ID   MNO_MYCS8               Reviewed;         423 AA.
AC   C5MRT8;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=Methanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase {ECO:0000303|PubMed:19875438};
DE            Short=MDO {ECO:0000303|PubMed:19875438};
DE            EC=1.1.99.37 {ECO:0000269|PubMed:19875438};
DE   AltName: Full=Methanol dehydrogenase (nicotinoprotein) {ECO:0000305};
DE   AltName: Full=Methanol:NDMA oxidoreductase {ECO:0000303|PubMed:19875438};
OS   Mycobacterium sp. (strain DSM 3803 / JC1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=212194;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP   PHENOTYPE, INDUCTION, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=DSM 3803 / JC1;
RX   PubMed=19875438; DOI=10.1099/mic.0.034124-0;
RA   Park H., Lee H., Ro Y.T., Kim Y.M.;
RT   "Identification and functional characterization of a gene for the methanol:
RT   N,N'-dimethyl-4-nitrosoaniline oxidoreductase from Mycobacterium sp. strain
RT   JC1 (DSM 3803).";
RL   Microbiology 156:463-471(2010).
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. It is also able to use
CC       ethanol and formaldehyde with an activity comparable to methanol, and
CC       has a weak activity with methylamine as substrate.
CC       {ECO:0000269|PubMed:19875438}.
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:0000269|PubMed:19875438};
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: Constitutively expressed, with a significant increase of
CC       induction in the presence of methanol. {ECO:0000269|PubMed:19875438}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not grow on methanol.
CC       {ECO:0000269|PubMed:19875438}.
CC   -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; GQ161965; ACS29499.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5MRT8; -.
DR   SMR; C5MRT8; -.
DR   KEGG; ag:ACS29499; -.
DR   BioCyc; MetaCyc:MON-15637; -.
DR   BRENDA; 1.1.99.37; 3490.
DR   BRENDA; 1.2.98.1; 3490.
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; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0015946; P:methanol oxidation; IDA: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   Magnesium; Methanol utilization; NADP; Oxidoreductase; Zinc.
FT   CHAIN           1..423
FT                   /note="Methanol:N,N-dimethyl-4-nitrosoaniline
FT                   oxidoreductase"
FT                   /id="PRO_0000431561"
SQ   SEQUENCE   423 AA;  46223 MW;  E95BA3A9A50BB32B CRC64;
     MAIELNQIWD FPIKEFHPFP RALLGVGAHD IIGVEAKNLG FKRTLLMTTG LRGSGIIEEL
     TGKIEYQGVE VVLYDKVESN PKDYNVMEAA ALYQQERCDS IISIGGGSSH DAAKGARVVI
     AHDGRNINEF EGFAKSTNKQ NPPHIAVSTT AGTGSETSWA YVITDTSDME HPHKWVGFDE
     ATIVTLAIDD PLLYYTCPQH FTAYCGFDVL AHGSEPYVSR LDFAPSLGNA LYSVELVAKH
     LREAVFEPRN LKAREGMMNA QYIAGQAFNS GGLGIVHSIS HAVSAFFDSH HGLNNAIALP
     RVWEYNLPSR YERYAQLATA MGVDTRNMTT VQAADAAVEA AIRLSQDVGI PDNFSQVRVD
     SYDKNRMNTG KYAGKGEVIK GDDKSVLAIS EHIQGDWCTP GNPREVTVDS MIPVVGHAIN
     GTY