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Protein

L-threo-3-hydroxyaspartate ammonia-lyase

Gene

SRY1

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

Catalyzes the deamination of L-threo-3-hydroxyaspartate to oxaloacetate and ammonia. Shows a high specificity towards L-threo-3-hydroxyaspartate as other 3-hydroxyaminoacids, i.e. D,L-erythro- and D-threo-3-hydroxyaspartate, D-threonine, L-threonine, D,L-allothreonine, D-serine, and L-serine, are not substrates for this enzyme. Exhibits no detectable serine racemase activity. Is responsible for the 3-hydroxyaspartate resistance of S.cerevisiae, and thus may be involved in the detoxification of naturally occurring 3-hydroxyaspartate.1 Publication

Catalytic activityi

Threo-3-hydroxy-L-aspartate = oxaloacetate + NH3.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • pyridoxal 5'-phosphate1 Publication
  • Mn2+1 Publication, Mg2+1 Publication, Ca2+1 PublicationNote: Requires a divalent metal cation such as Mn2+, Mg2+, or Ca2+.1 Publication

Enzyme regulationi

Is strongly inhibited by hydroxylamine and EDTA in vitro.1 Publication

Kineticsi

  1. KM=3.9 mM for L-threo-3-hydroxyaspartate1 Publication
  1. Vmax=110 µmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei80Pyridoxal phosphateBy similarity1
Binding sitei304Pyridoxal phosphateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
LigandMagnesium, Manganese, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciYEAST:YKL218C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
L-threo-3-hydroxyaspartate ammonia-lyase1 Publication (EC:4.3.1.161 Publication)
Alternative name(s):
L-threo-3-hydroxyaspartate dehydratase1 Publication
Gene namesi
Name:SRY1
Ordered Locus Names:YKL218C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL218C.
SGDiS000001701. SRY1.

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene grow as well as the wild-type parent strain on SD medium, but fail to grow on hydroxyaspartate-containing agar plate.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001855891 – 326L-threo-3-hydroxyaspartate ammonia-lyaseAdd BLAST326

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei53N6-(pyridoxal phosphate)lysineBy similarity1

Proteomic databases

MaxQBiP36007.
PRIDEiP36007.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi33947. 132 interactors.
DIPiDIP-6523N.
IntActiP36007. 3 interactors.
STRINGi4932.YKL218C.

Structurei

3D structure databases

ProteinModelPortaliP36007.
SMRiP36007.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni179 – 183Pyridoxal phosphate bindingBy similarity5

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000075026.
HOGENOMiHOG000046974.
InParanoidiP36007.
OMAiLIHPFDH.
OrthoDBiEOG092C3P3F.

Family and domain databases

InterProiView protein in InterPro
IPR001926. PLP-dep.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR036052. Trypto_synt_PLP_dependent.
PfamiView protein in Pfam
PF00291. PALP. 1 hit.
SUPFAMiSSF53686. SSF53686. 1 hit.
PROSITEiView protein in PROSITE
PS00165. DEHYDRATASE_SER_THR. 1 hit.

Sequencei

Sequence statusi: Complete.

P36007-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIVPTYGDVL DASNRIKEYV NKTPVLTSRM LNDRLGAQIY FKGENFQRVG
60 70 80 90 100
AFKFRGAMNA VSKLSDEKRS KGVIAFSSGN HAQAIALSAK LLNVPATIVM
110 120 130 140 150
PEDAPALKVA ATAGYGAHII RYNRYTEDRE QIGRQLAAEH GFALIPPYDH
160 170 180 190 200
PDVIAGQGTS AKELLEEVGQ LDALFVPLGG GGLLSGSALA ARSLSPGCKI
210 220 230 240 250
FGVEPEAGND GQQSFRSGSI VHINTPKTIA DGAQTQHLGE YTFAIIRENV
260 270 280 290 300
DDILTVSDQE LVKCMHFLAE RMKVVVEPTA CLGFAGALLK KEELVGKKVG
310 320
IILSGGNVDM KRYATLISGK EDGPTI
Length:326
Mass (Da):34,899
Last modified:June 1, 1994 - v1
Checksum:i21CF7FEFC8AB4431
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75951 Genomic DNA. Translation: CAA53555.1.
Z28218 Genomic DNA. Translation: CAA82063.1.
BK006944 Genomic DNA. Translation: DAA08951.1.
PIRiS38061.
RefSeqiNP_012704.1. NM_001179783.1.

Genome annotation databases

EnsemblFungiiYKL218C; YKL218C; YKL218C.
GeneIDi853662.
KEGGisce:YKL218C.

Similar proteinsi

Entry informationi

Entry nameiLTHAD_YEAST
AccessioniPrimary (citable) accession number: P36007
Secondary accession number(s): D6VWY5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 25, 2017
This is version 138 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, 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 XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names