ID B9U6V8_9NEOP Unreviewed; 975 AA.
AC B9U6V8;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=carbamoyl-phosphate synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012738};
DE EC=6.3.5.5 {ECO:0000256|ARBA:ARBA00012738};
DE Flags: Fragment;
GN Name=CAD {ECO:0000313|EMBL:ACD01493.1};
OS Hemeroplanes ornatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Sphingidae; Macroglossinae; Dilophonotini; Hemeroplanes.
OX NCBI_TaxID=354539 {ECO:0000313|EMBL:ACD01493.1};
RN [1] {ECO:0000313|EMBL:ACD01493.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AToL-Lep-ID AYK-04-0003 {ECO:0000313|EMBL:ACD01493.1};
RX PubMed=19492095; DOI=10.1371/journal.pone.0005719;
RA Kawahara A.Y., Mignault A.A., Regier J.C., Kitching I.J., Mitter C.;
RT "Phylogeny and biogeography of hawkmoths (Lepidoptera: Sphingidae):
RT evidence from five nuclear genes.";
RL PLoS ONE 4:e5719-e5719(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:456216; EC=6.3.5.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001777};
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DR EMBL; EU479063; ACD01493.1; -; mRNA.
DR AlphaFoldDB; B9U6V8; -.
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}.
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:ACD01493.1"
FT NON_TER 975
FT /evidence="ECO:0000313|EMBL:ACD01493.1"
SQ SEQUENCE 975 AA; 108234 MW; 25E1973EA456665E CRC64;
GYPESLTDPS YHAQLLVLTY PLVGNYGVPD ETERDEHGIP RWFESERIWA SALIVGEVST
RACHWRAKRS LGAWLSAHGI PGLCDVDTRA LTYRLREGVT LGRIIQGVPP FDPLPPLADP
NFRNLVAEVS TKETKIFNPS GEITILAVDC GLKYNQIRCL IKRNAKVILV PWDHKLDPNQ
YDGLFISNGP GDPVVCKNVV DNLTAVLQNK NVKPVFGICL GHQLLSTAAG CKTYKTTYGN
RGHNLPCTHS GTGRCFMTSQ NHGFAVDTNT LPADWKILFT NENDKTNEGI IHKTAPFFSV
QFHPEHTAGP ADLECLFDIF IDAVKSYKNK ESCVIDDIIT QKLKYVPTIH ERPKKVLILG
SGGLSIGQAG EFDYSGSQGV KAMQEEKIQT VLINPNIATV QTSKGLADKV YFLPITPEYV
EQVIKAERPT GILLTFGGQT ALNCGVELQK SRIFEKYNVN VLGTPIQSIV DTEDRKIFAE
KINAIGEKVA PSAAVTSVDE ALTAAIQIGY PVMARSAFSL GGLGSGFANN EDELRALAHQ
ALSHSDQLII DKSLKGWKEV EYEVVRDAYD NCITVCNMEN VDPLGIHTGE SIVVAPSQTL
SNREYYMLRN TAIKVIRHFG IVGECNIQYA LNPNSEEFYI IEVNARLSRS SALASKATGY
PLAYVAAKLA LGIPLPVIKN SVTGVTTACF EPSLDYCVVK IPRWDLAKFN RVSTKIGSSM
KSVGEVMSIG RSFEEAFQKA LRMVDENVNG FDPNIKKVNE NDLREPTDKR MFVLAAALKE
GYSVEKLYEL TKIDQWFLEK FKNIIDYYKT LDAYDSGSVT FDILKRAKKI GFSDKQIAAA
IKSTELAVRK LREEYKITPF VKQIDTVAAE WPASTNYLYL TYNGSTHDLD FPGEFVMVLG
SGVYRIGSSV EFDWCAVGCL RELRNQGKNT IMVNYNPETV STDYDMSDRL YFEEISFEVV
MDIYNIEHPS GVILS
//