DHM1_METEA
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 03-AUG-2022, entry version 165.
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 Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS 9133 / AM1) (Methylobacterium extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
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 moxJ
RT 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 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA Lidstrom M.E.;
RT "Methylobacterium genome sequences: a reference blueprint to investigate
RT microbial metabolism of C1 compounds from natural and industrial sources.";
RL PLoS ONE 4:E5584-E5584(2009).
RN [3]
RP PROTEIN SEQUENCE OF 28-53, AND SUBUNIT.
RX PubMed=2504152; DOI=10.1042/bj2600857;
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 bridge
RT 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 OF
RP CYS-130; CYS-131 AND ASP-330, CATALYTIC ACTIVITY, AND REACTION 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., Anthony C.;
RT "Site-directed mutagenesis and X-ray crystallography of the PQQ-containing
RT quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome
RT c(L).";
RL Biochemistry 40:9799-9809(2001).
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 Evidence={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 disulfide
CC 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 protein;
CC Periplasmic side. Note=Periplasmic, but associated with 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; WP_003599114.1; NC_012988.1.
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 AlphaFoldDB; P16027; -.
DR SMR; P16027; -.
DR STRING; 272630.MexAM1_META1p4538; -.
DR EnsemblBacteria; ACS42169; ACS42169; MexAM1_META1p4538.
DR KEGG; mea:Mex_1p4538; -.
DR eggNOG; COG4993; Bacteria.
DR HOGENOM; CLU_018478_0_0_5; -.
DR OrthoDB; 1377603at2; -.
DR BioCyc; MetaCyc:MON-3921; -.
DR BRENDA; 1.1.2.7; 3296.
DR EvolutionaryTrace; P16027; -.
DR Proteomes; UP000009081; Chromosome.
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; 1.
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 3D-structure; Calcium; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Membrane; Metal-binding;
KW Methanol utilization; Oxidoreductase; PQQ; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:2504152"
FT CHAIN 28..626
FT /note="Methanol dehydrogenase [cytochrome c] subunit 1"
FT /id="PRO_0000025566"
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 BINDING 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT DISULFID 130..131
FT /evidence="ECO:0000269|PubMed:7656012"
FT DISULFID 413..442
FT /evidence="ECO:0000269|PubMed:7656012"
FT MUTAGEN 130
FT /note="C->S: Inactive."
FT /evidence="ECO:0000269|PubMed:11502173"
FT MUTAGEN 131
FT /note="C->S: Inactive."
FT /evidence="ECO:0000269|PubMed:11502173"
FT MUTAGEN 330
FT /note="D->E: Lower affinity for methanol."
FT /evidence="ECO:0000269|PubMed:11502173"
FT HELIX 29..35
FT /evidence="ECO:0007829|PDB:1W6S"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1W6S"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:1W6S"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:1W6S"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:1W6S"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:1W6S"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:1W6S"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:1W6S"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 221..229
FT /evidence="ECO:0007829|PDB:1W6S"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:1W6S"
FT TURN 238..243
FT /evidence="ECO:0007829|PDB:1W6S"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:1W6S"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:1W6S"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:1H4J"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:1W6S"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:1W6S"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 360..366
FT /evidence="ECO:0007829|PDB:1W6S"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 372..379
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:1W6S"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:1W6S"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:1W6S"
FT TURN 429..432
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 433..439
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 441..447
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 461..467
FT /evidence="ECO:0007829|PDB:1W6S"
FT TURN 473..476
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 480..485
FT /evidence="ECO:0007829|PDB:1W6S"
FT TURN 487..489
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 492..500
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:1W6S"
FT TURN 510..512
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 513..517
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 521..527
FT /evidence="ECO:0007829|PDB:1W6S"
FT TURN 528..530
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 533..538
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 548..552
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 555..562
FT /evidence="ECO:0007829|PDB:1W6S"
FT TURN 566..569
FT /evidence="ECO:0007829|PDB:1W6S"
FT HELIX 570..574
FT /evidence="ECO:0007829|PDB:1W6S"
FT TURN 579..581
FT /evidence="ECO:0007829|PDB:1H4I"
FT HELIX 582..584
FT /evidence="ECO:0007829|PDB:1W6S"
FT HELIX 585..588
FT /evidence="ECO:0007829|PDB:1W6S"
FT TURN 589..591
FT /evidence="ECO:0007829|PDB:1W6S"
FT HELIX 592..594
FT /evidence="ECO:0007829|PDB:1W6S"
FT STRAND 601..607
FT /evidence="ECO:0007829|PDB:1W6S"
FT HELIX 612..614
FT /evidence="ECO:0007829|PDB:1H4I"
FT TURN 616..619
FT /evidence="ECO:0007829|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
