ID L8AAI1_9CUCU Unreviewed; 316 AA.
AC L8AAI1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:AGE44352.1};
OS Clypastraea fasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Coccinelloidea; Corylophidae; Clypastraea.
OX NCBI_TaxID=764616 {ECO:0000313|EMBL:AGE44352.1};
RN [1] {ECO:0000313|EMBL:AGE44352.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CO603 {ECO:0000313|EMBL:AGE44352.1};
RA Robertson J.A., Slipinski A., Hiatt K., Miller K.B., Whiting M.F.,
RA McHugh J.V.;
RT "Molecules, morphology, and minute hooded beetles: a phylogenetic study
RT with implications for the evolution and classification of Corylophidae
RT (Coleoptera: Cucujoidea).";
RL Syst. Entomol. 38:209-232(2013).
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; JX845061; AGE44352.1; -; Genomic_DNA.
DR AlphaFoldDB; L8AAI1; -.
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:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
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};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 237..314
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT ACT_SITE 1
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 57
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 59
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AGE44352.1"
FT NON_TER 316
FT /evidence="ECO:0000313|EMBL:AGE44352.1"
SQ SEQUENCE 316 AA; 34528 MW; 763E6C6A2FA0DEB0 CRC64;
CVHATTGRCY MTSQNHGFAI DSNSIPEDWS VFFTNANDGT NEGLIHKKLP FFTVQFHPEH
MAGPEDLEGL FDVYLDCVQR WTVGDKVVVS NLVDEKLRFV NKNPLVEAQR PKKVLIIGSG
GLSIGQAGEF DYSGSQAIKA LKEENIQTVL INPNIATVQT SRGLADKVYF LPLLPEYVEQ
VIRSERPDGV LLTFGGQTGL NCGVELEKAG IFAKYNTRVL GTPIQAIIDT EDRKVFSEKI
HEIGEKVAPS LAAHSVEEAL QAAEQLGYPV MARAAFSLGG LGSGFANTKE ELKVLAQQAL
AHSSQLIIDK SLKGWK
//
