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
//