Methanol dehydrogenase subunit 1 - Methylophilus methylotrophus

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Reviewed, UniProtKB/Swiss-Prot P38539 (DHM1_METME)

Last modified June 16, 2009. Version 76. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names	Recommended name: Methanol dehydrogenase subunit 1 EC=1.1.99.8 Alternative name(s): MDH large subunit alpha MEDH
Organism	Methylophilus methylotrophus (Bacterium W3A1)
Taxonomic identifier	17 [NCBI]
Taxonomic lineage	Bacteria › Proteobacteria › Betaproteobacteria › Methylophilales › Methylophilaceae › Methylophilus

Protein attributes

Sequence length	573 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	A primary alcohol + acceptor = an aldehyde + reduced acceptor.
Cofactor	Binds 1 calcium ion per subunit. Binds 1 PQQ per subunit. PQQ is inserted between disulfide Cys-105-Cys-106 and the indole ring of Trp-239.
Subunit structure	Heterotetramer of 2 alpha and 2 beta subunits.
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.

Ontologies

Keywords
Biological process	Methanol utilization
Cellular component	Cell inner membrane Cell membrane Membrane
Ligand	Calcium Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond PQQ
Technical term	3D-structure
Gene Ontology (GO)
Biological process	methanol metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alcohol dehydrogenase (acceptor) activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

573

Methanol dehydrogenase subunit 1

PRO_0000205342

Sites

Active site

1

Proton acceptor

Metal binding

1

Calcium

Metal binding

1

Calcium

Amino acid modifications

Disulfide bond

Disulfide bond

Disulfide bond

Secondary structure

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573

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P38539-1 [UniParc].

Last modified November 8, 2002. Version 2.
Checksum: A06C9B3091BB8F0C
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573

62,635

        10         20         30         40         50         60 
MADADLDKQV NTAGAWPIAT GGYYSQHNSP LAQINKSNVK NVKAAWSFST GVLNGHEGAP 

        70         80         90        100        110        120 
LVIGDMMYVH SAFPNNTYAL NLNDPGKIVW QHKPKQDAST KAVMCCDVVD RGLAYGAGQI 

       130        140        150        160        170        180 
VKKQANGHLL ALDAKTGKIN WEVEVCDPKV GSTLTQAPFV AKDTVLMGCS GAELGVRGAV 

       190        200        210        220        230        240 
NAFDLKTGEL KWRAFATGSD DSVRLAKDFN SANPHYGQFG LGTKTWEGDA WKIGGGTNWG 

       250        260        270        280        290        300 
WYAYDPKLNL FYYGSGNPAP WNETMRPGDN KWTMTIWGRD LDTGMAKWGY QKTPHDEWDF 

       310        320        330        340        350        360 
AGVNQMVLTD QPVNGKMTPL LSHIDRNGIL YTLNRENGNL IVAEKVDPAV NVFKKVDLKT 

       370        380        390        400        410        420 
GTPVRDPEFA TRMDHKGTNI CPSAMGFHNQ GVDSYDPESR TLYAGLNHIC MDWEPFMLPY 

       430        440        450        460        470        480 
RAGQFFVGAT LAMYPGPNGP TKKEMGQIRA FDLTTGKAKW TKWEKFAAWG GTLYTKGGLV 

       490        500        510        520        530        540 
WYATLDGYLK ALDNKDGKEL WNFKMPSGGI GSPMTYSFKG KQYIGSMYGV GGWPGVGLVF 

       550        560        570 
DLTDPSAGLG AVGAFRELQN HTQMGGGLMV FSL

References

[1]	"Determination of the gene sequence and the three-dimensional structure at 2.4 angstroms resolution of methanol dehydrogenase from Methylophilus W3A1." Xia Z.-X., Dai W.-W., Zhang Y.-F., White S.A., Boyd G.D., Mathews F.S. J. Mol. Biol. 259:480-501(1996) [PubMed: 8676383] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[2]	"Pyrroloquinoline quinone (PQQ) and quinoprotein enzymes." Anthony C. Antioxid. Redox Signal. 3:757-774(2001) [PubMed: 11761326] [Abstract] Cited for: REVIEW.
[3]	"The active site structure of the calcium-containing quinoprotein methanol dehydrogenase." White S.A., Boyd G.D., Mathews F.S., Xia Z.-X., Dai W.-W., Zhang Y.-F., Davidson V.L. Biochemistry 32:12955-12958(1993) [PubMed: 8241148] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[4]	"The three-dimensional structures of methanol dehydrogenase from two methylotrophic bacteria at 2.6-A resolution." Xia Z.-X., Dai W.-W., Xiong J.-P., Hao Z.-P., Davidson V.L., White S.A., Mathews F.S. J. Biol. Chem. 267:22289-22297(1992) [PubMed: 1331050] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

U41040 Genomic DNA. Translation: AAA83765.1.

PIR

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G72	X-ray	1.90	A/C	1-573	[»]
2AD6	X-ray	1.50	A/C	3-573	[»]
2AD7	X-ray	1.50	A/C	3-573	[»]
2AD8	X-ray	1.60	A/C	3-573	[»]
4AAH	X-ray	2.40	A/C	3-573	[»]

ModBase

Enzyme and pathway databases

BRENDA

1.1.99.8. 1880.

Family and domain databases

InterPro

IPR019556. PQQ-dependent_C.
IPR019551. PQQ-dependent_N.
IPR018391. PQQ_beta_propeller_repeat.
IPR017512. PQQ_MeOH/EtOH_DH.
IPR002372. PQQ_repeat.
IPR011047. Quino_AlcDH-like.
IPR001479. Quinoprotein_DH_CS.
[Graphical view]

Gene3D

G3DSA:2.140.10.10. Quinoprotein_alc_DH-like. 1 hit.

Pfam

PF01011. PQQ. 5 hits.
PF10535. PQQ_C. 1 hit.
PF10527. PQQ_N. 1 hit.
[Graphical view]

SMART

SM00564. PQQ. 4 hits.
[Graphical view]

TIGRFAMs

TIGR03075. PQQ_enz_alc_DH. 1 hit.

PROSITE

PS00363. BACTERIAL_PQQ_1. False negative.
PS00364. BACTERIAL_PQQ_2. 1 hit.
[Graphical view]

ProtoNet

Entry information

Entry name

DHM1_METME

Accession

Primary (citable) accession number: P38539
Secondary accession number(s): Q59540

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	November 8, 2002
Last modified:	June 16, 2009
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents