ID Q29HK5_DROPS Unreviewed; 2238 AA.
AC Q29HK5; A0A6I8UFP4;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 2.
DT 27-MAR-2024, entry version 119.
DE SubName: Full=CAD protein {ECO:0000313|RefSeq:XP_001354698.2, ECO:0000313|RefSeq:XP_015041573.1};
GN Name=LOC4814491 {ECO:0000313|RefSeq:XP_001354698.2,
GN ECO:0000313|RefSeq:XP_015041573.1};
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245 {ECO:0000313|RefSeq:XP_001354698.2};
RN [1] {ECO:0000313|RefSeq:XP_001354698.2}
RP IDENTIFICATION.
RC STRAIN=MV2-25 {ECO:0000313|RefSeq:XP_001354698.2,
RC ECO:0000313|RefSeq:XP_015041573.1};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_001354698.2,
RC ECO:0000313|RefSeq:XP_015041573.1};
RG RefSeq;
RL Submitted (APR-2022) 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_001354698.2; XM_001354662.4.
DR RefSeq; XP_015041573.1; XM_015186087.2.
DR STRING; 46245.Q29HK5; -.
DR EnsemblMetazoa; FBtr0284836; FBpp0283274; FBgn0075021.
DR EnsemblMetazoa; FBtr0375789; FBpp0337133; FBgn0075021.
DR GeneID; 4814491; -.
DR KEGG; dpo:4814491; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_2_0_1; -.
DR OMA; WSPFNGK; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000001819; Chromosome X.
DR Bgee; FBgn0075021; Expressed in female reproductive system and 3 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 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; 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:UP000001819};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 523..715
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1063..1254
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1319..1474
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT ACT_SITE 265
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 349
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 351
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2238 AA; 247616 MW; A65A45453ADC3C1B CRC64;
MRQVDCYLVL EDGTVMPGLS FGHVAKNSPV GGEVVFQTGM VGYTEALTDR SYSGQILVLT
YPLIGNYGVP CPEEDEHGLP KHFEWLKGAV QATALVVGEV AECAWHWRSS KTLPKWLAEH
KVPGISGVDT RALTKKLREQ GSLLGRIVYK APKEGPNKLI FEDPNTRNLA KECSVRKKMV
FGDATSGKGP RIAIIDCGLK LNQLRCLLQR GASVQLLPWS ADLKDEDYDA LFLSNGPGNP
ESCDAIVEEV RRVIRAGTKP IFGICLGHQL LAKAIGCSTF KMKYGNRGHN LPCLHRATGR
CLMTSQNHGY AVDLQDLPGE WEELFVNAND GTNEGIVHRS KPYFSVQFHP EHHAGPCDTE
FLFDVFMESI RTPQLSVPEL ISRRLRPAKL LPVQPKPRKV LILGSGGLSI GQAGEFDYSG
SQAIKAMRES GIQTVLINPN IATVQTSKGM ADKCYFLPLT PHYVEEVIKS ERPNGVLLTF
GGQTALNCGV ELDRAGVFEK YNVRILGTPI QSIIETEDRK LFAQRVNDIG EQVAPSEAVY
SVAEALEAAG RLGYPVMARA AFSLGGLGSG FANNEQELEN LAEQALAHSS QLIVDKSLKG
WKEVEYEVVR DAFDNCITVC NMENFDPLGI HTGESIVVAP SQTLSDREYQ MLRNTALKVI
RHLGVVGECN IQYALCPHSE QFYIIEVNAR LSRSSALASK ATGYPLAYVA AKLALGLPLP
EIKNSVTGNT TACFEPSLDY CVVKIPRWDL AKFTRVSKHI GSSMKSVGEV MSIGRSFEEA
FQKALRMVDS DVLGFDADVV VVDEQKLADQ LSEPTDRRPF FLAAALTMGM DIQQLHKLTK
IDQWFLHKLE RIVFFNHHLS RLNASGSQLG PDLLLKAKRL GFSDKQIAKA TKSTELVVRQ
QRHQLGIRPF VKQIDTVAGE WPASTNYLYT TYHGTEHDVE FPGGHIIVVG SGVYRIGSSV
EFDWCAVGCL RELRKLQKPT IMINYNPETV STDYDMCDRL YFEEISFEVV MDIYELESSE
GIILSMGGQL PNNIAMDLHR QQAKVLGTSP DSIDCAENRF KFSRMLDRKG ILQPRWKELT
NLKSAIEFCE EVGYPCLVRP SYVLSGAAMN VAYSNQDLET YLNAASEVSR EHPVVISKFL
TEAKEIDVDA VAADGQILCM AVSEHVENAG VHSGDATLVT PPQDLNAETL EAIKRITCAL
ASLLDVTGPF NMQLIAKNNE LKVIECNVRV SRSFPFVSKT LDHDFVATAT RAIVGMDVEP
IDVLHGVGKV GVKVPQFSFS RLAGADVQLG VEMASTGEVA GFGDNRYEAY LKAMMSTGFQ
IPKNAVLLSI GSFKHKMELL PSIRDLAKMG YKLYASMGTG DFYAEHGVDV ESVQWTFDKT
TPDDINGELR HLAEFLANKQ FDLVINLPMS GGGVRRVSSF MTHGYRTRRL AVDYSIPLVT
DVKCTKLLVE SMRLMGGQPA MKTHTDCMTS RRIVKLPGFI DVHVHLREPG ATHKEDFSSG
TAAALAGGVT LVCAMPNTNP SIVDKETFAQ FQELARLGAR CDYALYLGAS DANWAQAHEL
ASQACGLKMY LNDTYGTLRL SDMTAWQRHL SHWPKRAPIV CHAEKQSMAA VVLLAHLLDR
HVHICHVARK EEIQLIRAAK EKGIKVTCEV CPHHLFLSTK DVDRLGSGMS EVRPLLCSPE
DQEALWEHME YIDVFATDHA PHTLEEKQSE RPPPGFPGLE TILPLLLQAV HEGRLTMEDI
KRKLHRNPRN IFNLPEQPHT YVEVDLDEEW TISGSELKTK AGWTPFEGTK VTGRVHRVVL
RGEVAFIDGQ VLVQPGFGQN VRNKAGAQQL LSEATQELPS DRDANDTFAR LLTVEGAAKV
HFVDEANNSN SFLRPISPSP RHRLDSSSNT TLRDYLQRTA MSVSGSASGS VAANQYSQPS
PNPVAHSLVG KHILAVDMFS KDHLNDIFNL AQLLKSRVTK DRPLDDLLRG KIMASVFYEV
STRTQCSFAA AMLRLGGRVI SMDQLTSSVK KGESLEDSIK VMASYADVMV LRHPLPGAVA
RAALYSRKPV INAGDGVGEH PTQALLDIFT IREEIGTVNG LTITMCGDLK NGRTVHSLAR
LLTLYNVTLQ YVAPETLQMP DEITKFVNER GVKQVFYNAL ALDALADTDV LYMTRIQRER
FDSDSEYQKC NGPFIVTPKL MTLAKKRMIV LHPLPRLDEI SRDFDLDPRA AYFRQAEYGM
YIRMALLAMV VGCRSTAL
//
