ID B3FBA9_9MUSC Unreviewed; 468 AA.
AC B3FBA9;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Carbamoylphosphate synthase {ECO:0000313|EMBL:ABY59327.1};
DE Flags: Fragment;
GN Name=CAD {ECO:0000313|EMBL:ABY59327.1};
OS Leptogaster cylindrica.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Asiloidea;
OC Asilidae; Leptogastrinae; Leptogaster.
OX NCBI_TaxID=468752 {ECO:0000313|EMBL:ABY59327.1};
RN [1] {ECO:0000313|EMBL:ABY59327.1}
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; EF650339; ABY59327.1; -; Genomic_DNA.
DR AlphaFoldDB; B3FBA9; -.
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:ABY59327.1"
FT NON_TER 468
FT /evidence="ECO:0000313|EMBL:ABY59327.1"
SQ SEQUENCE 468 AA; 52444 MW; 8779A4FED9EEE2A6 CRC64;
SLDYCVVKIP RWDLAKFTRV SKNIGSSMKS VGEVMAIGRK FEEAFQKALR MVDENVDGFD
PYVKPVKEEE LIQATDKRMF VLAAALKANY SVKKLHELTK IDPWFLHKMK NIVDYTTLLE
NCGSDLTDDI LLKAKQLGFS DKQIGTAIKS TGVAVRRLRE EMDITPFVKQ IDTVAGEWPA
STNYLYITYN ARSHDVDFPG NYMMVLGSGV YRIGSSVEFD WCAVGCLREL RNLGRQTIMI
NYNPETVSTD YDMCDRLYFE EISFEVVMAF SQLENPEGVI LCMGGQLPNN IAMDLHRQQA
RVLGTSPDSI DSAENRFKFS RMLDRKGILQ PRWKELTTLQ SAIEFCEEVG YPCLVRPSYV
LSGAAMNVAY SNQDLETYLN AASEVSKEHP VVISKFLTEA KEIDVDAVAA DGEILCLAVC
EHVENAGVHS GDATLVTPPQ DINTETLEKI KEIARDLAAL LDVTGPFN
//
