ID A1E3Z2_9MUSC Unreviewed; 233 AA.
AC A1E3Z2;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 47.
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:ABL07745.1};
OS Chromatomyia scolopendri.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Opomyzoidea;
OC Agromyzidae; Phytomyzinae; Chromatomyia.
OX NCBI_TaxID=414264 {ECO:0000313|EMBL:ABL07745.1};
RN [1] {ECO:0000313|EMBL:ABL07745.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17291785; DOI=10.1016/j.ympev.2006.12.018;
RA Scheffer S.J., Winkler I.S., Wiegmann B.M.;
RT "Phylogenetic relationships within the leaf-mining flies (Diptera:
RT Agromyzidae) inferred from sequence data from multiple genes.";
RL Mol. Phylogenet. Evol. 42:756-775(2007).
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; EF104780; ABL07745.1; -; Genomic_DNA.
DR AlphaFoldDB; A1E3Z2; -.
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; 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..93
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:ABL07745.1"
FT NON_TER 233
FT /evidence="ECO:0000313|EMBL:ABL07745.1"
SQ SEQUENCE 233 AA; 26068 MW; B487219F969B7825 CRC64;
ILVLTYPLIG NYGIPSIKEI DEYGMPKHFE WFENISVSAL IVGEVCEKPS HWRAQETLSM
WMSKHNVPGI SGIDTRALTK KIRENGTILG RITYEKPTNI QNLQINDPNT RNLVAECSVT
TPKIFNAEGS PRICAIDCGL KLNQIKCFLA RGARVELVPW NYRLDESQFD GLFISNGPGN
PVVCKDVVTQ IRQILKNGKK PIFGICLGHQ LLATAIGCQT YKMKYGNRGH NLP
//