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P00927

- THDH_YEAST

UniProt

P00927 - THDH_YEAST

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Protein

Threonine dehydratase, mitochondrial

Gene

ILV1

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

Functioni

Catalytic activityi

L-threonine = 2-oxobutanoate + NH3.1 Publication

Cofactori

Enzyme regulationi

Isoleucine allosterically inhibits while valine allosterically activates this enzyme.1 Publication

Pathwayi

GO - Molecular functioni

  1. L-threonine ammonia-lyase activity Source: SGD
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. isoleucine biosynthetic process Source: SGD
  2. threonine catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Isoleucine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciYEAST:YER086W-MONOMER.
UniPathwayiUPA00047; UER00054.

Names & Taxonomyi

Protein namesi
Recommended name:
Threonine dehydratase, mitochondrial (EC:4.3.1.19)
Alternative name(s):
Threonine deaminase
Gene namesi
Name:ILV1
Ordered Locus Names:YER086W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome V

Organism-specific databases

CYGDiYER086w.
SGDiS000000888. ILV1.

Subcellular locationi

Mitochondrion 3 Publications

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 576Threonine dehydratase, mitochondrialPRO_0000033616
Transit peptidei1 – ?MitochondrionSequence Analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei109 – 1091N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

MaxQBiP00927.
PaxDbiP00927.
PeptideAtlasiP00927.

Expressioni

Inductioni

In response to starvation for tryptophan and branched-chain amino acid imbalance.1 Publication

Gene expression databases

GenevestigatoriP00927.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi36830. 204 interactions.
DIPiDIP-4029N.
IntActiP00927. 34 interactions.
MINTiMINT-565661.
STRINGi4932.YER086W.

Structurei

3D structure databases

ProteinModelPortaliP00927.
SMRiP00927. Positions 57-388.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini393 – 47381ACT-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini495 – 56672ACT-like 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 ACT-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

eggNOGiCOG1171.
GeneTreeiENSGT00600000084626.
HOGENOMiHOG000046975.
InParanoidiP00927.
KOiK01754.
OMAiATLEYSS.
OrthoDBiEOG75XGVN.

Family and domain databases

InterProiIPR001721. ACT-like_dom.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR005787. Thr_deHydtase_biosynth.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
PF00585. Thr_dehydrat_C. 2 hits.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01124. ilvA_2Cterm. 1 hit.
PROSITEiPS51672. ACT_LIKE. 2 hits.
PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00927-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSATLLKQPL CTVVRQGKQS KVSGLNLLRL KAHLHRQHLS PSLIKLHSEL
60 70 80 90 100
KLDELQTDNT PDYVRLVLRS SVYDVINESP ISQGVGLSSR LNTNVILKRE
110 120 130 140 150
DLLPVFSFKL RGAYNMIAKL DDSQRNQGVI ACSAGNHAQG VAFAAKHLKI
160 170 180 190 200
PATIVMPVCT PSIKYQNVSR LGSQVVLYGN DFDEAKAECA KLAEERGLTN
210 220 230 240 250
IPPFDHPYVI AGQGTVAMEI LRQVRTANKI GAVFVPVGGG GLIAGIGAYL
260 270 280 290 300
KRVAPHIKII GVETYDAATL HNSLQRNQRT PLPVVGTFAD GTSVRMIGEE
310 320 330 340 350
TFRVAQQVVD EVVLVNTDEI CAAVKDIFED TRSIVEPSGA LSVAGMKKYI
360 370 380 390 400
STVHPEIDHT KNTYVPILSG ANMNFDRLRF VSERAVLGEG KEVFMLVTLP
410 420 430 440 450
DVPGAFKKMQ KIIHPRSVTE FSYRYNEHRH ESSSEVPKAY IYTSFSVVDR
460 470 480 490 500
EKEIKQVMQQ LNALGFEAVD ISDNELAKSH GRYLVGGASK VPNERIISFE
510 520 530 540 550
FPERPGALTR FLGGLSDSWN LTLFHYRNHG ADIGKVLAGI SVPPRENLTF
560 570
QKFLEDLGYT YHDETDNTVY QKFLKY
Length:576
Mass (Da):63,831
Last modified:February 1, 1995 - v2
Checksum:i0801BCBD7EEDDC1F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti259 – 2591I → T in AAA34705. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36383 Genomic DNA. Translation: AAA34705.1.
X01466 Genomic DNA. Translation: CAA25696.1.
U18839 Genomic DNA. Translation: AAB64641.1.
BK006939 Genomic DNA. Translation: DAA07746.1.
PIRiS50589. DWBYT.
RefSeqiNP_011009.1. NM_001178977.1.

