ID D8UZK5_9SCAR Unreviewed; 299 AA.
AC D8UZK5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=carbamoyl-phosphate synthase (ammonia) {ECO:0000256|ARBA:ARBA00044063};
DE EC=6.3.4.16 {ECO:0000256|ARBA:ARBA00044063};
DE Flags: Fragment;
GN Name=CAD {ECO:0000313|EMBL:ADI47186.1};
OS Macroderes amplior.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC Scarabaeidae; Scarabaeinae; Scarabaeinae incertae sedis; Macroderes.
OX NCBI_TaxID=763516 {ECO:0000313|EMBL:ADI47186.1};
RN [1] {ECO:0000313|EMBL:ADI47186.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MARP01 {ECO:0000313|EMBL:ADI47186.1};
RX PubMed=20416384; DOI=10.1016/j.ympev.2010.04.023;
RA Sole C.L., Scholtz C.H.;
RT "Did dung beetles arise in Africa? A phylogenetic hypothesis based on five
RT gene regions.";
RL Mol. Phylogenet. Evol. 56:631-641(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};
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; GQ289978; ADI47186.1; -; 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; 3.40.50.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
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 InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR PANTHER; PTHR11405:SF4; CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC SMALL CHAIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00098; CPSASE.
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; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 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}.
FT DOMAIN 237..291
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADI47186.1"
FT NON_TER 299
FT /evidence="ECO:0000313|EMBL:ADI47186.1"
SQ SEQUENCE 299 AA; 32548 MW; D26EEBBF8FE21AEE CRC64;
PCIHXGTGRC YTTSQNHGFA VNSDKLPADW EVLFYNANDK TNEGIIHKSL PYFSVQFHPE
HTAGPEDLEC LFDIFLEGIR LYASSSTVNI KEKLTKMLQY EPVYKMINDL PRKVLIIGSG
GLSIGQAGEF DYSGSQAIKA LKEENIKTVL INPNIATVQT SKGLADKVYF LPLVPEYVEQ
VIKAERPGGV LLTFGGQTAL NCGVELQRCG VFDRYGVKIL GTPIQAIIDT EDRKIFSERI
AAIGEKVAPS LAAFSVQEAL DAAEKLGYPV MARAAFSLGG LGSGFADNKE ELKLLASQA
//
