ID   MNO_RHOER               Reviewed;         423 AA.
AC   Q53062; P81938;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Methanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase {ECO:0000303|PubMed:7575099};
DE            Short=MNO {ECO:0000303|PubMed:7575099};
DE            EC=1.1.99.37 {ECO:0000250|UniProtKB:C5MRT8};
DE   AltName: Full=Methanol dehydrogenase (nicotinoprotein) {ECO:0000305};
DE   AltName: Full=Methanol:NDMA oxidoreductase {ECO:0000250|UniProtKB:C5MRT8};
GN   Name=thcE;
OS   Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC   Rhodococcus erythropolis group.
OX   NCBI_TaxID=1833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19; 88-105 AND
RP   180-195, AND INDUCTION.
RC   STRAIN=NI86/21;
RX   PubMed=7575099; DOI=10.1007/bf00272133;
RA   Nagy I., Verheijen S., De Schrijver A., Van Damme J., Proost P.,
RA   Schoofs G., Vanderleyden J., De Mot R.;
RT   "Characterization of the Rhodococcus sp. NI86/21 gene encoding
RT   alcohol:N,N'-dimethyl-4-nitrosoaniline oxidoreductase inducible by atrazine
RT   and thiocarbamate herbicides.";
RL   Arch. Microbiol. 163:439-446(1995).
CC   -!- FUNCTION: Catalyzes the oxidation of methanol to yield formaldehyde.
CC       While the in vivo electron acceptor is not known, N,N-dimethyl-4-
CC       nitrosoaniline (NDMA) can serve this function in vitro and is reduced
CC       to 4-(hydroxylamino)-N,N-dimethylaniline.
CC       {ECO:0000250|UniProtKB:C5MRT8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + methanol = AH2 + formaldehyde; Xref=Rhea:RHEA:33571,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:16842, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:17790; EC=1.1.99.37;
CC         Evidence={ECO:0000250|UniProtKB:C5MRT8};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9RCG0};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q9RCG0};
CC   -!- COFACTOR:
CC       Name=NADPH; Xref=ChEBI:CHEBI:57783;
CC         Evidence={ECO:0000250|UniProtKB:Q9RCG0};
CC   -!- SUBUNIT: Homodecamer. {ECO:0000250|UniProtKB:Q9RCG0}.
CC   -!- INDUCTION: Expressed during degradation of thiocarbamates and atrazine.
CC       {ECO:0000269|PubMed:7575099}.
CC   -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U21071; AAB80771.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q53062; -.
DR   SMR; Q53062; -.
DR   STRING; 1833.XU06_08765; -.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0070402; F:NADPH binding; ISS:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0015946; P:methanol oxidation; ISS:UniProtKB.
DR   InterPro; IPR001670; ADH_Fe/GldA.
DR   InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR   InterPro; IPR026338; NDMA_methanol_DH.
DR   PANTHER; PTHR11496; PTHR11496; 1.
DR   Pfam; PF00465; Fe-ADH; 1.
DR   TIGRFAMs; TIGR04266; NDMA_methanol; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Magnesium; Methanol utilization; NADP;
KW   Oxidoreductase; Zinc.
FT   CHAIN           1..423
FT                   /note="Methanol:N,N-dimethyl-4-nitrosoaniline
FT                   oxidoreductase"
FT                   /id="PRO_0000247755"
SQ   SEQUENCE   423 AA;  46356 MW;  5DB811D6BFDDA820 CRC64;
     AIELNQIWDF PIKEFHPFPR ALMGVGAHDI IGVEAKNLGF KRTLLMTTGL RGSGIIEELV
     GKIEYQGVEV VLYDKVESNP KDYNVMEAAA LYQKEKCDSI ISIGGGSSHD AAKGARVVIA
     HDGRNINEFE GFAKSTNKEN PPHIAVSTTA GTGSETSWAY VITDTSDMNN PHKWVGFDEA
     TIVTLAIDDP LLYYTCPQHF TAYCGFDVLA HGSEPFVSRL DFAPSLGNAI YSVELVAKNL
     REAVFEPRNL KAREGMMNAQ YIAGQAFNSG GLGIVHSISH AVSAFFDSHH GLNNAIALPR
     VWEYNLPSRY ERYAQLAGAL GVDTRNLTTV QAADAAVEAA IRLAKDVGIP DNFGQVRTDS
     YAKNQMNTKK YEGRGDVIKG DEKTVRAISE HIQDDWCTPG NPREVTVESM IPVVDHAINK
     SYF