ID A0FIF6_9HYME Unreviewed; 562 AA.
AC A0FIF6;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 24-JAN-2024, entry version 63.
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;
GN Name=CAD {ECO:0000313|EMBL:ABJ98964.1};
OS Baryscapus sp. CD015.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Eulophidae; Tetrastichinae; Baryscapus.
OX NCBI_TaxID=405225 {ECO:0000313|EMBL:ABJ98964.1};
RN [1] {ECO:0000313|EMBL:ABJ98964.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17911033; DOI=10.1016/j.ympev.2007.08.004;
RA Desjardins C.A., Regier J.C., Mitter C.;
RT "Phylogeny of pteromalid parasitic wasps (Hymenoptera: Pteromalidae):
RT initial evidence from four protein-coding nuclear genes.";
RL Mol. Phylogenet. Evol. 45:454-469(2007).
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; DQ999908; ABJ98964.1; -; mRNA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_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; IPR035686; CPSase_GATase1.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00098; CPSASE.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal 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; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 2: Evidence at transcript level;
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 485..562
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT ACT_SITE 220
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 304
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 306
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABJ98964.1"
FT NON_TER 562
FT /evidence="ECO:0000313|EMBL:ABJ98964.1"
SQ SEQUENCE 562 AA; 62184 MW; 86232E51973057FA CRC64;
GYPESLTDPS YCEQILVLTY PLIGNYGVPN KEKDEHELLR WFESHKIWAA GLVVSEHCDT
PSHWRQTKSL SDWMKEEGIP GIQNVDTRAL TKVIREKGTI LGRIVHQLPE KINSLPAIVD
PNXQNLVAKV SRSSKVTYNP NGSPRICVVD CGLKYNQIRC LISRGARVDI VPWNHKIQNE
DFDGLFLSNG PGDPSMCKET LDNLQKILNX AKKKPIFGIC LGHQLLSLAA GCKSYKMRYG
NRGHNQPAIH HGTKRCYMTS QNHGFAIDAK SLPKDWEALF TNANDDSNEG IVHSTLPYFS
VQFHPEHTAG PQDLECLFDV FLETVKQQXL TGKSDVSVKD RLQEKLTYVP TRPVNAERPK
KVLILGSGGL SIGQAGEFDY SGSQAIKALR EEHIQTVLIN PNIATVQTSK GMADKVYFLP
ILPEYVEQVL QSERPDGVLL TFGGQTALNC GVELQKQGIF ERYGVRILGT PIESIIETED
RKIFADRVNE IGEKVAPSCA VYSIQEACEA AEKLGYPVMA RAAFSLGGLG SGFANSKEEL
VTLAQQALAH SSQLIIDKSL QG
//