ID G8D1R7_9DIPT Unreviewed; 268 AA.
AC G8D1R7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:AEQ62204.1};
OS Thalassomyia frauenfeldi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Thalassomyia.
OX NCBI_TaxID=903472 {ECO:0000313|EMBL:AEQ62204.1};
RN [1] {ECO:0000313|EMBL:AEQ62204.1}
RP NUCLEOTIDE SEQUENCE.
RA Cranston P.S., Hardy N.B., Morse G.E.;
RT "A dated molecular phylogeny for the Chironomidae (Diptera).";
RL Syst. Entomol. 37:172-188(2012).
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; HQ440385; AEQ62204.1; -; Genomic_DNA.
DR AlphaFoldDB; G8D1R7; -.
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; PR00097; ANTSNTHASEII.
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..95
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:AEQ62204.1"
FT NON_TER 268
FT /evidence="ECO:0000313|EMBL:AEQ62204.1"
SQ SEQUENCE 268 AA; 30277 MW; BC71D14305E5671C CRC64;
HGQILVLTYP LIGNYGIPEE EFDENELSKY FESNHKIWTS GLVVGELCEV PSHWRQKYTL
EEWMIKHNIP GISGIDTRAL TKRIRENGTV LGKIILQDNG PFLELEFKDQ NMRNLVNEVS
VKKPITYNSS GSPRICAIDC GLKLNQIRCF LKRGARVDVV PWDFELNGKN FDGLFISNGP
GDPVMCQKTV KNIQCLMKSP DAKPIFGICL GHQLLSTAIG CKTYKMKYGN RGHNLPCVHH
GTNRCFMTSQ NHGFAVDVSK IDSHWEAL
//
