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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)DescriptionActionsGraphical viewLength
Binding sitei48Thiamine pyrophosphateBy similarity1
Metal bindingi429MagnesiumBy similarity1
Metal bindingi456MagnesiumBy similarity1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000908211 – 545Indole-3-pyruvate decarboxylaseAdd BLAST545

Interactioni

Protein-protein interaction databases

STRINGi1064539.AZOBR_40354.

Structurei

Secondary structure

1545
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 13Combined sources11
Beta strandi19 – 21Combined sources3
Helixi25 – 27Combined sources3
Helixi28 – 37Combined sources10
Beta strandi42 – 44Combined sources3
Helixi48 – 62Combined sources15
Beta strandi66 – 70Combined sources5
Helixi74 – 77Combined sources4
Helixi80 – 88Combined sources9
Beta strandi93 – 99Combined sources7
Turni102 – 105Combined sources4
Helixi120 – 125Combined sources6
Helixi126 – 128Combined sources3
Beta strandi132 – 134Combined sources3
Turni138 – 140Combined sources3
Helixi141 – 155Combined sources15
Beta strandi159 – 164Combined sources6
Helixi165 – 167Combined sources3
Helixi185 – 201Combined sources17
Beta strandi203 – 209Combined sources7
Helixi211 – 215Combined sources5
Helixi219 – 229Combined sources11
Beta strandi233 – 235Combined sources3
Helixi237 – 239Combined sources3
Turni240 – 245Combined sources6
Beta strandi246 – 248Combined sources3
Beta strandi251 – 253Combined sources3
Helixi256 – 258Combined sources3
Helixi261 – 268Combined sources8
Beta strandi271 – 277Combined sources7
Helixi282 – 285Combined sources4
Turni289 – 291Combined sources3
Helixi294 – 296Combined sources3
Beta strandi297 – 301Combined sources5
Beta strandi304 – 307Combined sources4
Beta strandi310 – 314Combined sources5
Helixi317 – 326Combined sources10
Beta strandi350 – 353Combined sources4
Helixi356 – 368Combined sources13
Beta strandi375 – 378Combined sources4
Helixi382 – 387Combined sources6
Turni399 – 401Combined sources3
Helixi407 – 417Combined sources11
Turni418 – 420Combined sources3
Beta strandi423 – 428Combined sources6
Helixi429 – 435Combined sources7
Helixi436 – 441Combined sources6
Helixi442 – 445Combined sources4
Beta strandi450 – 455Combined sources6
Helixi460 – 465Combined sources6
Helixi470 – 472Combined sources3
Helixi479 – 482Combined sources4
Helixi484 – 486Combined sources3
Beta strandi488 – 493Combined sources6
Helixi496 – 508Combined sources13
Beta strandi514 – 519Combined sources6
Helixi527 – 538Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51852.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni382 – 460Thiamine pyrophosphate bindingAdd BLAST79

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
PDB 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.
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 2, 2016
This is version 87 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.