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Reviewed, UniProtKB/Swiss-Prot P22619 (DHML_PARDE)

Last modified February 9, 2010. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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Names and origin

Protein namesRecommended name:
    Methylamine dehydrogenase light chain
      Short name=MADH
    EC=1.4.99.3
Gene names
Name: mauA
OrganismParacoccus denitrificans
Taxonomic identifier266 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus

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Protein attributes

Sequence length188 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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

Catalytic activity

RCH2NH2 + H2O + acceptor = RCHO + NH3 + reduced acceptor.

Cofactor

Contains 1 tryptophan tryptophylquinone per subunit.

Pathway

One-carbon metabolism; methylamine degradation; formaldehyde from methylamine: step 1/1.

Subunit structure

Heterotetramer of two light and two heavy chains.

Subcellular location

Periplasm.

Post-translational modification

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.

Tryptophan tryptophylquinone (TTQ) is formed by oxidation of the indole ring of a tryptophan to form tryptophylquinone followed by covalent cross-linking with another tryptophan residue.

Sequence similarities

Belongs to the aromatic amine dehydrogenase light chain family.

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Ontologies

Keywords
   Biological processElectron transport
Transport
   Cellular componentPeriplasm
   DomainSignal
   Molecular functionOxidoreductase
   PTMDisulfide bond
TTQ
   Technical term3D-structure
Gene Ontology (GO)
   Biological processamine metabolic process

Inferred from electronic annotation. Source: InterPro

electron transport chain

Inferred from electronic annotation. Source: UniProtKB-KW

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentouter membrane-bounded periplasmic space

Inferred from electronic annotation. Source: InterPro

   Molecular functionamine dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 5757Tat-type signal Potential
Chain58 – 188131Methylamine dehydrogenase light chain
PRO_0000025575

Amino acid modifications

Modified residue1141Tryptophylquinone Ref.3
Disulfide bond80 ↔ 145
Disulfide bond86 ↔ 118
Disulfide bond93 ↔ 178
Disulfide bond95 ↔ 143
Disulfide bond103 ↔ 134
Disulfide bond135 ↔ 166
Cross-link114 ↔ 165Tryptophan tryptophylquinone (Trp-Trp) Ref.3

Secondary structure

1 .......................... 188
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P22619-1 [UniParc].

Last modified April 1, 1993. Version 2.
Checksum: E3D9DE4454268BE8

FASTA18820,393
        10         20         30         40         50         60 
MLGNFRFDDM VEKLSRRVAG QTSRRSVIGK LGTAMLGIGL VPLLPVDRRG RVSRANAADA 

        70         80         90        100        110        120 
PAGTDPRAKW VPQDNDIQAC DYWRHCSIDG NICDCSGGSL TNCPPGTKLA TASWVASCYN 

       130        140        150        160        170        180 
PTDGQSYLIA YRDCCGYNVS GRCPCLNTEG ELPVYRPEFA NDIIWCFGAE DDAMTYHCTI 


SPIVGKAS

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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: 1590782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation."
van Spanning R.J.M., Wansell C.W., Reijnders W.N.M., Oltmann L.F., Stouthamer A.H.
FEBS Lett. 275:217-220(1990) [PubMed: 2261991] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 158-188.
Strain: ATCC 19367 / IFO 13301 / NCIMB 8944 / NRRL B-3785.
[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: 1409575] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 64-188.
[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: 1599920] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 64-188 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: 8140419] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M90098 Genomic DNA. Translation: AAA25578.1.
X55665 Genomic DNA. Translation: CAA39198.1.
PIRJH0661.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MG2X-ray2.25B/F/J/N58-188[»]
1MG3X-ray2.40B/F/J/N58-188[»]
2BBKX-ray1.75L/M64-188[»]
2GC4X-ray1.90B/F/J/N58-188[»]
2GC7X-ray1.90B/F/J/N58-188[»]
2J55X-ray2.15L/M58-188[»]
2J56X-ray2.10L/M58-188[»]
2J57X-ray2.25K/L/M/N58-188[»]
2MTAX-ray2.40L64-188[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-6254N.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3910.
BRENDA1.4.99.3. 59.

Family and domain databases

InterProIPR016008. Amine_DH_bsu.
IPR004229. MeN_DH_Ltc.
IPR013504. MeN_DH_Ltc_C.
IPR006311. TAT_signal.
[Graphical view]
Gene3DG3DSA:2.60.30.10. MADH_Lt_C. 1 hit.
PfamPF02975. Me-amine-dh_L. 1 hit.
[Graphical view]
PIRSFPIRSF000192. Amine_dh_beta. 1 hit.
TIGRFAMsTIGR01409. TAT_signal_seq. 1 hit.
TIGR02659. TTQ_MADH_Lt. 1 hit.
PROSITEPS51318. TAT. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameDHML_PARDE
AccessionPrimary (citable) accession number: P22619
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: April 1, 1993
Last modified: February 9, 2010
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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