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Database: UniProt
Entry: P16027
LinkDB: P16027
Original site: P16027 
ID   DHM1_METEA              Reviewed;         626 AA.
AC   P16027; C5AQA9;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   26-NOV-2014, entry version 117.
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; Synonyms=mxaF; OrderedLocusNames=MexAM1_META1p4538;
OS   Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=272630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2116368; DOI=10.1016/0378-1119(90)90457-3;
RA   Anderson D.J., Morris C.J., Nunn D.N., Anthony C., Lidstrom M.E.;
RT   "Nucleotide sequence of the Methylobacterium extorquens AM1 moxF and
RT   moxJ genes involved in methanol oxidation.";
RL   Gene 90:173-176(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14718 / DSM 1338 / AM1;
RX   PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA   Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A.,
RA   Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C.,
RA   Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S.,
RA   Muller E., Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G.,
RA   Roche D., Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z.,
RA   Marx C.J., Vorholt J.A., Olson M.V., Kaul R., Weissenbach J.,
RA   Medigue C., Lidstrom M.E.;
RT   "Methylobacterium genome sequences: a reference blueprint to
RT   investigate microbial metabolism of C1 compounds from natural and
RT   industrial sources.";
RL   PLoS ONE 4:E5584-E5584(2009).
RN   [3]
RP   PROTEIN SEQUENCE OF 28-53, AND SUBUNIT.
RX   PubMed=2504152;
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   [4]
RP   REVIEW.
RX   PubMed=11761326; DOI=10.1089/15230860152664966;
RA   Anthony C.;
RT   "Pyrroloquinoline quinone (PQQ) and quinoprotein enzymes.";
RL   Antioxid. Redox Signal. 3:757-774(2001).
RN   [5]
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
RT   bridge between adjacent cysteine residues.";
RL   Nat. Struct. Biol. 1:102-105(1994).
RN   [6]
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   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF MUTANT GLU-330, MUTAGENESIS
RP   OF CYS-130; CYS-131 AND ASP-330, 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.,
RA   Anthony C.;
RT   "Site-directed mutagenesis and X-ray crystallography of the PQQ-
RT   containing quinoprotein methanol dehydrogenase and its electron
RT   acceptor, cytochrome c(L).";
RL   Biochemistry 40:9799-9809(2001).
CC   -!- FUNCTION: Catalyzes the oxidation of primary alcohols including
CC       methanol.
CC   -!- CATALYTIC ACTIVITY: A primary alcohol + 2 cytochrome c(L) = an
CC       aldehyde + 2 reduced cytochrome c(L) + 2 H(+).
CC       {ECO:0000269|PubMed:11502173}.
CC   -!- COFACTOR:
CC       Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC       Note=Binds 1 PQQ group per subunit. PQQ is inserted between
CC       disulfide Cys-130-Cys-131 and the indole ring of Trp-270.;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC       Note=Binds 1 Ca(2+) ion per subunit.;
CC   -!- SUBUNIT: Heterotetramer composed of 2 alpha and 2 beta subunits.
CC       {ECO:0000269|PubMed:2504152}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane
CC       protein; Periplasmic side. Note=Periplasmic, but associated with
CC       inner membrane.
CC   -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACS42169.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M31108; AAA25380.1; -; Genomic_DNA.
DR   EMBL; CP001510; ACS42169.1; ALT_INIT; Genomic_DNA.
DR   PIR; JQ0706; JQ0706.
DR   RefSeq; YP_002965446.1; NC_012808.1.
DR   PDB; 1H4I; X-ray; 1.94 A; A/C=28-626.
DR   PDB; 1H4J; X-ray; 3.00 A; A/C/E/G=28-626.
DR   PDB; 1W6S; X-ray; 1.20 A; A/C=28-626.
DR   PDBsum; 1H4I; -.
DR   PDBsum; 1H4J; -.
DR   PDBsum; 1W6S; -.
DR   ProteinModelPortal; P16027; -.
DR   SMR; P16027; 28-622.
DR   EnsemblBacteria; ACS42169; ACS42169; MexAM1_META1p4538.
DR   GeneID; 7994324; -.
DR   KEGG; mea:Mex_1p4538; -.
DR   PATRIC; 22514719; VBIMetExt101010_4414.
DR   eggNOG; COG4993; -.
DR   HOGENOM; HOG000217982; -.
DR   KO; K14028; -.
DR   OrthoDB; EOG6FNHJ2; -.
DR   BioCyc; MetaCyc:MONOMER-3921; -.
DR   BioCyc; MEXT272630:GBY6-4283-MONOMER; -.
