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Protein

Transaminated amino acid decarboxylase

Gene

ARO10

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

One of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) involved in amino acid catabolism. The enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids (alpha-keto-acids). In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids derived from phenylalanine (phenylpyruvate), tryptophan (3-(indol-3-yl)pyruvate), and probably tyrosine (4-hydroxyphenylpyruvate), but also isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate) and methionine (4-methylthio-2-oxobutanoate), whereas transaminated leucine (4-methyl-2-oxopentanoate, also alpha-keto-isocaproate) is a low efficiency substrate and transaminated valine and pyruvate are no substrates. In analogy to the pyruvate decarboxylases the enzyme may in a side-reaction catalyze condensation (or carboligation) reactions leading to the formation of 2-hydroxy ketone, collectively called acyloins.5 Publications

Miscellaneous

Present with 6560 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

4-methyl-2-oxopentanoate = 3-methylbutanal + CO2.1 Publication
(3S)-3-methyl-2-oxopentanoate = 2-methylbutanal + CO2.1 Publication
3-(indol-3-yl)pyruvate = 2-(indol-3-yl)acetaldehyde + CO2.2 Publications
Phenylpyruvate = phenylacetaldehyde + CO2.2 Publications
4-methylsulfanyl-2-oxobutanoate = 3-methylthiopropanal + CO2.2 Publications
4-hydroxyphenylpyruvate = 4-hydroxyphenylacetaldehyde + CO2.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarityNote: Binds 1 Mg2+ per subunit.By similarity
  • thiamine diphosphateBy similarityNote: Binds 1 thiamine pyrophosphate per subunit.By similarity

Kineticsi

  1. KM=0.14 mM for phenylpyruvate1 Publication
  2. KM=12 mM for 3-methyl-2-oxobutanoate1 Publication
  3. KM=2.1 mM for 4-methyl-2-oxopentanoate1 Publication
  4. KM=4.7 mM for 3-methyl-2-oxopentanoate1 Publication
  5. KM=5.36 mM for 4-methylthio-2-oxobutanoate1 Publication
  6. KM=0.03 mM for 3-(indol-3-yl)pyruvate1 Publication
  7. KM=0.09 mM for 4-hydroxyphenylpyruvate1 Publication
  1. Vmax=201 µmol/min/mg enzyme for phenylpyruvate1 Publication
  2. Vmax=103 µmol/min/mg enzyme for 3-methyl-2-oxobutanoate1 Publication
  3. Vmax=103 µmol/min/mg enzyme for 4-methyl-2-oxopentanoate1 Publication
  4. Vmax=103 µmol/min/mg enzyme for 3-methyl-2-oxopentanoate1 Publication
  5. Vmax=85 µmol/min/mg enzyme for 4-methylthio-2-oxobutanoate1 Publication

pH dependencei

Optimum pH is 6.5-7.0.1 Publication

Pathwayi: Ehrlich pathway

This protein is involved in the pathway Ehrlich pathway, which is part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the pathway Ehrlich pathway and in Amino-acid degradation.

GO - Molecular functioni

GO - Biological processi

  • aromatic amino acid family catabolic process to alcohol via Ehrlich pathway Source: SGD
  • branched-chain amino acid catabolic process to alcohol via Ehrlich pathway Source: SGD
  • ethanol metabolic process Source: GO_Central
  • leucine catabolic process Source: SGD
  • L-phenylalanine catabolic process Source: SGD
  • methionine catabolic process to 3-methylthiopropanol Source: SGD
  • pyruvate metabolic process Source: GO_Central
  • tryptophan catabolic process Source: SGD
  • tyrosine catabolic process Source: UniProtKB-KW

Keywordsi

Molecular functionDecarboxylase, Lyase
Biological processBranched-chain amino acid catabolism, Phenylalanine catabolism, Tryptophan catabolism, Tyrosine catabolism
LigandMagnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-398.
YEAST:MONOMER3O-398.
BRENDAi4.1.1.43. 984.
UniPathwayiUPA00866.

Names & Taxonomyi

Protein namesi
Recommended name:
Transaminated amino acid decarboxylase (EC:4.1.1.-1 Publication, EC:4.1.1.432 Publications, EC:4.1.1.722 Publications, EC:4.1.1.742 Publications, EC:4.1.1.801 Publication)
Alternative name(s):
Thiamine diphosphate-dependent phenylpyruvate decarboxylase1 Publication
Short name:
PPDC1 Publication
Thiamine pyrophosphate-dependent 2-oxo-acid decarboxylase
Short name:
2ODC
Transaminated branched-chain amino acid decarboxylase
Gene namesi
Name:ARO10
Ordered Locus Names:YDR380W
ORF Names:D9481.3
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR380W.
SGDiS000002788. ARO10.

