ID D2WIS6_9NEOP Unreviewed; 976 AA.
AC D2WIS6;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Carbamoylphosphate synthetase {ECO:0000313|EMBL:ACT87611.1};
DE Flags: Fragment;
GN Name=CAD {ECO:0000313|EMBL:ACT87611.1};
OS Hyblaea firmamentum.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Hyblaeoidea;
OC Hyblaeidae; Hyblaea.
OX NCBI_TaxID=655042 {ECO:0000313|EMBL:ACT87611.1};
RN [1] {ECO:0000313|EMBL:ACT87611.1}
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; GQ283545; ACT87611.1; -; 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:ACT87611.1"
FT NON_TER 976
FT /evidence="ECO:0000313|EMBL:ACT87611.1"
SQ SEQUENCE 976 AA; 108477 MW; 5C64FA57E3BDF366 CRC64;
GYPESLTDPS YHAQLLVLTF PLIGNYGIPD ENERDEHGLP RWFESSRIWA AGLIVGEVST
RACHWRARXS LGSWLXANGI PGLCDIDTRA LTHRLREGVT LGRIIQGVQP FGPLPSISDP
NERNLVAEVS TKEKTVFNPN GEITILAVDC GLKYNQIRCL IKRNAKVILV PWNHKLNPND
YDGLFISNGP GDPVVCKQVV DNLRVVATDK NNVKPIFGIC LGHQLLATAI GCKTYKTSYG
NRGHNLPCRH SGTGRCFMTS QNHGFAVDTD TIPDGWKVLF TNENDKTNEG IIHKTSPFFS
VQFHPEHTAG PTDLECLFDI FIDAVKAFKV QKQYIIDDKI TESLKYTPNL YERPKKVLIL
GSGGLSIGQA GEFDYSGSQG VKAMQEEKIQ TVLINPNIAT VQTSKGLADK VYFLPITPEY
VEQVIKAERP TGVLLTFGGQ TALNCGVELQ KSKVFEKYNV NVLGTPIQSI VDTEDRKIFS
EKINAIGEKV APSAAVTSVE EAVAAASQIG YPVMARSAFS LGGLGSGFAN NEEELRALAH
QALSHSDQLI IDKSLKGWKE VEYEVVRDAF DNCITVCNME NVDPLGIHTG ESIVVAPSQT
LSNREYYMLR NTALKVIRHF GIVGECNIQY ALNPNSEEFY IIEVNARLSR SSALASKATG
YPLAYVAAKL ALGIPLPDIK NSVTGVTTAC FEPSLDYCVV KIPRWDLAKF NRVSTKIGSS
MKSVGEVMSI GRNFEEAFQK ALRMVDENVH GFDPYIKKVN ENELREPTDK RMFVLAAALR
EGYSIDKLYE LTKIDKWFLE KFKNIIDYYK TLESVGLGSV TKEILLKAKK IGFSDKQIAA
AARSTELAVR KLREEYKITP FVKKIDTVAA EWPASTNYLY LTYNGNTHDL DFPGEFIXVL
GSGVYRIGSS VEFDWCAVGC LRELRNLGKK TIMINYNPET VSTDYDMSDR LYFEEISFEV
VMDIYNIEKP FGVILS
//
