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Protein

Catabolic L-serine/threonine dehydratase

Gene

CHA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-serine = pyruvate + NH3.
L-threonine = 2-oxobutanoate + NH3.

Cofactori

GO - Molecular functioni

  • L-serine ammonia-lyase activity Source: SGD
  • L-threonine ammonia-lyase activity Source: SGD
  • pyridoxal phosphate binding Source: GO_Central

GO - Biological processi

  • L-serine catabolic process Source: SGD
  • threonine catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciYEAST:YCL064C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Catabolic L-serine/threonine dehydratase
Including the following 2 domains:
L-serine dehydratase (EC:4.3.1.17)
Alternative name(s):
L-serine deaminase
L-threonine dehydratase (EC:4.3.1.19)
Alternative name(s):
L-threonine deaminase
Gene namesi
Name:CHA1
Ordered Locus Names:YCL064C
ORF Names:YCL64C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:YCL064C.
SGDiS000000569. CHA1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial nucleoid Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 360359Catabolic L-serine/threonine dehydratasePRO_0000185598Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei37 – 371N6-(pyridoxal phosphate)lysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP25379.

Interactioni

Protein-protein interaction databases

BioGridi30924. 34 interactions.
DIPiDIP-7970N.
IntActiP25379. 7 interactions.
MINTiMINT-2785091.

Structurei

3D structure databases

ProteinModelPortaliP25379.
SMRiP25379. Positions 7-327.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000074775.
HOGENOMiHOG000046976.
InParanoidiP25379.
KOiK17989.
OMAiREIFCAS.
OrthoDBiEOG092C371W.

Family and domain databases

InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P25379-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIVYNKTPL LRQFFPGKAS AQFFLKYECL QPSGSFKSRG IGNLIMKSAI
60 70 80 90 100
RIQKDGKRSP QVFASSGGNA GFAAATACQR LSLPCTVVVP TATKKRMVDK
110 120 130 140 150
IRNTGAQVIV SGAYWKEADT FLKTNVMNKI DSQVIEPIYV HPFDNPDIWE
160 170 180 190 200
GHSSMIDEIV QDLKSQHISV NKVKGIVCSV GGGGLYNGII QGLERYGLAD
210 220 230 240 250
RIPIVGVETN GCHVFNTSLK IGQPVQFKKI TSIATSLGTA VISNQTFEYA
260 270 280 290 300
RKYNTRSVVI EDKDVIETCL KYTHQFNMVI EPACGAALHL GYNTKILENA
310 320 330 340 350
LGSKLAADDI VIIIACGGSS NTIKDLEEAL DSMRKKDTPV IEVADNFIFP
360
EKNIVNLKSA
Length:360
Mass (Da):39,301
Last modified:March 15, 2004 - v2
Checksum:iFC905FF3D111187D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341G → A in AAA35040 (PubMed:1628804).Curated
Sequence conflicti268 – 2681T → P in AAA35040 (PubMed:1628804).Curated
Sequence conflicti317 – 3182GG → AS in AAA35040 (PubMed:1628804).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M85194 Genomic DNA. Translation: AAA35040.1.
X59720 Genomic DNA. Translation: CAA42403.2.
BK006937 Genomic DNA. Translation: DAA07423.1.
PIRiS19395. DWBYLH.
RefSeqiNP_001018030.1. NM_001178706.1.

Genome annotation databases

EnsemblFungiiCAA42403; CAA42403; CAA42403.
YCL064C; YCL064C; YCL064C.
GeneIDi850295.
KEGGisce:YCL064C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M85194 Genomic DNA. Translation: AAA35040.1.
X59720 Genomic DNA. Translation: CAA42403.2.
BK006937 Genomic DNA. Translation: DAA07423.1.
PIRiS19395. DWBYLH.
RefSeqiNP_001018030.1. NM_001178706.1.

3D structure databases

ProteinModelPortaliP25379.
SMRiP25379. Positions 7-327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi30924. 34 interactions.
DIPiDIP-7970N.
IntActiP25379. 7 interactions.
MINTiMINT-2785091.

Proteomic databases

MaxQBiP25379.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAA42403; CAA42403; CAA42403.
YCL064C; YCL064C; YCL064C.
GeneIDi850295.
KEGGisce:YCL064C.

Organism-specific databases

EuPathDBiFungiDB:YCL064C.
SGDiS000000569. CHA1.

Phylogenomic databases

GeneTreeiENSGT00550000074775.
HOGENOMiHOG000046976.
InParanoidiP25379.
KOiK17989.
OMAiREIFCAS.
OrthoDBiEOG092C371W.

Enzyme and pathway databases

BioCyciYEAST:YCL064C-MONOMER.

Miscellaneous databases

PROiP25379.

Family and domain databases

InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSTDH_YEAST
AccessioniPrimary (citable) accession number: P25379
Secondary accession number(s): D6VQV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: March 15, 2004
Last modified: September 7, 2016
This is version 134 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 36600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

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.