ID Q6WVA2_9MUSC Unreviewed; 455 AA.
AC Q6WVA2;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Carbamoylphosphate synthetase {ECO:0000313|EMBL:AAQ54677.1};
DE Flags: Fragment;
GN Name=CAD {ECO:0000313|EMBL:AAQ54677.1};
OS Henicomyia hubbardi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Asiloidea;
OC Therevidae; Xestomyzinae; Henicomyia.
OX NCBI_TaxID=95063 {ECO:0000313|EMBL:AAQ54677.1};
RN [1] {ECO:0000313|EMBL:AAQ54677.1}
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};
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; AY267609; AAQ54677.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6WVA2; -.
DR MEROPS; C26.956; -.
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: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}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT DOMAIN 228..420
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAQ54677.1"
FT NON_TER 455
FT /evidence="ECO:0000313|EMBL:AAQ54677.1"
SQ SEQUENCE 455 AA; 49709 MW; AD9E44E1DC796032 CRC64;
TSQNHGFAVD SNTLPTGWEP LFTNANDNTN EGIIHKEKPY FSVQFHPEHT AGPQDLELLF
DVFLETVKEH RINPSPSVSV KDRLIAALSY SLKEGSIPEV KPRKVLILGS GGLSIGQAGE
FDYSGSQAIK AMREEKIQTI LINPNIATVQ TSKGLADKVY FLPLTREYVE QVIKAERPNG
VLLTFGGQTA LNCGVELERA GIFSKYNVKI LGTPITSIIE TEDRKIFAER VAEIGEKVAP
SEAVYSVQAA LDAAGRLGYP VMARAAFSLG GLGSGFASDE EELKNLAQQA LAHSNQLVID
KSLKGWKEVE YEVVRDAYDN CITVCNMENL DPLGIHTGES IVVAPSQTLS NREYNLLRTT
AIKVIRHFGV VGECNIQYAL NPESEEYYII EVNARLSRSS ALASKATGYP LAYVAAKLSL
GVPLPKIKNS VTGVTTACFE PSLDYCVVKI PRWDL
//
