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Reviewed, UniProtKB/Swiss-Prot P22641 (DHML_PARVE)

Last modified February 9, 2010. Version 84. 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
Alternative name(s):
    Methylamine dehydrogenase subunit beta
Gene names
Name: mauA
Synonyms: madB
OrganismParacoccus versutus (Thiobacillus versutus)
Taxonomic identifier34007 [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 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
Direct protein sequencing
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 Ref.2 Ref.3
Chain58 – 188131Methylamine dehydrogenase light chain
PRO_0000025576

Amino acid modifications

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

Experimental info

Sequence conflict891D → A AA sequence Ref.2
Sequence conflict971G → A AA sequence Ref.2
Sequence conflict1021N → S AA sequence Ref.2
Sequence conflict108 – 1125KLATA → LVASG AA sequence Ref.2
Sequence conflict1161A → G AA sequence Ref.2
Sequence conflict122 – 1298TDGQSYLI → PDPNKYIT AA sequence Ref.2
Sequence conflict1441P → A AA sequence Ref.2
Sequence conflict156 – 1594RPEF → NKD AA sequence Ref.2
Sequence conflict1691A → G AA sequence Ref.2
Sequence conflict172 – 1732DA → G AA sequence Ref.2
Sequence conflict1791T → S AA sequence Ref.2
Sequence conflict183 – 1886IVGKAS → VSGA AA sequence Ref.2

Secondary structure

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

Details...

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Sequences

Sequence LengthMass (Da)Tools
P22641-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 923C5461737C63FA

FASTA18820,358
        10         20         30         40         50         60 
MLGNFRFDDM VEKLSRRVAG RTSRRGAIGR LGTVLAGAAL VPLLPVDRRG RVSRANAAGP 

        70         80         90        100        110        120 
AEGVDPRAKW QPQDNDIQAC DYWRHCSIDG NICDCSGGSL TNCPPGTKLA TASWVASCYN 

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


SPIVGKAS

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References

[1]"Cloning, sequencing and expression studies of the genes encoding amicyanin and the beta-subunit of methylamine dehydrogenase from Thiobacillus versutus."
Ubbink M., van Kleef M.A., Kleinjan D.J., Hoitink C.W., Huitema F., Beintema J.J., Duine J.A., Canters G.W.
Eur. J. Biochem. 202:1003-1012(1991) [PubMed: 1765062] [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: 2792083] [Abstract]
Cited for: PROTEIN SEQUENCE OF 58-188, X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
[3]"N-terminal heterogeneity of methylamine dehydrogenase from Thiobacillus versutus."
Van Beeumen J., Van Driessche G., Huitema F., Duine J.A., Canters G.W.
FEBS Lett. 333:188-192(1993) [PubMed: 7901050] [Abstract]
Cited for: PROTEIN SEQUENCE OF 58-66.
[4]"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: 2085423] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M58001 Genomic DNA. Translation: AAA50570.1.
PIRS19731.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MAEX-ray2.80L64-187[»]
1MAFX-ray2.60L64-187[»]
2MADX-ray2.25L64-187[»]
3C75X-ray2.50L/M1-188[»]
ModBaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3902.
BRENDA1.4.99.3. 277244.

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_PARVE
AccessionPrimary (citable) accession number: P22641
Secondary accession number(s): Q56458
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1997
Last modified: February 9, 2010
This is version 84 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