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Database: UniProt
Entry: Q6WVA6_9MUSC
LinkDB: Q6WVA6_9MUSC
Original site: Q6WVA6_9MUSC 
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
//
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