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Database: UniProt
Entry: D5L6M0_9CUCU
LinkDB: D5L6M0_9CUCU
Original site: D5L6M0_9CUCU 
ID   D5L6M0_9CUCU            Unreviewed;       170 AA.
AC   D5L6M0;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=CAD {ECO:0000313|EMBL:ADF27316.1};
DE   Flags: Fragment;
GN   Name=CAD {ECO:0000313|EMBL:ADF27316.1};
OS   Xylosandrus sp. n. 342 SAD-2010.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Curculionidae; Scolytinae; Xylosandrus.
OX   NCBI_TaxID=748752 {ECO:0000313|EMBL:ADF27316.1};
RN   [1] {ECO:0000313|EMBL:ADF27316.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Xyo342 {ECO:0000313|EMBL:ADF27316.1};
RX   PubMed=19925873; DOI=10.1016/j.ympev.2009.11.011;
RA   Dole S.A., Jordal B.H., Cognato A.I.;
RT   "Polyphyly of Xylosandrus Reitter inferred from nuclear and mitochondrial
RT   genes (Coleoptera: Curculionidae: Scolytinae).";
RL   Mol. Phylogenet. Evol. 54:773-782(2010).
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; GU808647; ADF27316.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5L6M0; -.
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          20..146
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADF27316.1"
FT   NON_TER         170
FT                   /evidence="ECO:0000313|EMBL:ADF27316.1"
SQ   SEQUENCE   170 AA;  18563 MW;  8312F08A0BFAF922 CRC64;
     GFANTNEELT VLATQALAHS SQLVIDKSLK GWKEVEYEVV RDAYDNCITV CNMENVDPLG
     IHTGESIVVA PSQTLSNREY NMLRTTAIKV IRHFGVVGEC NIQYALSPFS EEYYIIEVNA
     RLSRSSALAS KATGYPLAYV AAKLSLGIPL PEIKNSVTGD TTACFEPSLD
//
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