Mersacidin decarboxylase

Details

Name
Mersacidin decarboxylase
Synonyms
  • 4.1.1.-
  • Mersacidin-modifying enzyme MrsD
Gene Name
mrsD
Organism
Bacillus sp. (strain HIL-Y85/54728)
Amino acid sequence
>lcl|BSEQ0012097|Mersacidin decarboxylase
MSISILKDKKLLIGICGSISSVGISSYLLYFKSFFKEIRVVMTKTAEDLIPAHTVSYFCD
HVYSEHGENGKRHSHVEIGRWADIYCIIPATANILGQTANGVAMNLVATTVLAHPHNTIF
FPNMNDLMWNKTVVSRNIEQLRKDGHIVIEPVEIMAFEIATGTRKPNRGLITPDKALLAI
EKGFKERTKHPSLT
Number of residues
194
Molecular Weight
21677.045
Theoretical pI
9.14
GO Classification
Functions
lyase activity / oxidoreductase activity
Processes
antibiotic biosynthetic process / oxidation-reduction process
General Function
Oxidoreductase activity
Specific Function
Catalyzes the oxidative decarboxylation of the C-terminal cysteine residue of mersacidin to an aminoenethiol residue.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0005842|585 bp
TTATGTTAGTGAGGGGTGTTTTGTTCTTTCTTTAAAACCTTTTTCTATTGCTAATAAAGC
TTTGTCGGGTGTAATTAGACCACGATTAGGTTTTCTTGTACCCGTCGCAATCTCAAACGC
CATAATTTCAACTGGTTCAATAACAATATGCCCATCTTTTCTTAATTGTTCAATATTCCT
GGAAACAACTGTTTTATTCCACATTAAATCGTTCATATTAGGAAAGAAAATAGTGTTATG
TGGATGAGCTAATACAGTAGTTGCAACTAAATTCATTGCTACACCATTAGCAGTTTGTCC
TAAGATGTTCGCTGTAGCTGGAATAATGCAATATATGTCCGCCCAGCGGCCAATTTCTAC
GTGGCTATGTCTTTTTCCGTTTTCCCCATGTTCTGAGTATACATGGTCACAAAAATAAGA
AACAGTATGAGCTGGAATAAGGTCTTCCGCTGTTTTTGTCATAACAACCCTTATTTCCTT
AAAGAAGCTTTTAAAATATAAGAGATACGAGGAGATGCCGACAGATGAGATTGATCCGCA
AATCCCGATCAATAACTTTTTATCTTTTAATATTGAAATACTCAT
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ9RC23
UniProtKB Entry NameMRSD_BACSY
GenBank Gene IDAJ250862
General References
  1. Altena K, Guder A, Cramer C, Bierbaum G: Biosynthesis of the lantibiotic mersacidin: organization of a type B lantibiotic gene cluster. Appl Environ Microbiol. 2000 Jun;66(6):2565-71. [Article]
  2. Majer F, Schmid DG, Altena K, Bierbaum G, Kupke T: The flavoprotein MrsD catalyzes the oxidative decarboxylation reaction involved in formation of the peptidoglycan biosynthesis inhibitor mersacidin. J Bacteriol. 2002 Mar;184(5):1234-43. [Article]
  3. Blaesse M, Kupke T, Huber R, Steinbacher S: Structure of MrsD, an FAD-binding protein of the HFCD family. Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1414-21. Epub 2003 Jul 23. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03147Flavin adenine dinucleotideapprovedunknownDetails