ID B9U6X3_9NEOP Unreviewed; 976 AA.
AC B9U6X3;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Carbamoylphosphate synthetase/aspartate transcarbamylase/dihydroorotase {ECO:0000313|EMBL:ACD01508.1};
DE Flags: Fragment;
GN Name=CAD {ECO:0000313|EMBL:ACD01508.1};
OS Notonagemia analis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Sphingidae; Sphinginae; Sphingini; Notonagemia.
OX NCBI_TaxID=1652094 {ECO:0000313|EMBL:ACD01508.1};
RN [1] {ECO:0000313|EMBL:ACD01508.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AToL-Lep-ID AYK-04-2579 {ECO:0000313|EMBL:ACD01508.1};
RX PubMed=19492095; DOI=10.1371/journal.pone.0005719;
RA Kawahara A.Y., Mignault A.A., Regier J.C., Kitching I.J., Mitter C.;
RT "Phylogeny and biogeography of hawkmoths (Lepidoptera: Sphingidae):
RT evidence from five nuclear genes.";
RL PLoS ONE 4:e5719-e5719(2009).
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};
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DR EMBL; EU479078; ACD01508.1; -; mRNA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
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 InterPro; IPR011761; ATP-grasp.
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; IPR017926; GATASE.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00098; CPSASE.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01097; CPSase_sm_chain; 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; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT DOMAIN 480..672
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT ACT_SITE 220
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 304
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 306
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACD01508.1"
FT NON_TER 976
FT /evidence="ECO:0000313|EMBL:ACD01508.1"
SQ SEQUENCE 976 AA; 108828 MW; 755BEB543F5EFABC CRC64;
GYPESLTDPS YHAQLLVLTY PLVGNYGVPD ETERDEHGIP RWFESERIWA SALIVGEVST
RACHWRAKRS LGKWLSAHGI PGLCDVDTRS LTYRLREGVT LGRIVQGVPP FXPLPPLADP
NXRNLVAEVS TKEAKIFNPN GEVTIVAVDC GLKFNQIRCL IKRNAKVILV PWNYQLDTTQ
YDGLFISNGP GDPEVCKNVV DNLKLXLQNK DKIKPIFGIC LGHQLLSTAA GCKTYKTKYG
NRGHNLPCTH SGTGRCFMTS QNHGFAVDTN TLPEDWKVLF TNENDKTNEG IIHKSEPYFS
VQFHPEHTAG PTDLECLFDI FIDAVKSYKQ KVPCVIDDMI IEKLKFIPRI HERPKKVLIL
GSGGLSIGQA GEFDYSGSQG VKAMQEEKIQ TVLINPNIAT VQTSKGLADK VYFLPITPEY
VEQVIKAERP TGILLTFGGQ TALNCGVELQ KSKIFEKYNV NVLGTPIQSI VDTEDRKIFA
EKINAIGEKV APSAAVTSVE EALAAAVQIG YPVMARSAFS LGGMGSGFAN NEEELKALAH
QALSHSDQLI IDKSLKGWKE VEYEVVRDAY DNCITVCNME NVDPLGIHTG ESIVIAPSQT
LSNREYYMLR NTAIKVIRHF GIVGECNIQY ALNPYSEEFY IIEVNARLSR SSALASKATG
YPLAYVAAKL ALGIPLPTIK NSVTGVTTAC FEPSLDYCVV KIPRWDLAKF NRVSTKIGSS
MKSVGEVMSI GRSFEEAFQK ALRMVDENVN GFDPNIKKVN ENDLREPTDK RMFVLAAALK
EGYTVEKLYE LTKIDRWFLE KFKNIIDYYK TLDAYDSGSV TFDILKRAKK IGFSDKQIAA
AIKSTELAVR KLREEYKITP FVKQIDTVAA EWPASTNYLY LTYNGNAHDL DFPSDYVMVL
GSGVYRIGSS VEFDWCAVGC LRELRNQGKX TIMVNYNPET VSTDYDMSDR LYFEEISFEV
VMDIYNIERP SGVILS
//
