ID   SMD_ASPFN               Reviewed;         289 AA.
AC   B8NQ51;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Sphingomyelinase D {ECO:0000303|PubMed:24223912};
DE            Short=SMase D {ECO:0000303|PubMed:24223912};
DE            EC=3.1.4.41 {ECO:0000269|PubMed:24223912};
DE   Flags: Precursor;
GN   ORFNames=AFLA_004420 {ECO:0000312|EMBL:EED47801.1};
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
RN   [2]
RP   IDENTIFICATION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, DOMAIN, AND
RP   FUNCTION.
RX   PubMed=24223912; DOI=10.1371/journal.pone.0079240;
RA   Dias-Lopes C., Neshich I.A., Neshich G., Ortega J.M., Granier C.,
RA   Chavez-Olortegui C., Molina F., Felicori L.;
RT   "Identification of new sphingomyelinases D in pathogenic fungi and other
RT   pathogenic organisms.";
RL   PLoS ONE 8:E79240-E79240(2013).
CC   -!- FUNCTION: Catalyzes the hydrolysis of sphingomyelin. Sphingomyelinases
CC       D are produced by some spider in their venoms, but also by arthropods
CC       such as ticks, or pathogenic bacteria and fungi. They might play a role
CC       in pathogenicity through different mechanisms, such as membrane
CC       destabilization and host cell penetration, but also pulmonary
CC       inflammation and cutaneous lesions. {ECO:0000269|PubMed:24223912}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a sphingomyelin + H2O = an N-acylsphing-4-enine 1-phosphate +
CC         choline + H(+); Xref=Rhea:RHEA:20984, ChEBI:CHEBI:15354,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17636,
CC         ChEBI:CHEBI:57674; EC=3.1.4.41;
CC         Evidence={ECO:0000269|PubMed:24223912};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q8I914};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8I914};
CC   -!- ACTIVITY REGULATION: Sphingomyelinase activity is reduced by 33 percent
CC       following addition of EDTA. {ECO:0000269|PubMed:24223912}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- DOMAIN: The SMD-tail motif is highly conserved and may be responsible
CC       for structural stabilization. {ECO:0000303|PubMed:24223912}.
CC   -!- SIMILARITY: Belongs to the sphingomyelinase D/phospholipase D family.
CC       {ECO:0000305}.
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DR   EMBL; EQ963482; EED47801.1; -; Genomic_DNA.
DR   RefSeq; XP_002382643.1; XM_002382602.1.
DR   AlphaFoldDB; B8NQ51; -.
DR   SMR; B8NQ51; -.
DR   STRING; 5059.CADAFLAP00010508; -.
DR   EnsemblFungi; EED47801; EED47801; AFLA_004420.
DR   VEuPathDB; FungiDB:AFLA_004420; -.
DR   eggNOG; ENOG502S5U7; Eukaryota.
DR   HOGENOM; CLU_059400_0_0_1; -.
DR   OMA; SWQCANA; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050290; F:sphingomyelin phosphodiesterase D activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.190; -; 1.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR016674; SMase_D/PLipase_D.
DR   PIRSF; PIRSF016632; Phospholipase_actinobac/fun; 1.
DR   SUPFAM; SSF51695; SSF51695; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Magnesium; Metal-binding;
KW   Secreted; Signal; Virulence.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..289
FT                   /note="Sphingomyelinase D"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000431992"
FT   MOTIF           282..289
FT                   /note="SMD-tail"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        34
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         54
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         56
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         103
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
SQ   SEQUENCE   289 AA;  32525 MW;  3403518A6BCDB301 CRC64;
     MQSISVLICV LLALSILNFT VASLTQRPIY AIAHRVLRNE AVTAALSHGA NALEVDLTAW
     YFGWWADHDG KLFSAGSTAR DLFKFIAQKQ WTKDYNISFV WLDIKNPDFC RKGRPCSIEA
     LRDLAREILE PAGIRVLYGF FETAESRGFK VIRDGLNSNE AVVLSGETST ILHLYNISGA
     GIPVKQMVMD FGDSWLRKGV DIYPELRYGS WKRDHGKLGK VFSWTSAQGD TEMVRYLLRE
     AGIDGLIYGY QTDEYNDKSG PKSALKDIVD FVEAHSDTHR MATEDDAPW