ID H9U6C4_9CARA Unreviewed; 718 AA.
AC H9U6C4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 27.
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 punctatostriatum.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Adephaga; Caraboidea; Carabidae;
OC Trechinae; Bembidiini; Bembidion; Odontium subgenus complex; Bracteon.
OX NCBI_TaxID=1166754 {ECO:0000313|EMBL:AFG32878.1};
RN [1] {ECO:0000313|EMBL:AFG32878.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22421212; DOI=10.1016/j.ympev.2012.01.015;
RA Maddison D.R.;
RT "Phylogeny of Bembidion and related ground beetles (Coleoptera: Carabidae:
RT Trechinae: Bembidiini: Bembidiina).";
RL Mol. Phylogenet. Evol. 63:533-576(2012).
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};
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DR EMBL; JN170886; AFG32878.1; -; Genomic_DNA.
DR MEROPS; C26.956; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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}.
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:AFG32878.1"
FT NON_TER 718
FT /evidence="ECO:0000313|EMBL:AFG32878.1"
SQ SEQUENCE 718 AA; 80065 MW; D76A50C02083122C CRC64;
CFMTSQNHGF AVDSKTLSNG WKPLFTNAND NTNEGIIHES LPYFSVQFHP EHTAGPQDLE
CLFDVFIEAI NTYCPANAIN 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 NREYNLLRXT
AINVIRHFGV VGECNIQYAV NPYAEEYYII EVNARLSRSS ALASKATGYP LAYVAAKLAL
GIPLSKIKNS VTGQTTACFE PSLDYCVVKI PRWDLSKFSR VSTKIGSSMK SVGEVMAIGR
KFEEAFQKAL RMVDENVNGF DPYLRKVDDE ELKEPTDKRM FVVAAALKEG YTVDKLYELT
KIDRWFLQKM KHIIDYQTLL EQKDQHSLTY TDLLRAKQIG FSDKQIAASV KSTELAIRKQ
REECGVLPFV KQIDTVAAEW PATTNYLYIT YNASSHDLEF KEEHTMVLGS GVYRIGSSVE
FDWCAVGCLR ELRKLGRKTI MVNYNPETVS TDYDMSDRLY FEEISFEVVM DIYNLENP
//