DR   EvolutionaryTrace; P16027; -.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0052932; F:2-chloroethanol cytochrome-c oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0052931; F:ethanol cytochrome-c oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052930; F:methanol ferricytochrome-c oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015945; P:methanol metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.140.10.10; -; 1.
DR   InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR   InterPro; IPR017512; PQQ_MeOH/EtOH_DH.
DR   InterPro; IPR002372; PQQ_repeat.
DR   InterPro; IPR027295; Quinonprotein_ADH-like_fam.
DR   InterPro; IPR011047; Quinonprotein_ADH-like_supfam.
DR   InterPro; IPR001479; Quinoprotein_DH_CS.
DR   Pfam; PF01011; PQQ; 4.
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   3D-structure; Calcium; Cell inner membrane; Cell membrane;
KW   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   Membrane; Metal-binding; Methanol utilization; Oxidoreductase; PQQ;
KW   Reference proteome; Signal.
FT   SIGNAL        1     27       {ECO:0000269|PubMed:2504152}.
FT   CHAIN        28    626       Methanol dehydrogenase [cytochrome c]
FT                                subunit 1.
FT                                /FTId=PRO_0000025566.
FT   ACT_SITE    330    330       Proton acceptor. {ECO:0000250}.
FT   METAL       204    204       Calcium.
FT   METAL       288    288       Calcium.
FT   DISULFID    130    131       {ECO:0000269|PubMed:7656012}.
FT   DISULFID    413    442       {ECO:0000269|PubMed:7656012}.
FT   MUTAGEN     130    130       C->S: Inactive.
FT                                {ECO:0000269|PubMed:11502173}.
FT   MUTAGEN     131    131       C->S: Inactive.
FT                                {ECO:0000269|PubMed:11502173}.
FT   MUTAGEN     330    330       D->E: Lower affinity for methanol.
FT                                {ECO:0000269|PubMed:11502173}.
FT   HELIX        29     35       {ECO:0000244|PDB:1W6S}.
FT   TURN         61     63       {ECO:0000244|PDB:1W6S}.
FT   HELIX        64     66       {ECO:0000244|PDB:1W6S}.
FT   STRAND       67     74       {ECO:0000244|PDB:1W6S}.
FT   STRAND       86     88       {ECO:0000244|PDB:1W6S}.
FT   STRAND       91     95       {ECO:0000244|PDB:1W6S}.
FT   TURN         98    100       {ECO:0000244|PDB:1W6S}.
FT   STRAND      102    106       {ECO:0000244|PDB:1W6S}.
FT   STRAND      112    117       {ECO:0000244|PDB:1W6S}.
FT   HELIX       123    128       {ECO:0000244|PDB:1W6S}.
FT   STRAND      139    141       {ECO:0000244|PDB:1W6S}.
FT   STRAND      145    147       {ECO:0000244|PDB:1W6S}.
FT   STRAND      150    154       {ECO:0000244|PDB:1W6S}.
FT   STRAND      158    164       {ECO:0000244|PDB:1W6S}.
FT   TURN        165    167       {ECO:0000244|PDB:1W6S}.
FT   STRAND      170    175       {ECO:0000244|PDB:1W6S}.
FT   HELIX       179    181       {ECO:0000244|PDB:1W6S}.
FT   STRAND      190    192       {ECO:0000244|PDB:1W6S}.
FT   STRAND      195    198       {ECO:0000244|PDB:1W6S}.
FT   HELIX       203    205       {ECO:0000244|PDB:1W6S}.
FT   STRAND      210    215       {ECO:0000244|PDB:1W6S}.
FT   TURN        216    218       {ECO:0000244|PDB:1W6S}.
FT   STRAND      221    229       {ECO:0000244|PDB:1W6S}.
FT   HELIX       231    234       {ECO:0000244|PDB:1W6S}.
FT   TURN        238    243       {ECO:0000244|PDB:1W6S}.
FT   HELIX       245    247       {ECO:0000244|PDB:1W6S}.
FT   HELIX       252    255       {ECO:0000244|PDB:1W6S}.
FT   HELIX       261    264       {ECO:0000244|PDB:1W6S}.
FT   STRAND      274    276       {ECO:0000244|PDB:1H4J}.
FT   TURN        277    279       {ECO:0000244|PDB:1W6S}.
FT   STRAND      281    285       {ECO:0000244|PDB:1W6S}.
FT   HELIX       294    296       {ECO:0000244|PDB:1W6S}.
FT   STRAND      304    311       {ECO:0000244|PDB:1W6S}.
FT   TURN        312    314       {ECO:0000244|PDB:1W6S}.
FT   STRAND      317    324       {ECO:0000244|PDB:1W6S}.
