ID   PCYOX_PONAB             Reviewed;         505 AA.
AC   Q5R748;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Prenylcysteine oxidase 1;
DE            EC=1.8.3.5 {ECO:0000250|UniProtKB:Q9UHG3};
DE   Flags: Precursor;
GN   Name=PCYOX1 {ECO:0000250|UniProtKB:Q9UHG3};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Prenylcysteine oxidase that cleaves the thioether bond of
CC       prenyl-L-cysteines, such as farnesylcysteine and geranylgeranylcysteine
CC       (By similarity). Only active against free prenylcysteines and not
CC       prenylcysteine residues within prenylated proteins or peptides (By
CC       similarity). Involved in the final step in the degradation of
CC       prenylated proteins, by degrading prenylcysteines after the protein has
CC       been degraded (By similarity). {ECO:0000250|UniProtKB:F1N2K1,
CC       ECO:0000250|UniProtKB:Q9UHG3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an S-prenyl-L-cysteine + H2O + O2 = a prenal + H2O2 + L-
CC         cysteine; Xref=Rhea:RHEA:53892, Rhea:RHEA-COMP:13675, Rhea:RHEA-
CC         COMP:13676, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:137934, ChEBI:CHEBI:137935;
CC         EC=1.8.3.5; Evidence={ECO:0000250|UniProtKB:Q9UHG3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53893;
CC         Evidence={ECO:0000250|UniProtKB:Q9UHG3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + S-(2E,6E)-farnesyl-L-cysteine = (2E,6E)-farnesal +
CC         H2O2 + L-cysteine; Xref=Rhea:RHEA:30231, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:15894, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:62141; EC=1.8.3.5;
CC         Evidence={ECO:0000250|UniProtKB:Q9UHG3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30232;
CC         Evidence={ECO:0000250|UniProtKB:Q9UHG3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(2E,6E,10E)-geranylgeranyl]-L-cysteine + H2O + O2 =
CC         (2E,6E,10E)-geranylgeranial + H2O2 + L-cysteine;
CC         Xref=Rhea:RHEA:70407, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:35235, ChEBI:CHEBI:189549,
CC         ChEBI:CHEBI:189554; EC=1.8.3.5;
CC         Evidence={ECO:0000250|UniProtKB:Q9UHG3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70408;
CC         Evidence={ECO:0000250|UniProtKB:Q9UHG3};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q9UHG3};
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q9UHG3}.
CC   -!- SIMILARITY: Belongs to the prenylcysteine oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; CR860270; CAH92412.1; -; mRNA.
DR   RefSeq; NP_001126422.1; NM_001132950.1.
DR   AlphaFoldDB; Q5R748; -.
DR   STRING; 9601.ENSPPYP00000013746; -.
DR   GeneID; 100457284; -.
DR   KEGG; pon:100457284; -.
DR   CTD; 51449; -.
DR   eggNOG; ENOG502QSHJ; Eukaryota.
DR   InParanoid; Q5R748; -.
DR   OrthoDB; 1114069at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0102149; F:farnesylcysteine lyase activity; IEA:RHEA.
DR   GO; GO:0001735; F:prenylcysteine oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030328; P:prenylcysteine catabolic process; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR010795; Prenylcys_lyase.
DR   InterPro; IPR017046; Prenylcysteine_Oxase.
DR   PANTHER; PTHR15944; PTHR15944; 1.
DR   Pfam; PF07156; Prenylcys_lyase; 1.
DR   PIRSF; PIRSF036292; Prenylcysteine_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Glycoprotein; Lysosome; Oxidoreductase;
KW   Reference proteome; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..505
FT                   /note="Prenylcysteine oxidase 1"
FT                   /id="PRO_0000023301"
FT   CARBOHYD        196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        353
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   505 AA;  56752 MW;  EA49ACA2F23D1313 CRC64;
     MGRVVAELVS SLLGLWLLLC SCGCPEGAEL RAPPDKIAII GAGIGGTSAA YYLRQKFGKD
     VKIDLFEREE VGGRLATMMV QGQEYEAGGS VIHPLNLRMK RFVKDLGLST VQASGGLLGI
     YNGETLVFEE SNWFIINVIK LVWRYGFQSL RMHMWVEDVL DKFMRIYRYQ SHDYAFSSVE
     KLLHALGGDD FLGMLNRTLL ETLQKAGFSE KFLNEMIAPV MRVNYGQSTD INAFVGAVSL
     SCSDSGLWAV EGGNKLVCSG LLQASKSNLI SGSVMYIEEK TKTKHTGNPT KMYEVVYQIG
     TETRSDFYDI VLVATPLNRK MSNITFLNFD PPIEEFHQYY QHIVTTLVKG ELNTSIFSSR
     PIDKFGLNTV LTTDNSDLFI NSIGIVSSVR EKEDPEPSTD GTYVWKIFSQ ETLTKAQILK
     LFLSYDYAVK KPWLAYPHYK PPEKCPSIIL HDRLYYLNGI ECAASAMEMS AIAAHNAALL
     AYHRWNRHTD MIDQDGLYEK LKTEL