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Reviewed, UniProtKB/Swiss-Prot P23006 (DHMH_PARVE)

Last modified June 16, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
    Methylamine dehydrogenase heavy chain
      Short name=MADH
    EC=1.4.99.3
Gene names
Name: mauB
Synonyms: madA
OrganismParacoccus versutus (Thiobacillus versutus)
Taxonomic identifier34007 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

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

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

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

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionamine dehydrogenase 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

Sequences

Sequence LengthMass (Da)Tools
P23006-1 [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: 8407797] [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: 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: 2085423] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

L08575 Genomic DNA. Translation: AAA72335.1.
PIRA36934.

3D structure databases

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

Enzyme and pathway databases

BioCycMetaCyc:MON-3901.
BRENDA1.4.99.3. 277244.

Family and domain databases

InterProIPR013476. MeN_DH_hvc.
IPR009451. Metamine_DH_Hsu.
IPR015943. WD40/YVTN_repeat-like.
[Graphical view]
Gene3DG3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
PfamPF06433. Me-amine-dh_H. 1 hit.
[Graphical view]
PIRSFPIRSF017797. TTQ_MADH_Hv. 1 hit.
TIGRFAMsTIGR02658. TTQ_MADH_Hv. 1 hit.
ProtoNetSearch...

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: June 16, 2009
This is version 66 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)

Relevant documents

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