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Reviewed, UniProtKB/Swiss-Prot Q48303 (DHDM_HYPSX)

Last modified December 16, 2008. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
    Dimethylamine dehydrogenase
      Short name=DMADh
    EC=1.5.8.1
Gene names
Name: dmd
OrganismHyphomicrobium sp. (strain x)
Taxonomic identifier79673 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesHyphomicrobiaceaeHyphomicrobium

Protein attributes

Sequence length736 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

Dimethylamine + H(2)O + electron-transferring flavoprotein = methylamine + formaldehyde + reduced electron-transferring flavoprotein.

Cofactor

Binds 1 FMN covalently per subunit By similarity.

Binds 1 4Fe-4S cluster per subunit By similarity.

Sequence similarities

In the N-terminal section; belongs to the NADH:flavin oxidoreductase/NADH oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 736735Dimethylamine dehydrogenase
PRO_0000194471

Regions

Nucleotide binding398 – 42730ADP By similarity
Region176 – 1794Substrate-binding By similarity

Sites

Active site1811Proton donor By similarity
Metal binding3521Iron-sulfur (4Fe-4S) By similarity
Metal binding3551Iron-sulfur (4Fe-4S) By similarity
Metal binding3581Iron-sulfur (4Fe-4S) By similarity
Metal binding3711Iron-sulfur (4Fe-4S) By similarity
Binding site2291FMN By similarity
Binding site3291FMN By similarity

Amino acid modifications

Modified residue311S-6-FMN cysteine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q48303-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A3EE943F5617851B

FASTA73682,655
        10         20         30         40         50         60 
MARDPRFDIL FTPLKLGSKT IRNRFYQVPH CNGAGTNSPG MNMAHRGIKA EGGWGAVNTE 

        70         80         90        100        110        120 
QCSIHPECDD TLRITARIWD QGDMRNLRAM VDHVHSHGSL AGCELFYGGP HAPAIESRTI 

       130        140        150        160        170        180 
SRGPSQYNSE FATVPGCPGF TYNHEADIDE LERLQQQYVD AALRARDTGF DLVNVYGAHA 

       190        200        210        220        230        240 
YGPMQWLNPY YNRRTDKYGG SFDNRARFWI ETLEKIRRAV NDDVALVTRC ATDTLYGTKG 

       250        260        270        280        290        300 
VELTEDGLRF IELASPYLDL WDVNIGDIAE WGEDAGPSRF YPIAHENDWI RHIKQATNKP 

       310        320        330        340        350        360 
VVGVGRYYDP EKMLQVIKAG IIDIIGAARP SIADPWLPRK IDEGRVDDIR TCIGCNVCIS 

       370        380        390        400        410        420 
RWEMGGVPFI CTQNATAGEE YRRGWHPEKF EPKKSDHDVL IVGAGPAGSE CARVLMERGY 

       430        440        450        460        470        480 
TVHLVDTREK TGGYVNDVAT LPGLGEWSFH RDYRQTQLEK LLKKNPECQI ALKQKPMTAD 

       490        500        510        520        530        540 
DILQYGASRV VIATGAKWST TGVNHRTHEP IPGADASLPH VLTPEQVYEG KKAVGKRVMI 

       550        560        570        580        590        600 
INYDAYYTAP SLAEKFARAG HDVTVATVCG LGAYMEYTLE GANMQRLIHE LGIKVLGETG 

       610        620        630        640        650        660 
CSRVEQGRVE LFNIWGEGYK RSYKGAGQLP RNENTSHEWH ECDTVILVTS RRSEDTLYRE 

       670        680        690        700        710        720 
LKARKGEWEA NGITNVFVIG DAESPRIIAD ATFDGHRLAR EIEDADPQHQ KPYKREQRAW 

       730 
GTAYNPDENP DLVWRV 

« Hide

References

[1]"The primary structure of Hyphomicrobium X dimethylamine dehydrogenase. Relationship to trimethylamine dehydrogenase and implications for substrate recognition."
Yang C.C., Packman L.C., Scrutton N.S.
Eur. J. Biochem. 232:264-271(1995) [PubMed: 7556160] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

X89575 Genomic DNA. Translation: CAA61752.1.

3D structure databases

HSSPHSSP built from PDB template 1O94 based on UniProtKB P16099.
ModBaseSearch...

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR001155. OxRdtase_FMN_N.
IPR001100. Pyr_nuc-diS_OxRdtase.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PfamPF00724. Oxidored_FMN. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00411. PNDRDTASEI.
ProtoNetSearch...

Entry information

Entry nameDHDM_HYPSX
AccessionPrimary (citable) accession number: Q48303
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: December 16, 2008
This is version 56 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

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