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Database: UniProt
Entry: Q0SBI1_RHOJR
LinkDB: Q0SBI1_RHOJR
Original site: Q0SBI1_RHOJR 
ID   Q0SBI1_RHOJR            Unreviewed;       378 AA.
AC   Q0SBI1;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   SubName: Full=Sarcosine oxidase {ECO:0000313|EMBL:ABG95105.1};
DE            EC=1.5.3.1 {ECO:0000313|EMBL:ABG95105.1};
GN   Name=soxA2 {ECO:0000313|EMBL:ABG95105.1};
GN   OrderedLocusNames=RHA1_ro03302 {ECO:0000313|EMBL:ABG95105.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG95105.1, ECO:0000313|Proteomes:UP000008710};
RN   [1] {ECO:0000313|Proteomes:UP000008710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP000431; ABG95105.1; -; Genomic_DNA.
DR   RefSeq; WP_011595951.1; NC_008268.1.
DR   AlphaFoldDB; Q0SBI1; -.
DR   KEGG; rha:RHA1_ro03302; -.
DR   PATRIC; fig|101510.16.peg.3327; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_2_1_11; -.
DR   OrthoDB; 9806452at2; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0008115; F:sarcosine oxidase activity; IEA:UniProtKB-EC.
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   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   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:ABG95105.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT   DOMAIN          8..358
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   378 AA;  40794 MW;  EB5E8B9AFF911776 CRC64;
     MTTTRTGVAV IGTGTMGSAI MWRLSERGVP AVGLEQFTPG HDRGSGHGES RIFRTAYHED
     PAYVPMLRAA LRGWRELGEQ TGEPVLTMTG GLSIGPSTGV IVGGSLEAAK VHALTQEILD
     PAEFATRFPT QRLREGDTAI WEKDAGVIRP ELAITGAARR ACELGASVRP ESRVLNIEDG
     PGDTVLVRLD DEVIRADHVV VAAGAWIPGL LPAAQLPLTV ERKILAWFPA EDPTQFGPDR
     FPVFLRDSPE GTWYGFPSMD GKTVKIALHL GGRETDPDEL DRVVHDEDTA PLRDLVRRYL
     PGLGSRPVRA AVCMYTNTPD GHFVIGNPPA YRNVTVISAC SGHGFKFAPV IGEIAADLSC
     GSTPEFPLEL FDVNRFAD
//
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