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Database: UniProt
Entry: Q1L548_SCECA
LinkDB: Q1L548_SCECA
Original site: Q1L548_SCECA 
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
//
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