LTHAD_YEAST
ID LTHAD_YEAST Reviewed; 326 AA.
AC P36007; D6VWY5;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=L-threo-3-hydroxyaspartate ammonia-lyase {ECO:0000305|PubMed:12951240};
DE EC=4.3.1.16 {ECO:0000269|PubMed:12951240};
DE AltName: Full=L-threo-3-hydroxyaspartate dehydratase {ECO:0000303|PubMed:12951240};
GN Name=SRY1; OrderedLocusNames=YKL218C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7941750; DOI=10.1002/yea.320100511;
RA Tzermia M., Horaitis O., Alexandraki D.;
RT "The complete sequencing of a 24.6 kb segment of yeast chromosome XI
RT identified the known loci URA1, SAC1 and TRP3, and revealed 6 new open
RT reading frames including homologues to the threonine dehydratases, membrane
RT transporters, hydantoinases and the phospholipase A2-activating protein.";
RL Yeast 10:663-679(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=12951240; DOI=10.1016/s0378-1097(03)00484-1;
RA Wada M., Nakamori S., Takagi H.;
RT "Serine racemase homologue of Saccharomyces cerevisiae has L-threo-3-
RT hydroxyaspartate dehydratase activity.";
RL FEMS Microbiol. Lett. 225:189-193(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Catalyzes the deamination of L-threo-3-hydroxyaspartate to
CC oxaloacetate and ammonia. Shows a high specificity towards L-threo-3-
CC hydroxyaspartate as other 3-hydroxyaminoacids, i.e. D,L-erythro- and D-
CC threo-3-hydroxyaspartate, D-threonine, L-threonine, D,L-allothreonine,
CC D-serine, and L-serine, are not substrates for this enzyme. Exhibits no
CC detectable serine racemase activity. Is responsible for the 3-
CC hydroxyaspartate resistance of S.cerevisiae, and thus may be involved
CC in the detoxification of naturally occurring 3-hydroxyaspartate.
CC {ECO:0000269|PubMed:12951240}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3-hydroxy-L-aspartate = NH4(+) + oxaloacetate;
CC Xref=Rhea:RHEA:12424, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57251; EC=4.3.1.16;
CC Evidence={ECO:0000269|PubMed:12951240};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:12951240};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12951240};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12951240};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:12951240};
CC Note=Requires a divalent metal cation such as Mn(2+), Mg(2+), or
CC Ca(2+). {ECO:0000269|PubMed:12951240};
CC -!- ACTIVITY REGULATION: Is strongly inhibited by hydroxylamine and EDTA in
CC vitro. {ECO:0000269|PubMed:12951240}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.9 mM for L-threo-3-hydroxyaspartate
CC {ECO:0000269|PubMed:12951240};
CC Vmax=110 umol/min/mg enzyme {ECO:0000269|PubMed:12951240};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12951240}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow as well as the wild-
CC type parent strain on SD medium, but fail to grow on hydroxyaspartate-
CC containing agar plate. {ECO:0000269|PubMed:12951240}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000305}.
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DR EMBL; X75951; CAA53555.1; -; Genomic_DNA.
DR EMBL; Z28218; CAA82063.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08951.1; -; Genomic_DNA.
DR PIR; S38061; S38061.
DR RefSeq; NP_012704.1; NM_001179783.1.
DR AlphaFoldDB; P36007; -.
DR SMR; P36007; -.
DR BioGRID; 33947; 137.
DR DIP; DIP-6523N; -.
DR IntAct; P36007; 3.
DR MINT; P36007; -.
DR STRING; 4932.YKL218C; -.
DR iPTMnet; P36007; -.
DR MaxQB; P36007; -.
DR PaxDb; P36007; -.
DR PRIDE; P36007; -.
DR EnsemblFungi; YKL218C_mRNA; YKL218C; YKL218C.
DR GeneID; 853662; -.
DR KEGG; sce:YKL218C; -.
DR SGD; S000001701; SRY1.
DR VEuPathDB; FungiDB:YKL218C; -.
DR eggNOG; KOG1251; Eukaryota.
DR HOGENOM; CLU_021152_4_2_1; -.
DR InParanoid; P36007; -.
DR OMA; LIHPFDH; -.
DR BioCyc; YEAST:YKL218C-MON; -.
DR Reactome; R-SCE-977347; Serine biosynthesis.
DR SABIO-RK; P36007; -.
DR PRO; PR:P36007; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36007; protein.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0008721; F:D-serine ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0030378; F:serine racemase activity; IBA:GO_Central.
DR GO; GO:0030848; F:threo-3-hydroxyaspartate ammonia-lyase activity; IDA:SGD.
DR GO; GO:0018114; F:threonine racemase activity; IBA:GO_Central.
DR GO; GO:0042219; P:cellular modified amino acid catabolic process; IDA:SGD.
DR GO; GO:0070179; P:D-serine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006563; P:L-serine metabolic process; IBA:GO_Central.
DR GO; GO:0042866; P:pyruvate biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Manganese; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..326
FT /note="L-threo-3-hydroxyaspartate ammonia-lyase"
FT /id="PRO_0000185589"
FT BINDING 80
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P04968"
FT BINDING 179..183
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P04968"
FT BINDING 304
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P04968"
FT MOD_RES 53
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P04968"
SQ SEQUENCE 326 AA; 34899 MW; 21CF7FEFC8AB4431 CRC64;
MIVPTYGDVL DASNRIKEYV NKTPVLTSRM LNDRLGAQIY FKGENFQRVG AFKFRGAMNA
VSKLSDEKRS KGVIAFSSGN HAQAIALSAK LLNVPATIVM PEDAPALKVA ATAGYGAHII
RYNRYTEDRE QIGRQLAAEH GFALIPPYDH PDVIAGQGTS AKELLEEVGQ LDALFVPLGG
GGLLSGSALA ARSLSPGCKI FGVEPEAGND GQQSFRSGSI VHINTPKTIA DGAQTQHLGE
YTFAIIRENV DDILTVSDQE LVKCMHFLAE RMKVVVEPTA CLGFAGALLK KEELVGKKVG
IILSGGNVDM KRYATLISGK EDGPTI
