ID L7QNH8_9NEOP Unreviewed; 976 AA.
AC L7QNH8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Carbamoylphosphate synthetase/aspartate transcarbamylase/dihydroorotase {ECO:0000313|EMBL:AGB86119.1};
DE Flags: Fragment;
OS Autosticha modicella.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Gelechioidea;
OC Autostichidae; Autostichinae; Autosticha.
OX NCBI_TaxID=454304 {ECO:0000313|EMBL:AGB86119.1};
RN [1] {ECO:0000313|EMBL:AGB86119.1}
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:AGB86119.1}
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; JQ784309; AGB86119.1; -; 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:AGB86119.1"
FT NON_TER 976
FT /evidence="ECO:0000313|EMBL:AGB86119.1"
SQ SEQUENCE 976 AA; 108680 MW; EC2C826C853721FE CRC64;
GYPESLTDPS YHAQLLVLTY PLVGNYGVPD ENDRDEHGLP XWFESNRIWA AGLIVGEVST
RACHWRARRS LGSWLAAHNI PGVCDVDTRA LTFRLRAGVA LGRIIQGLPP FGPLPPLSDP
NTRNLVAEVS VNEITTFNPN GEITIMAIDC GLKYNQIRCL IKRNAKVILV PWDHKLDPTQ
FDGLFISNGP GDPEVCKKVV NNIKNVVNAK NDIKPIFGIC LGHQLLSTAV GCKTYKTSYG
NRGHNLPCTH SXTGRCFMTS QNHGFAVDVN TLPEGWKILF TNENDKTNEG IIHKSLPYFS
VQFHPEHTAG PTDLECLFDV FIDAVKSFKN KKKYIIDEMI TKTLQYTPIL HERPKKVLIL
GSGGLSIGQA GEFDYSGSQG VKAMQEEKIQ TVLINPNIAT VQTSKGLADK VYFLPITPEY
VEQVIKAERP TGVLLTFGGQ TALNCGVELQ KSKVFERYNV NVLGTPIESI VNTEDRKIFA
EKINSIEEKV APSAAVSSVD EALAAAXQIG YPVMARSAFS LGGLGSGFAN NEEELRTLAH
QALSHSDQLI IDKSLKGWKE VEYEVVRDAY DNCITVCNME NVDPLGIHTG ESIVVAPSQT
LSNREYYMLR NTALKVIRHF GIVGECNIQY ALNPNSEEYY IIEVNARLSR SSALASKATG
YPLAYVAAKL ALGVPLPEIK NSVTGVTTAC FEPSLDYCVV KIPRWDLAKF NKVSTKIGSS
MKSVGEVMSI GRNFEEAFQK ALRMVDENVN GFDPNVKKVN ENELREPTDK RMFVLAAALK
QGYTVEKLYE LTKIDRWFLE KFKNIIDYYK NLEKVNTQSI TFDTLKKAKQ IGFSDKQIAA
AIKSTEVAVR KLREEHKITP FVKQIDTVAA EWPASTNYLY LTYNGITHDI DFPGDYVMVL
GSGVYRIGSS VEFDWCAVGC LRELRNQGKK TIMVNYNPET VSTDYDMSDK LYFEEISFEV
VMDIYNIERP NGVILS
//
