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Protein

Indole-3-pyruvate decarboxylase

Gene

ipdC

Organism
Enterobacter cloacae
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

Pathwayi: auxin biosynthesis

This protein is involved in the pathway auxin biosynthesis, which is part of Plant hormone metabolism.
View all proteins of this organism that are known to be involved in the pathway auxin biosynthesis and in Plant hormone metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei52 – 521Thiamine pyrophosphate1 Publication
Metal bindingi435 – 4351Magnesium1 Publication
Metal bindingi462 – 4621Magnesium1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Ligandi

Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-7781.
BRENDAi4.1.1.74. 155.
SABIO-RKP23234.
UniPathwayiUPA00151.

Names & Taxonomyi

Protein namesi
Recommended name:
Indole-3-pyruvate decarboxylase (EC:4.1.1.74)
Short name:
Indolepyruvate decarboxylase
Gene namesi
Name:ipdC
OrganismiEnterobacter cloacae
Taxonomic identifieri550 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacterEnterobacter cloacae complex

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 552552Indole-3-pyruvate decarboxylasePRO_0000090822Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi1045856.EcWSU1_03228.

Structurei

Secondary structure

1
552
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 1711Combined sources
Beta strandi22 – 254Combined sources
Helixi29 – 313Combined sources
Helixi32 – 409Combined sources
Beta strandi45 – 484Combined sources
Helixi52 – 6615Combined sources
Beta strandi69 – 746Combined sources
Helixi77 – 815Combined sources
Helixi83 – 919Combined sources
Beta strandi96 – 1027Combined sources
Helixi105 – 1106Combined sources
Beta strandi119 – 1213Combined sources
Helixi125 – 1295Combined sources
Helixi131 – 1333Combined sources
Beta strandi135 – 1395Combined sources
Turni142 – 1443Combined sources
Helixi145 – 15915Combined sources
Beta strandi163 – 1686Combined sources
Helixi169 – 1735Combined sources
Helixi192 – 20716Combined sources
Beta strandi212 – 2165Combined sources
Helixi218 – 2225Combined sources
Helixi226 – 23510Combined sources
Beta strandi239 – 2424Combined sources
Helixi244 – 2463Combined sources
Helixi263 – 2653Combined sources
Helixi268 – 2758Combined sources
Beta strandi277 – 2848Combined sources
Turni289 – 2957Combined sources
Turni301 – 3033Combined sources
Beta strandi304 – 3074Combined sources
Beta strandi309 – 3146Combined sources
Beta strandi317 – 3215Combined sources
Helixi324 – 33613Combined sources
Helixi362 – 37211Combined sources
Beta strandi378 – 3814Combined sources
Helixi385 – 3906Combined sources
Beta strandi400 – 4023Combined sources
Turni405 – 4073Combined sources
Helixi412 – 42312Combined sources
Beta strandi429 – 4346Combined sources
Helixi435 – 4417Combined sources
Helixi444 – 4507Combined sources
Beta strandi456 – 4649Combined sources
Helixi466 – 4716Combined sources
Helixi477 – 4793Combined sources
Helixi486 – 4883Combined sources
Turni490 – 4923Combined sources
Beta strandi499 – 5046Combined sources
Helixi507 – 51711Combined sources
Beta strandi521 – 5299Combined sources
Helixi537 – 55014Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OVMX-ray2.65A/B/C/D1-552[»]
ProteinModelPortaliP23234.
SMRiP23234. Positions 3-551.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23234.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni385 – 46682Thiamine pyrophosphate bindingAdd
BLAST

Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Phylogenomic databases

eggNOGiENOG4107RA9. Bacteria.
COG3961. LUCA.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR017764. IPDC_Enterobacteriaceae.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR012110. TPP_enzyme.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PANTHERiPTHR18968:SF4. PTHR18968:SF4. 1 hit.
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
PIRSFiPIRSF036565. Pyruvt_ip_decrb. 1 hit.
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR03393. indolpyr_decarb. 1 hit.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23234-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTPYCVADY LLDRLTDCGA DHLFGVPGDY NLQFLDHVID SPDICWVGCA
60 70 80 90 100
NELNASYAAD GYARCKGFAA LLTTFGVGEL SAMNGIAGSY AEHVPVLHIV
110 120 130 140 150
GAPGTAAQQR GELLHHTLGD GEFRHFYHMS EPITVAQAVL TEQNACYEID
160 170 180 190 200
RVLTTMLRER RPGYLMLPAD VAKKAATPPV NALTHKQAHA DSACLKAFRD
210 220 230 240 250
AAENKLAMSK RTALLADFLV LRHGLKHALQ KWVKEVPMAH ATMLMGKGIF
260 270 280 290 300
DERQAGFYGT YSGSASTGAV KEAIEGADTV LCVGTRFTDT LTAGFTHQLT
310 320 330 340 350
PAQTIEVQPH AARVGDVWFT GIPMNQAIET LVELCKQHVH AGLMSSSSGA
360 370 380 390 400
IPFPQPDGSL TQENFWRTLQ TFIRPGDIIL ADQGTSAFGA IDLRLPADVN
410 420 430 440 450
FIVQPLWGSI GYTLAAAFGA QTACPNRRVI VLTGDGAAQL TIQELGSMLR
460 470 480 490 500
DKQHPIILVL NNEGYTVERA IHGAEQRYND IALWNWTHIP QALSLDPQSE
510 520 530 540 550
CWRVSEAEQL ADVLEKVAHH ERLSLIEVML PKADIPPLLG ALTKALEACN

NA
Length:552
Mass (Da):60,024
Last modified:November 1, 1991 - v1
Checksum:iDAC80952738D3729
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90214 Genomic DNA. Translation: BAA14242.1.
PIRiS16013.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90214 Genomic DNA. Translation: BAA14242.1.
PIRiS16013.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OVMX-ray2.65A/B/C/D1-552[»]
ProteinModelPortaliP23234.
SMRiP23234. Positions 3-551.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1045856.EcWSU1_03228.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107RA9. Bacteria.
COG3961. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00151.
BioCyciMetaCyc:MONOMER-7781.
BRENDAi4.1.1.74. 155.
SABIO-RKP23234.

Miscellaneous databases

EvolutionaryTraceiP23234.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR017764. IPDC_Enterobacteriaceae.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR012110. TPP_enzyme.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PANTHERiPTHR18968:SF4. PTHR18968:SF4. 1 hit.
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
PIRSFiPIRSF036565. Pyruvt_ip_decrb. 1 hit.
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR03393. indolpyr_decarb. 1 hit.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDCIP_ENTCL
AccessioniPrimary (citable) accession number: P23234
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: November 11, 2015
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.