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 27-MAR-2024, entry version 131. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.GCA_000378225_01347; -. 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 CDD; cd10278; PQQ_MDH; 1. DR Gene3D; 2.140.10.10; Quinoprotein alcohol dehydrogenase-like superfamily; 1. 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 NCBIfam; TIGR03075; PQQ_enz_alc_DH; 1. DR PANTHER; PTHR32303:SF22; METHANOL DEHYDROGENASE LARGE SUBUNIT-LIKE PROTEIN; 1. DR PANTHER; PTHR32303; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1. DR Pfam; PF13360; PQQ_2; 2. DR SMART; SM00564; PQQ; 4. DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 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 //