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Database: UniProt
Entry: B3TDY4_SPOFR
LinkDB: B3TDY4_SPOFR
Original site: B3TDY4_SPOFR 
ID   B3TDY4_SPOFR            Unreviewed;       557 AA.
AC   B3TDY4;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Putative CAD trifunctional protein {ECO:0000313|EMBL:ABW39017.1};
DE   Flags: Fragment;
OS   Spodoptera frugiperda (Fall armyworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Amphipyrinae; Spodoptera.
OX   NCBI_TaxID=7108 {ECO:0000313|EMBL:ABW39017.1};
RN   [1] {ECO:0000313|EMBL:ABW39017.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Regier J.C.;
RT   "PCR primers that amplify across Panarthropoda.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; EU032750; ABW39017.1; -; mRNA.
DR   AlphaFoldDB; B3TDY4; -.
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; -; 1.
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   InterPro; IPR011761; ATP-grasp.
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; 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; SM01097; CPSase_sm_chain; 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; 1.
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..557
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:ABW39017.1"
FT   NON_TER         557
FT                   /evidence="ECO:0000313|EMBL:ABW39017.1"
SQ   SEQUENCE   557 AA;  60841 MW;  D56844CA1DDE32FA CRC64;
     GYPESLTDPS YHAQLLVLTY PLVGNYGVPD EDERDEHGIP KWFESNRIWA AGLIVGEVST
     NACHWRAKRS LGAWLAARGI PGVCDVDTRA LTFRLRAGVT LGRIIQGVPP FGPLPALSDP
     NNRNLVAEVS VKEPKIYNPD GQVTIMAVDC GLKYNQIRCL IKRNAKVILV PWDHKLDPSQ
     YDGLFISNGP GDPVKCKKLV DNMRTIIGDK NSVKPLFGIC LGHQLLSTAA GCKTYKTSYG
     NRGHNLPCTH NGTGRCFMTS QNHGFAVDAD SLPEGWKILF TNENDKTNEG VIHETLPYFS
     VQFHPEHTAG PTDLECLFDV FIDAVKSYKN KQTYNVDNAI TEKIKFVPTI HERPKKVLIL
     GSGGLSIGQA GEFDYSGSQA VKALQEEKIQ TVLINPNIAT VQTSKGLADK VYFLPITPEY
     VEQVIKAERP TGVLLTFGGQ TALNCGVELE KSKILEKYNV SVLGTPIQSI VDTEDRKIFA
     EKIHAIGEKV APSAAVTTIE EALIAAKQIG YPVMARSAFS LGGLGSGFAN NEDELRTLAH
     HGLSHSDQLI IDKSLKG
//
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