ID   SOX_RABIT               Reviewed;         390 AA.
AC   P79371;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   27-MAR-2024, entry version 96.
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; Synonyms=PSO, SOX;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   TISSUE=Liver;
RX   PubMed=9045710; DOI=10.1074/jbc.272.10.6766;
RA   Reuber B.E., Karl C., Reimann S.A., Mihalik S.J., Dodt G.;
RT   "Cloning and functional expression of a mammalian gene for a peroxisomal
RT   sarcosine oxidase.";
RL   J. Biol. Chem. 272:6766-6776(1997).
CC   -!- FUNCTION: Metabolizes sarcosine, L-pipecolic acid and L-proline.
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;
CC       Note=Binds 1 FAD per subunit.;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- TISSUE SPECIFICITY: Kidney and liver.
CC   -!- SIMILARITY: Belongs to the MSOX/MTOX family. {ECO:0000305}.
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DR   EMBL; U82267; AAB48443.1; -; mRNA.
DR   RefSeq; NP_001075851.1; NM_001082382.1.
DR   AlphaFoldDB; P79371; -.
DR   SMR; P79371; -.
DR   STRING; 9986.ENSOCUP00000013124; -.
DR   GeneID; 100009239; -.
DR   CTD; 51268; -.
DR   InParanoid; P79371; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0050031; F:L-pipecolate oxidase activity; ISS:UniProtKB.
DR   GO; GO:0008115; F:sarcosine oxidase activity; ISS:UniProtKB.
DR   GO; GO:0033514; P:L-lysine catabolic process to acetyl-CoA via L-pipecolate; ISS:UniProtKB.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR045170; MTOX.
DR   InterPro; IPR006281; SoxA_mon.
DR   NCBIfam; TIGR01377; soxA_mon; 1.
DR   PANTHER; PTHR10961; PEROXISOMAL SARCOSINE OXIDASE; 1.
DR   PANTHER; PTHR10961:SF7; PEROXISOMAL SARCOSINE OXIDASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   1: Evidence at protein level;
KW   Acetylation; FAD; Flavoprotein; Oxidoreductase; Peroxisome;
KW   Reference proteome.
FT   CHAIN           1..390
FT                   /note="Peroxisomal sarcosine oxidase"
FT                   /id="PRO_0000213775"
FT   MOTIF           388..390
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         319
FT                   /note="S-8alpha-FAD cysteine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   390 AA;  44122 MW;  E8715FEB607A4335 CRC64;
     MAAQKDLWDA IVIGAGIQGC FTVYHLVKHR KRILLLEQFF LPHSRGSSHG QSRIIRKAYL
     EDFYTRMMHE CYQIWAQLEH EAGTQLHRQT GLLLLGMKEN QELKTIQANL SRQRVEHQCL
     SSEELKQRFP NIRLPRGEVG LLDNSGGVIY AYKALRALQD AIRQLGGIVR DGEKVVEINP
     GLLVTVKTTS RSYQAKSLVI TAGPWTNQLL RPLGIEMPLQ TLRINVCYWR EMVPGSYGVS
     QAFPCFLWLG LCPHHIYGLP TGEYPGLMKV SYHHGNHADP EERDCPTART DIGDVQILSS
     FVRDHLPDLK PEPAVIESCM YTNTPDEQFI LDRHPKYDNI VIGAGFSGHG FKLAPVVGKI
     LYELSMKLTP SYDLAPFRIS RFPSLGKAHL
//