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Protein

Indole-3-pyruvate decarboxylase

Gene

ipdC

Organism
Azospirillum brasilense
Status
Reviewed-Annotation score: Annotation score: 3 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 sitei48 – 481Thiamine pyrophosphateBy similarity
Metal bindingi429 – 4291MagnesiumBy similarity
Metal bindingi456 – 4561MagnesiumBy similarity

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

BRENDAi4.1.1.74. 611.
UniPathwayiUPA00151.

Names & Taxonomyi

Protein namesi
Recommended name:
Indole-3-pyruvate decarboxylase (EC:4.1.1.74)
Short name:
Indolepyruvate decarboxylase
Gene namesi
Name:ipdC
OrganismiAzospirillum brasilense
Taxonomic identifieri192 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeAzospirillum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 545545Indole-3-pyruvate decarboxylasePRO_0000090821Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi1064539.AZOBR_40354.

Structurei

Secondary structure

1
545
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1311Combined sources
Beta strandi19 – 213Combined sources
Helixi25 – 273Combined sources
Helixi28 – 3710Combined sources
Beta strandi42 – 443Combined sources
Helixi48 – 6215Combined sources
Beta strandi66 – 705Combined sources
Helixi74 – 774Combined sources
Helixi80 – 889Combined sources
Beta strandi93 – 997Combined sources
Turni102 – 1054Combined sources
Helixi120 – 1256Combined sources
Helixi126 – 1283Combined sources
Beta strandi132 – 1343Combined sources
Turni138 – 1403Combined sources
Helixi141 – 15515Combined sources
Beta strandi159 – 1646Combined sources
Helixi165 – 1673Combined sources
Helixi185 – 20117Combined sources
Beta strandi203 – 2097Combined sources
Helixi211 – 2155Combined sources
Helixi219 – 22911Combined sources
Beta strandi233 – 2353Combined sources
Helixi237 – 2393Combined sources
Turni240 – 2456Combined sources
Beta strandi246 – 2483Combined sources
Beta strandi251 – 2533Combined sources
Helixi256 – 2583Combined sources
Helixi261 – 2688Combined sources
Beta strandi271 – 2777Combined sources
Helixi282 – 2854Combined sources
Turni289 – 2913Combined sources
Helixi294 – 2963Combined sources
Beta strandi297 – 3015Combined sources
Beta strandi304 – 3074Combined sources
Beta strandi310 – 3145Combined sources
Helixi317 – 32610Combined sources
Beta strandi350 – 3534Combined sources
Helixi356 – 36813Combined sources
Beta strandi375 – 3784Combined sources
Helixi382 – 3876Combined sources
Turni399 – 4013Combined sources
Helixi407 – 41711Combined sources
Turni418 – 4203Combined sources
Beta strandi423 – 4286Combined sources
Helixi429 – 4357Combined sources
Helixi436 – 4416Combined sources
Helixi442 – 4454Combined sources
Beta strandi450 – 4556Combined sources
Helixi460 – 4656Combined sources
Helixi470 – 4723Combined sources
Helixi479 – 4824Combined sources
Helixi484 – 4863Combined sources
Beta strandi488 – 4936Combined sources
Helixi496 – 50813Combined sources
Beta strandi514 – 5196Combined sources
Helixi527 – 53812Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NXWX-ray1.50A/B1-545[»]
2Q5JX-ray3.20A/B1-545[»]
2Q5LX-ray1.85A/B1-545[»]
2Q5OX-ray2.15A/B1-545[»]
2Q5QX-ray1.90A/B1-545[»]
5ABMX-ray1.70A/B/C/D2-501[»]
ProteinModelPortaliP51852.
SMRiP51852. Positions 1-535.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51852.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni382 – 46079Thiamine 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.
IPR017765. IPDC.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR012110. TPP_enzyme.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
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.
TIGRFAMsiTIGR03394. indol_phenyl_DC. 1 hit.

Sequencei

Sequence statusi: Complete.

P51852-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLAEALLRA LKDRGAQAMF GIPGDFALPF FKVAEETQIL PLHTLSHEPA
60 70 80 90 100
VGFAADAAAR YSSTLGVAAV TYGAGAFNMV NAVAGAYAEK SPVVVISGAP
110 120 130 140 150
GTTEGNAGLL LHHQGRTLDT QFQVFKEITV AQARLDDPAK APAEIARVLG
160 170 180 190 200
AARALSRPVY LEIPRNMVNA EVEPVGDDPA WPVDRDALAA CADEVLAAMR
210 220 230 240 250
SATSPVLMVC VEVRRYGLEA KVAELAQRLG VPVVTTFMGR GLLADAPTPP
260 270 280 290 300
LGTYIGVAGD AEITRLVEES DGLFLLGAIL SDTNFAVSQR KIDLRKTIHA
310 320 330 340 350
FDRAVTLGYH TYADIPLAGL VDALLEGLPP SDRTTRGKEP HAYPTGLQAD
360 370 380 390 400
GEPIAPMDIA RAVNDRVRAG QEPLLIAADM GDCLFTAMDM IDAGLMAPGY
410 420 430 440 450
YAGMGFGVPA GIGAQCVSGG KRILTVVGDG AFQMTGWELG NCRRLGIDPI
460 470 480 490 500
VILFNNASWE MLRTFQPESA FNDLDDWRFA DMAAGMGGDG VRVRTRAELK
510 520 530 540
AALDKAFATR GRFQLIEAMI PRGVLSDTLA RFVQGQKRLH AAPRE
Length:545
Mass (Da):57,981
Last modified:October 1, 1996 - v1
Checksum:iC636A081729B8CD3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26240 Unassigned DNA. Translation: AAC36886.1.
PIRiS44486.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26240 Unassigned DNA. Translation: AAC36886.1.
PIRiS44486.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NXWX-ray1.50A/B1-545[»]
2Q5JX-ray3.20A/B1-545[»]
2Q5LX-ray1.85A/B1-545[»]
2Q5OX-ray2.15A/B1-545[»]
2Q5QX-ray1.90A/B1-545[»]
5ABMX-ray1.70A/B/C/D2-501[»]
ProteinModelPortaliP51852.
SMRiP51852. Positions 1-535.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1064539.AZOBR_40354.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107RA9. Bacteria.
COG3961. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00151.
BRENDAi4.1.1.74. 611.

Miscellaneous databases

EvolutionaryTraceiP51852.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR017765. IPDC.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR012110. TPP_enzyme.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
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.
TIGRFAMsiTIGR03394. indol_phenyl_DC. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDCIP_AZOBR
AccessioniPrimary (citable) accession number: P51852
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 11, 2015
This is version 85 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.