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Database: UniProt
Entry: G1ERC6_9NEOP
LinkDB: G1ERC6_9NEOP
Original site: G1ERC6_9NEOP 
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
//
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