P29898 (DHM2_PARDE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 31, 2011.
Version 67.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Methanol dehydrogenase [cytochrome c] subunit 2 EC=1.1.2.7 Alternative name(s): MDH small subunit beta MDH-associated peptide MEDH | ||
| Gene names |
| ||
| Organism | Paracoccus denitrificans | ||
| Taxonomic identifier | 266 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus |
Protein attributes
| Sequence length | 103 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the oxidation of primary alcohols including methanol By similarity. |
| Catalytic activity | A primary alcohol + 2 cytochrome c(L) = an aldehyde + 2 reduced cytochrome c(L). |
| Subunit structure | Heterotetramer composed of 2 alpha and 2 beta subunits. Ref.2 |
| Subcellular location | |
| Sequence similarities | Belongs to the methanol dehydrogenase subunit 2 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Methanol utilization |
| Cellular component | Periplasm |
| Domain | Signal |
| Molecular function | Oxidoreductase |
| PTM | Disulfide bond |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | methanol oxidation Inferred from electronic annotation. Source: InterPro |
| Cellular component | periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | alcohol dehydrogenase (NAD) 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 | |||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 20 | 20 | Potential | ||||||||||||
| Chain | 21 – 103 | 83 | Methanol dehydrogenase [cytochrome c] subunit 2 | PRO_0000025571 | |||||||||||
Amino acid modifications | |||||||||||||||
| Disulfide bond | 26 ↔ 32 | Ref.2 | |||||||||||||
Secondary structure | |||||||||||||||
Helix Strand Turn | |||||||||||||||
| Helix | 54 – 57 | 4 | |||||||||||||
| Helix | 59 – 81 | 23 | |||||||||||||
| Helix | 88 – 90 | 3 | |||||||||||||
Sequences
References
| [1] | "Isolation and characterization of the moxJ, moxG, moxI, and moxR genes of Paracoccus denitrificans: inactivation of moxJ, moxG, and moxR and the resultant effect on methylotrophic growth." van Spanning R.J.M., Wansell C.W., de Boer T., Hazelaar M.J., Anazawa H., Harms N., Oltmann L.F., Stouthamer A.H. J. Bacteriol. 173:6948-6961(1991) [PubMed: 1657871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [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 21-103 IN COMPLEX WITH ALPHA SUBUNIT, SUBUNIT, DISULFIDE BOND. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | M57684 Genomic DNA. Translation: AAA25584.1. | ||||||||||||
| PIR | C41377. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P29898. | ||||||||||||
| SMR | P29898. Positions 21-103. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | MetaCyc:MONOMER-3924. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR003420. Meth_DH_bsu. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:4.10.160.10. Meth_DH_beta. 1 hit. | ||||||||||||
| Pfam | PF02315. MDH. 1 hit. [Graphical view] | ||||||||||||
| PIRSF | PIRSF029163. Meth_DH_beta. 1 hit. | ||||||||||||
| SUPFAM | SSF48666. Meth_DH_beta. 1 hit. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | DHM2_PARDE | ||||||||
| Accession | Primary (citable) accession number: P29898 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

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