ID L7QPF7_9NEOP Unreviewed; 976 AA.
AC L7QPF7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Carbamoylphosphate synthetase/aspartate transcarbamylase/dihydroorotase {ECO:0000313|EMBL:AGB86439.1};
DE Flags: Fragment;
OS Lepidotarphius perornatellus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Yponomeutoidea;
OC Glyphipterigidae; Lepidotarphius.
OX NCBI_TaxID=1178303 {ECO:0000313|EMBL:AGB86439.1};
RN [1] {ECO:0000313|EMBL:AGB86439.1}
RP NUCLEOTIDE SEQUENCE.
RA Regier J.C., Mitter C., Solis M.A., Hayden J.E., Landry B., Nuss M.,
RA Simonsen T.J., Yen S.-H., Zwick A., Cummings M.P.;
RT "A molecular phylogeny for the pyraloid moths (Lepidoptera: Pyraloidea) and
RT its implications for higher-level classification.";
RL Syst. Entomol. 37:635-656(2012).
RN [2] {ECO:0000313|EMBL:AGB86439.1}
RP NUCLEOTIDE SEQUENCE.
RG LepTree.net;
RA Regier J.C.;
RT "Assembling the Tree of Life Lepidoptera.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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; JQ784629; AGB86439.1; -; 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 UNSURE 678
FT /note="D or N"
FT /evidence="ECO:0000313|EMBL:AGB86439.1"
FT UNSURE 711
FT /note="D or N"
FT /evidence="ECO:0000313|EMBL:AGB86439.1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AGB86439.1"
FT NON_TER 976
FT /evidence="ECO:0000313|EMBL:AGB86439.1"
SQ SEQUENCE 976 AA; 108620 MW; 593CD48A1E5EFA15 CRC64;
GYPESLTDPS YHSQLLVLTY PLIGNYGVPD EHEMDENGLP KWFESNRIWA AGLIVGEVNT
RAWHWRARRS LGTWLAAHGV PGLCGVDTRA LTVRLRAGVM LGRIIQGTPP FGILPPIADP
NKRNLVAEVS VQESRIFNKN GEVTILAVDC GLKYNQIRCL TKRNAKVVLV PWNYPLNPDN
YDGLFISNGP GDPEICNEVV ENIKAVINDN NIIKPVFGIC LGHQLLSTAV GCKTFKMSYG
NRGHNLPCTH NGTGRCFMTS QNHGFAVDTN TLPKGWTVLF TNENDKTNEG IIHEERPFFS
VQFHPEHTAG PTDLECLFDI FVDAVKAYKD KKKFNIKNMI IENIKFVPTI HERPKKVLIL
GSGGLSIGQA GEFDYSGSQG VKALQEEKIQ TVLINPNIAT VQTSKGLADK VYFLPITPEY
VEQVIKAERP TGVLLTFGGQ TALNCGVQLK KSGVFEKYNV NVLGTPIQSI IDTEDRKIFA
EKVNYIGEKV APSAAVSSVE EALEAAKQIG YPVMSRAAFA LGGLGSGFAN NEDELRXLAH
QGLSHSEQLI IDKSLKGWKE XEYEVVRDAY DNCITVCNME NLDPLGIHTG ESIVVAPSQT
LSNREYYMLR NTAIKVIRHF GVIGECNIQY ALNPNSEEFY IIEVNARLSR SSALASKATG
YPLAYVAAKL ALGIPLPDIK NSVTAVTTAC FEPSLDYCVV KIPRWDLAKF DRVSTKIGSS
MKSVGEVMSI GRNFEEAFQK ALRMVDENVN GFDPNIKAVN DDDLREPTDK RIFVLAAAIK
KGYTIEKLYE LTKIDGWFLE KLKHIIDYYV ALESITHDTI DIELLKESKR VGFSDKQISV
AIKSTELAVR KLREEFKIFP FVKRIDTVAA EWPATTNYLY MTYNGTTHDT DFPGDAIMVL
GSGVYRIGSS VEFDWCAVGC LRELRSQGKK TIMVNYNPET VSTDYDMSDR LYFEEISFEV
VMDIYNLEQP NGVILC
//
