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P23234 (DCIP_ENTCL) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Indole-3-pyruvate decarboxylase
Short name=Indolepyruvate decarboxylase
EC=4.1.1.74
Gene names
Name:ipdC
OrganismEnterobacter cloacae
Taxonomic identifier550 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Enterobacter › Enterobacter cloacae complex

Protein attributes

Sequence length552 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

3-(indol-3-yl)pyruvate = 2-(indol-3-yl)acetaldehyde + CO2.

Cofactor

Binds 1 metal ion per subunit.

Binds 1 thiamine pyrophosphate per subunit.

Pathway

Plant hormone metabolism; auxin biosynthesis.

Subunit structure

Homotetramer. Ref.2

Sequence similarities

Belongs to the TPP enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 552552Indole-3-pyruvate decarboxylase
PRO_0000090822

Regions

Region385 – 46682Thiamine pyrophosphate binding

Sites

Metal binding4351Magnesium
Metal binding4621Magnesium
Binding site521Thiamine pyrophosphate

Secondary structure

1 .................................................................................................... 552
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23234 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: DAC80952738D3729

FASTA55260,024
        10         20         30         40         50         60 
MRTPYCVADY LLDRLTDCGA DHLFGVPGDY NLQFLDHVID SPDICWVGCA NELNASYAAD 

        70         80         90        100        110        120 
GYARCKGFAA LLTTFGVGEL SAMNGIAGSY AEHVPVLHIV GAPGTAAQQR GELLHHTLGD 

       130        140        150        160        170        180 
GEFRHFYHMS EPITVAQAVL TEQNACYEID RVLTTMLRER RPGYLMLPAD VAKKAATPPV 

       190        200        210        220        230        240 
NALTHKQAHA DSACLKAFRD AAENKLAMSK RTALLADFLV LRHGLKHALQ KWVKEVPMAH 

       250        260        270        280        290        300 
ATMLMGKGIF DERQAGFYGT YSGSASTGAV KEAIEGADTV LCVGTRFTDT LTAGFTHQLT 

       310        320        330        340        350        360 
PAQTIEVQPH AARVGDVWFT GIPMNQAIET LVELCKQHVH AGLMSSSSGA IPFPQPDGSL 

       370        380        390        400        410        420 
TQENFWRTLQ TFIRPGDIIL ADQGTSAFGA IDLRLPADVN FIVQPLWGSI GYTLAAAFGA 

       430        440        450        460        470        480 
QTACPNRRVI VLTGDGAAQL TIQELGSMLR DKQHPIILVL NNEGYTVERA IHGAEQRYND 

       490        500        510        520        530        540 
IALWNWTHIP QALSLDPQSE CWRVSEAEQL ADVLEKVAHH ERLSLIEVML PKADIPPLLG 

       550 
ALTKALEACN NA

« Hide

References

[1]"Molecular cloning of the gene for indolepyruvate decarboxylase from Enterobacter cloacae."
Koga J., Adachi T., Hidaka H.
Mol. Gen. Genet. 226:10-16(1991) [PubMed: 2034209] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: FERM BP-1529.
[2]"Crystal structure of thiamindiphosphate-dependent indolepyruvate decarboxylase from Enterobacter cloacae, an enzyme involved in the biosynthesis of the plant hormone indole-3-acetic acid."
Schuetz A., Sandalova T., Ricagno S., Huebner G., Koenig S., Schneider G.
Eur. J. Biochem. 270:2312-2321(2003) [PubMed: 12752451] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH THIAMINE PYROPHOSPHATE AND MAGNESIUM, HOMOTETRAMERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D90214 Genomic DNA. Translation: BAA14242.1.
PIRS16013.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OVMX-ray2.65A/B/C/D1-552[»]
ProteinModelPortalP23234.
SMRP23234. Positions 3-551.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-7781.

Family and domain databases

InterProIPR017764. Indolepyruvate_decarboxylase.
IPR012110. Pyruvt_ip_decrb.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PANTHERPTHR18968:SF4. PTHR18968:SF4. 1 hit.
PfamPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
PIRSFPIRSF036565. Pyruvt_ip_decrb. 1 hit.
TIGRFAMsTIGR03393. Indolpyr_decarb. 1 hit.
PROSITEPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDCIP_ENTCL
AccessionPrimary (citable) accession number: P23234
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: October 19, 2011
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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