MSOX_BACB0
ID MSOX_BACB0 Reviewed; 390 AA.
AC P40859;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Monomeric sarcosine oxidase;
DE Short=MSOX;
DE EC=1.5.3.1;
GN Name=soxA; Synonyms=sox;
OS Bacillus sp. (strain B-0618).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=69000;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Suzuki K., Sagai H., Imamura S., Sugiyama M.;
RT "Cloning, sequencing, overexpression in Escherichia coil of a sarcosine
RT oxidase-encoding gene linked to the Bacillus creatinase gene.";
RL J. Ferment. Bioeng. 77:231-234(1994).
RN [2]
RP SEQUENCE REVISION TO 117.
RA Suzuki K.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CHARACTERIZATION, PROTEIN SEQUENCE OF 313-319, AND MASS SPECTROMETRY.
RX PubMed=10220347; DOI=10.1021/bi982955o;
RA Wagner M.A., Khanna P., Jorns M.S.;
RT "Structure of the flavocoenzyme of two homologous amine oxidases: monomeric
RT sarcosine oxidase and N-methyltryptophan oxidase.";
RL Biochemistry 38:5588-5595(1999).
RN [4]
RP CHARACTERIZATION.
RX PubMed=10913293; DOI=10.1021/bi000350y;
RA Wagner M.A., Jorns M.S.;
RT "Monomeric sarcosine oxidase: 2. Kinetic studies with sarcosine, alternate
RT substrates, and a substrate analogue.";
RL Biochemistry 39:8825-8829(2000).
RN [5]
RP CHARACTERIZATION.
RX PubMed=11087383; DOI=10.1021/bi001421w;
RA Zhao G., Qu J., Davis F.A., Jorns M.S.;
RT "Inactivation of monomeric sarcosine oxidase by reaction with N-
RT (cyclopropyl)glycine.";
RL Biochemistry 39:14341-14347(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=10368302; DOI=10.1016/s0969-2126(99)80043-4;
RA Trickey P., Wagner M.A., Jorns M.S., Mathews F.S.;
RT "Monomeric sarcosine oxidase: structure of a covalently flavinylated amine
RT oxidizing enzyme.";
RL Structure 7:331-345(1999).
CC -!- FUNCTION: Catalyzes the oxidative demethylation of sarcosine. Can also
CC oxidize other secondary amino acids such as N-methyl-L-alanine.
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 -!- ACTIVITY REGULATION: Pyrrole-2-carboxylate is a competitive inhibitor.
CC N-(cyclopropyl)glycine (CPG) is a mechanism-based inhibitor and
CC inactivates the enzyme by covalently modifying the flavin.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MASS SPECTROMETRY: Mass=43839; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10220347};
CC -!- SIMILARITY: Belongs to the MSOX/MTOX family. MSOX subfamily.
CC {ECO:0000305}.
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DR EMBL; D16521; BAA03967.1; -; Genomic_DNA.
DR PIR; I39975; I39975.
DR PDB; 1EL5; X-ray; 1.80 A; A/B=2-390.
DR PDB; 1EL7; X-ray; 1.90 A; A/B=2-390.
DR PDB; 1EL8; X-ray; 1.90 A; A/B=2-390.
DR PDB; 1EL9; X-ray; 2.00 A; A/B=2-390.
DR PDB; 1ELI; X-ray; 2.00 A; A/B=2-390.
DR PDB; 1L9C; X-ray; 1.90 A; A/B=2-390.
DR PDB; 1L9D; X-ray; 1.95 A; A/B=2-390.
DR PDB; 1L9E; X-ray; 1.85 A; A/B=2-390.
DR PDB; 2A89; X-ray; 1.85 A; A/B=2-390.
DR PDB; 2GB0; X-ray; 1.85 A; A/B=2-390.
DR PDB; 2GF3; X-ray; 1.30 A; A/B=2-390.
DR PDB; 3BHF; X-ray; 2.10 A; A/B=1-390.
DR PDB; 3BHK; X-ray; 1.71 A; A/B=1-390.
DR PDB; 3M0O; X-ray; 1.60 A; A/B=2-390.
DR PDB; 3M12; X-ray; 1.60 A; A/B=2-390.
DR PDB; 3M13; X-ray; 2.10 A; A/B/C/D=2-382.
