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Database: UniProt
Entry: B9U714_XYLCH
LinkDB: B9U714_XYLCH
Original site: B9U714_XYLCH 
ID   B9U714_XYLCH            Unreviewed;       976 AA.
AC   B9U714;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 49.
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:ACD01549.1};
OS   Xylophanes chiron (Sphinx moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Macroglossinae; Macroglossini; Xylophanes.
OX   NCBI_TaxID=283838 {ECO:0000313|EMBL:ACD01549.1};
RN   [1] {ECO:0000313|EMBL:ACD01549.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AToL-Lep-ID IJK-02-5904 {ECO:0000313|EMBL:ACD01549.1};
RX   PubMed=19492095; DOI=10.1371/journal.pone.0005719;
RA   Kawahara A.Y., Mignault A.A., Regier J.C., Kitching I.J., Mitter C.;
RT   "Phylogeny and biogeography of hawkmoths (Lepidoptera: Sphingidae):
RT   evidence from five nuclear genes.";
RL   PLoS ONE 4:e5719-e5719(2009).
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};
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DR   EMBL; EU479119; ACD01549.1; -; mRNA.
DR   AlphaFoldDB; B9U714; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01744; GATase1_CPSase; 1.
DR   Gene3D; 3.40.50.20; -; 2.
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; IPR006274; CarbamoylP_synth_ssu.
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; IPR035686; CPSase_GATase1.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   NCBIfam; TIGR01368; CPSaseIIsmall; 1.
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; PR00097; ANTSNTHASEII.
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; 2.
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};
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          480..672
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   ACT_SITE        220
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        304
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        306
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACD01549.1"
FT   NON_TER         976
FT                   /evidence="ECO:0000313|EMBL:ACD01549.1"
SQ   SEQUENCE   976 AA;  108349 MW;  8E9CCF027A98DC2D CRC64;
     GYPESLTDPS YHAQLLVLTY PLVGNYGVPD EKERDEHGIP RWFESERIWA SALIVGEVST
     RACHWRAKRS LGAWLSAHGI PGLCDVDTRA LTKRLRDGVT LGRIVQGVPP FGPLPALADP
     NSRNLVAEVT TKETKIFNPK GEVTILAVDC GLKFNQIRCL IKRNAKVILV PWNHKFDPSQ
     YDGLFISNGP GDPDICKEAV DNLKTVLQNK NNVKPIFGIC LGHQLLSTAA GCKTYKTTYG
     NRGHNLPCTH SGTGRCFMTS QNHGFAVDTD TLPAEWKILF TNENDKTNEG IIHETAPFFS
     VQFHPEHTAG PTDLECLFDI FIDAVKSYKN KVSCVIDDMI TERLKYVPTI HERPKKVLIL
     GSGGLSIGQA GEFDYSGSQG VKAMQEEKIQ TVLINPNIAT VQTSKGLADK VYFLPITPEY
     VEQVIKAERP TGVLLTFGGQ TALNCGVELE KSKIFEKYNV NVLGTPIQSI VDTEDRKIFA
     EKINAIGEKV APSAAVTSVD EAIAAAIQIG YPVMARSAFS LGGLGSGFAN NEEELRALAH
     QALSHSDQLI IDKSLKGWKE VEYEVVRDAY DNCITVCNME NVDPLGIHTG ESIVVAPSQT
     LSNREYYMLR NTAIKVIRHF GIVGECNIQY ALNPYSEEFY IIEVNARLSR SSALASKATG
     YPLAYVAAKL ALGIPLPIIK NSVTGVTTAC FEPSLDYCVV KIPRWDLAKF NRVSTKIGSS
     MKSVGEVMSI GRSFEEAFQK ALRMVDENVN GFDPNIKKVN DTDLREPTDK RMFILAAALR
     EGYTVEKLYE LTKIDRWFLE KFKNIIDYYK TLDAYDSGSV TCDVLKRAKK IGFSDKQIAA
     AIKSTELAVR KLREEYKITP FVKQIDTVAA EWPASTNYLY LTYNGSTHDI EFPGELVMVL
     GSGVYRIGSS VEFDWCAVGC LRELRNQGKK TIMVNYNPET VSTDYDMSDR LYFEEISFEV
     VMDIYNIEHP SGVILS
//
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