ID A8GD05_SERP5 Unreviewed; 371 AA.
AC A8GD05;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=N-methyl-L-tryptophan oxidase {ECO:0000256|HAMAP-Rule:MF_00515};
DE Short=MTOX {ECO:0000256|HAMAP-Rule:MF_00515};
DE EC=1.5.3.- {ECO:0000256|HAMAP-Rule:MF_00515};
GN Name=solA {ECO:0000256|HAMAP-Rule:MF_00515};
GN OrderedLocusNames=Spro_1892 {ECO:0000313|EMBL:ABV40995.1};
OS Serratia proteamaculans (strain 568).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=399741 {ECO:0000313|EMBL:ABV40995.1};
RN [1] {ECO:0000313|EMBL:ABV40995.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=568 {ECO:0000313|EMBL:ABV40995.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxidative demethylation of N-methyl-L-
CC tryptophan. {ECO:0000256|HAMAP-Rule:MF_00515}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(alpha)-methyl-L-tryptophan + O2 = formaldehyde + H2O2
CC + L-tryptophan; Xref=Rhea:RHEA:28006, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16842,
CC ChEBI:CHEBI:57283, ChEBI:CHEBI:57912; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00515};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00515};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|HAMAP-Rule:MF_00515};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00515}.
CC -!- SIMILARITY: Belongs to the MSOX/MTOX family. MTOX subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00515}.
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DR EMBL; CP000826; ABV40995.1; -; Genomic_DNA.
DR AlphaFoldDB; A8GD05; -.
DR STRING; 399741.Spro_1892; -.
DR KEGG; spe:Spro_1892; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_2_1_6; -.
DR OrthoDB; 9806257at2; -.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0050131; F:N-methyl-L-amino-acid oxidase activity; IEA:InterPro.
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 HAMAP; MF_00515; MTOX; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023493; Me_Trp_Oxase_MTOX.
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 3: Inferred from homology;
KW FAD {ECO:0000256|HAMAP-Rule:MF_00515};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00515};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00515,
KW ECO:0000313|EMBL:ABV40995.1}.
FT DOMAIN 4..350
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT BINDING 4..34
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00515"
FT MOD_RES 307
FT /note="S-8alpha-FAD cysteine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00515"
SQ SEQUENCE 371 AA; 40539 MW; 370E0B1567929393 CRC64;
MEYDLIVVGS GSVGAAAGYY ATRAGLKVLM IDSAMPPHRN GSHHGDTRII RHAYGEGEKY
VPLILRAQAL WNALIKQTGE ELFQDCGVLN MGPLDSEFIN NAQHSAQKFR LNTQSLSAEQ
INQRWPEFNA PEGYVGVFEP DAGFLRSELA VASFIKLAKD AGCGQLFNCP VSAVQPIDGG
VEVITPEGRF QGRKAVVTAG TWVKTLLPQL PIAPLRKVFS WHQADGRYSV NNRFPAFTVE
AQDGNHYYGF PADNDGLKVG KHDGGQPMET PEQRKPFGSF TTDGTEVFHF LRQFLPGVGV
CLHGEACSYD MSPDEDFIID TLPGCDRLMV ISGLSGHGFK FASVLGEIAA LFAEDKTPPV
DITPFSLKRF I
//
