Q06408 (ARO10_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transaminated amino acid decarboxylase
EC=4.1.1.-

Alternative name(s):
Transaminated branched-chain amino acid decarboxylase

Gene names

Name:	ARO10
Ordered Locus Names:	YDR380W
ORF Names:	D9481.3

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	635 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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, phenylalanine, tryptophan, (and probably tyrosine), but also isoleucine, whereas leucine is a low efficiency and 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. Ref.3 Ref.4 Ref.6
Catalytic activity	A 2-oxo acid = an aldehyde + CO2. Phenylpyruvate = phenylacetaldehyde + CO2. 3-(indol-3-yl)pyruvate = 2-(indol-3-yl)acetaldehyde + CO2.
Cofactor	Binds 1 magnesium per subunit By similarity. Binds 1 thiamine pyrophosphate per subunit By similarity.
Pathway	Amino-acid degradation; Ehrlich pathway.
Subcellular location	Cytoplasm Ref.7.
Induction	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. Ref.3
Biotechnological use	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.
Miscellaneous	Present with 6560 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the TPP enzyme family.

Ontologies

Keywords
Biological process	Branched-chain amino acid catabolism Phenylalanine catabolism Tryptophan catabolism Tyrosine catabolism
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding Thiamine pyrophosphate
Molecular function	Decarboxylase Lyase
PTM	Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-phenylalanine catabolic process Inferred from direct assay Ref.5. Source: SGD aromatic amino acid family catabolic process to alcohol via Ehrlich pathway Inferred from genetic interaction Ref.6. Source: SGD branched-chain amino acid catabolic process to alcohol via Ehrlich pathway Inferred from genetic interaction Ref.6. Source: SGD leucine catabolic process Inferred from mutant phenotype Ref.4. Source: SGD methionine catabolic process to 3-methylthiopropanol Inferred from mutant phenotype PubMed 16423070. Source: SGD tryptophan catabolic process Inferred from genetic interaction Ref.6. Source: SGD tyrosine catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay Ref.7. Source: SGD
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: InterPro phenylpyruvate decarboxylase activity Inferred from direct assay Ref.5. Source: SGD pyruvate decarboxylase activity Inferred from sequence or structural similarity PubMed 8962070. Source: SGD thiamine pyrophosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 635	635	Transaminated amino acid decarboxylase		PRO_0000090835
Amino acid modifications
	Cross-link	588		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Q06408 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 616DF7E06DA82415	FASTA	635	71,384
	10 20 30 40 50 60 MAPVTIEKFV NQEERHLVSN RSATIPFGEY IFKRLLSIDT KSVFGVPGDF NLSLLEYLYS 70 80 90 100 110 120 PSVESAGLRW VGTCNELNAA YAADGYSRYS NKIGCLITTY GVGELSALNG IAGSFAENVK 130 140 150 160 170 180 VLHIVGVAKS IDSRSSNFSD RNLHHLVPQL HDSNFKGPNH KVYHDMVKDR VACSVAYLED 190 200 210 220 230 240 IETACDQVDN VIRDIYKYSK PGYIFVPADF ADMSVTCDNL VNVPRISQQD CIVYPSENQL 250 260 270 280 290 300 SDIINKITSW IYSSKTPAIL GDVLTDRYGV SNFLNKLICK TGIWNFSTVM GKSVIDESNP 310 320 330 340 350 360 TYMGQYNGKE GLKQVYEHFE LCDLVLHFGV DINEINNGHY TFTYKPNAKI IQFHPNYIRL 370 380 390 400 410 420 VDTRQGNEQM FKGINFAPIL KELYKRIDVS KLSLQYDSNV TQYTNETMRL EDPTNGQSSI 430 440 450 460 470 480 ITQVHLQKTM PKFLNPGDVV VCETGSFQFS VRDFAFPSQL KYISQGFFLS IGMALPAALG 490 500 510 520 530 540 VGIAMQDHSN AHINGGNVKE DYKPRLILFE GDGAAQMTIQ ELSTILKCNI PLEVIIWNNN 550 560 570 580 590 600 GYTIERAIMG PTRSYNDVMS WKWTKLFEAF GDFDGKYTNS TLIQCPSKLA LKLEELKNSN 610 620 630 KRSGIELLEV KLGELDFPEQ LKCMVEAAAL KRNKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Transcriptional induction by aromatic amino acids in Saccharomyces cerevisiae." Iraqui I., Vissers S., Andre B., Urrestarazu A. Mol. Cell. Biol. 19:3360-3371(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, REGULATION OF EXPRESSION.
[4]	"An investigation of the metabolism of isoleucine to active Amyl alcohol in Saccharomyces cerevisiae." Dickinson J.R., Harrison S.J., Dickinson J.A., Hewlins M.J. J. Biol. Chem. 275:10937-10942(2000) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN ISOLEUCINE CATABOLISM.
[5]	"Identification and characterization of phenylpyruvate decarboxylase genes in Saccharomyces cerevisiae." Vuralhan Z., Morais M.A., Tai S.L., Piper M.D., Pronk J.T. Appl. Environ. Microbiol. 69:4534-4541(2003) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[6]	"The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae." Dickinson J.R., Salgado L.E., Hewlins M.J. J. Biol. Chem. 278:8028-8034(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN PHENYLALANINE; TRYPTOPHAN AND LEUCINE CATABOLISM.
[7]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"A proteomics approach to understanding protein ubiquitination." Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P. Nat. Biotechnol. 21:921-926(2003) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-588, MASS SPECTROMETRY. Strain: SUB592.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U28373 Genomic DNA. Translation: AAB64816.1. BK006938 Genomic DNA. Translation: DAA12223.1.
PIR	S61175.
RefSeq	NP_010668.3. NM_001180688.3.
3D structure databases
ProteinModelPortal	Q06408.
SMR	Q06408. Positions 23-630.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5252N.
IntAct	Q06408. 2 interactions.
MINT	MINT-546662.
STRING	4932.YDR380W.
Proteomic databases
PaxDb	Q06408.
PeptideAtlas	Q06408.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDR380W; YDR380W; YDR380W.
GeneID	851987.
KEGG	sce:YDR380W. sce:YDR383C.
Organism-specific databases
CYGD	YDR380w.
SGD	S000002788. ARO10.
Phylogenomic databases
eggNOG	COG3961.
GeneTree	ENSGT00550000075465.
HOGENOM	HOG000061334.
KO	K12732.
OMA	PTRSYND.
OrthoDB	EOG4BZRB3.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-11837.
UniPathway	UPA00866.
Gene expression databases
Genevestigator	Q06408.
GermOnline	YDR380W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR012000. Thiamin_PyroP_enz_cen_dom. IPR012001. Thiamin_PyroP_enz_TPP-bd_dom. IPR012110. TPP_enzyme. IPR011766. TPP_enzyme-bd_C. [Graphical view]
PANTHER	PTHR18968:SF4. PTHR18968:SF4. 1 hit.
Pfam	PF02775. TPP_enzyme_C. 1 hit. PF00205. TPP_enzyme_M. 1 hit. PF02776. TPP_enzyme_N. 1 hit. [Graphical view]
PIRSF	PIRSF036565. Pyruvt_ip_decrb. 1 hit.
ProtoNet	Search...
Other
NextBio	970145.

Entry information

Entry name

ARO10_YEAST

Accession

Primary (citable) accession number: Q06408
Secondary accession number(s): D6VT13

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program