MSOX_ARTST
ID MSOX_ARTST Reviewed; 389 AA.
AC P40873; O66180;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Monomeric sarcosine oxidase;
DE Short=MSOX;
DE EC=1.5.3.1;
GN Name=soxA;
OS Arthrobacter sp. (strain TE1826).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=68999;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-6.
RA Nishiya Y., Imanaka T.;
RT "Cloning and sequencing of the sarcosine oxidase gene from Arthrobacter sp.
RT TE1826.";
RL J. Ferment. Bioeng. 75:239-244(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9563845; DOI=10.1007/s004380050685;
RA Nishiya Y., Toda A., Imanaka T.;
RT "Gene cluster for creatinine degradation in Arthrobacter sp. TE1826.";
RL Mol. Gen. Genet. 257:581-586(1998).
RN [3]
RP MUTAGENESIS OF CYS-265 AND CYS-318.
RX PubMed=7887617; DOI=10.1128/aem.61.1.367-370.1995;
RA Nishiya Y., Zuihara S., Imanaka T.;
RT "Active site analysis and stabilization of sarcosine oxidase by the
RT substitution of cysteine residues.";
RL Appl. Environ. Microbiol. 61:367-370(1995).
RN [4]
RP MUTAGENESIS OF GLY-13; ALA-14; GLY-15; SER-16; MET-17; GLY-18 AND ASP-36.
RX PubMed=8779579; DOI=10.1128/aem.62.7.2405-2410.1996;
RA Nishiya Y., Imanaka T.;
RT "Analysis of interaction between the Arthrobacter sarcosine oxidase and the
RT coenzyme flavin adenine dinucleotide by site-directed mutagenesis.";
RL Appl. Environ. Microbiol. 62:2405-2410(1996).
RN [5]
RP MUTAGENESIS OF CYS-318.
RX PubMed=11035956; DOI=10.1006/prep.2000.1299;
RA Nishiya Y.;
RT "A mutant sarcosine oxidase in which activity depends on flavin adenine
RT dinucleotide.";
RL Protein Expr. Purif. 20:95-97(2000).
CC -!- FUNCTION: Catalyzes the oxidative demethylation of sarcosine.
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Decreases in function by replacement in the G-X-G-X-X-G
CC motif are suppressed by chloride or bromide ion.
CC -!- SIMILARITY: Belongs to the MSOX/MTOX family. MSOX subfamily.
CC {ECO:0000305}.
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DR EMBL; D63413; BAA09716.1; -; Genomic_DNA.
DR EMBL; AB007122; BAA25926.1; -; Genomic_DNA.
DR PIR; T44248; T44248.
DR AlphaFoldDB; P40873; -.
DR SMR; P40873; -.
DR BioCyc; MetaCyc:MON-11002; -.
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 Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.1"
FT CHAIN 2..389
FT /note="Monomeric sarcosine oxidase"
FT /id="PRO_0000213760"
FT BINDING 8..38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT MOD_RES 318
FT /note="S-8alpha-FAD cysteine"
FT /evidence="ECO:0000305"
FT MUTAGEN 13
FT /note="G->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8779579"
FT MUTAGEN 14
FT /note="A->D,K: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8779579"
FT MUTAGEN 14
FT /note="A->I,V: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:8779579"
FT MUTAGEN 14
FT /note="A->L,W,Y: Weak activity."
FT /evidence="ECO:0000269|PubMed:8779579"
FT MUTAGEN 15
FT /note="G->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8779579"
FT MUTAGEN 16
FT /note="S->P: Weak activity. Loss of activity; when
FT associated with G-17."
FT /evidence="ECO:0000269|PubMed:8779579"
FT MUTAGEN 17
FT /note="M->G: Weak activity. Loss of activity; when
FT associated with P-16."
FT /evidence="ECO:0000269|PubMed:8779579"
FT MUTAGEN 18
FT /note="G->A: Weak activity."
FT /evidence="ECO:0000269|PubMed:8779579"
FT MUTAGEN 36
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8779579"
FT MUTAGEN 36
FT /note="D->E: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:8779579"
FT MUTAGEN 36
FT /note="D->N: 100-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:8779579"
FT MUTAGEN 265
FT /note="C->A,D: Decrease in activity. Stabilizes SoxA
FT against chemicals and metal ions."
FT /evidence="ECO:0000269|PubMed:7887617"
FT MUTAGEN 265
FT /note="C->R,S: Almost no change in activity. Stabilizes
FT SoxA against chemicals and metal ions."
FT /evidence="ECO:0000269|PubMed:7887617"
FT MUTAGEN 318
FT /note="C->S: Weak activity."
FT /evidence="ECO:0000269|PubMed:11035956,
FT ECO:0000269|PubMed:7887617"
FT CONFLICT 39
FT /note="H -> D (in Ref. 2; BAA09716/BAA25926)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="D -> A (in Ref. 2; BAA09716/BAA25926)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 389 AA; 43294 MW; 77437C4F12B4AC7F CRC64;
MSIKKDYDVI VVGAGSMGMA AGYYLSKQGV KTLLVDSFHP PHTNGSHHGD TRIIRHAYGE
GREYVPFALR AQELWYELEK ETHHKIFTKT GVLVFGPKGE APFVAETMEA AKEHSLDVDL
LEGSEINKRW PGVTVPENYN AIFEKNSGVL FSENCIRAYR ELAEANGAKV LTYTPVEDFE
IAEDFVKIQT AYGSFTASKL IVSMGAWNSK LLSKLNIEIP LQPYRQVVGF FECDEKKYSN
THGYPAFMVE VPTGIYYGFP SFGGCGLKIG YHTYGQKIDP DTINREFGIY PEDEGNIRKF
LETYMPGATG ELKSGDVCMY TKTPDEHFVI DLHPQFSNVA IAAGFSGHGF KFSSVVGETL
SQLAVTGKTE HDISIFSINR PALKQKETI
