Indole-3-pyruvate decarboxylase

Details

Name
Indole-3-pyruvate decarboxylase
Synonyms
  • 4.1.1.74
  • Indolepyruvate decarboxylase
Gene Name
ipdC
Organism
Enterobacter cloacae
Amino acid sequence
>lcl|BSEQ0012284|Indole-3-pyruvate decarboxylase
MRTPYCVADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAAD
GYARCKGFAALLTTFGVGELSAMNGIAGSYAEHVPVLHIVGAPGTAAQQRGELLHHTLGD
GEFRHFYHMSEPITVAQAVLTEQNACYEIDRVLTTMLRERRPGYLMLPADVAKKAATPPV
NALTHKQAHADSACLKAFRDAAENKLAMSKRTALLADFLVLRHGLKHALQKWVKEVPMAH
ATMLMGKGIFDERQAGFYGTYSGSASTGAVKEAIEGADTVLCVGTRFTDTLTAGFTHQLT
PAQTIEVQPHAARVGDVWFTGIPMNQAIETLVELCKQHVHAGLMSSSSGAIPFPQPDGSL
TQENFWRTLQTFIRPGDIILADQGTSAFGAIDLRLPADVNFIVQPLWGSIGYTLAAAFGA
QTACPNRRVIVLTGDGAAQLTIQELGSMLRDKQHPIILVLNNEGYTVERAIHGAEQRYND
IALWNWTHIPQALSLDPQSECWRVSEAEQLADVLEKVAHHERLSLIEVMLPKADIPPLLG
ALTKALEACNNA
Number of residues
552
Molecular Weight
60022.965
Theoretical pI
6.03
GO Classification
Functions
indolepyruvate decarboxylase activity / magnesium ion binding / thiamine pyrophosphate binding
Processes
auxin biosynthetic process
General Function
Thiamine pyrophosphate binding
Specific Function
Not Available
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0006384|1659 bp
ATGCGAACCCCATACTGCGTCGCCGATTACCTGCTGGACCGTCTTACAGATTGTGGTGCC
GATCATCTGTTTGGCGTGCCGGGCGACTATAACCTGCAGTTTCTCGACCACGTAATAGAC
AGCCCGGATATTTGTTGGGTGGGCTGTGCCAATGAGCTGAACGCATCCTATGCCGCTGAC
GGATACGCCCGATGTAAGGGCTTTGCCGCGCTACTGACCACATTCGGCGTTGGGGAGTTA
AGTGCCATGAACGGCATTGCCGGCAGCTATGCCGAGCATGTCCCGGTTTTACATATTGTG
GGGGCGCCGGGTACGGCGGCACAGCAAAGGGGAGAGTTGCTGCATCATACGTTGGGGGAT
GGGGAGTTCCGTCACTTTTATCATATGAGCGAGCCGATCACCGTCGCACAGGCGGTCCTT
ACCGAACAAAATGCCTGTTATGAAATCGACCGTGTGTTGACAACCATGCTTCGGGAACGC
CGCCCCGGTTATCTGATGTTACCCGCCGATGTGGCAAAAAAAGCCGCCACGCCGCCTGTA
AACGCTCTCACTCATAAGCAGGCTCATGCCGATAGCGCCTGCCTGAAAGCGTTCCGGGAT
GCTGCTGAGAACAAACTGGCGATGAGCAAACGTACCGCGCTGCTGGCCGACTTCCTTGTT
CTGCGCCATGGCCTGAAACATGCGCTACAGAAGTGGGTGAAAGAGGTACCGATGGCCCAT
GCCACCATGCTGATGGGGAAAGGGATATTCGACGAGCGTCAGGCGGGTTTTTACGGCACA
TACAGTGGTTCAGCCAGCACTGGCGCGGTAAAAGAGGCGATTGAAGGGGCTGACACGGTA
TTGTGTGTTGGCACGCGTTTTACCGATACCCTGACGGCCGGGTTCACGCACCAGCTTACC
CCGGCGCAGACCATTGAAGTTCAGCCGCATGCCGCACGCGTCGGGGATGTCTGGTTTACC
GGCATCCCAATGAACCAGGCGATTGAGACGCTGGTCGAACTCTGCAAACAGCACGTGCAT
GCTGGCCTTATGTCGTCATCATCCGGCGCAATACCGTTCCCGCAGCCGGACGGTTCGCTT
ACCCAGGAGAATTTCTGGAGAACGTTGCAAACCTTTATTCGCCCGGGGGACATTATCCTT
GCCGACCAGGGAACATCGGCCTTCGGCGCGATTGATCTGCGTTTACCGGCTGATGTGAAC
TTTATCGTCCAGCCGCTGTGGGGCTCGATTGGTTACACGCTGGCGGCGGCGTTTGGTGCA
CAAACCGCATGCCCGAACCGGCGCGTGATTGTGCTGACGGGGGATGGCGCTGCCCAGCTC
ACTATTCAGGAACTAGGCTCGATGCTGCGTGATAAACAGCACCCCATTATTCTGGTGCTC
AACAACGAAGGTTACACGGTTGAGAGGGCTATCCACGGGGCGGAGCAGCGGTATAACGAC
ATTGCTTTGTGGAACTGGACGCACATTCCGCAGGCGTTGAGCCTCGATCCTCAGTCTGAG
TGCTGGCGGGTCAGTGAAGCGGAACAGCTGGCGGACGTACTTGAAAAAGTGGCGCACCAC
GAGCGGCTCTCGTTGATTGAGGTGATGCTCCCGAAAGCGGATATCCCGCCGCTGCTCGGG
GCGCTTACCAAGGCTCTGGAAGCGTGTAATAACGCCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP23234
UniProtKB Entry NameDCIP_ENTCL
GenBank Gene IDD90214
General References
  1. Koga J, Adachi T, Hidaka H: Molecular cloning of the gene for indolepyruvate decarboxylase from Enterobacter cloacae. Mol Gen Genet. 1991 Apr;226(1-2):10-6. [Article]
  2. Schutz A, Sandalova T, Ricagno S, Hubner G, Konig S, Schneider G: Crystal structure of thiamindiphosphate-dependent indolepyruvate decarboxylase from Enterobacter cloacae, an enzyme involved in the biosynthesis of the plant hormone indole-3-acetic acid. Eur J Biochem. 2003 May;270(10):2312-21. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01987Cocarboxylaseapproved, experimentalunknownDetails