Sequence of DHM1_METEA
EC Number:1.1.2.7
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
methanol dehydrogenase (cytochrome c)
P16027
Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)
626
68434
Reaction
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
Other sequences found for EC No. 1.1.2.7
General information:
Sequence
0 MSRFVTSVSA LAMLALAPAA LSSGAYANDK LVELSKSDDN WVMPGKNYDS NNFSDLKQIN
60 KGNVKQLRPA WTFSTGLLNG HEGAPLVVDG KMYIHTSFPN NTFALGLDDP GTILWQDKPK
120 QNPAARAVAC CDLVNRGLAY WPGDGKTPAL ILKTQLDGNV AALNAETGET VWKVENSDIK
180 VGSTLTIAPY VVKDKVIIGS SGAELGVRGY LTAYDVKTGE QVWRAYATGP DKDLLLASDF
240 NIKNPHYGQK GLGTGTWEGD AWKIGGGTNW GWYAYDPGTN LIYFGTGNPA PWNETMRPGD
300 NKWTMTIFGR DADTGEAKFG YQKTPHDEWD YAGVNVMMLS EQKDKDGKAR KLLTHPDRNG
360 IVYTLDRTDG ALVSANKLDD TVNVFKSVDL KTGQPVRDPE YGTRMDHLAK DICPSAMGYH
420 NQGHDSYDPK RELFFMGINH ICMDWEPFML PYRAGQFFVG ATLNMYPGPK GDRQNYEGLG
480 QIKAYNAITG DYKWEKMERF AVWGGTMATA GDLVFYGTLD GYLKARDSDT GDLLWKFKIP
540 SGAIGYPMTY THKGTQYVAI YYGVGGWPGV GLVFDLADPT AGLGAVGAFK KLANYTQMGG
600 GVVVFSLDGK GPYDDPNVGE WKSAAK
Download this sequence
in fasta formatDownload all sequences for 1.1.2.7
in fasta format
in csv (Excel, OpenOffice) formatSequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
535520
Anderson D.J.,Morris C.J.,Nunn D.N.,Anthony C.,Lidstrom M.E.
Nucleotide sequence of the Methylobacterium extorquens AM1 moxF and moxJ genes involved in methanol oxidation.
Gene
90
173-176
1990
535521
Vuilleumier S.,Chistoserdova L.,Lee M.-C.,Bringel F.,Lajus A.,Zhou Y.,Gourion B.,Barbe V.,Chang J.,Cruveiller S.,Dossat C.,Gillett W.,Gruffaz C.,Haugen E.,Hourcade E.,Levy R.,Mangenot S.,Muller E.,Nadalig T.,Pagni M.,Penny C.,Peyraud R.,Robinson D.G.,Roche D.,Rouy Z.,Saenampechek C.,Salvignol G.,Vallenet D.,Wu Z.,Marx C.J.,Vorholt J.A.,Olson M.V.,Kaul R.,Weissenbach J.,Medigue C.,Lidstrom M.E.
Methylobacterium genome sequences: a reference blueprint to investigate microbial metabolism of C1 compounds from natural and industrial sources.
PLoS ONE
4
0-0
2009
535522
Nunn D.N.,Day D.,Anthony C.
The second subunit of methanol dehydrogenase of Methylobacterium extorquens AM1.
Biochem. J.
260
857-862
1989
535523
Anthony C.
Pyrroloquinoline quinone (PQQ) and quinoprotein enzymes.
Antioxid. Redox Signal.
3
757-774
2001
535524
Blake C.C.F.,Ghosh M.,Harlos K.,Avezoux A.,Anthony C.
The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues.
Nat. Struct. Biol.
1
102-105
1994
535525
Ghosh M.,Anthony C.,Harlos K.,Goodwin M.G.,Blake C.
The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 A.
Structure
3
177-187
1995
535526
Afolabi P.R.,Mohammed F.,Amaratunga K.,Majekodunmi O.,Dales S.L.,Gill R.,Thompson D.,Cooper J.B.,Wood S.P.,Goodwin P.M.,Anthony C.
Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome c(L).
Biochemistry
40
9799-9809
2001