FT   STRAND      338    343       {ECO:0000244|PDB:1W6S}.
FT   STRAND      349    356       {ECO:0000244|PDB:1W6S}.
FT   STRAND      360    366       {ECO:0000244|PDB:1W6S}.
FT   TURN        367    369       {ECO:0000244|PDB:1W6S}.
FT   STRAND      372    379       {ECO:0000244|PDB:1W6S}.
FT   STRAND      384    388       {ECO:0000244|PDB:1W6S}.
FT   TURN        390    392       {ECO:0000244|PDB:1W6S}.
FT   STRAND      395    397       {ECO:0000244|PDB:1W6S}.
FT   HELIX       399    401       {ECO:0000244|PDB:1W6S}.
FT   STRAND      409    414       {ECO:0000244|PDB:1W6S}.
FT   STRAND      426    428       {ECO:0000244|PDB:1W6S}.
FT   TURN        429    432       {ECO:0000244|PDB:1W6S}.
FT   STRAND      433    439       {ECO:0000244|PDB:1W6S}.
FT   STRAND      441    447       {ECO:0000244|PDB:1W6S}.
FT   STRAND      461    467       {ECO:0000244|PDB:1W6S}.
FT   TURN        473    476       {ECO:0000244|PDB:1W6S}.
FT   STRAND      480    485       {ECO:0000244|PDB:1W6S}.
FT   TURN        487    489       {ECO:0000244|PDB:1W6S}.
FT   STRAND      492    500       {ECO:0000244|PDB:1W6S}.
FT   STRAND      507    509       {ECO:0000244|PDB:1W6S}.
FT   TURN        510    512       {ECO:0000244|PDB:1W6S}.
FT   STRAND      513    517       {ECO:0000244|PDB:1W6S}.
FT   STRAND      521    527       {ECO:0000244|PDB:1W6S}.
FT   TURN        528    530       {ECO:0000244|PDB:1W6S}.
FT   STRAND      533    538       {ECO:0000244|PDB:1W6S}.
FT   STRAND      548    552       {ECO:0000244|PDB:1W6S}.
FT   STRAND      555    562       {ECO:0000244|PDB:1W6S}.
FT   TURN        566    569       {ECO:0000244|PDB:1W6S}.
FT   HELIX       570    574       {ECO:0000244|PDB:1W6S}.
FT   TURN        579    581       {ECO:0000244|PDB:1H4I}.
FT   HELIX       582    584       {ECO:0000244|PDB:1W6S}.
FT   HELIX       585    588       {ECO:0000244|PDB:1W6S}.
FT   TURN        589    591       {ECO:0000244|PDB:1W6S}.
FT   HELIX       592    594       {ECO:0000244|PDB:1W6S}.
FT   STRAND      601    607       {ECO:0000244|PDB:1W6S}.
FT   HELIX       612    614       {ECO:0000244|PDB:1H4I}.
FT   TURN        616    619       {ECO:0000244|PDB:1W6S}.
SQ   SEQUENCE   626 AA;  68434 MW;  64988D0AFD2AD34C CRC64;
     MSRFVTSVSA LAMLALAPAA LSSGAYANDK LVELSKSDDN WVMPGKNYDS NNFSDLKQIN
     KGNVKQLRPA WTFSTGLLNG HEGAPLVVDG KMYIHTSFPN NTFALGLDDP GTILWQDKPK
     QNPAARAVAC CDLVNRGLAY WPGDGKTPAL ILKTQLDGNV AALNAETGET VWKVENSDIK
     VGSTLTIAPY VVKDKVIIGS SGAELGVRGY LTAYDVKTGE QVWRAYATGP DKDLLLASDF
     NIKNPHYGQK GLGTGTWEGD AWKIGGGTNW GWYAYDPGTN LIYFGTGNPA PWNETMRPGD
     NKWTMTIFGR DADTGEAKFG YQKTPHDEWD YAGVNVMMLS EQKDKDGKAR KLLTHPDRNG
     IVYTLDRTDG ALVSANKLDD TVNVFKSVDL KTGQPVRDPE YGTRMDHLAK DICPSAMGYH
     NQGHDSYDPK RELFFMGINH ICMDWEPFML PYRAGQFFVG ATLNMYPGPK GDRQNYEGLG
     QIKAYNAITG DYKWEKMERF AVWGGTMATA GDLVFYGTLD GYLKARDSDT GDLLWKFKIP
     SGAIGYPMTY THKGTQYVAI YYGVGGWPGV GLVFDLADPT AGLGAVGAFK KLANYTQMGG
     GVVVFSLDGK GPYDDPNVGE WKSAAK
//
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