Genome annotation databases

EnsemblFungiiYER086W; YER086W; YER086W.
GeneIDi856819.
KEGGisce:YER086W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36383 Genomic DNA. Translation: AAA34705.1 .
X01466 Genomic DNA. Translation: CAA25696.1 .
U18839 Genomic DNA. Translation: AAB64641.1 .
BK006939 Genomic DNA. Translation: DAA07746.1 .
PIRi S50589. DWBYT.
RefSeqi NP_011009.1. NM_001178977.1.

3D structure databases

ProteinModelPortali P00927.
SMRi P00927. Positions 57-388.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36830. 204 interactions.
DIPi DIP-4029N.
IntActi P00927. 34 interactions.
MINTi MINT-565661.
STRINGi 4932.YER086W.

Proteomic databases

MaxQBi P00927.
PaxDbi P00927.
PeptideAtlasi P00927.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YER086W ; YER086W ; YER086W .
GeneIDi 856819.
KEGGi sce:YER086W.

Organism-specific databases

CYGDi YER086w.
SGDi S000000888. ILV1.

Phylogenomic databases

eggNOGi COG1171.
GeneTreei ENSGT00600000084626.
HOGENOMi HOG000046975.
InParanoidi P00927.
KOi K01754.
OMAi ATLEYSS.
OrthoDBi EOG75XGVN.

Enzyme and pathway databases

UniPathwayi UPA00047 ; UER00054 .
BioCyci YEAST:YER086W-MONOMER.

Miscellaneous databases

NextBioi 983097.
PROi P00927.

Gene expression databases

Genevestigatori P00927.

Family and domain databases

InterProi IPR001721. ACT-like_dom.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR005787. Thr_deHydtase_biosynth.
IPR001926. TrpB-like_PLP-dep.
[Graphical view ]
Pfami PF00291. PALP. 1 hit.
PF00585. Thr_dehydrat_C. 2 hits.
[Graphical view ]
SUPFAMi SSF53686. SSF53686. 1 hit.
TIGRFAMsi TIGR01124. ilvA_2Cterm. 1 hit.
PROSITEi PS51672. ACT_LIKE. 2 hits.
PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the gene for threonine deaminase (ILV1) of Saccharomyces cerevisiae."
    Kielland-Brandt M.C., Holmberg S., Petersen J.G.L., Nilsson-Tillgren T.
    Carlsberg Res. Commun. 49:567-575(1984)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Purification and properties of threonine deaminase from Saccharomyces cerevisiae."
    Ahmed S.I., Bollon A.P., Rogers S.J., Magee P.T.
    Biochimie 58:225-232(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  5. "Regulation of isoleucine-valine biosynthesis in Saccharomyces cerevisiae."
    Holmberg S., Petersen J.G.
    Curr. Genet. 13:207-217(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, INDUCTION.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  9. "Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics."
    Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.
    J. Proteome Res. 5:1543-1554(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTHDH_YEAST
AccessioniPrimary (citable) accession number: P00927
Secondary accession number(s): D3DLZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1995
Last modified: November 26, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 11900 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Allosteric enzyme, Complete proteome, 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 V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

External Data

Dasty 3