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Database: UniProt
Entry: B3TDU1_MANSE
LinkDB: B3TDU1_MANSE
Original site: B3TDU1_MANSE 
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
//
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