ID   B4YT16_CALSB            Unreviewed;       857 AA.
AC   B4YT16;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Carbamoylphosphate synthetase {ECO:0000313|EMBL:ACF35355.1};
DE   Flags: Fragment;
OS   Calosoma scrutator (Fiery searcher beetle) (Calodrepa scrutator).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Adephaga; Caraboidea; Carabidae;
OC   Carabinae; Carabini; Calosomina; Calosoma.
OX   NCBI_TaxID=60821 {ECO:0000313|EMBL:ACF35355.1};
RN   [1] {ECO:0000313|EMBL:ACF35355.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18644735; DOI=10.1016/j.ympev.2008.05.023;
RA   Wild A.L., Maddison D.R.;
RT   "Evaluating nuclear protein-coding genes for phylogenetic utility in
RT   beetles.";
RL   Mol. Phylogenet. Evol. 48:877-891(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC         phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC         ChEBI:CHEBI:456216; EC=6.3.4.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00043687};
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DR   EMBL; EU677530; ACF35355.1; -; Genomic_DNA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
DR   Gene3D; 3.40.50.20; -; 2.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR   Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR006275; CarbamoylP_synth_lsu.
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   NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR   PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR   PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR   Pfam; PF02786; CPSase_L_D2; 2.
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; 2.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
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}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT   DOMAIN          175..367
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          709..854
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACF35355.1"
FT   NON_TER         857
FT                   /evidence="ECO:0000313|EMBL:ACF35355.1"
SQ   SEQUENCE   857 AA;  94902 MW;  3793EEBCA23DAFFE CRC64;
     AGPQDLECLF DVFIDAVKQF SLTDAVNIRE MILSKLMYIP KVPYDMSIPK KVLIIGSGGL
     SIGQAGEFDY SGSQAIKALQ EENIQTVLIN PNIATVQTSK GLADKVYFLP LVPEYVEQVI
     RAERPGGVLL TFGGQTGLNC GVELQRAGVF AKYGVRILGT PIDAIIDTED RKIFSERISE
     IGEKVAPSCA VYSVQEALDA AEKLGYPVMA RAAFSLGGLG SGFADNKEEL KTLALQALAH
     SSQLIIDKSL KGWKEVEYEV VRDAYDNCIT VCNMENVDPL GIHTGESIVV APSQTLSNRE
     YNLLRTTAIS VIRHFGVVGE CNIQYAVNPN AEEYYIIEVN ARLSRSSALA SKATGYPLAY
     VAAKLALGIP LSKIKNSVTG VTTACFEPSL DYCVVKIPRW DLSKFSRVST KIGSSMKSVG
     EVMAIGRKFE EAFQKALRMV DENVIGFDPY IRNVDDEELK EPTDKRMFVV AAALKEGYTI
     DRLYDLTKID QWFLQKMKKI VDYTTLLESK DQHSLTHDDL LQAXQMGFSD KQIAVSVKST
     ELAIRQQREE YRVLPFVKQI DTVAAEWPAT TNYLYITYNA SSHDLEFNEE HIMVLGSGVY
     RIGSSVEFDW CAVGCLRELR NLHKKTIMVN YNPETVSTDY DMSDRLYFEE ISFEVVMDIY
     NLENPQGIIL CMGGQLPNNI AMDLHRQQAR ILGTSPESVD GAENRFKFSR MLDRIGILQP
     RWKELTNLKS AIEFCDQVGY PCLVRPSYVL SGAAMNVAHS PQDLETYLNA ASDVSKEHPV
     VISKFILESK EIDVDAVACD GVILCMAVSE HVENAGVHSG DATLVTPPQD INSETLLKIK
     TIVRAIAASL EVTGPFN
//