ID A0A232EWS7_9HYME Unreviewed; 165 AA.
AC A0A232EWS7;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 08-NOV-2023, entry version 21.
DE RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN ORFNames=TSAR_004608 {ECO:0000313|EMBL:OXU22804.1};
OS Trichomalopsis sarcophagae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU22804.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU22804.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU22804.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU22804.1};
RX PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL Curr. Biol. 27:2007-2013(2017).
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:OXU22804.1}.
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DR EMBL; NNAY01001823; OXU22804.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A232EWS7; -.
DR STRING; 543379.A0A232EWS7; -.
DR Proteomes; UP000215335; 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:SF0; FAD-LINKED SULFHYDRYL OXIDASE ALR; 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:UP000215335}.
FT DOMAIN 55..155
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000259|PROSITE:PS51324"
FT REGION 27..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 165 AA; 19264 MW; 0DC37491FFFC7EFB CRC64;
METMADGKPC RTCTDFKTWA KLQKQTFDSE KKSDQAKQGS DHKYTETMNA RRKDCPLDRD
ELGSRTWGFL HTMAAYYPES PTVEQRKDMK TFFHLISKFY PCNVCAEDLQ EQLKKSPPKT
DSQHQLSQWL CDVHNEVNKK LGKPVFDCSL INQRWRDGWL DGSCD
//