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Biotechnological usei

Fusel oils are important flavor and aroma compounds in yeast-fermented products contributing to the quality of beverages and food. In low concentration they are generally desirable, whereas high concentrations may spoil the product. By adjusting growth conditions and substrate their production is sought to be influenced. Phenylethanol, having a rose-like aroma, is an important fragrance in the cosmetic industry and can be produced by fermentation.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000908351 – 635Transaminated amino acid decarboxylaseAdd BLAST635

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki588Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ06408.
PRIDEiQ06408.

PTM databases

iPTMnetiQ06408.

Expressioni

Inductioni

Expression is induced by the presence of aromatic amino acids and the lack of preferred nitrogen sources (e.g. ammonia, glutamine) and requires the transcription activator ARO80.

Interactioni

Protein-protein interaction databases

BioGridi32440. 31 interactors.
DIPiDIP-5252N.
IntActiQ06408. 4 interactors.
MINTiMINT-546662.
STRINGi4932.YDR380W.

Structurei

3D structure databases

ProteinModelPortaliQ06408.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000075465.
HOGENOMiHOG000061334.
InParanoidiQ06408.
KOiK12732.
OMAiERCIHGR.
OrthoDBiEOG092C2L8F.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
InterProiView protein in InterPro
IPR029035. DHS-like_NAD/FAD-binding_dom.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR012110. TPP_enzyme.
IPR011766. TPP_enzyme-bd_C.
PfamiView protein in Pfam
PF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
PIRSFiPIRSF036565. Pyruvt_ip_decrb. 1 hit.
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.

Sequencei

Sequence statusi: Complete.

Q06408-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPVTIEKFV NQEERHLVSN RSATIPFGEY IFKRLLSIDT KSVFGVPGDF
60 70 80 90 100
NLSLLEYLYS PSVESAGLRW VGTCNELNAA YAADGYSRYS NKIGCLITTY
110 120 130 140 150
GVGELSALNG IAGSFAENVK VLHIVGVAKS IDSRSSNFSD RNLHHLVPQL
160 170 180 190 200
HDSNFKGPNH KVYHDMVKDR VACSVAYLED IETACDQVDN VIRDIYKYSK
210 220 230 240 250
PGYIFVPADF ADMSVTCDNL VNVPRISQQD CIVYPSENQL SDIINKITSW
260 270 280 290 300
IYSSKTPAIL GDVLTDRYGV SNFLNKLICK TGIWNFSTVM GKSVIDESNP
310 320 330 340 350
TYMGQYNGKE GLKQVYEHFE LCDLVLHFGV DINEINNGHY TFTYKPNAKI
360 370 380 390 400
IQFHPNYIRL VDTRQGNEQM FKGINFAPIL KELYKRIDVS KLSLQYDSNV
410 420 430 440 450
TQYTNETMRL EDPTNGQSSI ITQVHLQKTM PKFLNPGDVV VCETGSFQFS
460 470 480 490 500
VRDFAFPSQL KYISQGFFLS IGMALPAALG VGIAMQDHSN AHINGGNVKE
510 520 530 540 550
DYKPRLILFE GDGAAQMTIQ ELSTILKCNI PLEVIIWNNN GYTIERAIMG
560 570 580 590 600
PTRSYNDVMS WKWTKLFEAF GDFDGKYTNS TLIQCPSKLA LKLEELKNSN
610 620 630
KRSGIELLEV KLGELDFPEQ LKCMVEAAAL KRNKK
Length:635
Mass (Da):71,384
Last modified:November 1, 1996 - v1
Checksum:i616DF7E06DA82415
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28373 Genomic DNA. Translation: AAB64816.1.
BK006938 Genomic DNA. Translation: DAA12223.1.
PIRiS61175.
RefSeqiNP_010668.3. NM_001180688.3.

Genome annotation databases

EnsemblFungiiYDR380W; YDR380W; YDR380W.
GeneIDi851987.
KEGGisce:YDR380W.

Similar proteinsi

Entry informationi

Entry nameiARO10_YEAST
AccessioniPrimary (citable) accession number: Q06408
Secondary accession number(s): D6VT13
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: November 1, 1996
Last modified: November 22, 2017
This is version 150 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names