ID B3FAG9_9CARA Unreviewed; 713 AA.
AC B3FAG9;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=CADr {ECO:0000313|EMBL:ABR23882.1};
DE Flags: Fragment;
OS Bembidion rothfelsi.
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=447308 {ECO:0000313|EMBL:ABR23882.1};
RN [1] {ECO:0000313|EMBL:ABR23882.1}
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 + 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; EF649458; ABR23882.1; -; 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:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
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};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW 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 228..420
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT ACT_SITE 1
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 49
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 51
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABR23882.1"
FT NON_TER 713
FT /evidence="ECO:0000313|EMBL:ABR23882.1"
SQ SEQUENCE 713 AA; 79474 MW; 71223A7D071C177A CRC64;
CFMTSQNHGF AVDAKTLPTG WKPLFTNAND NTNEGIIHES LPYFSVQFHP EHTAGPQDLE
CLFDVFIEAV NTFCPANAIN VQELITRKLT YVPKVPYDMK IPKKVLIIGS GGLSIGQAGE
FDYSGSQAIK ALHEENIQTV LINPNIATVQ TSKGLADKVY FLPLVPEYVE QVIRAERPGG
VLLTFGGQTG LNCGVELQRA GVFQKYGVRI LGTPIDAIID TEDRKIFADR IAVIGEKVAP
SCAVYSVTEA VEAAEKLGYP VMARAAFSLG GLGSGFADNK EELKTLALQA LAHSSQLIID
KSLKGWKEVE YEVVRDAYDN CITVCNMENV DPLGIHTGES IVVAPSQTLS NREYNLLRTT
AINVIRHFGV VGECNIQYAV NPYAEEYYII EVNARLSRSS ALASKATGYP LAYVAAKLAL
GIPLSKIKNS VTGQTTACFE PSLDYCVVKI PRWDLSKFSR VSTKIGSSMK SVGEVMAIGR
KFEEAFQKAL RMVDENVNGF DPYLRKVDDE ELKEPTDKRM FVVAAALKEG YTVDKLYELT
KIDRWFLQKM KHIIDYQTLL EQKDQHXLTY IDLLRAKQIG FSDKQIAASV KSTELAIRKQ
REECGVLPFV KQIDTVAAEW PATTNYLYIT YNASSHDLEF KEEHTMVLGS GVYRIGSSVE
FDWCAVGCLR ELRKLGRKTI MVNYNPETVS TDYDMSDRLY FEEISFEVVM DIY
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