ID B3FAG5_9CARA Unreviewed; 706 AA.
AC B3FAG5;
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 louisella.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Adephaga; Caraboidea; Carabidae;
OC Trechinae; Bembidiini; Bembidion; Odontium subgenus complex;
OC Pseudoperyphus.
OX NCBI_TaxID=447307 {ECO:0000313|EMBL:ABR23878.1};
RN [1] {ECO:0000313|EMBL:ABR23878.1}
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; EF649454; ABR23878.1; -; Genomic_DNA.
DR AlphaFoldDB; B3FAG5; -.
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:ABR23878.1"
FT NON_TER 706
FT /evidence="ECO:0000313|EMBL:ABR23878.1"
SQ SEQUENCE 706 AA; 78518 MW; 6B49F8B06DDF1BB9 CRC64;
TSQNHGFAVD AKTLPTGWKP LFTNANDNTN EGIIHESLPY FSVQFHPEHT AGPQDLECLF
DVFIEAVNTY CPANAINVQE LITRKLTYVP KVPYDMKIPK KVLIIGSGGL SIGQAGEFDY
SGSQAIKALH 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 DQHSLTYIDL LRAKQIGCSD KQIAASVKST ELAIRKQREE
CGVLPFVKQI DTVAAEWPAT TNYLYITYNA SSHDLEFKEE HTMVLGSGVY RIGSSVEFDW
CAVGCLRELR KLGRKTIMVN YNPETVSTDY DMSDRLYFEE ISFEVV
//