ID   H9A5X9_9CARA            Unreviewed;       267 AA.
AC   H9A5X9;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Carbamoylphosphate synthetase {ECO:0000313|EMBL:AFC56817.1};
DE   Flags: Fragment;
GN   Name=CAD1 {ECO:0000313|EMBL:AFC56817.1};
OS   Nebria crassicornis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Adephaga; Caraboidea; Carabidae;
OC   Nebriinae; Nebriini; Nebria; Boreonebria.
OX   NCBI_TaxID=1149901 {ECO:0000313|EMBL:AFC56817.1};
RN   [1] {ECO:0000313|EMBL:AFC56817.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kavanaugh D.H., Archambeault S.L., Roopnarine P.D., Ledford J.;
RT   "A re-consideration of the taxonomic status of Nebria lacustris Casey
RT   (Coleoptera: Carabidae: Nebriini) based on multiple datasets--a single
RT   species or a species complex?";
RL   Zookeys 0:0-0(2012).
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; JN847556; AFC56817.1; -; Genomic_DNA.
DR   AlphaFoldDB; H9A5X9; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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   InterPro; IPR011761; ATP-grasp.
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   PRINTS; PR00098; CPSASE.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   PROSITE; PS50975; ATP_GRASP; 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          170..258
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFC56817.1"
FT   NON_TER         267
FT                   /evidence="ECO:0000313|EMBL:AFC56817.1"
SQ   SEQUENCE   267 AA;  29035 MW;  D359429A275A6C69 CRC64;
     LECLFDIFIE AVTTFTPDTR INIRDMFTQQ LTYVPKTPYD LRIPKKVLII GSGGLSIGQA
     GEFDYSGSQA IKALQEENIQ TVLINPNIAT VQTSKGLADK VYFLPLVPEY VEQVIRAERP
     GGVLLTFGGQ TGLNCGVALN GAGIFDKYNC RILGTPIEAI IDTEDRKIFS ERIAAIGEKV
     APSCAVYSVQ EAIDAAEKLG YPVMARAAFS LGGLGSGFAD NKEELKTLAL QALAHSSQLI
     IDKSLKGWKE VEYEVVRDAY DNCITVC
//