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P23006 (DHMH_PARVE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Methylamine dehydrogenase heavy chain
Short name=MADH
EC=1.4.9.1
Alternative name(s):
Methylamine dehydrogenase (amicyanin)
Gene names
Name:mauB
Synonyms:madA
OrganismParacoccus versutus (Thiobacillus versutus)
Taxonomic identifier34007 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus

Protein attributes

Sequence length426 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin.

Catalytic activity

Methylamine + H2O + amicyanin = formaldehyde + ammonia + reduced amicyanin.

Subunit structure

Tetramer of two light and two heavy chains.

Subcellular location

Periplasm.

Sequence similarities

Belongs to the aromatic amine dehydrogenase heavy chain family.

Ontologies

Keywords
   Biological processElectron transport
Transport
   Cellular componentPeriplasm
   DomainSignal
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processelectron transport chain

Inferred from electronic annotation. Source: UniProtKB-KW

methylamine metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionamine dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

methylamine dehydrogenase (amicyanin) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 426395Methylamine dehydrogenase heavy chain
PRO_0000025581

Amino acid modifications

Disulfide bond221 ↔ 236

Secondary structure

1 .................................................................................. 426
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23006 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 4ECDF8F6A7AE8696

FASTA42646,388
        10         20         30         40         50         60 
MASARESTPR YLTLIGATLA CSALALGAAQ AQTEPAEPEA PAETAAADAA GQTEGQRGAA 

        70         80         90        100        110        120 
EAAAALAAGE ADEPVILEAP APDARRVYIQ DPAHFAAITQ QFVIDGSTGR ILGMTDGGFL 

       130        140        150        160        170        180 
PHPVAAEDGS FFAQASTVFE RIARGKRTDY VEVFDPVTFL PIADIELPDA PRFLVGTYQW 

       190        200        210        220        230        240 
MNALTPDNKN LLFYQFSPAP AVGVVDLEGK TFDRMLDVPD CYHIFPASPT VFYMNCRDGS 

       250        260        270        280        290        300 
LARVDFADGE TKVTNTEVFH TEDELLINHP AFSLRSGRLV WPTYTGKIFQ ADLTAEGATF 

       310        320        330        340        350        360 
RAPIEALTEA ERADDWRPGG WQQTAYHRQS DRIYLLVDQR DEWKHKAASR FVVVLNAETG 

       370        380        390        400        410        420 
ERINKIELGH EIDSINVSQD AEPLLYALSA GTQTLHIYDA ATGEELRSVD QLGRGPQIIT 


THDMDS

« Hide

References

[1]"Cloning and sequencing of the gene coding for the large subunit of methylamine dehydrogenase from Thiobacillus versutus."
Huitema F., van Beeumen J., van Driessche G., Duine J.A., Canters G.W.
J. Bacteriol. 175:6254-6259(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structure of quinoprotein methylamine dehydrogenase at 2.25-A resolution."
Vellieux F.M.D., Huitema F., Groendijk H., Kalk K.H., Jzn J.F., Jongejan J.A., Duine J.A., Petratos K., Drenth J., Hol W.G.J.
EMBO J. 8:2171-2178(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
[3]"Structure determination of quinoprotein methylamine dehydrogenase from Thiobacillus versutus."
Vellieux F.M.D., Kalk K.H., Hol W.G.J.
Acta Crystallogr. B 46:806-823(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L08575 Genomic DNA. Translation: AAA72335.1.
PIRA36934.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MAEX-ray2.80H59-400[»]
1MAFX-ray2.60H59-400[»]
2MADX-ray2.25H59-400[»]
3C75X-ray2.50H/J1-426[»]
ProteinModelPortalP23006.
SMRP23006. Positions 72-424.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3901.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR013476. MeN_DH_Hvc.
IPR009451. Metamine_DH_Hvc.
IPR011044. Quino_amine_DH_bsu.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamPF06433. Me-amine-dh_H. 1 hit.
[Graphical view]
PIRSFPIRSF017797. TTQ_MADH_Hv. 1 hit.
SUPFAMSSF50969. Amine_DH_B_like. 1 hit.
TIGRFAMsTIGR02658. TTQ_MADH_Hv. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP23006.

Entry information

Entry nameDHMH_PARVE
AccessionPrimary (citable) accession number: P23006
Secondary accession number(s): Q60052
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1997
Last modified: April 3, 2013
This is version 84 of the entry and version 2 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

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