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Database: UniProt
Entry: B3FAA4_9CARA
LinkDB: B3FAA4_9CARA
Original site: B3FAA4_9CARA 
ID   B3FAA4_9CARA            Unreviewed;       706 AA.
AC   B3FAA4;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 41.
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   Bembidion confusum.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Adephaga; Caraboidea; Carabidae;
OC   Trechinae; Bembidiini; Bembidion; Odontium subgenus complex; Odontium.
OX   NCBI_TaxID=447299 {ECO:0000313|EMBL:ABR23817.1};
RN   [1] {ECO:0000313|EMBL:ABR23817.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Maddison D.R.;
RT   "Systematics of the North American beetle subgenus Pseudoperyphus
RT   (Coleoptera: Carabidae: Bembidion) based upon morphological, chromosomal,
RT   and molecular data.";
RL   Submitted (JUN-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};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
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DR   EMBL; EF649393; ABR23817.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3FAA4; -.
DR   MEROPS; C26.951; -.
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; -; 2.
DR   Gene3D; 3.40.50.880; -; 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; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
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   Pfam; PF00117; GATase; 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; 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   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}.
FT   DOMAIN          225..417
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABR23817.1"
FT   NON_TER         706
FT                   /evidence="ECO:0000313|EMBL:ABR23817.1"
SQ   SEQUENCE   706 AA;  78597 MW;  C5DD714768301B56 CRC64;
     TSQNHGFAVD SKTLPNGWKP LFTNANDNTN EGIIHESLPY FSVQFHPEHT AGPQDLECLF
     DVFIEAVNKY CPANAINVQE LITRKLTYVP KVPYDMKIPK KVLIIGSGGL SIGQAGEFDY
     SGSQAIKALQ EENIQTVLIN PNIATVQTSK GLADKVYFLP LVPEYVEQVI RAERPGGVLL
     TFGGQTGLNC GVELQRAGVF QKYGVRILGT PIDAIIDTED RKIFADRIAV IGEKVAPSCA
     VYSVTEAVEA AEKLGYPVMA RAAFSLGGLG SGFADNKEEL KTLALQALAH SSQLIIDKSL
     KGWKEVEYEV VRDAYDNCIT VCNMENVDPL GIHTGESIVV APSQTLSNRE YNLLRTTAIN
     VIRHFGVVGE CNIQYAVNPY AEEYYIIEVN ARLSRSSALA SKATGYPLAY VAAKLALGIP
     LSKIKNSVTG QTTACFEPSL DYCVVKIPRW DLSKFSRVST KIGSSMKSVG EVMAIGRKFE
     EAFQKALRMV DENVNGFDPY LRKVDDEELK EPTDKRMFVV AAALKEGYTV DKLYELTKID
     RWFLQKMKHI IDYQTLLEQK DQHSLTYTDL LRAKQIGFSD KQIAASVKST ELAIRKQREE
     CGVLPFVKQI DTVAAEWPAT TNYLYITYNA SSHDLEFKEE HTMVLGSGVY RIGSSVEFDW
     CAVGCLRELR KLGRKTIMVN YNPETVSTDY DMSDRLYFEE ISFEVV
//
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