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Database: UniProt
Entry: A0A3P8NFU8_ASTCA
LinkDB: A0A3P8NFU8_ASTCA
Original site: A0A3P8NFU8_ASTCA 
ID   A0A3P8NFU8_ASTCA        Unreviewed;      2234 AA.
AC   A0A3P8NFU8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 23.
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};
OS   Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX   NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000003644.1, ECO:0000313|Proteomes:UP000265100};
RN   [1] {ECO:0000313|Ensembl:ENSACLP00000003644.1, ECO:0000313|Proteomes:UP000265100}
RP   NUCLEOTIDE SEQUENCE.
RA   Datahose.;
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACLP00000003644.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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=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   STRING; 8154.ENSACLP00000003644; -.
DR   Ensembl; ENSACLT00000003724.1; ENSACLP00000003644.1; ENSACLG00000002358.1.
DR   GeneTree; ENSGT00940000157241; -.
DR   OMA; FTGDLRY; -.
DR   OrthoDB; 309at2759; -.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000265100; Chromosome 15.
DR   Bgee; ENSACLG00000002358; Expressed in liver and 7 other cell types or tissues.
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; 3.30.1490.20; 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   NCBIfam; TIGR00857; pyrC_multi; 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   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..1469
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
FT   REGION          1817..1863
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1832..1853
FT                   /note="Basic and acidic residues"
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;  247228 MW;  5DB7B372C3ED6999 CRC64;
     MANMATLILE DGTTFKGRQF GASVSVSGEV VFQTGMVGYP EALTDPSYRC QLLTLTYPLV
     GNYGVPMDEE GEFGLSKWFE SYKIHAAALI IGELSESPSH WSSAKSLDQW LKEQGIPGLQ
     GVDTRCLTKK IREKGTMLGK LIVDGTPEES IPFDNPDKRN LVREVSMKEP KVFNHSGSFR
     ITVVDCGIKY NQIRCLAQRG ARVTVVPWDH PLDTADFDGL FVSNGPGDPQ LCQATINNVR
     KVISVDQPKP VFGICLGHQL LSLVIGAKTY KMKYGNRGHN QPCIHNGTER CFITSQNHGF
     AVDPDTLPKD WDVLFTNAND HTNEGIVHNT KPLFSVQFHP EHMAGPTDLV GLFDVFIETV
     KDHKEGNTGK SVKQRLMDHL TFTGSPKAEG HVRSKKVLIL GSGGLSIGQA GEFDYSGSQA
     IKALKEENIQ TVLINPNIAT VQTSKDLADK VYFLPITAEY VTQVIKNERP DGVLLTFGGQ
     TALNCGVELT KLGVLEKYKV QVLGTPVSSI EMTEDRKIFV EKMEEINEHV APSEAALSVE
     QAVAAAERLG YPVLVRSAFA LGGLGSGFAN NREELTSLVT AAFAHTSQVL VDKSLKGWKE
     IEYEVVRDAY DNCVTVCNME NIDPLGIHTG ESIVVAPSQT LNDREYNMLR NTAIKVIRHL
     GIVGECNIQY ALNPESEQYY IIEVNARLSR SSALASKATG YPLAYVAAKL GLGIPLPQLK
     NSVTNSTTAN FEPSLDYCVV KVPRWDLSKF LRVSTKIGSS MKSVGEVMAI GRSFEEAFQK
     ALRMVDENCV GFDHTIKPVS EKELQTPTDK RIFVLAAAFK AGYTVEKLYE LTKIDRWFLH
     KMKNIADHEL LLETYNQDES SMPPEVMLKA KQLGFSDKQI ALAVQSTELA VRKLRHDWSI
     LPVVKQIDTV AAEWPAYTNY LYLTYHGTED DLSFNDQHVM VIGSGVYRIG SSVEFDWCAV
     GCITELRKMG YKTIMVNYNP ETVSTDYDMC DRLYFDEISF EVVMDIYERE NPEGVILSMG
     GQLPNNIAMS LHRQQCHILG TSPEFIDSAE NRFKFSRMLD TIGISQPQWK ELSDTESAVK
     FCETVGYPCL VRPSYVLSGA AMNVAYSDSD LEKYLSNAVA VSKEHPVVIS KFIQEAKEID
     VDAVACDGVV MGIAISEHVE NAGVHSGDAT LVTPPQDLNQ KTIERIMQIV HAIGQELQVT
     GPFNLQLIAK DDQLKVIECN VRVSRSFPFV SKTLGVDLVA LATQYIMGED VEPVGLMKGK
     GIVGVKVPQF SFSRLAGADV VLGVEMTSTG EVACFGENRY EAYLKAMLST GFKIPKKNIL
     LSIGSYKNKS ELLPTVQALE SLGYDLYASM GTADFYTEHG VKVTAIDWPF EEYDSDECAT
     KEKQRSIMNY LEENHFDLVI NLSMRNSGGR RLSSFVTKGY RTRRMAIDYS VPLIIDIKCT
     KLFVQALRQI GRTPPVKTHV DSMASQTLVR LPGLIDVHVH LREPGATHKE DFSSGTAAAL
     AGGVTLVCAM PNTSPAITDA NNLALVQKLA KAGSRCDYAL YVGAATDNAA VLPPIASQTA
     GLKMYLNDTY STLKMDNVSL WMEHFEKWPK QMPIVAHAEK QTVAAILMVA QLYQRPVHIC
     HVAKKEEILI IRAAKQKGIQ VTCEVAPHHL FLCEDNVAQI GDGRAQVRPM LGTREDMETL
     WENLDIIDCF ATDHAPHSVD EKNSERPPPG YPGLETMLPL LLTSVSDGRL TLDDITRRLY
     DNPRRIFNLP VQENTYVEVD LEQEWVIPQA MQFTKSKWTP FEGMKVKGKV RRVVLRGEVA
     YIDGQVLVPP GYGEDVKTWP TSSTHPPEPV KETPMTPERR RPTPPRDGVR TRAASPRRIG
     GESRYLLPPR IHRASDPGLP PEMVMLPPAA AVDGYSHPPP LSRLLSPQSG SGQVPPGQVS
     HLQMSPLLHP LVGQHILSVR QFSKEQISHL FNVAHTLRLM VQKERSLEIL KGKVMASIFY
     EVSTRTSSSF AAAMQRLGGS VVHSSEATSS SLKGESLADS VQIMSGYADV LVLRHPTPGA
     VESASRQCRK PLINAGDGVG EHPTQALLDV FTIREELGTV NGMTITMVGD LKHGRTVHSL
     AKLLTQYRIT LRYVAPKNLH MPAEIVSYVA SKGIKQEEFD SIEEALPDTD VLYMTRIQKE
     RFASEEEYKA CFGQFVLTPH IMTGAKQKMV VMHPLPRVNE ISVEVDTDPR AAYFRQAENG
     MYIRMALLAT VLGR
//
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