ID C6F5J6_9NEOP Unreviewed; 712 AA.
AC C6F5J6;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Carbamoyl-phosphate synthase {ECO:0000313|EMBL:ACK86523.1};
DE Flags: Fragment;
GN Name=CAD {ECO:0000313|EMBL:ACK86523.1};
OS Oliarces clara.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Neuroptera; Hemerobiiformia; Ithonidae; Oliarces.
OX NCBI_TaxID=63945 {ECO:0000313|EMBL:ACK86523.1};
RN [1] {ECO:0000313|EMBL:ACK86523.1}
RP NUCLEOTIDE SEQUENCE.
RA Winterton S.L., Hardy N.B., Wiegmann B.M.;
RT "On wings of lace: phylogeny and Bayesian divergence time estimates of
RT Neuropterida (Insecta) based on morphological and molecular data.";
RL Syst. Entomol. 35:349-378(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}.
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; EU860138; ACK86523.1; -; Genomic_DNA.
DR AlphaFoldDB; C6F5J6; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
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:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
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; 2.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00867; CPSASE_2; 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}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT DOMAIN 230..421
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACK86523.1"
FT NON_TER 712
FT /evidence="ECO:0000313|EMBL:ACK86523.1"
SQ SEQUENCE 712 AA; 79419 MW; B38E2ED9B54573FC CRC64;
YRCYMTSQNH GFAVDTESIP SDWEPLFTNA NDKTNEGIIH KTLPYFSVQF HPEHTAGPED
LECLFDVFLS SVRNSIDNKN VSIKELLIVH LNYKPNHSIS IDIPKKVLII GSGGLSIGQA
GEFDYSGSQA IKALKEENIQ TVLINPNIAT VQTSKGLADK VYFLPLVPEY VEQVIRSERP
GGVLLTFGGQ TALNCGVELE KAGIFEKYGC KILGTPIQSI IETEDRKMFT EKINEIGEKV
APSAAVYSVE EALNAAEKIG YPVMARAAFS LGGLGSGFAH NQEQLKCLAI QALAHSNQLI
MTITKGWKEV EYEVVRDAFD NCVTVCNMEN VDPLGIHTGE SIVVAPSQTL SNREYNMLRT
TAINVIRHFG VIGECNIQYA LNPHSEEYYI IEVNARLSRS SALASKATGY PLAYVAAKLA
LGAALPNIKN SVTGETTACF EPSLDYCVVK IPRWDLSKFS RVSSKIGSSM KSVGEVMAIG
RKFEEAFQKA LRMVDENVMG FDPDLQQISD EDLQEPTDKR MFVIAASLKN EYSIDHLYEL
TKIDRWFLQK MKNIIDLQNM LEKLDQHAVS REILLQAKRF GFSDKQIASV VKSTELAVRK
HREETGILPF VKQIDTVAAE WPASTNYLYL TYNASSHDIE FPGGYTIVIG SGVYRIGSSV
EFDWCAVGCL RELRKLNKKT IMVNYNPETV STDYDMCDRL YFEEISFEVV MD
//
