ID C9D9D9_9HYME Unreviewed; 189 AA.
AC C9D9D9;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Putative CAD trifunctional protein {ECO:0000313|EMBL:ACV89287.1};
DE Flags: Fragment;
GN Name=CAD {ECO:0000313|EMBL:ACV89287.1};
OS Muscidifurax raptorellus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Muscidifurax.
OX NCBI_TaxID=51938 {ECO:0000313|EMBL:ACV89287.1};
RN [1] {ECO:0000313|EMBL:ACV89287.1}
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};
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DR EMBL; GQ265605; ACV89287.1; -; mRNA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR PRINTS; PR00098; CPSASE.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00867; CPSASE_2; 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 18..185
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACV89287.1"
FT NON_TER 189
FT /evidence="ECO:0000313|EMBL:ACV89287.1"
SQ SEQUENCE 189 AA; 20724 MW; F1CD90816CF7D8B9 CRC64;
LGTPIESIIE TEDRKLFADR VNEIDEKVAP SCAVYSIQEA LEAAEKLGYP VMARAAFSLG
GLGSGFANTT DELKALAQQA LGHSSQLIID KSLQGWKQIX YEVVRDAYDN CITVCNMENV
DPLGIHXGET IVVAPSQTLS NREDNMLRTT AIKVIRHXGV VGECNIQYAL NPFSEECYII
EVNARLSRS
//