ID G1ERC6_9NEOP Unreviewed; 776 AA.
AC G1ERC6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-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 Gracillariidae gen. 1 sp. ex Schinus terebinthifolius.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Tineoidea;
OC Gracillariidae.
OX NCBI_TaxID=1075135 {ECO:0000313|EMBL:AEM24200.1};
RN [1] {ECO:0000313|EMBL:AEM24200.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21702958; DOI=10.1186/1471-2148-11-182;
RA Kawahara A.Y., Ohshima I., Kawakita A., Regier J.C., Mitter C.,
RA Cummings M.P., Davis D.R., Wagner D.L., De Prins J., Lopez-Vaamonde C.;
RT "Increased gene sampling strengthens support for higher-level groups within
RT leaf-mining moths and relatives (Lepidoptera: Gracillariidae).";
RL BMC Evol. Biol. 11:182-182(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:456216; EC=6.3.5.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001777};
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; JN125069; AEM24200.1; -; mRNA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
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:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00098; CPSASE.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
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; PS00867; CPSASE_2; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 2: Evidence at transcript level;
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 282..474
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEM24200.1"
FT NON_TER 776
FT /evidence="ECO:0000313|EMBL:AEM24200.1"
SQ SEQUENCE 776 AA; 86528 MW; D32FA06FC70B803E CRC64;
GYPESLTDPS YHAQILVLTY PLVGNYGVPD EEEVDQSGLP KWFESNRIWA AGLVVGEVSS
KAWHWRSKQS LGSWLSAHNV PGLHGIDTRS LTRRLREGVS LGRIVQGAPV IADPNIRNLV
AEVSTKETKT FNVNGEVTIL VVDCGLKYNQ IRCLVNRNAK VIVVPWDTPL DQVKYDGLFL
SNGPGDPFVC RKTVENIXKV LKPVFGICLG HQLLSTAAGC KTFKMSYGNR GHNLPCTHND
TGRCFMTGVE LMRLGVLEKY NVSVLGTPIE SIIDTEDRKI FAEKVNYLGE KVAPSAAVSS
VEEAVNAASL IGYPVMARAA FSLGGLGSGF ANNEEELRSL AHQAFSHSDQ LIIDKSLRGW
KEVEYEVVRD AYDNCITVCN MENVDPLGIH TGESIVIAPS QTLSNREYYM LRKTALKVIR
HFGIVGECNI QYALNPHSEE FYIIEVNARL SRSSALASKA TGYPLAYVAA KLSLGIPLPK
IRNSVTGVTT ACFEPSLDYC VVKIPRWDLA KFNRVSTKIG SSMKSVGEVM AIGRNFEEAF
QKALRMVDEN VNGFDPNIKE VNDNELREPT DKRMFVLAAA LKSGYSVDKL YELTKIDHWF
LNKFKNIIDH YKVLENEGAI QVDTLRKSKQ IGFSDKQIAM AIKSTEIAVR KLRESFNIIP
FVKQIDTVAA EWPAMTNYLY LTYNGNQHDI DFPGGYTIVL GSGVYRIGSS VEFDWCAVGC
LRELRQQGRK TIMINYNPET VSTDYDMSDR LYFEEISFEV VMDIYNLENP HGVILS
//