ID A0A091N199_9PASS Unreviewed; 593 AA.
AC A0A091N199;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
DE Flags: Fragment;
GN ORFNames=N310_05021 {ECO:0000313|EMBL:KFP83553.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP83553.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP83553.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP83553.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxidation of sulfhydryl groups in peptide and
CC protein thiols to disulfides with the reduction of oxygen to hydrogen
CC peroxide. {ECO:0000256|RuleBase:RU371123}.
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|ARBA:ARBA00000999,
CC 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|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; KK841099; KFP83553.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091N199; -.
DR Proteomes; UP000053537; 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 Gene3D; 1.20.120.310; ERV/ALR sulfhydryl oxidase domain; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
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; IPR041269; QSOX_Trx1.
DR InterPro; IPR039798; Sulfhydryl_oxidase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR22897; QUIESCIN Q6-RELATED SULFHYDRYL OXIDASE; 1.
DR PANTHER; PTHR22897:SF7; SULFHYDRYL OXIDASE 2; 1.
DR Pfam; PF04777; Evr1_Alr; 1.
DR Pfam; PF18371; FAD_SOX; 1.
DR Pfam; PF18108; QSOX_Trx1; 1.
DR SUPFAM; SSF69000; FAD-dependent thiol oxidase; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51324; ERV_ALR; 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:UP000053537};
KW Transmembrane {ECO:0000256|RuleBase:RU371123};
KW Transmembrane helix {ECO:0000256|RuleBase:RU371123}.
FT TRANSMEM 560..577
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU371123"
FT DOMAIN 315..424
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000259|PROSITE:PS51324"
FT REGION 468..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP83553.1"
FT NON_TER 593
FT /evidence="ECO:0000313|EMBL:KFP83553.1"
SQ SEQUENCE 593 AA; 67554 MW; A50DE37072F36329 CRC64;
DWESAIRVGV LDCGDEENYE TCKEYGIHYY PTFRYFKAFT KQFTTGENYQ GADRELQTVR
QMMIDFLQNH SQEVRPPACP QLDPVLSSDI PSLLDKNSHH YTAIVFESNS SYVGREVILD
LIQYENIIVK RALNFDKPLL EKLGVTSVPS CYLVQPNGSH GLINNLKPLR SFFSSYLKSL
PGVRKKLLLP LQLPAAENRE ESTETRVWKE FDKSKLYMAD LESGLHYLLR VELATHKMLE
GAELKTFKDF VTVSAKLFPG RQPVVKLLET LQEWLVSLPL DKIPYDAILD LVNNKMRISG
IFLTKKAQWV GCQGSRPELR GYSCSLWKLF HTLTVQAALR PKALLNTGLE DNPQVVLQVM
RRYIHHFFGC KACAQHFEEM AKESMDSVKT LDQAVLWLWE KHNVVNNRLA GDLTEDPKFP
KVQWPTPDIC PACHEEIKGL HSWNEEKVLQ FLKHHYSTEN ILHKYAESQT DSTEAEQGDT
GEVKDKHLLK KSGGSRENGM QEKENPLDSG SKGLDKPIAN PGAVQGSGRS SAAAGNLRET
RQAVSFLGIG FSNLDMSLCV ILYVASSLFL MIMYFFFRVR SKRWKVKYSR SSV
//
