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
//