ID B3TDX3_9NEOP Unreviewed; 976 AA.
AC B3TDX3;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Carbamoylphosphate synthetase {ECO:0000313|EMBL:ACT87637.1};
DE SubName: Full=Putative CAD trifunctional protein {ECO:0000313|EMBL:ABW39006.1};
DE Flags: Fragment;
GN Name=CAD {ECO:0000313|EMBL:ACT87637.1};
OS Mesocondyla dardusalis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Pyraloidea;
OC Crambidae; Spilomelinae; Mesocondyla.
OX NCBI_TaxID=82628 {ECO:0000313|EMBL:ABW39006.1};
RN [1] {ECO:0000313|EMBL:ABW39006.1}
RP NUCLEOTIDE SEQUENCE.
RA Regier J.C.;
RT "PCR primers that amplify across Panarthropoda.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACT87637.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19954545; DOI=10.1186/1471-2148-9-280;
RA Regier J.C., Zwick A., Cummings M.P., Kawahara A.Y., Cho S., Weller S.,
RA Roe A., Baixeras J., Brown J.W., Parr C., Davis D.R., Epstein M.,
RA Hallwachs W., Hausmann A., Janzen D.H., Kitching I.J., Solis M.A.,
RA Yen S.H., Bazinet A.L., Mitter C.;
RT "Toward reconstructing the evolution of advanced moths and butterflies
RT (Lepidoptera: Ditrysia): an initial molecular study.";
RL BMC Evol. Biol. 9:280-280(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; EU032739; ABW39006.1; -; mRNA.
DR EMBL; GQ283571; ACT87637.1; -; 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; 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; IPR017926; GATASE.
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; 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:ABW39006.1"
FT NON_TER 976
FT /evidence="ECO:0000313|EMBL:ABW39006.1"
SQ SEQUENCE 976 AA; 108483 MW; D9A770EDA855B817 CRC64;
GYPESLTDPS YHAQLLVLTY PMIGNYGVPD EEERDEHGLP KWFESSRIWA AGLIVGEVST
RACHWRARRS LGSWLASRGV PGLCDIDTRA LTYRLRSGVM LGRIVQGVPP FGPFPPLSDP
NTRNLVAEVS TKDIKTFNPQ GDVTIMAVDC GLKYNQIRCL VKRNVKVVLV PWDHKLNAKD
YDGLFISNGP GDPEVCKQVV KNLQEVIANK SNVKPIFGIC LGHQILSTAI GCKTYKTSYG
NRGHNLPCTH YDTGRCFMTS QNHGYAVDAG SLPENWKILF TNENDKTNEG IIHKSXPFFS
VQFHPEHTAG PTDLEHLFDI FIEAVRSFKT KKSYVINDEI TKKLTYTPTI HERPKKVLIL
GSGGLSIGQA GEFDYSGSQG VKAMQEEKIQ TVLINPNIAT VQTSKGLADK VYFLPITPQY
VEQVIKAERP TGVLLTFGGQ TALNCGVELQ KSGVFEKYNV AVLGTPIQSI VDTEDRKIFA
EKIHSIGEKV APSAAVTSVE EALAAALQIG YPVMARSAFS LGGLGSGFAN NEEELKALAH
QALSHSDQLI IDKSLKGWKE VEYEVVRDAF DNCITVCNME NVDPLGIHTG ESIVVAPSQT
LSNREYYMLR NTAIKVIKHF GIVGECNIQY ALNPNSEEFY IIEVNARLSR SSALASKATG
YPLAYVAAKL ALGIPLPVIK NSVTGVTTAC FEPSLDYCVV KIPRWDLAKF NKVSTKIGSS
MKSVGEVMSI GRNFEEAFQK ALRMVDENVN GFDPNIKKVN ENELQEPTDK RMFVLAAALK
EGYTVEKLYD LTKIDSWFLV KFKNIIDYYK NLQKVDSNTI TSDILRKAKK IGFSDKQIAA
AIKSTEVAVR KLREEYKITP FVKQIDTVAA EWPASTNYLY LTYNGSTHDL DFPGDFTMVL
GSGVYRIGSS VEFDWCAVGC LRELRNQNKK TIMINYNPET VSTDYDMSDR LYFEEISFEV
VMDIYKIEKP NGVILS
//
