Probable UbiX-like flavin prenyltransferase
Details
- Name
- Probable UbiX-like flavin prenyltransferase
- Synonyms
- 2.5.1.-
- 4-hydroxybenzoate decarboxylase subunit B
- pad1
- Phenolic acid decarboxylase subunit B
- Gene Name
- ecdB
- Organism
- Escherichia coli O157:H7
- Amino acid sequence
>lcl|BSEQ0016964|Probable UbiX-like flavin prenyltransferase MKLIVGMTGATGAPLGVALLQALREMPNVETHLVMSKWAKTTIELETPYSARDVAALADF SHNPADQAATISSGSFRTDGMIVIPCSMKTLAGIRAGYADGLVGRAADVVLKEGRKLVLV PREMPLSTIHLENMLALSRMGVAMVPPMPAFYNHPETVDDIVHHVVARVLDQFGLEHPYA RRWQGLPQARNFSQENE
- Number of residues
- 197
- Molecular Weight
- 21469.72
- Theoretical pI
- 6.89
- GO Classification
- Functionsprenyltransferase activity
- General Function
- Prenyltransferase activity
- Specific Function
- Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for phenolic acid decarboxylase C (By similarity). Involved in the decarboxylation and detoxification of phenolic derivatives under both aerobic and anaerobic conditions (PubMed:15979273).
- Pfam Domain Function
- Flavoprotein (PF02441)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0016965|Probable UbiX-like flavin prenyltransferase (ecdB) ATGAAACTGATCGTCGGGATGACAGGGGCTACCGGTGCGCYTCTTGGTGTGGCATTACTG CAAGCGCTGCGGGAGATGCCGAATGTCGAGACTCATCTGGTGATGTCGAAGTGGGCGAAA ACCACCATTGAACTGGAAACGCCTTACAGCGCCCGCGATGTTGCTGCCCTCGCTGACTTC AGCCATAACCCGGCGGATCAGGCGGCGACCATCTCCTCAGGTTCCTTTCGTACAGACGGC ATGATCGTTATTCCGTGCAGTATGAAAACGCTCGCCGGTATCCGCGCTGGTTACGCTGAT GGCCTGGTAGGGCGCGCGGCGGACGTCGTGCTTAAAGAAGGCCGCAAACTGGTGCTGGTG CCGCGTGAAATGCCGCTTAGCACCATCCATCTCGAAAATATGCTCGCACTTTCACGCATG GGCGTGGCGATGGTGCCGCCGATGCCTGCCTTTTATAACCATCCCGAAACGGTAGATGAC ATTGTCCACCACGTGGTAGCCCGCGTGCTGGATCAATTTGGCCTTGAACATCCCTACGCC AGGCGCTGGCAAGGATTGCCGCAGGCCCGGAATTTTTCTCAGGAGAATGAATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P69772 UniProtKB Entry Name PADL_ECO57 GenBank Gene ID AJ006210 - General References
- Perna NT, Plunkett G 3rd, Burland V, Mau B, Glasner JD, Rose DJ, Mayhew GF, Evans PS, Gregor J, Kirkpatrick HA, Posfai G, Hackett J, Klink S, Boutin A, Shao Y, Miller L, Grotbeck EJ, Davis NW, Lim A, Dimalanta ET, Potamousis KD, Apodaca J, Anantharaman TS, Lin J, Yen G, Schwartz DC, Welch RA, Blattner FR: Genome sequence of enterohaemorrhagic Escherichia coli O157:H7. Nature. 2001 Jan 25;409(6819):529-33. [Article]
- Hayashi T, Makino K, Ohnishi M, Kurokawa K, Ishii K, Yokoyama K, Han CG, Ohtsubo E, Nakayama K, Murata T, Tanaka M, Tobe T, Iida T, Takami H, Honda T, Sasakawa C, Ogasawara N, Yasunaga T, Kuhara S, Shiba T, Hattori M, Shinagawa H: Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12. DNA Res. 2001 Feb 28;8(1):11-22. [Article]
- Lupa B, Lyon D, Gibbs MD, Reeves RA, Wiegel J: Distribution of genes encoding the microbial non-oxidative reversible hydroxyarylic acid decarboxylases/phenol carboxylases. Genomics. 2005 Sep;86(3):342-51. [Article]
- Rangarajan ES, Li Y, Iannuzzi P, Tocilj A, Hung LW, Matte A, Cygler M: Crystal structure of a dodecameric FMN-dependent UbiX-like decarboxylase (Pad1) from Escherichia coli O157: H7. Protein Sci. 2004 Nov;13(11):3006-16. Epub 2004 Sep 30. [Article]