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Database: UniProt
Entry: C6F5H1_9NEOP
LinkDB: C6F5H1_9NEOP
Original site: C6F5H1_9NEOP 
ID   C6F5H1_9NEOP            Unreviewed;       467 AA.
AC   C6F5H1;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 41.
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:ACK86498.1};
OS   Drepanepteryx phalaenoides.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Neuroptera; Hemerobiiformia; Hemerobiidae;
OC   Drepanepteryx.
OX   NCBI_TaxID=560898 {ECO:0000313|EMBL:ACK86498.1};
RN   [1] {ECO:0000313|EMBL:ACK86498.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Winterton S.L., Hardy N.B., Wiegmann B.M.;
RT   "On wings of lace: phylogeny and Bayesian divergence time estimates of
RT   Neuropterida (Insecta) based on morphological and molecular data.";
RL   Syst. Entomol. 35:349-378(2010).
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; EU860113; ACK86498.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6F5H1; -.
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          227..419
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACK86498.1"
FT   NON_TER         467
FT                   /evidence="ECO:0000313|EMBL:ACK86498.1"
SQ   SEQUENCE   467 AA;  50943 MW;  849642A66D9310E1 CRC64;
     KRCYMTSQNH GYAVNVDTLT PDFEPLFTNA NDGTNEGIIH KTLPFFSVQF HPEHTAGPAD
     LECLFDIFID QCKSQSSKSV RTRLTDQLTY IPEIPIKIDI PKKVLIIGSG GLSIGQAGEF
     DYSGSQAIKA LKEHNIQTVL INPNIATVQT SKGLADKVYF LPLIPEYVEQ VIRSERPGGV
     LLTFGGQTAL NCGVELEKAN VFAKYGCKIL GTPIQSIIDT EDRRIFANRV LEIGEHVAPS
     DAVYSVEEAL AAAEVIGYPV MARAAFSLGG LGSGFANNKE ELIALANQAF ANSTQLIIDK
     SLKGWKEVEY EVVRDAFDNC ITVCNMENVD PLGIHTGESI VVAPSQTLSN REYNMLRTTA
     INVIRHFGVV GECNIQYALS PHSEEYYIIE VNARLSRSSA LASKATGYPL AYVAAKLALG
     ISLVNIKNSV TGETTACFEP SLDYCVVKIP RWDLSKFSRV STKIGSS
//
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