ID Q1L548_SCECA Unreviewed; 288 AA.
AC Q1L548;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 48.
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:AAZ20197.1};
OS Sceliphron caementarium (Black and yellow mud dauber wasp) (Sphex
OS caementaria).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Sphecidae; Sceliphrinae; Sceliphrina; Sceliphron.
OX NCBI_TaxID=253855 {ECO:0000313|EMBL:AAZ20197.1};
RN [1] {ECO:0000313|EMBL:AAZ20197.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16412668; DOI=10.1016/j.ympev.2005.09.022;
RA Danforth B.N., Fang J., Sipes S.;
RT "Analysis of family-level relationships in bees (Hymenoptera: Apiformes)
RT using 28S and two previously unexplored nuclear genes: CAD and RNA
RT polymerase II.";
RL Mol. Phylogenet. Evol. 39:358-372(2006).
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; DQ067125; AAZ20197.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1L548; -.
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; 3.30.470.20; 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 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 PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00867; CPSASE_2; 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 37..100
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAZ20197.1"
FT NON_TER 288
FT /evidence="ECO:0000313|EMBL:AAZ20197.1"
SQ SEQUENCE 288 AA; 32367 MW; 3AF5382B492DFBAA CRC64;
CITVCNMENV DPLGIHTGES IVVAPSQTLS NREYNMLRTT AINVIRHFGV IGECNIQYAL
NPSSEEYYII EVNARLSRSS ALASKASGYP LAYVAAKLAL GIRLPDINNS VTGNTTACFE
PSLDYCVVKI PRWDLGKFHR VSTKIGSSMK SVGEVMAIGR KFEEAFQKAL RMVDENVNGF
DPYLKSIDDE ELEKPTDKRM FVLAASIRAG YTIDRLYELT KIDRWFLEKM KNIITYYELL
ENLDQTKLSH KILLGAKQIG FSDKQIAAVV KSSELAVRIQ RQESNIRP
//