ID   SOX_BOVIN               Reviewed;         392 AA.
AC   Q29RU9; Q5E9H6;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Peroxisomal sarcosine oxidase;
DE            Short=PSO;
DE            EC=1.5.3.1;
DE            EC=1.5.3.7;
DE   AltName: Full=L-pipecolate oxidase;
DE   AltName: Full=L-pipecolic acid oxidase;
GN   Name=PIPOX;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Metabolizes sarcosine, L-pipecolic acid and L-proline.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + sarcosine = formaldehyde + glycine + H2O2;
CC         Xref=Rhea:RHEA:13313, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:16842, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:57433; EC=1.5.3.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-pipecolate + O2 = H(+) + H2O2 + L-1-piperideine-6-
CC         carboxylate; Xref=Rhea:RHEA:11992, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58769,
CC         ChEBI:CHEBI:61185; EC=1.5.3.7;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MSOX/MTOX family. {ECO:0000305}.
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DR   EMBL; BT020944; AAX08961.1; -; mRNA.
DR   EMBL; BC114006; AAI14007.1; -; mRNA.
DR   RefSeq; NP_001014878.2; NM_001014878.2.
DR   AlphaFoldDB; Q29RU9; -.
DR   SMR; Q29RU9; -.
DR   STRING; 9913.ENSBTAP00000010444; -.
DR   PaxDb; Q29RU9; -.
DR   PeptideAtlas; Q29RU9; -.
DR   PRIDE; Q29RU9; -.
DR   Ensembl; ENSBTAT00000010444; ENSBTAP00000010444; ENSBTAG00000007946.
DR   GeneID; 509102; -.
DR   KEGG; bta:509102; -.
DR   CTD; 51268; -.
DR   VEuPathDB; HostDB:ENSBTAG00000007946; -.
DR   VGNC; VGNC:32914; PIPOX.
DR   eggNOG; KOG2820; Eukaryota.
DR   GeneTree; ENSGT00390000011000; -.
DR   HOGENOM; CLU_007884_2_2_1; -.
DR   InParanoid; Q29RU9; -.
DR   OMA; QEQPAHF; -.
DR   OrthoDB; 752680at2759; -.
DR   TreeFam; TF313837; -.
DR   Reactome; R-BTA-71064; Lysine catabolism.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000007946; Expressed in metanephros cortex and 58 other tissues.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0050031; F:L-pipecolate oxidase activity; IBA:GO_Central.
DR   GO; GO:0008115; F:sarcosine oxidase activity; IBA:GO_Central.
DR   GO; GO:0033514; P:L-lysine catabolic process to acetyl-CoA via L-pipecolate; IBA:GO_Central.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR045170; MTOX.
DR   InterPro; IPR006281; SoxA_mon.
DR   PANTHER; PTHR10961; PTHR10961; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR01377; soxA_mon; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; FAD; Flavoprotein; Oxidoreductase; Peroxisome;
KW   Reference proteome.
FT   CHAIN           1..392
FT                   /note="Peroxisomal sarcosine oxidase"
FT                   /id="PRO_0000244375"
FT   MOTIF           390..392
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   BINDING         9..39
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         126
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D826"
FT   MOD_RES         321
FT                   /note="S-8alpha-FAD cysteine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        161
FT                   /note="A -> G (in Ref. 2; AAI14007)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   392 AA;  43820 MW;  E62446943F200F67 CRC64;
     MAAQRELYDA IVIGAGIQGC FTAYHLAKHS KKVLLLEQFF LPHSRGSSHG QSRIIRRAYP
     EDFYTQMMAE CYSLWAQLEH EAGTQLYRQT GLLLLGMKEN PELKIIQATL SRQGVEHQCL
     SSEELKQRFP NIRLARGEVG LLEVSGGVLY ADKALRALQD AIRQLGGIVH DGEKVVEIKS
     GLPVMVKTTS RSYQAKSLII TAGPWTNRLL RPLGAELPLQ TLRINVCYWQ EKVPGSYSVS
     QAFPCFMGLG LSLAPHHIYG LPSREYPGLM KVCYHHGNNA DPEERDCPAA FSDIQDVHIL
     SGFVRDHLPD LQPEPAVMEH CMYTNTPDGH FVLDRHPKYD NIVIGAGFSG HGFKLSPVVG
     KILYELSMKL TPSYDLTPFR ISRFPSLGKA HL