SOX_RABIT
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 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; 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 GeneID; 100009239; -.
DR KEGG; ocu: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; 3.50.50.60; -; 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 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
