ID A0A218UBS9_9PASE Unreviewed; 2266 AA.
AC A0A218UBS9;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=CAD protein {ECO:0000313|EMBL:OWK51217.1};
GN Name=CAD {ECO:0000313|EMBL:OWK51217.1};
GN ORFNames=RLOC_00007411 {ECO:0000313|EMBL:OWK51217.1};
OS Lonchura striata domestica (Bengalese finch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Lonchura.
OX NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK51217.1, ECO:0000313|Proteomes:UP000197619};
RN [1] {ECO:0000313|EMBL:OWK51217.1, ECO:0000313|Proteomes:UP000197619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=White83orange57 {ECO:0000313|EMBL:OWK51217.1};
RA Colquitt B.M., Brainard M.S.;
RT "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL Submitted (MAY-2017) 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=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}.
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:OWK51217.1}.
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DR EMBL; MUZQ01000458; OWK51217.1; -; Genomic_DNA.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000197619; 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; 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; 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:UP000197619};
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 1830..1897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1869..1896
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 253
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 337
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 339
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2266 AA; 248665 MW; ABBF7C7993B8C25A CRC64;
MARLVLQDGS VLPGRPFGAV GAAAAGEVVF QTGMVGYPEA LTDPSYKAQI LVLTYPLVGN
YGVPRDEPDA FGLSRWFESS KIHVAALVVG ECSETPSHWS ASRSLDQWLK EQNIPGLEGV
DTRALTKKIR EKGTLLGKLV LDGTPEGSVS FEDPNKKHLV QEVSLKAPRV FNPGGSPRVT
ALDCGLKNNQ IRCLCKRGAA VTVVPWDHPL DPADFDGLFI SNGPGDPQLC QETVSNLCQL
LDAPQPKPIF GICLGHQLLA LALGACTYKM KYGNRGHNQP CLHEDTQRCF ITAQNHGFAV
QAGSLPPGWL PLFTNANDGS NEGLVHQHKP FFSVQFHPEH CAGPTDLEGL FDVFLEVARD
LRDGHRTTRT VRERLRDWLA YTKAPAGDLE AARPRKVLIL GSGGLSIGQA GEFDYSGSQA
IKALKEENIQ TVLINPNIAT VQTSKGLADK VYFLPITPEY VSQVIRNERP DGVLLTFGGQ
TALNCGVELT KAGVLERYRV RVLGTPVASI EMTEDRKVFA EKMEEIGENV APSEAAASLE
QAQAAAERLG YPVLVRSAYA LGGLGSGFAN SREELVALVS QAFTHTSQVL VDKSLKGWKE
IEYEVVRDAY NNCVTVCNME NLDPLGIHTG ESIVVAPSQT LNDTEYFMLR RTAIKVVQHL
GIVGECNIQF ALNPESEQYY IIEMNARLSR SSALASKATG YPLAYVAAKL ALGIPLPVLR
NSVTNSTTAN FEPSLDYCVV KIPRWDLSKF LRVSTKIGSS MKSVGEVMAI GRNFEEAFQK
ALRMVDENCV GFDHTVKPVS DMELETPTDK RIFVLAAALR AGYSIERLYE LTKIDRWFLH
KMKNITDHAV LLESYRGEQG TMPPAVLKRA KQLGFSDKQV ALAVLSTELA VRKMRHDLKI
LPVVKQIDTV AAEWPAQTNY LYLTYNGSEH DLAFREPHVM VIGSGVYRIG SSVEFDWCAV
GCIQELRKMG FKTIMVNYNP ETVSTDYDMC DRLYFDEISF EVVMDIYELE NPEGVILSMG
GQLPNNIAMA LHRQQCRILG TSPEAIDSAE NRFKFSRLLD SIGISQPLWK KLSNMESAKH
FCCKVGYPCV VRPSYVLSGA AMNVAYSDSD LEKFLSNAVA VSKEQPVVIS KFIQEAKEID
VDAVACDGVV VAIAISEHVE NAGVHSGDAT LVTPPQDITS KTLERIKAIV HAIGQELQVT
GPFNLQLIAK DDQLKVIECN VRVSRSFPFV SKTLGVDLVA LASQVIMGED VEPVGLMTGT
GIVGVKVPQF SFSRLAGADV VLGVEMTSTG EVACFGENRC EAYLKAMLST GFKIPKKNIL
LTIGSYKNKS ELLPTVRTLE NLGYNLYASL GTADFYTEHG IKVKAVDWHF EEADSSEAGA
RETQRSILDY LAENHFEMVI NLSMRNSGGR RLSSFVTKGY RTRRLAVDYS VPLIIDIKCT
KLFVEALGQI GAAPPLKMHV DCMTSQKLIR LPGLIDVHVH LREPGGTHKE DFASGTAAAL
AGGVTMVCAM PNTSPAVTDA TSFALAQKLA EAGARCDFAL FLGASMDNAG TLGPLAGAAA
GLKMYLNDTF STLRMDDMSL WMEHLEQWPR HLPIVAHAER QTLAAVLMVA QLYQRPVHIC
HVARREEILL IKAAKQRGIP VTCEVAPHHL FLSQDDVGRL GKGRAAVRPE LGTRQDVEAL
WENMDIIDCF ATDHAPHTLE EKQGQEPPPG YPGLETMLPL LLTAVSEGRL SVEDIVQRLY
ENPRKIFGLP AQEDTYVEVD LEQEWIIPSS TVFSKARWTP FEGMQVKGTV RRVVLRGEVA
YIDGQVLVPP GYGQDVKKWT SGAALLPHGA STKESVKTSE PSRHVAGDVL RGRAPSPRRP
GPVGEGRFHL PPHIHRASDP GLPDEDTREK GSRRPAELDS AAVQDNLFHP LGPVPRQVSP
QRAPQTSSAL HPAAAMVGQH VLSVQQFSKD QLSHLFNVAH TLRLLVQKER SVEILKGKVM
ATMFYEVSTR TSSSFAAAMS RLGGSVLSFS EATSSVQKGE SLADSVQTMC CYADVLVLRH
PQPGAVELAA RHCRKPVINA GDGVGEHPTQ AMLDIFTIRE ELGTVNGMTI TMVGDLKHGR
TVHSLARLLT LYRVNLRYVT PPGLRMPSDI TSFVASRGIQ QVRSGVRGWP HTLSGPVAPR
DLKVLPQEEF GSIEEALPDT DVLYMTRIQK ERFQRAEEYE ACFGQFILTP HIMTRAKERM
VVMHPLPRVN EISVEVDSDP RAAYFRQAEN GMYIRMALLA TVLGRY
//
