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Database: UniProt
Entry: E7D8B6_9NEOP
LinkDB: E7D8B6_9NEOP
Original site: E7D8B6_9NEOP 
ID   E7D8B6_9NEOP            Unreviewed;       526 AA.
AC   E7D8B6;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 28.
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:ADU34093.1};
OS   Pseudopontia mabira.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Pieridae; Pseudopontiinae; Pseudopontia.
OX   NCBI_TaxID=940168 {ECO:0000313|EMBL:ADU34093.1};
RN   [1] {ECO:0000313|EMBL:ADU34093.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mitter K.T., Larsen T.B., De Prins W., De Prins J., Collins S.,
RA   Vande Weghe G., Safian S., Zakharov E.V., Hawthorne D.J., Kawahara A.,
RA   Regier J.C.;
RT   "The butterfly subfamily Pseudopontiinae is not monobasic: marked genetic
RT   diversity and morphology reveal three new species of Pseudopontia
RT   (Lepidoptera: Pieridae).";
RL   Syst. Entomol. 36:139-163(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};
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DR   EMBL; HQ174323; ADU34093.1; -; 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; 3.30.470.20; ATP-grasp fold, B 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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
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   PRINTS; PR00098; CPSASE.
DR   SMART; SM01096; CPSase_L_D3; 1.
DR   SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 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.
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          34..226
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADU34093.1"
FT   NON_TER         526
FT                   /evidence="ECO:0000313|EMBL:ADU34093.1"
SQ   SEQUENCE   526 AA;  58771 MW;  99C71EB94837EB19 CRC64;
     VELEKSNIFQ KYNVNVLGTP IQSIVDTEDR KIFAEKINSI GEKVAPSAAV SSVEEALSAA
     LHIGYPVMAR SAFSLGGLGS GXXXXXXXLK ALAHQALSYS EQLIIDKSLK GWKEVEYEVV
     RDAYDNCITV CNMENVDPLG IHTGESIVVA PSQTLSNRDY YMLRNTAIKV IRHFGIVGEC
     NIQYALNPNS EEFYIIEVNA RLSRSSALAS KATGYPLAYV AAKLALGIPL PEIKNTVTGV
     TTACFEPSLD YCVVKIPRWD LAKFNRVSTK IGSSMKSVGE VMAIGRTFEE AFQKALRMVD
     ENINGFDPYI KKVNDTDLKE PTDKRMFILA AALKEGYNVK QLYELTKIDP WFLNKMKNII
     DYYGTLESIN GPINLQLLKK AKQIGFSDKQ IAAAIKSTEL AVRKLREEYK ITPFVKKIDT
     VAAEWPASTN YLYLTYNGAM HDLDFPGEFI MVLGSGVYRI GSSVEFDWCA VGCLRELKEQ
     GKKTIMXNYN PETVSTDYDM SDRLYFEEIS FEVVMDIYNI EHPDGV
//
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