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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   01-OCT-2014, entry version 115.
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: 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: Binds 1 calcium 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-SubCell.
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
FT   TURN         61     63
FT   HELIX        64     66
FT   STRAND       67     74
FT   STRAND       86     88
FT   STRAND       91     95
FT   TURN         98    100
FT   STRAND      102    106
FT   STRAND      112    117
FT   HELIX       123    128
FT   STRAND      139    141
FT   STRAND      145    147
FT   STRAND      150    154
FT   STRAND      158    164
FT   TURN        165    167
FT   STRAND      170    175
FT   HELIX       179    181
FT   STRAND      190    192
FT   STRAND      195    198
FT   HELIX       203    205
FT   STRAND      210    215
FT   TURN        216    218
FT   STRAND      221    229
FT   HELIX       231    234
FT   TURN        238    243
FT   HELIX       245    247
FT   HELIX       252    255
FT   HELIX       261    264
FT   STRAND      274    276
FT   TURN        277    279
FT   STRAND      281    285
FT   HELIX       294    296
FT   STRAND      304    311
FT   TURN        312    314
FT   STRAND      317    324
FT   STRAND      338    343
FT   STRAND      349    356
FT   STRAND      360    366
FT   TURN        367    369
FT   STRAND      372    379
FT   STRAND      384    388
FT   TURN        390    392
FT   STRAND      395    397
FT   HELIX       399    401
FT   STRAND      409    414
FT   STRAND      426    428
FT   TURN        429    432
FT   STRAND      433    439
FT   STRAND      441    447
FT   STRAND      461    467
FT   TURN        473    476
FT   STRAND      480    485
FT   TURN        487    489
FT   STRAND      492    500
FT   STRAND      507    509
FT   TURN        510    512
FT   STRAND      513    517
FT   STRAND      521    527
FT   TURN        528    530
FT   STRAND      533    538
FT   STRAND      548    552
FT   STRAND      555    562
FT   TURN        566    569
FT   HELIX       570    574
FT   TURN        579    581
FT   HELIX       582    584
FT   HELIX       585    588
FT   TURN        589    591
FT   HELIX       592    594
FT   STRAND      601    607
FT   HELIX       612    614
FT   TURN        616    619
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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