Trimethylamine dehydrogenase

Details

Name
Trimethylamine dehydrogenase
Synonyms
  • 1.5.8.2
  • TMADh
Gene Name
tmd
Organism
Methylophilus methylotrophus
Amino acid sequence
>lcl|BSEQ0012125|Trimethylamine dehydrogenase
MARDPKHDILFEPIQIGPKTLRNRFYQVPHCIGAGSDKPGFQSAHRSVKAEGGWAALNTE
YCSINPESDDTHRLSARIWDEGDVRNLKAMTDEVHKYGALAGVELWYGGAHAPNMESRAT
PRGPSQYASEFETLSYCKEMDLSDIAQVQQFYVDAAKRSRDAGFDIVYVYGAHSYLPLQF
LNPYYNKRTDKYGGSLENRARFWLETLEKVKHAVGSDCAIATRFGVDTVYGPGQIEAEVD
GQKFVEMADSLVDMWDITIGDIAEWGEDAGPSRFYQQGHTIPWVKLVKQVSKKPVLGVGR
YTDPEKMIEIVTKGYADIIGCARPSIADPFLPQKVEQGRYDDIRVCIGCNVCISRWEIGG
PPMICTQNATAGEEYRRGWHPEKFRQTKNKDSVLIVGAGPSGSEAARVLMESGYTVHLTD
TAEKIGGHLNQVAALPGLGEWSYHRDYRETQITKLLKKNKESQLALGQKPMTADDVLQYG
ADKVIIATGARWNTDGTNCLTHDPIPGADASLPDQLTPEQVMDGKKKIGKRVVILNADTY
FMAPSLAEKLATAGHEVTIVSGVHLANYMHFTLEYPNMMRRLHELHVEELGDHFCSRIEP
GRMEIYNIWGDGSKRTYRGPGVSPRDANTSHRWIEFDSLVLVTGRHSECTLWNELKARES
EWAENDIKGIYLIGDAEAPRLIADATFTGHRVAREIEEANPQIAIPYKRETIAWGTPHMP
GGNFKIEYKV
Number of residues
730
Molecular Weight
81628.615
Theoretical pI
6.31
GO Classification
Functions
4 iron, 4 sulfur cluster binding / FMN binding / metal ion binding / trimethylamine dehydrogenase activity
General Function
Trimethylamine dehydrogenase activity
Specific Function
Not Available
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0005925|2193 bp
ATGGCACGAGATCCGAAGCATGATATTTTGTTTGAGCCAATACAAATTGGCCCCAAAACA
TTACGCAATCGCTTTTACCAGGTACCGCATTGTATCGGTGCTGGATCCGATAAGCCTGGC
TTTCAATCTGCACACCGTTCGGTTAAAGCTGAAGGCGGTTGGGCGGCTTTAAACACTGAA
TATTGCTCCATTAACCCTGAGTCAGATGATACACATCGTTTGTCCGCACGTATCTGGGAC
GAAGGTGATGTGCGTAACTTGAAAGCCATGACCGACGAAGTTCATAAGTACGGTGCATTA
GCCGGGGTCGAGTTATGGTACGGCGGTGCACACGCACCTAACATGGAGTCACGCGCGACC
CCACGTGGTCCAAGCCAATATGCGTCAGAGTTTGAGACGCTGTCCTACTGTAAAGAAATG
GATCTAAGCGATATCGCTCAGGTACAGCAGTTCTATGTTGATGCAGCGAAGCGCTCTCGT
GACGCTGGTTTTGACATTGTCTACGTATACGGTGCGCACTCTTATTTGCCGCTGCAATTC
CTGAATCCATACTACAACAAGCGTACAGACAAATACGGTGGCTCATTGGAGAACCGTGCG
CGCTTCTGGCTGGAAACACTAGAAAAAGTGAAGCATGCCGTGGGTTCAGATTGTGCGATT
GCGACACGTTTCGGCGTGGATACTGTGTATGGTCCAGGTCAAATCGAAGCAGAAGTGGAT
GGTCAGAAGTTTGTTGAAATGGCTGACTCACTGGTCGATATGTGGGATATCACAATTGGT
GATATTGCCGAGTGGGGCGAAGATGCGGGGCCGTCACGTTTCTACCAGCAAGGTCACACC
ATCCCTTGGGTTAAATTGGTCAAACAGGTTTCCAAAAAACCAGTATTAGGCGTTGGCCGT
TATACCGACCCTGAGAAAATGATCGAAATCGTCACCAAAGGCTATGCCGACATTATTGGT
