ID B9U6Y1_9NEOP Unreviewed; 731 AA.
AC B9U6Y1;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 39.
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:ACD01516.1};
OS Oryba kadeni.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Sphingidae; Macroglossinae; Dilophonotini; Oryba.
OX NCBI_TaxID=354545 {ECO:0000313|EMBL:ACD01516.1};
RN [1] {ECO:0000313|EMBL:ACD01516.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AToL-Lep-ID DHJ-04-55866 {ECO:0000313|EMBL:ACD01516.1};
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};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
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DR EMBL; EU479086; ACD01516.1; -; mRNA.
DR AlphaFoldDB; B9U6Y1; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
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; 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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
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; PF00117; GATase; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 235..427
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACD01516.1"
FT NON_TER 731
FT /evidence="ECO:0000313|EMBL:ACD01516.1"
SQ SEQUENCE 731 AA; 81279 MW; 9EEE525FF43A7B03 CRC64;
LPCTHSGTGR CFMTSQNHGF AVDTNSLPAD WKILFTNEND KTNEGIIHKS APFFSVQFHP
EHTAGPADLE CLFDIFIDAV KSYKTKAACV IDDMITEKLK YVPTIHERPK KVLILGSGGL
SIGQAGEFDY SGSQGVKAMQ EEKIQTVLIN PNIATVQTSK GLADKVYFLP ITPEYVEQVI
KAERPTGILL TFGGQTALNC GVELQKSKIF EKYNVNVLGT PIQSIVDTED RKIFAEKINA
IGEKVAPSAA VTSVDEALAA AIQIGYPVMA RSAFSLGGMG SGFANNEEEL KTLAHQALSH
SDQLIIDKSL KGWKEVEYEV VRDAYDNCIT VCNMENVDPL GIHTGESIVV APSQTLSNRE
YYMLRNTAIK VIRHFGIVGE CNIQYALNPY SEEFYIIEVN ARLSRSSALA SKATGYPLAY
VAAKLALGIP LPIIKNSVTG VTTACFEPSL DYCVVKIPRW DLAKFNRVST KIGSSMKSVG
EVMSIGRSFE EAFQKALRMV DENVNGFDPN IKKVNENDLR EPTDKRMFVL AAALREGYSV
EKLYELTKID RWFLEKFKNI IDYYQTLDAY DSGSVTFDIL KRAKKIGFSD KQIAAAIKST
ELAVRKLREE YKITPFVKQI DTVAAEWPAS TNYLYLTYNG STHDLDFPGE FVMVLGSGVY
RIGSSVEFDW CAVGCLRELR NQGKNTIMIN YNPETVSTDY DMSDRLYFEE ISFEVVMDIY
NIEHPSGVIL S
//