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P29894 (DHMH_PARDE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 91. 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

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
OrganismParacoccus denitrificans
Taxonomic identifier266 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Protein attributes

Sequence length417 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_processmethylamine 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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828Or 26 Potential
Chain29 – 417389Methylamine dehydrogenase heavy chain
PRO_0000025580

Amino acid modifications

Disulfide bond212 ↔ 227

Secondary structure

.............................................................................. 417
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29894 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 8187A8B694208BE2

FASTA41745,440
        10         20         30         40         50         60 
MALPPNFMPL FRASLIGLGL GCSALALAAS AQDAPEAETQ AQETQGQAAA RAAAADLAAG 

        70         80         90        100        110        120 
QDDEPRILEA PAPDARRVYV NDPAHFAAVT QQFVIDGEAG RVIGMIDGGF LPNPVVADDG 

       130        140        150        160        170        180 
SFIAHASTVF SRIARGERTD YVEVFDPVTL LPTADIELPD APRFLVGTYP WMTSLTPDGK 

       190        200        210        220        230        240 
TLLFYQFSPA PAVGVVDLEG KAFKRMLDVP DCYHIFPTAP DTFFMHCRDG SLAKVAFGTE 

       250        260        270        280        290        300 
GTPEITHTEV FHPEDEFLIN HPAYSQKAGR LVWPTYTGKI HQIDLSSGDA KFLPAVEALT 

       310        320        330        340        350        360 
EAERADGWRP GGWQQVAYHR ALDRIYLLVD QRDEWRHKTA SRLLVVLDAK TGERLAKFEM 

       370        380        390        400        410 
GHEIDSINVS QDEKPLLYAL STGDKTLYIH DAESGEELRS VNQLGHGPQV ITTADMG 

« Hide

References

[1]"The genetic organization of the mau gene cluster of the facultative autotroph Paracoccus denitrificans."
Chistoserdov A.Y., Boyd J., Mathews F.S., Lidstrom M.E.
Biochem. Biophys. Res. Commun. 184:1181-1189(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Expression of the mau genes involved in methylamine metabolism in Paracoccus denitrificans is under control of a LysR-type transcriptional activator."
van Spanning R.J.M., van der Palen C.J., Slotboom D.J., Reijnders W.N., Stouthamer A.H., Duine J.A.
Eur. J. Biochem. 226:201-210(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
Strain: ATCC 17741 / DSM 413 / NBRC 16712 / NCCB 22021 / NCIMB 11627.
[3]"Three-dimensional structure of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans determined by molecular replacement at 2.8-A resolution."
Chen L., Mathews F.S., Davidson V.L., Huizinga E.G., Vellieux F.M.D., Hol W.G.J.
Proteins 14:288-299(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[4]"Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin."
Chen L., Durley R., Poliks B.J., Hamada K., Chen Z., Mathews F.S., Davidson V.L., Satow Y., Huizinga E.G., Vellieux F.M.D., Hol W.G.J.
Biochemistry 31:4959-4964(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH AMICYANIN.
[5]"Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i."
Chen L., Durley R., Mathews F.S., Davidson V.L.
Science 264:86-90(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M90099 Genomic DNA. Translation: AAA25580.1.
U12464 Genomic DNA. Translation: AAA56724.1.
PIRJH0660.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MG2X-ray2.25A/E/I/M28-417[»]
1MG3X-ray2.40A/E/I/M28-417[»]
2BBKX-ray1.75H/J63-417[»]
2GC4X-ray1.90A/E/I/M32-417[»]
2GC7X-ray1.90A/E/I/M32-417[»]
2J55X-ray2.15H/J32-417[»]
2J56X-ray2.10H/J32-417[»]
2J57X-ray2.25G/H/I/J32-417[»]
2MTAX-ray2.40H45-417[»]
ProteinModelPortalP29894.
SMRP29894. Positions 36-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6253N.
IntActP29894. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3909.
SABIO-RKP29894.

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. SSF50969. 1 hit.
TIGRFAMsTIGR02658. TTQ_MADH_Hv. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP29894.

Entry information

Entry nameDHMH_PARDE
AccessionPrimary (citable) accession number: P29894
Secondary accession number(s): Q79D76
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: October 16, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references