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Database: UniProt
Entry: G9FV33_9HYME
LinkDB: G9FV33_9HYME
Original site: G9FV33_9HYME 
ID   G9FV33_9HYME            Unreviewed;       319 AA.
AC   G9FV33;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 31.
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;
OS   Heterospilus sp. ST34.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Ichneumonoidea; Braconidae;
OC   Doryctinae; Heterospilus.
OX   NCBI_TaxID=1096503 {ECO:0000313|EMBL:AET80350.1};
RN   [1] {ECO:0000313|EMBL:AET80350.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wild A.L., Marsh P.M., Whitfield J.B.;
RT   "The most useful taxonomic characters in Neotropical Heterospilus wasps
RT   evolve quickly.";
RL   Submitted (JUN-2011) 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; JN212557; AET80350.1; -; Genomic_DNA.
DR   AlphaFoldDB; G9FV33; -.
DR   MEROPS; C26.956; -.
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; 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..315
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AET80350.1"
FT   NON_TER         319
FT                   /evidence="ECO:0000313|EMBL:AET80350.1"
SQ   SEQUENCE   319 AA;  35078 MW;  D42DE543CAAC7568 CRC64;
     RCYMTSQNHG FAIDAQDLPQ GWEALFTNAN DESNEGIVHT SLPYFSVQFH PEHTAGPEDL
     ECLFDVFLEA VSHTKEKVNI KERLIERLKY IPANPEAIKR PKKVLILGSG GLSIGQAGEF
     DYSGSQAIKA LKEESIQTVL INPNIATVQT SKGMADKVYF LPIIPEYVEQ VIRSERPDGV
     LLTFGGQTAL NCGVELERAG TFAKYGVKIL GTPIKSIIET EDRKLFSDHI SEIAEKVAPS
     AAVYSIQEAL DAAEKLGYPV MARAAFSLGG LGSGFANTRE ELRTLAQQAL AHSSQLIIDK
     SLKGWKEVEY EVVRDAYDN
//
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