ID   DHM2_PARDE              Reviewed;         103 AA.
AC   P29898;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 100.
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   Paracoccus denitrificans.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=266;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1657871; DOI=10.1128/jb.173.21.6948-6961.1991;
RA   van Spanning R.J.M., Wansell C.W., de Boer T., Hazelaar M.J., Anazawa H.,
RA   Harms N., Oltmann L.F., Stouthamer A.H.;
RT   "Isolation and characterization of the moxJ, moxG, moxI, and moxR genes of
RT   Paracoccus denitrificans: inactivation of moxJ, moxG, and moxR and the
RT   resultant effect on methylotrophic growth.";
RL   J. Bacteriol. 173:6948-6961(1991).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 21-103 IN COMPLEX WITH ALPHA
RP   SUBUNIT, SUBUNIT, AND DISULFIDE BOND.
RX   PubMed=14505072; DOI=10.1007/s00775-003-0485-0;
RA   Xia Z.-X., Dai W.W., He Y.-N., White S.A., Mathews F.S., Davidson V.L.;
RT   "X-ray structure of methanol dehydrogenase from Paracoccus denitrificans
RT   and molecular modeling of its interactions with cytochrome c-551i.";
RL   J. Biol. Inorg. Chem. 8:843-854(2003).
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       {ECO:0000269|PubMed:14505072}.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the methanol dehydrogenase subunit 2 family.
CC       {ECO:0000305}.
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DR   EMBL; M57684; AAA25584.1; -; Genomic_DNA.
DR   PIR; C41377; C41377.
DR   RefSeq; WP_010399081.1; NZ_FOYK01000012.1.
DR   PDB; 1LRW; X-ray; 2.50 A; B/D=21-103.
DR   PDBsum; 1LRW; -.
DR   AlphaFoldDB; P29898; -.
DR   SMR; P29898; -.
DR   OMA; PGNCWEP; -.
DR   BioCyc; MetaCyc:MON-3924; -.
DR   EvolutionaryTrace; P29898; -.
DR   GO; GO:0042597; C:periplasmic space; 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; Disulfide bond; Methanol utilization; Oxidoreductase;
KW   Periplasm; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..103
FT                   /note="Methanol dehydrogenase [cytochrome c] subunit 2"
FT                   /id="PRO_0000025571"
FT   DISULFID        26..32
FT                   /evidence="ECO:0000269|PubMed:14505072"
FT   HELIX           54..57
FT                   /evidence="ECO:0007829|PDB:1LRW"
FT   HELIX           59..81
FT                   /evidence="ECO:0007829|PDB:1LRW"
FT   HELIX           88..90
FT                   /evidence="ECO:0007829|PDB:1LRW"
SQ   SEQUENCE   103 AA;  11458 MW;  7AF8E6BD3B8731AA CRC64;
     MKRILTLTVA ALALGTPALA YDGTNCKAPG NCWEPKPDYP AKVEGSKYDP QHDPAELSKQ
     GESLAVMDAR NEWRVWNMKK TGKFEYDVKK IDGYDETKAP PAE