DHM1_PARDE
ID DHM1_PARDE Reviewed; 631 AA.
AC P12293;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 124.
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;
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 33-49.
RX PubMed=3114231; DOI=10.1128/jb.169.9.3969-3975.1987;
RA Harms N., de Vries G.E., Maurer K., Hoogendijk J., Stouthamer A.H.;
RT "Isolation and nucleotide sequence of the methanol dehydrogenase structural
RT gene from Paracoccus denitrificans.";
RL J. Bacteriol. 169:3969-3975(1987).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 33-631 IN COMPLEX WITH BETA
RP SUBUNIT, SUBUNIT, COFACTOR, AND DISULFIDE BONDS.
RX PubMed=14505072; DOI=10.1007/s00775-003-0485-0;
RA Xia Z.-X., Dai W.W., He Y.-N., White S.A., Mathews F.S., Davidson V.L.;
RT "X-ray structure of methanol dehydrogenase from Paracoccus denitrificans
RT and molecular modeling of its interactions with cytochrome c-551i.";
RL J. Biol. Inorg. Chem. 8:843-854(2003).
CC -!- FUNCTION: Catalyzes the oxidation of primary alcohols including
CC methanol. {ECO:0000250}.
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=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC Evidence={ECO:0000269|PubMed:14505072};
CC Note=Binds 1 PQQ group per subunit. PQQ is inserted between disulfide
CC Cys-135-Cys-136 and the indole ring of Trp-275.
CC {ECO:0000269|PubMed:14505072};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:14505072};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:14505072};
CC -!- SUBUNIT: Heterotetramer composed of 2 alpha and 2 beta subunits.
CC {ECO:0000269|PubMed:14505072}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- MISCELLANEOUS: MDH is the major protein in the cell during growth on
CC methanol (in P.denitrificans MDH constitutes up to 15% of the total
CC cell protein).
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; M17339; AAA88366.1; -; Genomic_DNA.
DR PDB; 1LRW; X-ray; 2.50 A; A/C=33-631.
DR PDBsum; 1LRW; -.
DR AlphaFoldDB; P12293; -.
DR SMR; P12293; -.
DR BioCyc; MetaCyc:MON-3923; -.
DR BRENDA; 1.1.2.B2; 3341.
DR EvolutionaryTrace; P12293; -.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
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; 1.
DR SMART; SM00564; PQQ; 4.
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; Direct protein sequencing; Disulfide bond;
KW Metal-binding; Methanol utilization; Oxidoreductase; Periplasm; PQQ;
KW Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:3114231"
FT CHAIN 33..631
FT /note="Methanol dehydrogenase [cytochrome c] subunit 1"
FT /id="PRO_0000025568"
FT ACT_SITE 335
FT /note="Proton acceptor"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 293
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT DISULFID 135..136
FT /evidence="ECO:0000269|PubMed:14505072"
FT DISULFID 418..447
FT /evidence="ECO:0000269|PubMed:14505072"
FT HELIX 34..40
FT /evidence="ECO:0007829|PDB:1LRW"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:1LRW"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:1LRW"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:1LRW"
FT HELIX 128..133
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:1LRW"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:1LRW"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:1LRW"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:1LRW"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 226..234
FT /evidence="ECO:0007829|PDB:1LRW"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:1LRW"
FT TURN 243..246
FT /evidence="ECO:0007829|PDB:1LRW"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:1LRW"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:1LRW"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:1LRW"
FT TURN 282..285
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:1LRW"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:1LRW"
FT TURN 307..310
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:1LRW"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 322..329
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 343..348
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 354..361
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 365..371
FT /evidence="ECO:0007829|PDB:1LRW"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 377..384
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 389..393
FT /evidence="ECO:0007829|PDB:1LRW"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:1LRW"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 414..419
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:1LRW"
FT TURN 434..437
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 438..444
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 446..452
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 466..472
FT /evidence="ECO:0007829|PDB:1LRW"
FT TURN 478..481
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 484..490
FT /evidence="ECO:0007829|PDB:1LRW"
FT TURN 491..494
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 495..504
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 508..513
FT /evidence="ECO:0007829|PDB:1LRW"
FT TURN 514..516
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 517..521
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 525..531
FT /evidence="ECO:0007829|PDB:1LRW"
FT TURN 532..534
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 537..542
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 552..556
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 559..566
FT /evidence="ECO:0007829|PDB:1LRW"
FT HELIX 570..577
FT /evidence="ECO:0007829|PDB:1LRW"
FT HELIX 585..592
FT /evidence="ECO:0007829|PDB:1LRW"
FT TURN 593..595
FT /evidence="ECO:0007829|PDB:1LRW"
FT HELIX 596..598
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 605..611
FT /evidence="ECO:0007829|PDB:1LRW"
FT TURN 620..623
FT /evidence="ECO:0007829|PDB:1LRW"
FT STRAND 627..629
FT /evidence="ECO:0007829|PDB:1LRW"
SQ SEQUENCE 631 AA; 69799 MW; 0934DC93FFC5730B CRC64;
MNRNTPKARG ASSLAMAVAM GLAVLTTAPA TANDQLVELA KDPANWVMTG RDYNAQNYSE
MTDINKENVK QLRPAWSFST GVLHGHEGTP LVVGDRMFIH TPFPNTTFAL DLNEPGKILW
QNKPKQNPTA RTVACCDVVN RGLAYWPGDD QVKPLIFRTQ LDGHIVAMDA ETGETRWIME
NSDIKVGSTL TIAPYVIKDL VLVGSSGAEL GVRGYVTAYD VKSGEMRWRA FATGPDEELL
LAEDFNAPNP HYGQKNLGLE TWEGDAWKIG GGTNWGWYAY DPEVDLFYYG SGNPAPWNET
MRPGDNKWTM AIWGREATTG EAKFAYQKTP HDEWDYAGVN VMMLSEQEDK QGQMRKLLTH
PDRNGIVYTL DRTNGDLISA DKMDDTVNWV KEVQLDTGLP VRDPEFGTRM DHKARDICPS
AMGYHNQGHD SYDPERKVFM LGINHICMDW EPFMLPYRAG QFFVGATLTM YPGPKATAER
AGAGQIKAYD AISGEMKWEK MERFSVWGGT MATAGGLTFY VTLDGFIKAR DSDTGDLLWK
FKLPSGVIGH PMTYKHDGRQ YVAIMYGVGG WPGVGLVFDL ADPTAGLGSV GAFKRLQEFT
QMGGGVMVFS LDGESPYSDP NVGEYAPGEP T
