAMQRLGGS VVTLESSMSS LQKGESLHDS
VMMMAGYSDV IVMRHPTPGV MTEAVKMCRK PVINAGDGVG EHPTQALLDV FTIREEIGTV
NGLTITMVGD LKNGRTVHSL ARLLTQYRVN LCYVSPESLK MPEDVKRDVT AKGVSQAEFT
SLEDVLSDTD VLYMTRIQKE RFVSEEEYKK VCGQYVIVPE TMRKAKKKMV VMHPLPRVNE
IHPELDSDPR AAYFRQAENG MYVRMALLAL VLGKC
//
