ID H3A722_LATCH Unreviewed; 616 AA.
AC H3A722;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN Name=QSOX1 {ECO:0000313|Ensembl:ENSLACP00000005443.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000005443.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000005443.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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}.
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DR EMBL; AFYH01183515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01183516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01183517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01183518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01183519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01183520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01183521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01183522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3A722; -.
DR STRING; 7897.ENSLACP00000005443; -.
DR Ensembl; ENSLACT00000005491.1; ENSLACP00000005443.1; ENSLACG00000004842.1.
DR eggNOG; KOG1731; Eukaryota.
DR GeneTree; ENSGT00940000159504; -.
DR HOGENOM; CLU_020182_1_0_1; -.
DR InParanoid; H3A722; -.
DR OMA; WPNIAPY; -.
DR TreeFam; TF316749; -.
DR Proteomes; UP000008672; 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; 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; IPR041269; QSOX_Trx1.
DR InterPro; IPR039798; Sulfhydryl_oxidase.
DR PANTHER; PTHR22897; QUIESCIN Q6-RELATED SULFHYDRYL OXIDASE; 1.
DR PANTHER; PTHR22897:SF6; SULFHYDRYL OXIDASE 1; 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 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:UP000008672};
KW Transmembrane {ECO:0000256|RuleBase:RU371123};
KW Transmembrane helix {ECO:0000256|RuleBase:RU371123}.
FT TRANSMEM 585..602
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU371123"
FT DOMAIN 257..363
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000259|PROSITE:PS51324"
FT REGION 433..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..477
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 616 AA; 71602 MW; 6734D424803CCE0F CRC64;
DVQTLRHKII DLLETHEDVW PPACPPLEPA SMAEVRSFFQ TNSVHYLALI FEEEDSYIGR
EVTLDMLQYE NIAVRRVWRT EKAMVSQFGV KSFPSCYLYF NNGTHAQIQV EMQVRSFYTY
YLQRLPGVMR GGYKLMVIPD SQSGAIATTW KTFDSSKVYM ADLESALHYA LRVEVKPQRI
LAGEELAALK GFVSVLAKYF PGRPTVKNLL RSMDSWLGSY RVSELSYSTF QDVVNNKLEV
PSAVLADSVN WVGCQGSKPQ FRGYPCSLWT LFHVLTVQAA WKLLPGNKGG NPLEVLLAMH
GYVKYFFGCR DCATKFEAMA AESMENIKDL DGAILWLWSR HNRVNSRLAG AVSEDPKFPK
LQWPPPDLCP KCHNEVKGEH VWNMDAVLRF LKAHFYKENI SYDYLAREAH LLADQRDQLA
AWREAEQQKQ LRERKEKIKE ENEKGQNELE KEEQRKEEEE EEEEEDEDDE RNEQPEEGDE
TNVENVKQSR NPKPSFVQGK RKKKLQEEEI IVDLDSFIEH HYKSKALQAA AVRRNKGQRE
EQRQDQQVQQ DAEMIDYREG LVPKKKHWIM LLGVGFSRLD LSLCVLFYFL SSLCLLGMCL
YFRMRLKCRR ARHTYN
//