ID L7QSX2_9NEOP Unreviewed; 977 AA.
AC L7QSX2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Carbamoylphosphate synthetase/aspartate transcarbamylase/dihydroorotase {ECO:0000313|EMBL:AGB86391.1};
DE Flags: Fragment;
OS Homidiana sp. Hodn.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Geometroidea;
OC Sematuridae; Homidiana.
OX NCBI_TaxID=1181358 {ECO:0000313|EMBL:AGB86391.1};
RN [1] {ECO:0000313|EMBL:AGB86391.1}
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:AGB86391.1}
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; JQ784581; AGB86391.1; -; mRNA.
DR AlphaFoldDB; L7QSX2; -.
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; 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: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:AGB86391.1"
FT NON_TER 977
FT /evidence="ECO:0000313|EMBL:AGB86391.1"
SQ SEQUENCE 977 AA; 108543 MW; 2263EA43D7EAD926 CRC64;
GYPESLTDPS YHAQLLVLTY PLVGNYGVPD ENERDEFGLP RWFESSRIWA AGLIVGEVST
RACHWRARQS LGSWLAAHGV PGLCDIDTRA LTYRLRAGVT LGRIVQGVPP FGPLPALSDP
NSRNLVAEVS VKEKKIFNLN GEVTVVAVDC GLKYNQIRCL ARRNVKVILV PWNYKLDPNE
YDGLFLSNGP GDPEICKQVV ENLRDVFDKK ANVKPIFGIC LGHQLLSTAV GCKTYKTSYG
NRGHNLPCTH NGTGRCFMTS QNHGFAVDPD SMPEDWKVLF TNENDKTNEG IIHKSEPFFS
VQFHPEHTAG PTDLECLFDI FVDAVKSYKN KKICVIDQMI TEKLKFSPTI QERPKKVLIL
GSGGLSIGQA GEFDYSGSQG VKALQEEKIQ TVLINPNIAT VQTSKGLADK VYFLPITPEY
VEQVIKAERP TGVLLTFGGQ TALNCGVKLQ NNKIFEKYNV NVLGTPIQSI VDTEDRKIFA
EKINSIGEKV APSAAVNSVE EALAAAVQIG YPVMARSAFS LGGLGSGFAN NEEELRSLAH
QALSHSDQLI IDKSLKGWKE VEYEVVRDAY DNCITVCNME NVDPLGIHTG ESIVVAPSQT
LSNREYYMLR NTALKVIRHF GIVGECNIQY ALNPYSEEFY IIEVNARLSR SSALASKATG
YPLAYVAAKL ALGIPLPVIK NSVTGVTTAC FEPSLDYCVV KIPRWDLAKF NRVSTKIGSS
MKSVGEVMSI GRNFEEAFQK ALRMVDENVN GFDPNIKSVN EDELREPTDK RMFVLAAALK
QGYSVEKLYE LTKIDRWFLV KFKNIVDYYK NLESSGGSAT ITFDVLRNAK KIGFSDKQIA
AAIKSTEVAV RKLREEYKIT PFVKQIDTVA AEWPATTNYL YLTYNGSSHD LEFPGEFVMV
LGSGVYRIGS SVEFDWCAVG CLRELRNQGK KTIMVNYNPE TVSTDYDMSD RLYFEEISFE
VVMDIYNIEH PNGVILS
//
