ID B9U6X2_9NEOP Unreviewed; 976 AA.
AC B9U6X2;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Carbamoylphosphate synthetase/aspartate transcarbamylase/dihydroorotase {ECO:0000313|EMBL:ACD01507.1};
DE Flags: Fragment;
GN Name=CAD {ECO:0000313|EMBL:ACD01507.1};
OS Megacorma obliqua.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Sphingidae; Sphinginae; Acherontiini; Megacorma.
OX NCBI_TaxID=522844 {ECO:0000313|EMBL:ACD01507.1};
RN [1] {ECO:0000313|EMBL:ACD01507.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AToL-Lep-ID AYK-04-0154 {ECO:0000313|EMBL:ACD01507.1};
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).
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DR EMBL; EU479077; ACD01507.1; -; 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; 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 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:SF4; CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC SMALL CHAIN; 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; 2.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 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}.
FT DOMAIN 480..807
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:ACD01507.1"
FT NON_TER 976
FT /evidence="ECO:0000313|EMBL:ACD01507.1"
SQ SEQUENCE 976 AA; 108654 MW; 6FA5C0077C9FE783 CRC64;
GYPESLTDPS YHAQLLVLTY PLVGNYGVPD EKERDEHGIP RWFESERIWA SALIVGEVST
RACHWRAKRS LGKWLSAHGI PGLCDVDTRS LTYRLREGVT LGRIVQGVPP FDPLPPLADP
NSRNLVAEVS TKESKIFNPN GVVTIVAVDC GLKFNQIRCL XKRNAKVVLV PWNHQLDTTQ
YDGLFISNGP GDPEVCKSVV DNLRLILQNK DQIKPIFGIC LGHQLLSTAA GCKTYKTKYG
NRGHNLPCTH SGTGRCFMTS QNHGFAVDXN TLPDDWKVLF TNENDKTNEG IIHKSEPYFS
VQFHPEHTAG PTDLEGLFDV FIDTVKSFKE KVPCVIDDMI TKKLKFIPTI HERPKKVLIL
GSGGLSIGQA GEFDYSGSQG VKAMQEEKIQ TVLINPNIAT VQTSKGLADK VYFLPITPEY
VEQVIKAERP TGILLTFGGQ TALNCGVELQ KSKIFEKYNV NVLGTPIQSI VDTEDRKIFA
EKINAIGEKV APSAAVTSID EALAAALQIG YPVMARSAFS LGGLGSGFAN NEEELRALAH
QALSHSDQLI IDKSLKGXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXSLDYCVV KIPRWDLAKF NRVSTKIGSS
MKSVGEVMSI GRSFEEAFQK ALRMVDENVN GFDPNIKKVN ENDLREPTDK RMFVLAAALK
EGYSVEKLYG LTKIDRWFLE KFKNIIDYYK TLDAYDSGSV TFDVLKRAKK IGFSDKQIAA
AIKSTELAVR KLREEYKITP FVKQIDTVAA EWPASTNYLY LTYNGNAHDL DFPGDYVMVL
GSGVYRIGSS VEFDWCAVGC LRELRNQGKN TIMVNYNPET VSTDYDMSDR LYFEEISFEV
VMDIYNIERP SGVILS
//