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Database: UniProt
Entry: G9FV22_9HYME
LinkDB: G9FV22_9HYME
Original site: G9FV22_9HYME 
ID   G9FV22_9HYME            Unreviewed;       318 AA.
AC   G9FV22;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=carbamoyl-phosphate synthase (ammonia) {ECO:0000256|ARBA:ARBA00044063};
DE            EC=6.3.4.16 {ECO:0000256|ARBA:ARBA00044063};
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:AET80339.1};
RN   [1] {ECO:0000313|EMBL:AET80339.1}
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 + 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; JN212546; AET80339.1; -; Genomic_DNA.
DR   AlphaFoldDB; G9FV22; -.
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:SF4; CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC SMALL CHAIN; 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          226..314
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AET80339.1"
FT   NON_TER         318
FT                   /evidence="ECO:0000313|EMBL:AET80339.1"
SQ   SEQUENCE   318 AA;  34996 MW;  D06AC1C887E1DF0B CRC64;
     RCYMTSQNHG FAIDAKDLPE GWEALFTNAN DESNEGIIHT SLPYFSVQFH PEHTAGPEDL
     ECLFDVFLEA VREKVSVGLK ERLIKRLEYI PVNPEAIKRP RKVLILGSGG LSIGQAGEFD
     YSGSQAIKAL KEESIQTVLI NPNIATVQTS KGMADKVYFL PIIPEYVEQV IRSERPDGVL
     LTFGGQTALN CGVELEKAGT FAKYGVKILG TPIKSIIETE DRKLFSDHIS NIEEKVAPSA
     AVYSIQEALD AAEKLGYPVM ARAAFSLGGL GSGFANTREE LRTLAQQALA HSSQLIIDKS
     LKGWKEVEYE VVRDAYDN
//
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