DR PDB; 3QSE; X-ray; 1.75 A; A/B=2-390.
DR PDB; 3QSM; X-ray; 1.90 A; A/B=2-390.
DR PDB; 3QSS; X-ray; 1.85 A; A/B=2-390.
DR PDBsum; 1EL5; -.
DR PDBsum; 1EL7; -.
DR PDBsum; 1EL8; -.
DR PDBsum; 1EL9; -.
DR PDBsum; 1ELI; -.
DR PDBsum; 1L9C; -.
DR PDBsum; 1L9D; -.
DR PDBsum; 1L9E; -.
DR PDBsum; 2A89; -.
DR PDBsum; 2GB0; -.
DR PDBsum; 2GF3; -.
DR PDBsum; 3BHF; -.
DR PDBsum; 3BHK; -.
DR PDBsum; 3M0O; -.
DR PDBsum; 3M12; -.
DR PDBsum; 3M13; -.
DR PDBsum; 3QSE; -.
DR PDBsum; 3QSM; -.
DR PDBsum; 3QSS; -.
DR AlphaFoldDB; P40859; -.
DR SMR; P40859; -.
DR DrugBank; DB03098; [Methylseleno]Acetate.
DR DrugBank; DB01918; [Methyltelluro]Acetate.
DR DrugBank; DB03517; [Methylthio]Acetate.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugBank; DB03366; Imidazole.
DR DrugBank; DB02083; N,N-dimethylglycine.
DR DrugBank; DB02543; Pyrrole-2-Carboxylate.
DR KEGG; ag:BAA03967; -.
DR BRENDA; 1.5.3.1; 691.
DR EvolutionaryTrace; P40859; -.
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..390
FT /note="Monomeric sarcosine oxidase"
FT /id="PRO_0000213762"
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 5..10
FT /evidence="ECO:0007829|PDB:2GF3"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:2GF3"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:2GF3"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:2GF3"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:2GF3"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:2GF3"
FT HELIX 63..79
FT /evidence="ECO:0007829|PDB:2GF3"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:2GF3"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:3M0O"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:2GF3"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:2GF3"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:2GF3"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:2GF3"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:2GF3"
FT HELIX 150..163
FT /evidence="ECO:0007829|PDB:2GF3"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:2GF3"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:2GF3"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:2GF3"
FT STRAND 191..200
FT /evidence="ECO:0007829|PDB:2GF3"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:2GF3"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:2GF3"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:2GF3"
FT STRAND 220..229
FT /evidence="ECO:0007829|PDB:2GF3"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:2GF3"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:2GF3"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:2GF3"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:2GF3"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:2GF3"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:2GF3"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:3BHF"
FT HELIX 290..302
FT /evidence="ECO:0007829|PDB:2GF3"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:2GF3"
FT STRAND 310..320
FT /evidence="ECO:0007829|PDB:2GF3"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:1L9E"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:2GF3"
FT STRAND 334..341
FT /evidence="ECO:0007829|PDB:2GF3"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:2GF3"
FT HELIX 351..364
FT /evidence="ECO:0007829|PDB:2GF3"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:2GF3"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:2GF3"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:2GB0"
SQ SEQUENCE 390 AA; 43182 MW; D830491B80230BCF CRC64;
MSTHFDVIVV GAGSMGMAAG YQLAKQGVKT LLVDAFDPPH TNGSHHGDTR IIRHAYGEGR
EYVPLALRSQ ELWYELEKET HHKIFTKTGV LVFGPKGESA FVAETMEAAK EHSLTVDLLE
GDEINKRWPG ITVPENYNAI FEPNSGVLFS ENCIRAYREL AEARGAKVLT HTRVEDFDIS
PDSVKIETAN GSYTADKLIV SMGAWNSKLL SKLNLDIPLQ PYRQVVGFFE SDESKYSNDI
DFPGFMVEVP NGIYYGFPSF GGCGLKLGYH TFGQKIDPDT INREFGVYPE DESNLRAFLE
EYMPGANGEL KRGAVCMYTK TLDEHFIIDL HPEHSNVVIA AGFSGHGFKF SSGVGEVLSQ
LALTGKTEHD ISIFSINRPA LKESLQKTTI
