DHM2_METEA
ID DHM2_METEA Reviewed; 96 AA.
AC P14775; C5AQA6;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 143.
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; Synonyms=mxaI; OrderedLocusNames=MexAM1_META1p4535;
OS Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS 9133 / AM1) (Methylobacterium extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=272630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2504152; DOI=10.1042/bj2600857;
RA Nunn D.N., Day D., Anthony C.;
RT "The second subunit of methanol dehydrogenase of Methylobacterium
RT extorquens AM1.";
RL Biochem. J. 260:857-862(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2842733; DOI=10.1093/nar/16.15.7722;
RA Nunn D.N., Anthony C.;
RT "The nucleotide sequence and deduced amino acid sequence of the genes for
RT cytochrome cL and a hypothetical second subunit of the methanol
RT dehydrogenase of Methylobacterium AM1.";
RL Nucleic Acids Res. 16:7722-7722(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA Lidstrom M.E.;
RT "Methylobacterium genome sequences: a reference blueprint to investigate
RT microbial metabolism of C1 compounds from natural and industrial sources.";
RL PLoS ONE 4:E5584-E5584(2009).
RN [4]
RP DISULFIDE BONDS.
RX PubMed=7656012; DOI=10.1038/nsb0294-102;
RA Blake C.C.F., Ghosh M., Harlos K., Avezoux A., Anthony C.;
RT "The active site of methanol dehydrogenase contains a disulphide bridge
RT between adjacent cysteine residues.";
RL Nat. Struct. Biol. 1:102-105(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS).
RX PubMed=7735834; DOI=10.1016/s0969-2126(01)00148-4;
RA Ghosh M., Anthony C., Harlos K., Goodwin M.G., Blake C.;
RT "The refined structure of the quinoprotein methanol dehydrogenase from
RT Methylobacterium extorquens at 1.94 A.";
RL Structure 3:177-187(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), CATALYTIC ACTIVITY, AND REACTION
RP MECHANISM.
RX PubMed=11502173; DOI=10.1021/bi002932l;
RA Afolabi P.R., Mohammed F., Amaratunga K., Majekodunmi O., Dales S.L.,
RA Gill R., Thompson D., Cooper J.B., Wood S.P., Goodwin P.M., Anthony C.;
RT "Site-directed mutagenesis and X-ray crystallography of the PQQ-containing
RT quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome
RT c(L).";
RL Biochemistry 40:9799-9809(2001).
CC -!- FUNCTION: Catalyzes the oxidation of primary alcohols including
CC methanol.
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 Evidence={ECO:0000269|PubMed:11502173};
CC -!- SUBUNIT: Heterotetramer composed of 2 alpha and 2 beta subunits.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the methanol dehydrogenase subunit 2 family.
CC {ECO:0000305}.
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DR EMBL; X15792; CAA33796.1; -; Genomic_DNA.
DR EMBL; X07856; CAA30705.1; -; Genomic_DNA.
DR EMBL; CP001510; ACS42166.1; -; Genomic_DNA.
DR RefSeq; WP_003599120.1; NC_012808.1.
DR PDB; 1H4I; X-ray; 1.94 A; B/D=23-96.
DR PDB; 1H4J; X-ray; 3.00 A; B/D/F/H=23-96.
DR PDB; 1W6S; X-ray; 1.20 A; B/D=23-96.
DR PDBsum; 1H4I; -.
DR PDBsum; 1H4J; -.
DR PDBsum; 1W6S; -.
DR AlphaFoldDB; P14775; -.
DR SMR; P14775; -.
DR STRING; 272630.MexAM1_META1p4535; -.
DR EnsemblBacteria; ACS42166; ACS42166; MexAM1_META1p4535.
DR KEGG; mea:Mex_1p4535; -.
DR eggNOG; ENOG5032TB9; Bacteria.
DR HOGENOM; CLU_2356482_0_0_5; -.
DR OMA; PGNCWEP; -.
DR OrthoDB; 2000979at2; -.
DR BioCyc; MetaCyc:MON-3922; -.
DR BRENDA; 1.1.2.7; 3296.
DR EvolutionaryTrace; P14775; -.
DR Proteomes; UP000009081; Chromosome.
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; Direct protein sequencing; Disulfide bond;
KW Methanol utilization; Oxidoreductase; Periplasm; Signal.
FT SIGNAL 1..22
FT CHAIN 23..96
FT /note="Methanol dehydrogenase [cytochrome c] subunit 2"
FT /id="PRO_0000025569"
FT REGION 45..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 28..34
FT /evidence="ECO:0000269|PubMed:7656012"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:1W6S"
FT HELIX 61..83
FT /evidence="ECO:0007829|PDB:1W6S"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1W6S"
SQ SEQUENCE 96 AA; 10512 MW; 9C082124F26F3159 CRC64;
MKTTLIAAAI VALSGLAAPA LAYDGTKCKA AGNCWEPKPG FPEKIAGSKY DPKHDPKELN
KQADSIKQME ERNKKRVENF KKTGKFEYDV AKISAN
