ID Q6WVA6_9MUSC Unreviewed; 480 AA.
AC Q6WVA6;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=carbamoyl-phosphate synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012738};
DE EC=6.3.5.5 {ECO:0000256|ARBA:ARBA00012738};
DE Flags: Fragment;
GN Name=CAD {ECO:0000313|EMBL:AAQ54673.1};
OS Chromolepida pruinosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Asiloidea;
OC Therevidae; Therevinae; Chromolepida.
OX NCBI_TaxID=91323 {ECO:0000313|EMBL:AAQ54673.1};
RN [1] {ECO:0000313|EMBL:AAQ54673.1}
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 + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:456216; EC=6.3.5.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001777};
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; AY267605; AAQ54673.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6WVA6; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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: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 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 251..443
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAQ54673.1"
FT NON_TER 480
FT /evidence="ECO:0000313|EMBL:AAQ54673.1"
SQ SEQUENCE 480 AA; 52649 MW; 04EAB81C1F6DAAD8 CRC64;
YKMKYGNRGH NLPCVHHGTG RCFMTSQNHG FAVDTNTLPT DWEPLFTNAN DQTNEGVIHK
SKPYFSVQFH PEHTAGPQDL EVLFDVFLDV VKEHRTNVAS ISVKNKLSER LAYTPVPNSI
PKTKPRKVLI LGSGGLSIGQ AGEFDYSGSQ AIKAMREEKI QTILINPNIA TVQTSKGLAD
KVYFLPLTRD YVEQVIKAER PNGVLLTFGG QTALNCGVEL ERAGIFEKYN VKILGTPIKS
IIETEDRKIF AERVAEIGEK VAPSEAVYSV QEALEAAEKL GYPVMARAAF SLGGLGSGFA
NNKEELISLA QQALPHSHQL IIDKSLKGWK EVEYEVVRDA YDNCITVCNM ENLDPLGIHT
GESIVVAPSQ TLSNREYNLL RTTAINVIRH FGVVGECNIQ YALNPLSEEY YIIEVNARLS
RSSALASKAT GYPLAYVAAK LSLGIPLPDI KNSVTGVTTA CFEPSLDYCV VKIPSVGFGQ
//