Benzoylformate decarboxylase

Details

Name
Benzoylformate decarboxylase
Synonyms
  • 4.1.1.7
  • BFD
Gene Name
mdlC
Organism
Pseudomonas putida
Amino acid sequence
>lcl|BSEQ0010897|Benzoylformate decarboxylase
MASVHGTTYELLRRQGIDTVFGNPGSNELPFLKDFPEDFRYILALQEACVVGIADGYAQA
SRKPAFINLHSAAGTGNAMGALSNAWNSHSPLIVTAGQQTRAMIGVEALLTNVDAANLPR
PLVKWSYEPASAAEVPHAMSRAIHMASMAPQGPVYLSVPYDDWDKDADPQSHHLFDRHVS
SSVRLNDQDLDILVKALNSASNPAIVLGPDVDAANANADCVMLAERLKAPVWVAPSAPRC
PFPTRHPCFRGLMPAGIAAISQLLEGHDVVLVIGAPVFRYHQYDPGQYLKPGTRLISVTC
DPLEAARAPMGDAIVADIGAMASALANLVEESSRQLPTAAPEPAKVDQDAGRLHPETVFD
TLNDMAPENAIYLNESTSTTAQMWQRLNMRNPGSYYFCAAGGLGFALPAAIGVQLAEPER
QVIAVIGDGSANYSISALWTAAQYNIPTIFVIMNNGTYGALRWFAGVLEAENVPGLDVPG
IDFRALAKGYGVQALKADNLEQLKGSLQEALSAKGPVLIEVSTVSPVK
Number of residues
528
Molecular Weight
56354.475
Theoretical pI
4.95
GO Classification
Functions
benzoylformate decarboxylase activity / magnesium ion binding / thiamine pyrophosphate binding
Processes
mandelate catabolic process
General Function
Thiamine pyrophosphate binding
Specific Function
Not Available
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0002557|1587 bp
TCACTTCACCGGGCTTACGGTGCTTACTTCGATAAGTACCGGGCCTTTGGCAGAAAGCGC
TTCTTGTAGCGAACCCTTGAGCTGCTCAAGGTTGTCGGCTTTCAGCGCTTGGACACCATA
GCCCTTGGCGAGTGCGCGGAAGTCGATCCCTGGCACATCCAGCCCAGGAACGTTTTCTGC
TTCGAGAACGCCGGCAAACCATCGCAACGCACCGTAGGTGCCGTTGTTCATGATCACGAA
GATAGTGGGGATGTTGTACTGAGCTGCAGTCCACAACGCACTAATGCTGTAGTTCGCCGA
TCCGTCGCCAATGACGGCGATGACTTGTCGCTCGGGTTCTGCGAGTTGAACGCCAATTGC
TGCAGGCAGGGCGAAGCCCAGTCCGCCAGCTGCACAGAAGTAGTAGCTACCAGGGTTGCG
CATGTTCAGGCGCTGCCACATTTGGGCGGTCGTTGAAGTCGACTCGTTCAGGTAAATCGC
ATTCTCCGGGGCCATGTCGTTCAGTGTGTCGAACACTGTCTCTGGGTGAAGTCGGCCAGC
GTCTTGGTCAACCTTCGCGGGTTCCGGAGCTGCAGTTGGGAGCTGGCGGCTGCTCTCTTC
AACCAAGTTGGCAAGAGCGCTAGCCATCGCACCAATGTCTGCCACGATCGCATCGCCCAT
TGGCGCGCGTGCAGCTTCGAGCGGGTCGCAGGTCACCGAAATCAATCGCGTGCCAGGTTT
GAGATATTGACCTGGGTCGTATTGGTGGTAACGGAACACTGGAGCGCCGATTACCAAAAC
CACATCGTGACCTTCGAGCAGCTGAGAAATCGCTGCGATGCCAGCTGGCATCAATCCACG
GAAGCAAGGATGACGGGTAGGGAATGGGCAGCGTGGAGCGGATGGCGCAACCCAAACCGG
AGCTTTGAGGCGTTCGGCCAACATGACGCAGTCTGCGTTCGCATTTGCTGCGTCGACGTC
CGGGCCCAGGACGATCGCCGGGTTGGATGCGCTGTTGAGAGCTTTCACCAGAATATCGAG
ATCCTGGTCGTTCAGGCGTACTGATGAACTGACATGGCGATCAAAAAGGTGGTGGGACTG
AGGATCAGCATCCTTATCCCAATCGTCATATGGCACCGAAAGATAGACAGGGCCTTGTGG
CGCCATGCTTGCCATATGGATAGCCCTGCTCATCGCATGAGGGACTTCTGCTGCGCTTGC
GGGCTCGTAGCTCCATTTGACAAGTGGTCGTGGCAGGTTGGCGGCATCGACGTTGGTCAG
CAGAGCTTCAACGCCAATCATCGCCCTGGTCTGCTGGCCGGCAGTGACGATCAGCGGGGA
ATGTGAGTTCCAGGCGTTACTGAGTGCACCCATAGCATTGCCGGTACCAGCAGCAGAATG
CAGGTTAATGAAAGCCGGCTTCCGACTGGCTTGCGCATAGCCGTCTGCAATGCCCACCAC
ACACGCTTCCTGCAAAGCCAGGATGTATCGAAAGTCCTCTGGAAAGTCCTTCAAAAACGG
GAGCTCGTTCGAGCCAGGATTGCCGAAGACCGTATCGATGCCTTGACGTCGCAAGAGTTC
GTATGTGGTGCCGTGTACCGAAGCCAT
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP20906
UniProtKB Entry NameMDLC_PSEPU
GenBank Protein ID3093419
GenBank Gene IDAY143338
General References
  1. Tsou AY, Ransom SC, Gerlt JA, Buechter DD, Babbitt PC, Kenyon GL: Mandelate pathway of Pseudomonas putida: sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli. Biochemistry. 1990 Oct 23;29(42):9856-62. [Article]
  2. Hasson MS, Muscate A, Henehan GT, Guidinger PF, Petsko GA, Ringe D, Kenyon GL: Purification and crystallization of benzoylformate decarboxylase. Protein Sci. 1995 May;4(5):955-9. [Article]
  3. Hasson MS, Muscate A, McLeish MJ, Polovnikova LS, Gerlt JA, Kenyon GL, Petsko GA, Ringe D: The crystal structure of benzoylformate decarboxylase at 1.6 A resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes. Biochemistry. 1998 Jul 14;37(28):9918-30. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02280(R)-Mandelic acidexperimentalunknownDetails
DB01987Cocarboxylaseapproved, experimentalunknownDetails