ID G0M7T4_CAEBE Unreviewed; 665 AA.
AC G0M7T4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN ORFNames=CAEBREN_05731 {ECO:0000313|EMBL:EGT30669.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) 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 -!- SIMILARITY: Belongs to the quiescin-sulfhydryl oxidase (QSOX) family.
CC {ECO:0000256|ARBA:ARBA00006041}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU371123}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL379786; EGT30669.1; -; Genomic_DNA.
DR AlphaFoldDB; G0M7T4; -.
DR STRING; 135651.G0M7T4; -.
DR EnsemblMetazoa; CBN05731.1; CBN05731.1; WBGene00144456.
DR eggNOG; KOG1731; Eukaryota.
DR HOGENOM; CLU_020182_0_0_1; -.
DR InParanoid; G0M7T4; -.
DR OMA; HNFVNKR; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016971; F:flavin-dependent sulfhydryl oxidase activity; IEA:InterPro.
DR CDD; cd02992; PDI_a_QSOX; 1.
DR Gene3D; 1.20.120.310; ERV/ALR sulfhydryl oxidase domain; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.20.120.1960; QSOX sulfhydryl oxidase domain; 1.
DR InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR InterPro; IPR040986; QSOX_FAD-bd_dom.
DR InterPro; IPR042568; QSOX_FAD-bd_sf.
DR InterPro; IPR039798; Sulfhydryl_oxidase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR22897; QUIESCIN Q6-RELATED SULFHYDRYL OXIDASE; 1.
DR PANTHER; PTHR22897:SF8; SULFHYDRYL OXIDASE; 1.
DR Pfam; PF04777; Evr1_Alr; 1.
DR Pfam; PF18371; FAD_SOX; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF69000; FAD-dependent thiol oxidase; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51324; ERV_ALR; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
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}; Membrane {ECO:0000256|RuleBase:RU371123};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU371123};
KW Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW Transmembrane {ECO:0000256|RuleBase:RU371123};
KW Transmembrane helix {ECO:0000256|RuleBase:RU371123}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU371123"
FT TRANSMEM 628..646
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU371123"
FT DOMAIN 42..164
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 410..517
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000259|PROSITE:PS51324"
SQ SEQUENCE 665 AA; 75556 MW; AC593E19DB2544F0 CRC64;
MIDEEPGVGN SFCVAGIITG VFMLFILVVI LAFSAGRGNS ESLYDKDDPI LELDVDTFGP
AIYGVKKAHF VEFYSSWCGA CIGYAPTFKK FAKQLEKWSP LVQVTVVNCA EDKNMPLCRE
HSVSSYPSLR YFKYDSATKD DGMKYSGDKY DINKLAHDIA GLAQADAQKQ NPEHWPSFLP
LSETTSLEDV FKSTGSTPYL AIIVQDSPEV IAWANLINYH GNNGLKVAYV SQKHQIAEKY
FTDGGVHALL FSNGNAEPLW KSSSPVEKWI DVEEKIEELI GDKIAAKAPT IQPINAAPVI
AAPSSPLNNQ YEVQLVDLKS AMSYMLYKEI PRREEIRDEP LAALKQWMHT LKKYAPGTTP
MRRLFFRLDE WIQLRAVVTA NEWIAKVDEI QQALGNPLPK EITWMACAGS KPNLRGYTCG
LWTLAHSITV EAYKQEKHNT AFKPVIDVLE PFRAFIFHFL SCSECAQNFT KEAEKNQLHL
VTRAEDVYAW LWRVHNFVNK RLSGSLTDDP SFKKQQFPPK SICPDCYDSN GDIDESKALP
FVFKYYSNIK TDPSENLPGY KVVEYKEGKT LSAGQRHLNP KFQVHAGKVD QLEANEKVKN
VLDAAPQRTW RDIDGYDNLP ETSRSHHYFI WLSLIGVALI VIYCKYRKNR SKFWKTFYYQ
NDFKL
//