ID L7QPT6_9NEOP Unreviewed; 975 AA.
AC L7QPT6;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Carbamoylphosphate synthetase/aspartate transcarbamylase/dihydroorotase {ECO:0000313|EMBL:AGB86609.1};
DE Flags: Fragment;
OS Rhamphura sp. Rham.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Gelechioidea;
OC Scythrididae; Rhamphura.
OX NCBI_TaxID=1181378 {ECO:0000313|EMBL:AGB86609.1};
RN [1] {ECO:0000313|EMBL:AGB86609.1}
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:AGB86609.1}
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; JQ784799; AGB86609.1; -; mRNA.
DR AlphaFoldDB; L7QPT6; -.
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 479..671
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT ACT_SITE 219
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 303
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 305
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AGB86609.1"
FT NON_TER 975
FT /evidence="ECO:0000313|EMBL:AGB86609.1"
SQ SEQUENCE 975 AA; 108624 MW; FA29B157B4AAAA7B CRC64;
GYPESLTDPS YHAQLLVLTY PLIGNYGVPD EQERDEHGIP RWFESWRIWA AGLIVGEVST
YACHWRAHQS LGAWLAARGI PGLCDVDTRA LTKRLREGVT LGRIVQGIPP FGPLPPLKDP
NLRNLVAEVS VKENKVFNPK GEVTIMAVDC GLKYNQIRCF LKRNVKVILV PWNHKLNADD
YDGLFISNGP GDPEICNEVV QNLRNVMNTP KVKPIFGICL GHQLLATAAG CKTFKTSYGN
RGHNLPCTHS GTGRCFMTSQ NHGFAVDTDT IPGDWKILFT NENDKTNEGI IHKTKPFFSV
QFHPEHTAGP TDLECLFDIF IEKVKSYKNE KTCNIDQMIT QKLQYTPTIH DRPKKVLILG
SGGLSIGQAG EFDYSGSQGV KALQEEKIQT VLINPNIATV QTSKGLADKV YFLPITPEYV
EQVIKAERPT GVLLTFGGQT ALNCGVELER SKVFDKYNVQ VLGTPIQSIV DTEDRKIFAE
KINAIGEKVA PSAAVSSVEE AIAAASQIGY PVMTRSAFSL GGLGSGFANN DDELRTLAHH
ALSHSDQLII DKSLKGWKEV EYEVVRDAFD NCITVCNMEN VDPLGIHTGE SIVVAPSQTL
SNRDYYMLRN TAIKVIRHFG IVGECNIQYA LNPNSEEFYI IEVNARLSRS SALASKATGY
PLAYVAAKLA LGIPLPQIKN SVTGVTTACF EPSLDYCVVK IPRWDLAKFN RVSTKIGSSM
KSVGEVMSIG RNFEEAFQKA LRMVDENVNG FDPNIQTVNE DELREPTDKR MFVLAAALRK
GYSIDKLYEL TKIDRWFLEK FKNIIDYHVS LENLKTTSIS LEMLKNAKKI GFSDKQIAAA
IKSTEVAVRK LREEYKIIPS VKQIDTVAAE WPAHTNYLYL TYNGNSHDLD FPGEFIMVLG
SGVYRIGSSV EFDWCAVGCL RELRNQGKNT IMINYNPETV STDYDMSDRL YFEEISFETV
MDIYNIEHPN GVILS
//
