ID   D7GJE7_9DIPT            Unreviewed;       285 AA.
AC   D7GJE7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-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;
GN   Name=cad {ECO:0000313|EMBL:CBL58597.1};
OS   Micropsectra polita.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC   Chironominae; Micropsectra.
OX   NCBI_TaxID=403552 {ECO:0000313|EMBL:CBL58597.1};
RN   [1] {ECO:0000313|EMBL:CBL58597.1}
RP   NUCLEOTIDE SEQUENCE.
RX   DOI=10.1016/j.ympev.2010.06.006;
RA   Ekrem T., Willassen E., Stur E.;
RT   "Phylogenetic utility of five genes for dipteran phylogeny: a test case in
RT   the Chironomidae leads to generic synonymies.";
RL   Mol. Phylogenet. Evol. 57:561-571(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   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC       phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077}.
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   -!- SIMILARITY: Belongs to the CarA family.
CC       {ECO:0000256|ARBA:ARBA00007800}.
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; FN807004; CBL58597.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7GJE7; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
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; IPR006274; CarbamoylP_synth_ssu.
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   NCBIfam; TIGR01368; CPSaseIIsmall; 1.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          1..105
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:CBL58597.1"
FT   NON_TER         285
FT                   /evidence="ECO:0000313|EMBL:CBL58597.1"
SQ   SEQUENCE   285 AA;  31995 MW;  469852C0AE62AABD CRC64;
     VESMTDPSYH GQMLVLTYPL IGNYGVPSDE EFDENNLIKH FESNNKIWVS GLIVGELCET
     PSHWRLKYKL SEWMEKHKIV GISGIDTREL TKKIRENGTI LGKIIQQPTA TFNGLTFKDH
     NERNLVAEVS TKKVVTYNPK GSPRICAVDC GLKLNQIRCF LKRGARVDVV PWDQKLDAQQ
     FDGLFLSNGP GDPVTCSKTV KNIQQVLKTS EKPIFGICLG HQLLSTAIGC KTYKMKYGNR
     GHNLPALHHG TNRCYMTSQN HGFAVDPTSL EDGWEALFTN LNDNS
//