ID B3TDU1_MANSE Unreviewed; 976 AA.
AC B3TDU1;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 48.
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 Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Sphingidae; Sphinginae; Sphingini; Manduca.
OX NCBI_TaxID=7130 {ECO:0000313|EMBL:ABW38974.1};
RN [1] {ECO:0000313|EMBL:ABW38974.1}
RP NUCLEOTIDE SEQUENCE.
RA Regier J.C.;
RT "PCR primers that amplify across Panarthropoda.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; EU032707; ABW38974.1; -; mRNA.
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:ABW38974.1"
FT NON_TER 976
FT /evidence="ECO:0000313|EMBL:ABW38974.1"
SQ SEQUENCE 976 AA; 108565 MW; 99EB5A57DD92AE25 CRC64;
GYPESLTDPS YHAQLLVLTY PLVGNYGVPD EKERDEHGIP RWFESERIWA SALIVGEVST
RACHWRAKRS LGNWLSALGI PGLCDVDTRS LTYRLREGVT LGRIVQGVPP FNPLPPLADP
NSRNLVAEVS TKEAKIFNPN GEVTIVAVDC GLKYNQIRCL IKRNAKVILV PWNHRLDCAE
YDGLFISNGP GDPEMCKNVV DNLXSVLQNK GKIKPIFGIC LGHQLLSTAA GCKTYKTKYG
NRGHNLPCTH SGTGRCFMTS QNHGFAVDTN TLPEDWKVLF TNENDKTNEG IIHKSEPYFS
VQFHPEHTAG PTDLECLFDI FIEAVKSFKQ NVPCVINDMI XKNLKFVPTI HERPKKVLIL
GSGGLXIGQA GEFDYSGSQG VKAMQEEKIQ TVLINPNIAT VQTSKGLADK VYFLPITPEY
VEQVIKAERP TGILLTFGGQ TALNCGVELQ KSKIFEKYNV NVLGTPIQSI VDTEDRKIFA
EKINAIGEKV APSAAVTSVD EALAAAIQIG YPVMARSAFS LGGLGSGFAN NEEELRTLAH
QALSHSDQLI IDKSLKGWKE VEYEVVRDAY DNCITVCNME NVDPLGIHTG ESIVVAPSQT
LSNREYYMLR NTAIKVIRHF GIVGECNIQY ALNPYSEEFY IIEVNARLSR SSALASKATG
YPLAYVAAKL ALGIPLPVIK NSVTGVTTAC FEPSLDYCVV KIPRWDLAKF NRVSTKIGSS
MKSVGEVMSI GRSFEEAFQK ALRMVDENVN GFDPNIKKVN ENDLREPTDK RMFVLAAALK
EGYSVEKLYE LTKIDRWFLE KFKNIIDYYK TLGAYDSGSV TFDILKRAKK IGFSDKQIAA
AIKSTELAVR KLREEYKITP FVKQIDTVAA EWPASTNYLY LTYNGNAHDL NFPGEYVMVL
GSGVYRIGSS VEFDWCAVGC LRELRNQGKN TIMVNYNPET VSTDYDMSDR LYFEEISFEV
VMDIYNIERP SGVILS
//