ID J7GNG8_9CUCU Unreviewed; 225 AA.
AC J7GNG8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Carbamoyl-phosphate synthetase 2 {ECO:0000313|EMBL:AFP75519.1};
DE Flags: Fragment;
GN Name=CAD {ECO:0000313|EMBL:AFP75519.1};
OS Lymantor coryli.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Lymantor.
OX NCBI_TaxID=190776 {ECO:0000313|EMBL:AFP75519.1};
RN [1] {ECO:0000313|EMBL:AFP75519.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22852794; DOI=10.1186/1471-2148-12-133;
RA Jordal B.H., Cognato A.I.;
RT "Molecular phylogeny of bark and ambrosia beetles reveals multiple origins
RT of fungus farming during periods of global warming.";
RL BMC Evol. Biol. 12:133-133(2012).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JX264029; AFP75519.1; -; Genomic_DNA.
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 4: Predicted;
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 1..177
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFP75519.1"
FT NON_TER 225
FT /evidence="ECO:0000313|EMBL:AFP75519.1"
SQ SEQUENCE 225 AA; 24434 MW; F28BF2A022746FB8 CRC64;
VYSVKEALSA ADQLGYPVMT RAAFSLGGLG SGFAKTKEEL AVLATQALAH SSQLIVDKSL
KGWKEVEYEV VRDAYDNCIT VCNMENVDPL GIHTGESIVV APSQTLSNRE YNMLRTTAIK
VIRHFGIVGE CNIQYALSPF SEDYYIIEVN ARLSRSSALA SKATGYPLAY VAAKLSLGIA
LPDIKNSVTG NTTACFEPSL DYCVVKIPRW DLHKFSRVST XIGSS
//
