ID Q6WV96_9MUSC Unreviewed; 512 AA.
AC Q6WV96;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Carbamoylphosphate synthetase {ECO:0000313|EMBL:AAQ54683.1};
DE Flags: Fragment;
GN Name=CAD {ECO:0000313|EMBL:AAQ54683.1};
OS Penniverpa sp. MEI 090271.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Asiloidea;
OC Therevidae; Therevinae; Penniverpa.
OX NCBI_TaxID=95073 {ECO:0000313|EMBL:AAQ54683.1};
RN [1] {ECO:0000313|EMBL:AAQ54683.1}
RP NUCLEOTIDE SEQUENCE.
RA Hill H.N., Wiegmann B.M.;
RT "Investigation of the phylogenetic utility of two new nuclear genes: opsin
RT and CAD within the stiletto flies (Diptera: Therevidae).";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
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; AY267615; AAQ54683.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6WV96; -.
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:SF5; CAD PROTEIN; 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 PRINTS; PR00099; CPSGATASE.
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; 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};
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}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT DOMAIN 253..445
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 73
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 75
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAQ54683.1"
FT NON_TER 512
FT /evidence="ECO:0000313|EMBL:AAQ54683.1"
SQ SEQUENCE 512 AA; 56766 MW; 721FF3CC7E507EF5 CRC64;
CKTYKMKYGN RGHNLPCVHH GTGRCFMTSQ NHGFAVDTNT LPPNWEPLFT NANDQTNEGI
IHQSKPYFSV QFHPEHTAGP QDLELLFDVF LDIVKEHKTH TTSTSVRNKL IERLSYAPAN
NSIPTTKPRK VLFRIWRLSI GQAGEFDYSG SQAIKAMREE KIQTILINPN IATVQTSKGL
ADKVYFLPLT RDYVEQVIKA ERPNGVLLTF GGQTALNCGV ELERAGIFKK YNVKILGTPI
KSIIETEDRK IFAERVAEIG EKVAPSEAVY SVQEALDAAD RLGYPVMARA AFSLGGLGSG
FANSKEELVS LAEQALPHSH QLIIDKSLKG WKEVEYEVVR DAYDNCITVC NMENLDPLGI
HTGESIVVAP SQTLSNREYN LLRTTAINVI RHFGVVGECN IQYALNPLSE EYYIIEVNAR
LSRSSALASK ATGYPLAYVA AKLSLGIPLP DIKNSVTGVT TACFEPSLDY CVVKIPRWDL
AKFTRVSKNI GSSMKSVGEV MAIGRNFEEA FK
//
