ID G9FV06_9HYME Unreviewed; 317 AA.
AC G9FV06;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 34.
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. ALW-2011.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Ichneumonoidea; Braconidae;
OC Doryctinae; Heterospilus.
OX NCBI_TaxID=1115622 {ECO:0000313|EMBL:AET80323.1};
RN [1] {ECO:0000313|EMBL:AET80323.1}
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JN212530; AET80323.1; -; Genomic_DNA.
DR AlphaFoldDB; G9FV06; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
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};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 225..313
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT ACT_SITE 1
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 49
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 51
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AET80323.1"
FT NON_TER 317
FT /evidence="ECO:0000313|EMBL:AET80323.1"
SQ SEQUENCE 317 AA; 34791 MW; E30A5E1E93314215 CRC64;
CYMTSQNHGF AIDAKDLPTG WEALFTNAND GSNEGIVHTS LPYFSVQFHP EHTAGPEDLE
CLFDVFLETV KEKVNVNIKE KLIKKLEYIP VNPDAIKRPK KVLILGSGGL SIGQAGEFDY
SGSQAIKALK EEHIQTVLIN PNIATVQTSK GMADKVYFLP IIPEYVEQVI RSERPDGVLL
TFGGQTALNC GVELERAGTF AKYGVKILGT PIKSIIETED RKLFSDHISN IKEKVAPSAA
VYSIQEALDA AEKLGYPVMA RAAFSLGGLG SGFANTREEL RTLAQQALAH SSQLIIDKSL
KGWKEVEYEV VRDAYDN
//