TGTGCACGCCCTTCTATTGCTGATCCGTTCTTGCCACAAAAGGTTGAGCAGGGTCGCTAC
GACGATATCCGTGTATGTATTGGTTGTAACGTGTGTATTTCCCGCTGGGAAATCGGTGGT
CCTCCAATGATTTGTACCCAGAATGCGACAGCAGGTGAAGAGTACCGTCGTGGTTGGCAT
CCAGAGAAATTCCGTCAAACCAAGAACAAGGATTCTGTATTGATCGTTGGTGCAGGCCCA
TCCGGTTCTGAAGCAGCCCGCGTATTGATGGAAAGCGGTTATACCGTGCACTTGACCGAT
ACCGCAGAGAAAATCGGTGGTCACTTGAACCAGGTGGCAGCGTTGCCTGGCTTGGGTGAG
TGGAGCTATCACCGCGATTATCGTGAAACACAAATCACCAAGTTGCTGAAGAAGAACAAA
GAAAGCCAATTGGCATTGGGTCAAAAACCAATGACGGCTGACGACGTGCTGCAATATGGT
GCTGACAAAGTCATCATCGCTACCGGTGCGCGCTGGAATACCGATGGTACCAACTGCCTG
ACGCATGACCCAATTCCAGGGGCAGATGCTTCCTTGCCAGATCAACTGACACCAGAGCAA
GTCATGGATGGTAAGAAGAAGATTGGTAAGCGCGTGGTGATTCTGAATGCGGATACTTAT
TTCATGGCGCCTAGCCTGGCTGAGAAGCTTGCGACGGCTGGTCACGAAGTAACCATCGTT
TCTGGCGTGCACCTGGCTAACTACATGCACTTCACGCTGGAATATCCAAACATGATGCGT
CGTTTGCACGAACTGCATGTTGAAGAGTTGGGCGATCACTTCTGCTCACGTATCGAACCA
GGCCGTATGGAAATCTACAACATCTGGGGCGATGGTTCCAAACGTACTTACCGTGGCCCA
GGCGTTTCTCCGCGTGATGCCAATACCTCGCATCGTTGGATTGAGTTTGACTCCCTGGTG
CTGGTGACAGGCCGTCATTCAGAGTGCACGCTGTGGAATGAGTTAAAAGCCCGTGAATCT
GAGTGGGCTGAGAACGACATTAAAGGTATCTACCTGATTGGTGATGCTGAGGCGCCTCGT
TTGATTGCTGATGCCACATTTACGGGTCACCGTGTGGCCCGTGAAATTGAAGAAGCAAAC
CCACAAATTGCCATCCCATACAAGCGTGAAACCATCGCATGGGGCACGCCGCATATGCCA
GGTGGTAATTTCAAAATTGAGTACAAAGTTTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP16099
UniProtKB Entry NameDHTM_METME
GenBank Gene IDX68079
General References
  1. Boyd G, Mathews FS, Packman LC, Scrutton NS: Trimethylamine dehydrogenase of bacterium W3A1. Molecular cloning, sequence determination and over-expression of the gene. FEBS Lett. 1992 Aug 24;308(3):271-6. [Article]
  2. Kenney WC, McIntire W, Steenkamp DJ: Amino acid sequence of a cofactor peptide from trimethylamine dehydrogenase. FEBS Lett. 1978 Jan 1;85(1):137-40. [Article]
  3. Barber MJ, Neame PJ, Lim LW, White S, Matthews FS: Correlation of x-ray deduced and experimental amino acid sequences of trimethylamine dehydrogenase. J Biol Chem. 1992 Apr 5;267(10):6611-9. [Article]
  4. Leys D, Basran J, Talfournier F, Sutcliffe MJ, Scrutton NS: Extensive conformational sampling in a ternary electron transfer complex. Nat Struct Biol. 2003 Mar;10(3):219-25. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03247Flavin mononucleotideapproved, investigationalunknownDetails