ID A0A1F7ZQK9_9EURO Unreviewed; 392 AA.
AC A0A1F7ZQK9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 19.
DE SubName: Full=Dioxygenase {ECO:0000313|EMBL:OGM41746.1};
GN ORFNames=ABOM_009486 {ECO:0000313|EMBL:OGM41746.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM41746.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM41746.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGM41746.1}.
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DR EMBL; LYCR01000104; OGM41746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7ZQK9; -.
DR STRING; 109264.A0A1F7ZQK9; -.
DR OrthoDB; 226459at2759; -.
DR Proteomes; UP000179179; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR024884; NAPE-PLD.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR15032; N-ACYL-PHOSPHATIDYLETHANOLAMINE-HYDROLYZING PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR15032:SF4; N-ACYL-PHOSPHATIDYLETHANOLAMINE-HYDROLYZING PHOSPHOLIPASE D; 1.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR PIRSF; PIRSF038896; NAPE-PLD; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000313|EMBL:OGM41746.1};
KW Oxidoreductase {ECO:0000313|EMBL:OGM41746.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000179179};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..392
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009534023"
FT DOMAIN 106..349
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
FT REGION 60..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 151
FT /ligand="N-acyl-1,2-diacyl-sn-glycero-3-
FT phosphoethanolamine"
FT /ligand_id="ChEBI:CHEBI:62537"
FT /evidence="ECO:0000256|PIRSR:PIRSR038896-50"
FT BINDING 326
FT /ligand="N-acyl-1,2-diacyl-sn-glycero-3-
FT phosphoethanolamine"
FT /ligand_id="ChEBI:CHEBI:62537"
FT /evidence="ECO:0000256|PIRSR:PIRSR038896-50"
SQ SEQUENCE 392 AA; 44091 MW; F665D7CEFF5508D3 CRC64;
MSSSSVAVLY ALTLSIPSTS TGPEDANEKK HHVSGGFTNP WDSYTNPAVH RFFLRQINGK
ANRPDTTPPT VPVQKPEFLP SRDTPKLRAT WLGHACYYVE YPSGLRVLFD PVFEDRCSPF
SWLGPKRYTE MPCQIKDIPI IDAVVISHNH YDHLSYPTVK EISKRHPNCH FFVPLGNEEW
FKSSGIDNVT ELDWWEERDI VLSPSQSTGT QVKESAGNGG SSPGDIKGRV GCLPCQHTSN
RGVFDRAKTL WASWYIESGG RKVYFAGDTG YRSVPELPDS ADDHAPEYDF PVCPAFKQTG
EFRGPFDLGL IPIGAYGPRF VWSPVHADPH DAVQIFQDTK CKKALGMHWG TWVLTEEDVL
EPPRKLRDAL RKYEIPEDGV FDICDIGESR EF
//
