DHM1_METME
ID DHM1_METME Reviewed; 573 AA.
AC P38539; Q59540;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 125.
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;
OS Methylophilus methylotrophus (Bacterium W3A1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylophilus.
OX NCBI_TaxID=17;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (2.4
RP ANGSTROMS).
RX PubMed=8676383; DOI=10.1006/jmbi.1996.0334;
RA Xia Z.-X., Dai W.-W., Zhang Y.-F., White S.A., Boyd G.D., Mathews F.S.;
RT "Determination of the gene sequence and the three-dimensional structure at
RT 2.4 angstroms resolution of methanol dehydrogenase from Methylophilus
RT W3A1.";
RL J. Mol. Biol. 259:480-501(1996).
RN [2]
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 [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=8241148; DOI=10.1021/bi00211a002;
RA White S.A., Boyd G.D., Mathews F.S., Xia Z.-X., Dai W.-W., Zhang Y.-F.,
RA Davidson V.L.;
RT "The active site structure of the calcium-containing quinoprotein methanol
RT dehydrogenase.";
RL Biochemistry 32:12955-12958(1993).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=1331050; DOI=10.1016/s0021-9258(18)41668-7;
RA Xia Z.-X., Dai W.-W., Xiong J.-P., Hao Z.-P., Davidson V.L., White S.A.,
RA Mathews F.S.;
RT "The three-dimensional structures of methanol dehydrogenase from two
RT methylotrophic bacteria at 2.6-A resolution.";
RL J. Biol. Chem. 267:22289-22297(1992).
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 1 Ca(2+) ion per subunit.;
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC Note=Binds 1 PQQ per subunit. PQQ is inserted between disulfide Cys-
CC 105-Cys-106 and the indole ring of Trp-239.;
CC -!- SUBUNIT: Heterotetramer 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; U41040; AAA83765.1; -; Genomic_DNA.
DR PIR; S68591; S68591.
DR PDB; 1G72; X-ray; 1.90 A; A/C=1-573.
DR PDB; 2AD6; X-ray; 1.50 A; A/C=3-573.
DR PDB; 2AD7; X-ray; 1.50 A; A/C=3-573.
DR PDB; 2AD8; X-ray; 1.60 A; A/C=3-573.
DR PDB; 4AAH; X-ray; 2.40 A; A/C=3-573.
DR PDBsum; 1G72; -.
DR PDBsum; 2AD6; -.
DR PDBsum; 2AD7; -.
DR PDBsum; 2AD8; -.
DR PDBsum; 4AAH; -.
DR AlphaFoldDB; P38539; -.
DR SMR; P38539; -.
DR STRING; 1122236.KB905142_gene321; -.
DR BRENDA; 1.1.2.7; 3319.
DR BRENDA; 1.2.2.B2; 3319.
DR SABIO-RK; P38539; -.
DR EvolutionaryTrace; P38539; -.
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; PF13360; PQQ_2; 2.
DR SMART; SM00564; PQQ; 4.
DR SUPFAM; SSF50998; SSF50998; 1.
DR TIGRFAMs; TIGR03075; PQQ_enz_alc_DH; 1.
DR PROSITE; PS00364; BACTERIAL_PQQ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell inner membrane; Cell membrane; Disulfide bond;
KW Membrane; Metal-binding; Methanol utilization; Oxidoreductase; PQQ.
FT CHAIN 1..573
FT /note="Methanol dehydrogenase [cytochrome c] subunit 1"
FT /id="PRO_0000205342"
FT ACT_SITE 299
FT /note="Proton acceptor"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT DISULFID 105..106
FT DISULFID 146..169
FT DISULFID 381..410
FT HELIX 4..10
FT /evidence="ECO:0007829|PDB:2AD6"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:2AD6"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:2AD6"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:2AD6"
FT HELIX 98..103
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:2AD6"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:2AD6"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:2AD6"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:2AD6"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:2AD6"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:2AD6"
FT TURN 207..212
FT /evidence="ECO:0007829|PDB:2AD6"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:2AD6"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:2AD6"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:2AD6"
FT TURN 246..249
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:4AAH"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:2AD6"
FT TURN 271..274
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:2AD6"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 286..293
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 316..324
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 328..334
FT /evidence="ECO:0007829|PDB:2AD6"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 340..347
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:2AD6"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:2AD6"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:2AD6"
FT TURN 397..400
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 401..407
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 409..415
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 429..435
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 446..451
FT /evidence="ECO:0007829|PDB:2AD6"
FT TURN 453..455
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 458..466
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:2AD6"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 479..483
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 487..493
FT /evidence="ECO:0007829|PDB:2AD6"
FT TURN 494..496
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 499..504
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 514..518
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 521..528
FT /evidence="ECO:0007829|PDB:2AD6"
FT TURN 532..535
FT /evidence="ECO:0007829|PDB:2AD6"
FT HELIX 536..539
FT /evidence="ECO:0007829|PDB:2AD6"
FT HELIX 547..550
FT /evidence="ECO:0007829|PDB:2AD6"
FT HELIX 551..554
FT /evidence="ECO:0007829|PDB:2AD6"
FT TURN 555..557
FT /evidence="ECO:0007829|PDB:2AD6"
FT HELIX 558..560
FT /evidence="ECO:0007829|PDB:2AD6"
FT STRAND 567..572
FT /evidence="ECO:0007829|PDB:2AD6"
SQ SEQUENCE 573 AA; 62635 MW; A06C9B3091BB8F0C CRC64;
MADADLDKQV NTAGAWPIAT GGYYSQHNSP LAQINKSNVK NVKAAWSFST GVLNGHEGAP
LVIGDMMYVH SAFPNNTYAL NLNDPGKIVW QHKPKQDAST KAVMCCDVVD RGLAYGAGQI
VKKQANGHLL ALDAKTGKIN WEVEVCDPKV GSTLTQAPFV AKDTVLMGCS GAELGVRGAV
NAFDLKTGEL KWRAFATGSD DSVRLAKDFN SANPHYGQFG LGTKTWEGDA WKIGGGTNWG
WYAYDPKLNL FYYGSGNPAP WNETMRPGDN KWTMTIWGRD LDTGMAKWGY QKTPHDEWDF
AGVNQMVLTD QPVNGKMTPL LSHIDRNGIL YTLNRENGNL IVAEKVDPAV NVFKKVDLKT
GTPVRDPEFA TRMDHKGTNI CPSAMGFHNQ GVDSYDPESR TLYAGLNHIC MDWEPFMLPY
RAGQFFVGAT LAMYPGPNGP TKKEMGQIRA FDLTTGKAKW TKWEKFAAWG GTLYTKGGLV
WYATLDGYLK ALDNKDGKEL WNFKMPSGGI GSPMTYSFKG KQYIGSMYGV GGWPGVGLVF
DLTDPSAGLG AVGAFRELQN HTQMGGGLMV FSL
