ID A0A2H9THI2_9FUNG Unreviewed; 187 AA.
AC A0A2H9THI2;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 08-NOV-2023, entry version 18.
DE RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN ORFNames=PSACC_02998 {ECO:0000313|EMBL:PJF17201.1};
OS Paramicrosporidium saccamoebae.
OC Eukaryota; Fungi; Fungi incertae sedis; Cryptomycota;
OC Cryptomycota incertae sedis; Paramicrosporidium.
OX NCBI_TaxID=1246581 {ECO:0000313|EMBL:PJF17201.1, ECO:0000313|Proteomes:UP000240830};
RN [1] {ECO:0000313|EMBL:PJF17201.1, ECO:0000313|Proteomes:UP000240830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSL3 {ECO:0000313|EMBL:PJF17201.1,
RC ECO:0000313|Proteomes:UP000240830};
RA Quandt C.A., Beaudet D., Corsaro D., Michel R., Corradi N., James T.;
RT "The genome of Paramicrosporidium saccamoebae is the missing link in
RT understanding Cryptomycota and Microsporidia evolution.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR';
CC Xref=Rhea:RHEA:17357, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:16520, ChEBI:CHEBI:17412; EC=1.8.3.2;
CC Evidence={ECO:0000256|RuleBase:RU371123};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU371123};
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:PJF17201.1}.
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DR EMBL; MTSL01000186; PJF17201.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9THI2; -.
DR STRING; 1246581.A0A2H9THI2; -.
DR Proteomes; UP000240830; Unassembled WGS sequence.
DR GO; GO:0016971; F:flavin-dependent sulfhydryl oxidase activity; IEA:InterPro.
DR Gene3D; 1.20.120.310; ERV/ALR sulfhydryl oxidase domain; 1.
DR InterPro; IPR039799; ALR/ERV.
DR InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR PANTHER; PTHR12645; ALR/ERV; 1.
DR PANTHER; PTHR12645:SF1; FAD-LINKED SULFHYDRYL OXIDASE ERV2; 1.
DR Pfam; PF04777; Evr1_Alr; 1.
DR SUPFAM; SSF69000; FAD-dependent thiol oxidase; 1.
DR PROSITE; PS51324; ERV_ALR; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU371123};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU371123};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU371123};
KW Reference proteome {ECO:0000313|Proteomes:UP000240830}.
FT DOMAIN 57..154
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000259|PROSITE:PS51324"
FT REGION 166..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 187 AA; 21212 MW; 4F40629AE2E5C0B1 CRC64;
MDCSDNSAVF AERRCLCKAK DRRRKCHLDR THPLAVASIS YSLESTSEVE NDVGPKDEEE
FRKLLGNATW RLLHTLAARY PDEPTDVDKT RMDQFMGLIS HLYPCPKCAR HMRQMLIDNP
PKAEFSQYVC TIHNIVNKRL GKPEFSCEDV DAHYDCGCDL LDDDEDDEKA EGTTGGQSPV
KPVSRSC
//
