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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)DescriptionActionsGraphical viewLength
Binding sitei52Thiamine pyrophosphate1 Publication1
Metal bindingi435Magnesium1 Publication1
Metal bindingi462Magnesium1 Publication1

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEnterobacterEnterobacter cloacae complex

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000908221 – 552Indole-3-pyruvate decarboxylaseAdd BLAST552

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi1045856.EcWSU1_03228.

Structurei

Secondary structure

1552
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 17Combined sources11
Beta strandi22 – 25Combined sources4
Helixi29 – 31Combined sources3
Helixi32 – 40Combined sources9
Beta strandi45 – 48Combined sources4
Helixi52 – 66Combined sources15
Beta strandi69 – 74Combined sources6
Helixi77 – 81Combined sources5
Helixi83 – 91Combined sources9
Beta strandi96 – 102Combined sources7
Helixi105 – 110Combined sources6
Beta strandi119 – 121Combined sources3
Helixi125 – 129Combined sources5
Helixi131 – 133Combined sources3
Beta strandi135 – 139Combined sources5
Turni142 – 144Combined sources3
Helixi145 – 159Combined sources15
Beta strandi163 – 168Combined sources6
Helixi169 – 173Combined sources5
Helixi192 – 207Combined sources16
Beta strandi212 – 216Combined sources5
Helixi218 – 222Combined sources5
Helixi226 – 235Combined sources10
Beta strandi239 – 242Combined sources4
Helixi244 – 246Combined sources3
Helixi263 – 265Combined sources3
Helixi268 – 275Combined sources8
Beta strandi277 – 284Combined sources8
Turni289 – 295Combined sources7
Turni301 – 303Combined sources3
Beta strandi304 – 307Combined sources4
Beta strandi309 – 314Combined sources6
Beta strandi317 – 321Combined sources5
Helixi324 – 336Combined sources13
Helixi362 – 372Combined sources11
Beta strandi378 – 381Combined sources4
Helixi385 – 390Combined sources6
Beta strandi400 – 402Combined sources3
Turni405 – 407Combined sources3
Helixi412 – 423Combined sources12
Beta strandi429 – 434Combined sources6
Helixi435 – 441Combined sources7
Helixi444 – 450Combined sources7
Beta strandi456 – 464Combined sources9
Helixi466 – 471Combined sources6
Helixi477 – 479Combined sources3
Helixi486 – 488Combined sources3
Turni490 – 492Combined sources3
Beta strandi499 – 504Combined sources6
Helixi507 – 517Combined sources11
Beta strandi521 – 529Combined sources9
Helixi537 – 550Combined sources14

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP23234.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni385 – 466Thiamine pyrophosphate bindingAdd BLAST82

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OVMX-ray2.65A/B/C/D1-552[»]
ProteinModelPortaliP23234.
SMRiP23234.
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 2, 2016
This is version 98 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.