ID   D9ZHK6_9MUSC            Unreviewed;       282 AA.
AC   D9ZHK6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 32.
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   Toxonevra superba.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC   Pallopteridae; Toxonevra.
OX   NCBI_TaxID=286525 {ECO:0000313|EMBL:ADK93189.1};
RN   [1] {ECO:0000313|EMBL:ADK93189.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20362064; DOI=10.1016/j.ympev.2010.03.026;
RA   Gibson J.F., Skevington J.H., Kelso S.;
RT   "Placement of Conopidae (Diptera) within Schizophora based on mtDNA and
RT   nrDNA gene regions.";
RL   Mol. Phylogenet. Evol. 56:91-103(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC         Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359;
CC         Evidence={ECO:0000256|ARBA:ARBA00043737};
CC   -!- SUBUNIT: Heterodimer composed of 2 chains; the small (or glutamine)
CC       chain promotes the hydrolysis of glutamine to ammonia, which is used by
CC       the large (or ammonia) chain to synthesize carbamoyl phosphate.
CC       {ECO:0000256|ARBA:ARBA00044031}.
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; HM062734; ADK93189.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9ZHK6; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   CDD; cd01744; GATase1_CPSase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR   InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR   InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR035686; CPSase_GATase1.
DR   InterPro; IPR017926; GATASE.
DR   PANTHER; PTHR11405:SF4; CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC SMALL CHAIN; 1.
DR   PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR   Pfam; PF00988; CPSase_sm_chain; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PRINTS; PR00099; CPSGATASE.
DR   PRINTS; PR00096; GATASE.
DR   SMART; SM01097; CPSase_sm_chain; 1.
DR   SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          1..100
FT                   /note="Carbamoyl-phosphate synthase small subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01097"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADK93189.1"
FT   NON_TER         282
FT                   /evidence="ECO:0000313|EMBL:ADK93189.1"
SQ   SEQUENCE   282 AA;  31336 MW;  E5D94D86BB29CF0B CRC64;
     ERSYRAQILV LTYPLIGNYG IPSAKEFDEH GLPKHFEWIE GISVAALVVG EICETPSHWR
     AHETLSKWME SHGVPGISGI DTRALTKKIR EHGTILGRIV YEAPENPKLL TFKDPNSRNL
     VAECSVKEPM IFNASGSPRI CAIDCGLKLN QIKCFVTRGA RVELVPWNHT LDESQFDGLF
     ISNGPGDPVV CKDTVKQIMR VLDNGKKPIF GICLGHQLLS TAIGCRTYKM KYGNRGHNLP
     CIHNGTGRCF MTSQNHGFAV DTTTLPSDWE SLFTNANDNT NE
//