ID C9D9D4_9NEOP Unreviewed; 669 AA.
AC C9D9D4;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Putative CAD trifunctional protein {ECO:0000313|EMBL:ACV89282.1};
DE Flags: Fragment;
GN Name=CAD {ECO:0000313|EMBL:ACV89282.1};
OS Austroneurorthus brunneipennis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Neuroptera; Nevrorthiformia; Nevrorthidae;
OC Austroneurorthus.
OX NCBI_TaxID=560892 {ECO:0000313|EMBL:ACV89282.1};
RN [1] {ECO:0000313|EMBL:ACV89282.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19552814; DOI=10.1186/1741-7007-7-34;
RA Wiegmann B.M., Trautwein M.D., Kim J.W., Cassel B.K., Bertone M.A.,
RA Winterton S.L., Yeates D.K.;
RT "Single-copy nuclear genes resolve the phylogeny of the holometabolous
RT insects.";
RL BMC Biol. 7:34-34(2009).
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};
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; GQ265600; ACV89282.1; -; mRNA.
DR AlphaFoldDB; C9D9D4; -.
DR MEROPS; C26.956; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
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}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT DOMAIN 185..377
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACV89282.1"
FT NON_TER 669
FT /evidence="ECO:0000313|EMBL:ACV89282.1"
SQ SEQUENCE 669 AA; 74664 MW; 578822A041197FEA CRC64;
DATSLPENWE ILFTNANDTT NEGIIHSKLP YFSVQFHPEH TAGPQDLECL FDIFLDTVPK
KVLIIGSGGL SIGQAGEFDY SGSQAIKALK EEGIQTVLIN PNIATVQTSK GLADKVYFLP
LVPEYVEEVI RSERPSGVLL TFGGQTALNC GVELDKANVF EKYGCKILGT PIQSIIQTED
RKIFAERISE IGEKVAPSVA VDCVDEALEA AEKLGYPVMA RAAFSLGGLG SGFADNKEEL
KTLAIQALAH SSQLIIDKSL RGWKEVEYEV DRDAYDNCIT VCNMENVDPL GIHTGESIVV
APSQTLCNKE YNMLRSTAIN VIRHFGIVGE CNIQYALNPH SEQYYIIEVN ARLSRSSALA
SKATGYPLAY VAAKLALGIP LPDIRNSVTG ETTACFEPSL DYCVVKIPRW DLSKFTRVST
KIGSSMKSVG EVMAIGRKFE EAFQKALRMV DENVMGFDPS IKNLNDKDLE EPTDKRMFVL
AASLKAGYTV DRLYDLTKID RWFLHKMKKI IDFNIFLENL DQHDLTKDIL LYAKRYGFSD
KQIATAVKST ELSVRKQREE SRIVPFVKQI DTVAAEWPAN TNYLYLTYNA SSHDLEFPQG
YVMVIGSGVY RIGSSVEFDW CAVGCLRELR NLNKKTIMVN YNPETVSTDY DMCDRLYFEE
ISFEVVMDI
//
