MSOX_BACSN
ID MSOX_BACSN Reviewed; 387 AA.
AC P23342;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Monomeric sarcosine oxidase;
DE Short=MSOX;
DE EC=1.5.3.1;
GN Name=soxA;
OS Bacillus sp. (strain NS-129).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1419;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-34.
RX PubMed=1368683; DOI=10.1271/bbb1961.55.1259;
RA Koyama Y., Yamamoto-Otake H., Suzuki M., Nakano E.;
RT "Cloning and expression of the sarcosine oxidase gene from Bacillus sp. NS-
RT 129 in Escherichia coli.";
RL Agric. Biol. Chem. 55:1259-1263(1991).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 2-387 IN COMPLEX WITH FAD.
RX DOI=10.2183/pjab.81.220;
RA Nagata K., Sasaki H., Ohtsuka J., Hua M., Okai M., Kubota K., Kamo M.,
RA Ito K., Ichikawa T., Koyama Y., Tanokura M.;
RT "Crystal structure of monomeric sarcosine oxidase from Bacillus sp. NS-129
RT reveals multiple conformations at the active-site loop.";
RL Proc. Jpn. Acad. 81:220-224(2005).
CC -!- FUNCTION: Catalyzes the oxidative demethylation of sarcosine.
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per subunit.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By sarcosine.
CC -!- SIMILARITY: Belongs to the MSOX/MTOX family. MSOX subfamily.
CC {ECO:0000305}.
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DR EMBL; D10553; BAA01410.1; -; Genomic_DNA.
DR PIR; JU0461; JU0461.
DR PDB; 1ZOV; X-ray; 1.86 A; A/B=2-387.
DR PDBsum; 1ZOV; -.
DR AlphaFoldDB; P23342; -.
DR SMR; P23342; -.
DR EvolutionaryTrace; P23342; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0008115; F:sarcosine oxidase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; -; 1.
DR HAMAP; MF_00516; MSOX; 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 3D-structure; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein;
KW Oxidoreductase.
FT CHAIN 1..387
FT /note="Monomeric sarcosine oxidase"
FT /id="PRO_0000213761"
FT BINDING 6..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT MOD_RES 316
FT /note="S-8alpha-FAD cysteine"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:1ZOV"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:1ZOV"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1ZOV"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1ZOV"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:1ZOV"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:1ZOV"
FT HELIX 62..79
FT /evidence="ECO:0007829|PDB:1ZOV"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1ZOV"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:1ZOV"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:1ZOV"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:1ZOV"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:1ZOV"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:1ZOV"
FT HELIX 150..163
FT /evidence="ECO:0007829|PDB:1ZOV"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:1ZOV"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:1ZOV"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:1ZOV"
FT STRAND 191..200
FT /evidence="ECO:0007829|PDB:1ZOV"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:1ZOV"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:1ZOV"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:1ZOV"
FT STRAND 220..229
FT /evidence="ECO:0007829|PDB:1ZOV"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:1ZOV"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:1ZOV"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:1ZOV"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:1ZOV"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:1ZOV"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:1ZOV"
FT HELIX 290..302
FT /evidence="ECO:0007829|PDB:1ZOV"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:1ZOV"
FT STRAND 310..320
FT /evidence="ECO:0007829|PDB:1ZOV"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:1ZOV"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:1ZOV"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:1ZOV"
FT HELIX 351..364
FT /evidence="ECO:0007829|PDB:1ZOV"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:1ZOV"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:1ZOV"
SQ SEQUENCE 387 AA; 42873 MW; 7A960CC422841F98 CRC64;
MSTHFDVIVV GAGSMGMAAG YYLAKQGVKT LLVDSFDPPH TNGSHHGDTR IIRHAYGEGR
EYVPFALRAQ ELWYELEKET HHKIFTQTGV LVYGPKGGSA FVSETMEAAN IHSLEHELFE
GKQLTDRWAG VEVPDNYEAI FEPNSGVLFS ENCIQAYREL AEAHGATVLT YTPVEDFEVT
EDLVTIKTAK GSYTANKLVV SMGAWNSKLL SKLDVEIPLQ PYRQVVGFFE CDEAKYSNNA
HYPAFMVEVE NGIYYGFPSF GGSGLKIGYH SYGQQIDPDT INREFGAYPE DEANLRKFLE
QYMPGANGEL KKGAVCMYTK TPDEHFVIDL HPKYSNVAIA AGFSGHGFKF SSVVGETLAQ
LATTGKTEHD ISIFSLNRDA LKKEAVK
