Skip Header

Contribute Send feedback
Read comments (?) or add your own

P16027 (DHM1_METEA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methanol dehydrogenase [cytochrome c] subunit 1
EC=1.1.2.7
Alternative name(s):
MDH large subunit alpha
MEDH
Gene names
Name:moxF
Synonyms:mxaF
Ordered Locus Names:MexAM1_META1p4538
OrganismMethylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1) [Complete proteome] [HAMAP]
Taxonomic identifier272630 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Methylobacteriaceae › Methylobacterium

Protein attributes

Sequence length626 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation of primary alcohols including methanol.

Catalytic activity

A primary alcohol + 2 cytochrome c(L) = an aldehyde + 2 reduced cytochrome c(L). Ref.7

Cofactor

Binds 1 PQQ group per subunit. PQQ is inserted between disulfide Cys-130-Cys-131 and the indole ring of Trp-270.

Binds 1 calcium ion per subunit.

Subunit structure

Heterotetramer composed of 2 alpha and 2 beta subunits. Ref.3

Subcellular location

Cell inner membrane; Peripheral membrane protein; Periplasmic side. Note: Periplasmic, but associated with inner membrane.

Sequence similarities

Belongs to the bacterial PQQ dehydrogenase family.

Sequence caution

The sequence ACS42169.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.3
Chain28 – 626599Methanol dehydrogenase [cytochrome c] subunit 1
PRO_0000025566

Sites

Active site3301Proton acceptor By similarity
Metal binding2041Calcium
Metal binding2881Calcium

Amino acid modifications

Disulfide bond130 ↔ 131 Ref.5
Disulfide bond413 ↔ 442 Ref.5

Experimental info

Mutagenesis1301C → S: Inactive. Ref.7
Mutagenesis1311C → S: Inactive. Ref.7
Mutagenesis3301D → E: Lower affinity for methanol. Ref.7

Secondary structure

1 ............................................................................................................................ 626
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16027 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 64988D0AFD2AD34C

FASTA62668,434
        10         20         30         40         50         60 
MSRFVTSVSA LAMLALAPAA LSSGAYANDK LVELSKSDDN WVMPGKNYDS NNFSDLKQIN 

        70         80         90        100        110        120 
KGNVKQLRPA WTFSTGLLNG HEGAPLVVDG KMYIHTSFPN NTFALGLDDP GTILWQDKPK 

       130        140        150        160        170        180 
QNPAARAVAC CDLVNRGLAY WPGDGKTPAL ILKTQLDGNV AALNAETGET VWKVENSDIK 

       190        200        210        220        230        240 
VGSTLTIAPY VVKDKVIIGS SGAELGVRGY LTAYDVKTGE QVWRAYATGP DKDLLLASDF 

       250        260        270        280        290        300 
NIKNPHYGQK GLGTGTWEGD AWKIGGGTNW GWYAYDPGTN LIYFGTGNPA PWNETMRPGD 

       310        320        330        340        350        360 
NKWTMTIFGR DADTGEAKFG YQKTPHDEWD YAGVNVMMLS EQKDKDGKAR KLLTHPDRNG 

       370        380        390        400        410        420 
IVYTLDRTDG ALVSANKLDD TVNVFKSVDL KTGQPVRDPE YGTRMDHLAK DICPSAMGYH 

       430        440        450        460        470        480 
NQGHDSYDPK RELFFMGINH ICMDWEPFML PYRAGQFFVG ATLNMYPGPK GDRQNYEGLG 

       490        500        510        520        530        540 
QIKAYNAITG DYKWEKMERF AVWGGTMATA GDLVFYGTLD GYLKARDSDT GDLLWKFKIP 

       550        560        570        580        590        600 
SGAIGYPMTY THKGTQYVAI YYGVGGWPGV GLVFDLADPT AGLGAVGAFK KLANYTQMGG 

       610        620 
GVVVFSLDGK GPYDDPNVGE WKSAAK

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the Methylobacterium extorquens AM1 moxF and moxJ genes involved in methanol oxidation."
Anderson D.J., Morris C.J., Nunn D.N., Anthony C., Lidstrom M.E.
Gene 90:173-176(1990) [PubMed: 2116368] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Methylobacterium genome sequences: a reference blueprint to investigate microbial metabolism of C1 compounds from natural and industrial sources."
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. expand/collapse author list , 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.
PLoS ONE 4:E5584-E5584(2009) [PubMed: 19440302] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14718 / DSM 1338 / AM1.
[3]"The second subunit of methanol dehydrogenase of Methylobacterium extorquens AM1."
Nunn D.N., Day D., Anthony C.
Biochem. J. 260:857-862(1989) [PubMed: 2504152] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-53, SUBUNIT.
[4]"Pyrroloquinoline quinone (PQQ) and quinoprotein enzymes."
Anthony C.
Antioxid. Redox Signal. 3:757-774(2001) [PubMed: 11761326] [Abstract]
Cited for: REVIEW.
[5]"The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues."
Blake C.C.F., Ghosh M., Harlos K., Avezoux A., Anthony C.
Nat. Struct. Biol. 1:102-105(1994) [PubMed: 7656012] [Abstract]
Cited for: DISULFIDE BONDS.
[6]"The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 A."
Ghosh M., Anthony C., Harlos K., Goodwin M.G., Blake C.
Structure 3:177-187(1995) [PubMed: 7735834] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS).
[7]"Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome c(L)."
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.
Biochemistry 40:9799-9809(2001) [PubMed: 11502173] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF MUTANT GLU-330, MUTAGENESIS OF CYS-130; CYS-131 AND ASP-330, CATALYTIC ACTIVITY, REACTION MECHANISM.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M31108 Genomic DNA. Translation: AAA25380.1.
CP001510 Genomic DNA. Translation: ACS42169.1. Different initiation.
PIRJQ0706.
RefSeqYP_002965446.1. NC_012808.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H4IX-ray1.94A/C28-626[»]
1H4JX-ray3.00A/C/E/G28-626[»]
1W6SX-ray1.20A/C28-626[»]
ProteinModelPortalP16027.
SMRP16027. Positions 28-622.
ModBaseSearch...

Protein-protein interaction databases

STRINGP16027.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7994324.
PATRIC22514719. VBIMetExt101010_4414.

Organism-specific databases

CMRSearch...

Phylogenomic databases

ProtClustDBCLSK931615.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3921.

Family and domain databases

InterProIPR019556. PQQ-dependent_C.
IPR019551. PQQ-dependent_N.
IPR018391. PQQ_beta_propeller_repeat.
IPR017512. PQQ_MeOH/EtOH_DH.
IPR002372. PQQ_repeat.
IPR011047. Quinonprotein_ADH-like.
IPR001479. Quinoprotein_DH_CS.
[Graphical view]
Gene3DG3DSA:2.140.10.10. Quinoprotein_alc_DH-like. 1 hit.
PfamPF01011. PQQ. 4 hits.
PF10535. PQQ_C. 1 hit.
PF10527. PQQ_N. 1 hit.
[Graphical view]
SMARTSM00564. PQQ. 3 hits.
[Graphical view]
SUPFAMSSF50998. Quin_alc_DH_like. 1 hit.
TIGRFAMsTIGR03075. PQQ_enz_alc_DH. 1 hit.
PROSITEPS00363. BACTERIAL_PQQ_1. 1 hit.
PS00364. BACTERIAL_PQQ_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDHM1_METEA
AccessionPrimary (citable) accession number: P16027
Secondary accession number(s): C5AQA9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: January 25, 2012
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents