ID A0A1A6GFV5_NEOLE Unreviewed; 746 AA.
AC A0A1A6GFV5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN ORFNames=A6R68_06720 {ECO:0000313|EMBL:OBS64739.1};
OS Neotoma lepida (Desert woodrat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Neotominae; Neotoma.
OX NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS64739.1, ECO:0000313|Proteomes:UP000092124};
RN [1] {ECO:0000313|EMBL:OBS64739.1, ECO:0000313|Proteomes:UP000092124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=417 {ECO:0000313|EMBL:OBS64739.1};
RC TISSUE=Liver {ECO:0000313|EMBL:OBS64739.1};
RA Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT lepida.";
RL Submitted (JUN-2016) 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|ARBA:ARBA00006041, 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:OBS64739.1}.
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DR EMBL; LZPO01097144; OBS64739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A6GFV5; -.
DR STRING; 56216.A0A1A6GFV5; -.
DR Proteomes; UP000092124; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 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 InterPro; IPR013766; Thioredoxin_domain.
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 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:UP000092124};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|RuleBase:RU371123};
KW Transmembrane helix {ECO:0000256|RuleBase:RU371123}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..746
FT /note="Sulfhydryl oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008345573"
FT TRANSMEM 713..730
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU371123"
FT DOMAIN 13..156
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 398..505
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000259|PROSITE:PS51324"
FT REGION 587..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 746 AA; 83346 MW; D9664A16275A41CE CRC64;
MRRCGRHSGS PSQLLLLLLP PLLLAVPGAG AAKLSVLYSS SDPLKLLDAD TLRPTVLHSS
SAWVVEFFAS WCGHCIAFAP TWRELANDVK DWRPALYLAV LDCADETNTA VCRDFNILGF
PTVRVCVKRE RGVGDGSVAG ANVQTLRRRL IDALESHNDT WPSACPPLKP AKYFGMKEIN
KFFIRTNTEY LALIFENKDS YLGREVILDL SQHRILVLRV LDTEKDVVNK FGVTDFPSCY
LLFRNGSASR VPALMESRSS YTSYLRELSG LTREAPSTTA PPATAENIAP TVWKIVDHSK
IYMADLESSL HYILHVEVGK FSVLEGHRLA ALKKFMTVLA KYFHGRPLVQ NFLYSINDWL
YKQQRKKIPY SYFRAALDDR QKDSVLAKKV NWVGCLGSEP HFRGFPCSLW VLFHFLTVQA
SRYSENNPEP PADGQEVLQA MRNYVRFFFG CRDCANHFEQ MAAASMHRVT SPRSAVLWLW
TSHNKVNARL SGAPSDDPYF PKVQWPPRDL CFACHNELSG QQPVWDLDAT FNFLKAHFSP
ENIIMDFPAA EPTTLRGPQN PEATPELVMD ALELETRNSV LGHEWAASTE SPGATALDGP
AENPEASGPQ ELYTGLRMSG APPGQGPPEH MEELQRDTQE HAQGQEHLSK RDTEALLLPE
VNHLQGPLEI RCSPKQLASI PEGEPGARAI QGRGPWLQVL GGGFSHLDIS LCVGLYSVSF
MGLLAMYTYF RARMRTLKGH TSHPIA
//
