ID W0BVQ8_9HYME Unreviewed; 293 AA.
AC W0BVQ8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=ATPase domain protein {ECO:0000313|EMBL:AHE74612.1};
DE Flags: Fragment;
OS Osmia cerinthidis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Megachilidae; Megachilinae; Osmia.
OX NCBI_TaxID=1403991 {ECO:0000313|EMBL:AHE74612.1};
RN [1] {ECO:0000313|EMBL:AHE74612.1}
RP NUCLEOTIDE SEQUENCE.
RA Haider M., Dorn S., Sedivy C., Muller A.;
RT "Phylogeny and floral hosts of a predominantly pollen generalist group of
RT mason bees (Megachilidae, Osmiini).";
RL Biol. J. Linn. Soc. Lond. 111:78-91(2014).
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; KC709910; AHE74612.1; -; Genomic_DNA.
DR AlphaFoldDB; W0BVQ8; -.
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; 3.30.470.20; 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}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT DOMAIN 42..105
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AHE74612.1"
FT NON_TER 293
FT /evidence="ECO:0000313|EMBL:AHE74612.1"
SQ SEQUENCE 293 AA; 32875 MW; A0B2B69F2029D178 CRC64;
DAYDNCITVC NMENVDPLGI HTGESIVIAP SQTLSNKEYN MLRTTAINVI RHFGIIGECN
IQYALNPNTA EYYIIEVNAR LSRSSALASK ATGYPLAYVA AKLALGIRLP DIHNSVTGKT
TACFEPSLDY CVVKIPRWDL GKFQRVSTKI GSSMKSVGEV MAIGRKFEEA FQKALRMVDE
NITGFDPYVK TPNDEELEKP TDKRMFVLAA SIKAGYTIDR LYELTKIDRW FLHKMKNIID
YYVVLENTDH TKLSHDVLLG AKRIGFSDKQ IAAAVKSSEL AVRIQRQESN IRP
//
