ID Q5CX52_CRYPI Unreviewed; 655 AA.
AC Q5CX52;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN ORFNames=cgd6_2470 {ECO:0000313|EMBL:EAK89893.1};
OS Cryptosporidium parvum (strain Iowa II).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=353152 {ECO:0000313|EMBL:EAK89893.1, ECO:0000313|Proteomes:UP000006726};
RN [1] {ECO:0000313|EMBL:EAK89893.1, ECO:0000313|Proteomes:UP000006726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Iowa II {ECO:0000313|Proteomes:UP000006726};
RX PubMed=15044751; DOI=10.1126/science.1094786;
RA Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G.,
RA Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P.,
RA Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L.,
RA Anantharaman V., Aravind L., Kapur V.;
RT "Complete genome sequence of the apicomplexan, Cryptosporidium parvum.";
RL Science 304:441-445(2004).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:EAK89893.1}.
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DR EMBL; AAEE01000002; EAK89893.1; -; Genomic_DNA.
DR RefSeq; XP_627602.1; XM_627602.1.
DR AlphaFoldDB; Q5CX52; -.
DR STRING; 353152.Q5CX52; -.
DR EnsemblProtists; EAK89893; EAK89893; cgd6_2470.
DR GeneID; 3376133; -.
DR KEGG; cpv:cgd6_2470; -.
DR VEuPathDB; CryptoDB:cgd6_2470; -.
DR InParanoid; Q5CX52; -.
DR OMA; YYGFCNI; -.
DR OrthoDB; 196084at2759; -.
DR Proteomes; UP000006726; Chromosome 6.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016971; F:flavin-dependent sulfhydryl oxidase activity; IEA:InterPro.
DR CDD; cd02961; PDI_a_family; 1.
DR Gene3D; 1.20.120.310; ERV/ALR sulfhydryl oxidase domain; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
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; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF69000; FAD-dependent thiol oxidase; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 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}; Membrane {ECO:0000256|RuleBase:RU371123};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU371123};
KW Reference proteome {ECO:0000313|Proteomes:UP000006726};
KW Transmembrane {ECO:0000256|RuleBase:RU371123, ECO:0000313|EMBL:EAK89893.1};
KW Transmembrane helix {ECO:0000256|RuleBase:RU371123}.
FT TRANSMEM 30..52
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU371123"
FT TRANSMEM 624..642
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU371123"
FT DOMAIN 369..503
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000259|PROSITE:PS51324"
SQ SEQUENCE 655 AA; 75263 MW; 7E2AC8A5C9DA5629 CRC64;
MNRFSWKYKR ENHLIDKSNG ILSRMLWSRY IFCCLLFFIW YICTWFVGAH LLRIETKEGI
YTKSAFIKEL SSVGELRDIV LNDLHGPKVI IFYSSFCAYC HMASNPLKKV AESLTPTGVK
FYAFECGKGY SECSIWGIDG LPNLRLIGPE DKTINLESLI NYTEFSDINC TRKSEKHIVF
PEKHIPKLME VPYLKHLKSK SISMPVINEE TFLMCSIIRA FDLSNVFKPL NNSVLSTSAI
SQTKTGISNH FGRWSEESMQ ISPSHAIVDA ITTKFYILHN WVFFGNNVVN TSQFLEKRRL
NALYRFVETS WVLIPSKRTR AKLEEILVFL KNYMDNRDNS IYSKLSLESW QSFIKTVVVE
GISTTQNGSD PTFYICKKSL FCGIWLLFHS WSISLLKGVQ QQGKGCPLYN GPSLTPGQVV
NRIAETVKYF MVCQSCKEHF ETMINNNTCD RTSYIPPMNN NKFPVLLYEA EGLVFWLFRV
HNLVTLRVAT ESSYEHLKQK RSSSISYVGT GVSFPPIGSC FDCYRPNQTP AEVTNQMLSS
INDLTDDDYD KDIFEQGPVV AFLEAYYWKE GWILPKTTLD LQKSELASAY SFPNSNQIDP
FDSLNSFKRS AEIQVGSVFD IFPVLYPILT FFIFSLTVFY LVETGPFLQE QKIAI
//
