ID B3FB98_9MUSC Unreviewed; 468 AA.
AC B3FB98;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Carbamoylphosphate synthase {ECO:0000313|EMBL:ABY59316.1};
DE Flags: Fragment;
GN Name=CAD {ECO:0000313|EMBL:ABY59316.1};
OS Bombylius major.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Asiloidea;
OC Bombyliidae; Bombylius.
OX NCBI_TaxID=240869 {ECO:0000313|EMBL:ABY59316.1};
RN [1] {ECO:0000313|EMBL:ABY59316.1}
RP NUCLEOTIDE SEQUENCE.
RA Dikow T.;
RT "A phylogenetic hypothesis for Asilidae based on a total evidence analysis
RT of morphological and DNA sequence data (Insecta: Diptera: Brachycera:
RT Asiloidea).";
RL Org. Divers. Evol. 9:165-188(2009).
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; EF650328; ABY59316.1; -; Genomic_DNA.
DR AlphaFoldDB; B3FB98; -.
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:0006520; P:amino acid metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; 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 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; 2.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00866; CPSASE_1; 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}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 320..465
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABY59316.1"
FT NON_TER 468
FT /evidence="ECO:0000313|EMBL:ABY59316.1"
SQ SEQUENCE 468 AA; 52676 MW; B357E96A79B3B2C6 CRC64;
SLDYCVVKIP RWDLTKFTRV NKNIGSSMKS VGEVMAIGRK FEEAFQKALR MVDENVNGFD
PYIKEARETE LSQPTDKRIY VLAAAIKKNY SIEKLYELTK IDPWFLHKMK NIIDYLNLLE
AHGNNLTRDH LLAAKQLGFS DKQIAVAIKS TDLAVRKHRE EVDVTPFVKQ IDTVAGEWPA
TTNYLYITYN ASSHDIEFPG DFTIVVGSGV YRIGSSVEFD WCAVGCLREL RNLGKSTIMI
NYNPETVSTD YDMCDRLYFE EISFEVVMDI YQLENAEGII LSMGGQLPNN IAMDLHRQQA
RVLGTTPESI DSAENRFKFS RMLDRKGILQ PRWKELTNLQ SAIKFCEEVD YPCLVRPSYV
LSGAAMNVAY SNQDLEAYLN AASKVSKEHP VVISKFITEA KEIDVDAVAA DGEILCLAVS
EHIENAGIHS GDATLVTPPQ DINTETLEKI KEIARDLAAL LDVTGPFN
//
