ID D9ZHJ9_9MUSC Unreviewed; 372 AA.
AC D9ZHJ9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=CAD {ECO:0000313|EMBL:ADK93182.1};
DE Flags: Fragment;
OS Minettia lupulina.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Lauxanioidea;
OC Lauxaniidae; Minettia.
OX NCBI_TaxID=768769 {ECO:0000313|EMBL:ADK93182.1};
RN [1] {ECO:0000313|EMBL:ADK93182.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20362064; DOI=10.1016/j.ympev.2010.03.026;
RA Gibson J.F., Skevington J.H., Kelso S.;
RT "Placement of Conopidae (Diptera) within Schizophora based on mtDNA and
RT nrDNA gene regions.";
RL Mol. Phylogenet. Evol. 56:91-103(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 ---------------------------------------------------------------------------
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; HM062729; ADK93182.1; -; Genomic_DNA.
DR AlphaFoldDB; D9ZHJ9; -.
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; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 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; IPR013815; ATP_grasp_subdomain_1.
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; 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 PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 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; PS00866; CPSASE_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};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 257..345
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADK93182.1"
FT NON_TER 372
FT /evidence="ECO:0000313|EMBL:ADK93182.1"
SQ SEQUENCE 372 AA; 41856 MW; F2A8416E2DE397D6 CRC64;
HSVNNEELTQ PTDKRPFVLA AALRALYTVD ELHRLTQIDK WFLNKMKNII EFYFILEKSG
NTLTCEQILQ AKQIGFSDKQ IASAIRSTEL AVRKQRQEFG LIPFVKQIDT VAGEWPATTN
YLYTTYNAIE HDIQFPGGFT IVVGSGVYRI GSSVEFDWCA VGCLRELRNL GKSTIMINYN
PETVSTDYDM CDRLYFEEIS FEVVMDIYEL ERSDGIILSM GGQLPNNIAM DLHRQQARVL
GTSPESIDSA ENRFKFSRML DRKGILQPRW KELTNLQSAI EFCEEVGYPC LVRPSYVLSG
AAMNVAYSNQ DLETYLNAAS LVSKEHPVVI SKFLTEAKEI DVDAVAADGE ILCMAVSEHV
ENAGVHSGDA TL
//
