Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P12293 (DHM1_PARDE)

Last modified February 9, 2010. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Methanol dehydrogenase subunit 1
    EC=1.1.99.8
Alternative name(s):
    MDH large subunit alpha
    MEDH
Gene names
Name: moxF
OrganismParacoccus denitrificans
Taxonomic identifier266 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus

Hide | Top

Protein attributes

Sequence length631 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Catalytic activity

A primary alcohol + acceptor = an aldehyde + reduced acceptor.

Cofactor

Binds 1 PQQ group per subunit. PQQ is inserted between disulfide Cys-135-Cys-136 and the indole ring of Trp-275. Ref.2

Binds 1 calcium ion per subunit. Ref.2

Subunit structure

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

Subcellular location

Periplasm.

Miscellaneous

MDH is the major protein in the cell during growth on methanol (in P.denitrificans MDH constitutes up to 15% of the total cell protein).

Sequence similarities

Belongs to the bacterial PQQ dehydrogenase family.

Hide | Top

Ontologies

Keywords
   Biological processMethanol utilization
   Cellular componentPeriplasm
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionOxidoreductase
   PTMDisulfide bond
PQQ
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processmethanol metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmembrane

Inferred from electronic annotation. Source: InterPro

outer membrane-bounded periplasmic space

Inferred from electronic annotation. Source: InterPro

   Molecular functionalcohol dehydrogenase (acceptor) activity

Inferred from electronic annotation. Source: EC

calcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Ref.1
Chain33 – 631599Methanol dehydrogenase subunit 1
PRO_0000025568

Sites

Active site3351Proton acceptor
Metal binding2091Calcium
Metal binding2931Calcium

Amino acid modifications

Disulfide bond135 ↔ 136 Ref.2
Disulfide bond418 ↔ 447 Ref.2

Secondary structure

1 ........................................................................................................................... 631
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P12293-1 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 0934DC93FFC5730B

FASTA63169,799
        10         20         30         40         50         60 
MNRNTPKARG ASSLAMAVAM GLAVLTTAPA TANDQLVELA KDPANWVMTG RDYNAQNYSE 

        70         80         90        100        110        120 
MTDINKENVK QLRPAWSFST GVLHGHEGTP LVVGDRMFIH TPFPNTTFAL DLNEPGKILW 

       130        140        150        160        170        180 
QNKPKQNPTA RTVACCDVVN RGLAYWPGDD QVKPLIFRTQ LDGHIVAMDA ETGETRWIME 

       190        200        210        220        230        240 
NSDIKVGSTL TIAPYVIKDL VLVGSSGAEL GVRGYVTAYD VKSGEMRWRA FATGPDEELL 

       250        260        270        280        290        300 
LAEDFNAPNP HYGQKNLGLE TWEGDAWKIG GGTNWGWYAY DPEVDLFYYG SGNPAPWNET 

       310        320        330        340        350        360 
MRPGDNKWTM AIWGREATTG EAKFAYQKTP HDEWDYAGVN VMMLSEQEDK QGQMRKLLTH 

       370        380        390        400        410        420 
PDRNGIVYTL DRTNGDLISA DKMDDTVNWV KEVQLDTGLP VRDPEFGTRM DHKARDICPS 

       430        440        450        460        470        480 
AMGYHNQGHD SYDPERKVFM LGINHICMDW EPFMLPYRAG QFFVGATLTM YPGPKATAER 

       490        500        510        520        530        540 
AGAGQIKAYD AISGEMKWEK MERFSVWGGT MATAGGLTFY VTLDGFIKAR DSDTGDLLWK 

       550        560        570        580        590        600 
FKLPSGVIGH PMTYKHDGRQ YVAIMYGVGG WPGVGLVFDL ADPTAGLGSV GAFKRLQEFT 

       610        620        630 
QMGGGVMVFS LDGESPYSDP NVGEYAPGEP T

« Hide

Hide | Top

References

[1]"Isolation and nucleotide sequence of the methanol dehydrogenase structural gene from Paracoccus denitrificans."
Harms N., de Vries G.E., Maurer K., Hoogendijk J., Stouthamer A.H.
J. Bacteriol. 169:3969-3975(1987) [PubMed: 3114231] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 33-49.
[2]"X-ray structure of methanol dehydrogenase from Paracoccus denitrificans and molecular modeling of its interactions with cytochrome c-551i."
Xia Z.-X., Dai W.W., He Y.-N., White S.A., Mathews F.S., Davidson V.L.
J. Biol. Inorg. Chem. 8:843-854(2003) [PubMed: 14505072] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 33-631 IN COMPLEX WITH BETA SUBUNIT, SUBUNIT, COFACTOR, DISULFIDE BONDS.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M17339 Genomic DNA. Translation: AAA88366.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LRWX-ray2.50A/C33-631[»]
ModBaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3923.
BRENDA1.1.99.8. 59.

Family and domain databases

InterProIPR019556. PQQ-dependant_C.
IPR019551. PQQ-dependant_N.
IPR018391. PQQ_beta_propeller_repeat.
IPR017512. PQQ_MeOH/EtOH_DH.
IPR002372. PQQ_repeat.
IPR011047. Quino_AlcDH-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. 4 hits.
[Graphical view]
TIGRFAMsTIGR03075. PQQ_enz_alc_DH. 1 hit.
PROSITEPS00363. BACTERIAL_PQQ_1. 1 hit.
PS00364. BACTERIAL_PQQ_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameDHM1_PARDE
AccessionPrimary (citable) accession number: P12293
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: February 9, 2010
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

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