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Database: UniProt
Entry: B3FAF7_9CARA
LinkDB: B3FAF7_9CARA
Original site: B3FAF7_9CARA 
ID   B3FAF7_9CARA            Unreviewed;       703 AA.
AC   B3FAF7;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 40.
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 integrum.
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=447306 {ECO:0000313|EMBL:ABR23870.1};
RN   [1] {ECO:0000313|EMBL:ABR23870.1}
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; EF649446; ABR23870.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3FAF7; -.
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          222..414
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABR23870.1"
FT   NON_TER         703
FT                   /evidence="ECO:0000313|EMBL:ABR23870.1"
SQ   SEQUENCE   703 AA;  78249 MW;  6874AAFE8F0AEFC6 CRC64;
     NHGFAVDAKT LPTGWKPLFT NANDNTNEGI IHESLPYFSV QFHPEHTAGP QDLECLFDVF
     IEAVNTYCPA NAVNVQELIT RKLTYVPKEP YDMKIPKKVL IIGSGGLSIG QAGEFDYSGS
     QAIKALHEEN IQTVLINPNI ATVQTSKGLA DKVYFLPLVP EYVEQVIRAE RPGGVLLTFG
     GQTGLNCGVE LQRAGVFQKY GVRILGTPID AIIDTEDRKI FADRIAVIGE KVAPSCAVYS
     VTEAVEAAEK LGYPVMARAA FSLGGLGSGF ADNKEELKTL ALQALAHSSQ LIIDKSLKGW
     KEVEYEVVRD AYDNCITVCN MENVDPLGIH TGESIVVAPS QTLSNREYNL LRTTAINVIR
     HFGVVGECNI QYAVNPYAEE YYIIEVNARL SRSSALASKA TGYPLAYVAA KLALGIPLSK
     IKNSVTGQTT ACFEPSLDYC VVKIPRWDLS KFSRVSTKIG SSMKSVGEVM AIGRKFEEAF
     QKALRMVDEN VNGFDPYLRK VDDEELKEPT DKRMFVVAAA LKEGYTVDKL YELTKIDRWF
     LQKMKHIIDY QTLLEQKDQH SLTYTDLLRA KQIGFSDKQI AASVKSTELA IRKQREECGV
     LPFVKQIDTV AAEWPATTNY LYITYNASSH DLEFKEEHTM VLGSGVYRIG SSVEFDWCAV
     GCLRELRKLG RKTIMVNYNP ETVSTDYDMS DRLYFEEISF EVV
//
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