ID   DHM1_METOR              Reviewed;         626 AA.
AC   P15279;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Methanol dehydrogenase [cytochrome c] subunit 1;
DE            EC=1.1.2.7;
DE   AltName: Full=MDH large subunit alpha;
DE   AltName: Full=MEDH;
DE   Flags: Precursor;
GN   Name=moxF;
OS   Methylobacterium organophilum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 28-43.
RC   STRAIN=ATCC 27886 / DSM 760 / JCM 2833 / NBRC 15689 / NCIMB 11278 / VKM
RC   B-2066 / XX;
RX   PubMed=2459109; DOI=10.1128/jb.170.10.4739-4747.1988;
RA   Machlin S.M., Hanson R.S.;
RT   "Nucleotide sequence and transcriptional start site of the Methylobacterium
RT   organophilum XX methanol dehydrogenase structural gene.";
RL   J. Bacteriol. 170:4739-4747(1988).
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   -!- COFACTOR:
CC       Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 PQQ group per subunit. PQQ is inserted between disulfide
CC       Cys-130-Cys-131 and the indole ring of Trp-270. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
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 bacterial PQQ dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; M22629; AAA50289.1; -; Genomic_DNA.
DR   AlphaFoldDB; P15279; -.
DR   SMR; P15279; -.
DR   BioCyc; MetaCyc:MON-3927; -.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
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:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0015945; P:methanol metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR   InterPro; IPR017512; PQQ_MeOH/EtOH_DH.
DR   InterPro; IPR002372; PQQ_repeat.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR001479; Quinoprotein_DH_CS.
DR   Pfam; PF01011; PQQ; 2.
DR   Pfam; PF13360; PQQ_2; 1.
DR   SMART; SM00564; PQQ; 3.
DR   SUPFAM; SSF50998; SSF50998; 1.
DR   TIGRFAMs; TIGR03075; PQQ_enz_alc_DH; 1.
DR   PROSITE; PS00363; BACTERIAL_PQQ_1; 1.
DR   PROSITE; PS00364; BACTERIAL_PQQ_2; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell inner membrane; Cell membrane; Direct protein sequencing;
KW   Disulfide bond; Membrane; Metal-binding; Methanol utilization;
KW   Oxidoreductase; PQQ; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:2459109"
FT   CHAIN           28..626
FT                   /note="Methanol dehydrogenase [cytochrome c] subunit 1"
FT                   /id="PRO_0000025567"
FT   ACT_SITE        330
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         288
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        130..131
FT                   /evidence="ECO:0000250"
FT   DISULFID        413..442
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   626 AA;  68677 MW;  8768F6B8371E5DFF CRC64;
     MSRFVTSVSA LAMLALAPAA LSSVAYANDK LVELSKSDDN WVMPGKNYDS NNYSELKQVN
     KSNVKQLRPA WTFSTGLLNG HEGAPLVVDG KMYVHTSFPN NTFALDLDDP GHILWQDKPK
     QNPAARAVAC CDLVNRGLAY WPGDGKTPAL ILKTQLDRHV VALNAETGET VWKVENSDIK
     VGSTLTIAPY VVKDKVIIGS SGAELGVRGY LTAYDVKTGG QVWRAYATGP DKDLLLADDF
     NVKNAHYGQK GLGTATWEGD AWKIGGGTNW GWYAYDPGTN LIYFGTGNPA PWNETMRPGD
     NKWTMTIFGR DADTGEAKFG YQKTPHDEWD YAGVNVMMPS EQKDKDGKTR KLLTHPDRNG
     IVYTLDRTDG ALVSANKLDD TVNVFKTVDL KTGQPVRDPE YGTRMDHLAK DVCPSAMGYH
     NQGHDSYDPK RELFFMGINH ICMDWEPFML PYRAGQFFVG ATLNMYPGPK GDRQNYEGLG
     QIKAYNAITG SYKWEKMERF AVWGGTLATA GDLVFYGTLD GYLKARDSDT GDLLWKFKIP
     SGAIGYPMTY THKGTQYVAI YYGVGGWPGV GLVFDLADPT AGLGAVGAFK KLANYTQQGG
     GVIVFSLDGK GPYDDPNVGE WKSASK