ID   DHM2_METME              Reviewed;          91 AA.
AC   P38540; Q59541;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2002, sequence version 2.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Methanol dehydrogenase [cytochrome c] subunit 2;
DE            EC=1.1.2.7;
DE   AltName: Full=MDH small subunit beta;
DE   AltName: Full=MDH-associated peptide;
DE   AltName: Full=MEDH;
DE   Flags: Precursor;
GN   Name=moxI;
OS   Methylophilus methylotrophus (Bacterium W3A1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylophilus.
OX   NCBI_TaxID=17;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (2.4
RP   ANGSTROMS).
RX   PubMed=8676383; DOI=10.1006/jmbi.1996.0334;
RA   Xia Z.-X., Dai W.-W., Zhang Y.-F., White S.A., Boyd G.D., Mathews F.S.;
RT   "Determination of the gene sequence and the three-dimensional structure at
RT   2.4 angstroms resolution of methanol dehydrogenase from Methylophilus
RT   W3A1.";
RL   J. Mol. Biol. 259:480-501(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 23-53.
RC   STRAIN=ATCC 53528 / AS1 / DSM 46235 / LMG 6787 / NCIMB 10515;
RX   PubMed=1311606; DOI=10.1016/0167-4838(92)90240-e;
RA   Cox J.M., Day D.J., Anthony C.;
RT   "The interaction of methanol dehydrogenase and its electron acceptor,
RT   cytochrome cL in methylotrophic bacteria.";
RL   Biochim. Biophys. Acta 1119:97-106(1992).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX   PubMed=8241148; DOI=10.1021/bi00211a002;
RA   White S.A., Boyd G.D., Mathews F.S., Xia Z.-X., Dai W.-W., Zhang Y.-F.,
RA   Davidson V.L.;
RT   "The active site structure of the calcium-containing quinoprotein methanol
RT   dehydrogenase.";
RL   Biochemistry 32:12955-12958(1993).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX   PubMed=1331050; DOI=10.1016/s0021-9258(18)41668-7;
RA   Xia Z.-X., Dai W.-W., Xiong J.-P., Hao Z.-P., Davidson V.L., White S.A.,
RA   Mathews F.S.;
RT   "The three-dimensional structures of methanol dehydrogenase from two
RT   methylotrophic bacteria at 2.6-A resolution.";
RL   J. Biol. Chem. 267:22289-22297(1992).
CC   -!- FUNCTION: Catalyzes the oxidation of primary alcohols including
CC       methanol. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + 2 Fe(III)-[cytochrome cL] = an aldehyde +
CC         2 Fe(II)-[cytochrome cL] + 2 H(+); Xref=Rhea:RHEA:51004, Rhea:RHEA-
CC         COMP:12863, Rhea:RHEA-COMP:12864, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034; EC=1.1.2.7;
CC   -!- SUBUNIT: Heterotetramer composed of 2 alpha and 2 beta subunits.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein;
CC       Periplasmic side. Note=Periplasmic, but associated with inner membrane.
CC   -!- SIMILARITY: Belongs to the methanol dehydrogenase subunit 2 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA83766.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U41041; AAA83766.1; ALT_INIT; Genomic_DNA.
DR   PDB; 1G72; X-ray; 1.90 A; B/D=23-91.
DR   PDB; 2AD6; X-ray; 1.50 A; B/D=23-91.
DR   PDB; 2AD7; X-ray; 1.50 A; B/D=23-91.
DR   PDB; 2AD8; X-ray; 1.60 A; B/D=23-91.
DR   PDB; 4AAH; X-ray; 2.40 A; B/D=23-91.
DR   PDBsum; 1G72; -.
DR   PDBsum; 2AD6; -.
DR   PDBsum; 2AD7; -.
DR   PDBsum; 2AD8; -.
DR   PDBsum; 4AAH; -.
DR   AlphaFoldDB; P38540; -.
DR   SMR; P38540; -.
DR   STRING; 1122236.KB905142_gene324; -.
DR   BRENDA; 1.1.2.7; 3319.
DR   BRENDA; 1.2.2.B2; 3319.
DR   SABIO-RK; P38540; -.
DR   EvolutionaryTrace; P38540; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0052933; F:alcohol dehydrogenase (cytochrome c(L)) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0015946; P:methanol oxidation; IEA:InterPro.
DR   Gene3D; 4.10.160.10; -; 1.
DR   InterPro; IPR003420; Meth_DH_bsu.
DR   InterPro; IPR036557; Meth_DH_bsu_sf.
DR   Pfam; PF02315; MDH; 1.
DR   PIRSF; PIRSF029163; Meth_DH_beta; 1.
DR   SUPFAM; SSF48666; SSF48666; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane;
KW   Direct protein sequencing; Disulfide bond; Membrane; Methanol utilization;
KW   Oxidoreductase; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:1311606"
FT   CHAIN           23..91
FT                   /note="Methanol dehydrogenase [cytochrome c] subunit 2"
FT                   /id="PRO_0000025570"
FT   DISULFID        28..34
FT   CONFLICT        27
FT                   /note="N -> T (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        31
FT                   /note="P -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        37
FT                   /note="N -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           56..59
FT                   /evidence="ECO:0007829|PDB:2AD6"
FT   HELIX           61..83
FT                   /evidence="ECO:0007829|PDB:2AD6"
SQ   SEQUENCE   91 AA;  10037 MW;  0123300087E6716A CRC64;
     MKHVLTLLAL ASVFAVSNQA LAYDGQNCKE PGNCWENKPG YPEKIAGSKY DPKHDPVELN
     KQEESIKAMD ARNAKRIANA KSSGNFVFDV K