ID F5BGI3_9CUCU Unreviewed; 225 AA.
AC F5BGI3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Carbamoyl-phosphate synthetase 2 {ECO:0000313|EMBL:AEB32276.1};
DE Flags: Fragment;
GN Name=CAD {ECO:0000313|EMBL:AEB32276.1};
OS Campyloscelina gen. sp. B BHJ-2011.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Baridinae.
OX NCBI_TaxID=1002086 {ECO:0000313|EMBL:AEB32276.1};
RN [1] {ECO:0000313|EMBL:AEB32276.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21435394; DOI=10.1016/j.ympev.2011.03.016;
RA Jordal B.H., Sequeira A.S., Cognato A.I.;
RT "The age and phylogeny of wood boring weevils and the origin of
RT subsociality.";
RL Mol. Phylogenet. Evol. 59:708-724(2011).
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; HQ883769; AEB32276.1; -; Genomic_DNA.
DR AlphaFoldDB; F5BGI3; -.
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:AEB32276.1"
FT NON_TER 225
FT /evidence="ECO:0000313|EMBL:AEB32276.1"
SQ SEQUENCE 225 AA; 24469 MW; 3C06AD068FCCC265 CRC64;
VYSVEEALAA AEELGYPVMA RAAFSLGGLG SGFANTAKEL KVLANQALAH SNQLIIDKSL
KGWKEVEYEV VRDAFDNCIT VCNMENVDPL GIHTGESIVV APSQTLSNKE YNMLRTTALK
VIRHFGVIGE CNIQYALNPH SEEYYIIEVN ARLSRSSALA SKATGYPLAY VAAKLALAIP
LPQLKNSVTG VTTACFEPSL DYCVVKIPRW DLHKFSRVST KIGSS
//
