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L-threo-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.16) (L-threo-3-hydroxyaspartate dehydratase)

 LTHAD_YEAST             Reviewed;         326 AA.
P36007; D6VWY5;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
23-MAY-2018, entry version 141.
RecName: Full=L-threo-3-hydroxyaspartate ammonia-lyase {ECO:0000305|PubMed:12951240};
EC=4.3.1.16 {ECO:0000269|PubMed:12951240};
AltName: Full=L-threo-3-hydroxyaspartate dehydratase {ECO:0000303|PubMed:12951240};
Name=SRY1; OrderedLocusNames=YKL218C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7941750; DOI=10.1002/yea.320100511;
Tzermia M., Horaitis O., Alexandraki D.;
"The complete sequencing of a 24.6 kb segment of yeast chromosome XI
identified the known loci URA1, SAC1 and TRP3, and revealed 6 new open
reading frames including homologues to the threonine dehydratases,
membrane transporters, hydantoinases and the phospholipase A2-
activating protein.";
Yeast 10:663-679(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8196765; DOI=10.1038/369371a0;
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M.,
Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C.,
Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G.,
Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
SUBSTRATE SPECIFICITY, ENZYME REGULATION, SUBUNIT, AND DISRUPTION
PHENOTYPE.
STRAIN=ATCC 204508 / S288c;
PubMed=12951240; DOI=10.1016/S0378-1097(03)00484-1;
Wada M., Nakamori S., Takagi H.;
"Serine racemase homologue of Saccharomyces cerevisiae has L-threo-3-
hydroxyaspartate dehydratase activity.";
FEMS Microbiol. Lett. 225:189-193(2003).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: 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. {ECO:0000269|PubMed:12951240}.
-!- CATALYTIC ACTIVITY: Threo-3-hydroxy-L-aspartate = oxaloacetate +
NH(3). {ECO:0000269|PubMed:12951240}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000269|PubMed:12951240};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:12951240};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:12951240};
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:12951240};
Note=Requires a divalent metal cation such as Mn(2+), Mg(2+), or
Ca(2+). {ECO:0000269|PubMed:12951240};
-!- ENZYME REGULATION: Is strongly inhibited by hydroxylamine and EDTA
in vitro. {ECO:0000269|PubMed:12951240}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.9 mM for L-threo-3-hydroxyaspartate
{ECO:0000269|PubMed:12951240};
Vmax=110 umol/min/mg enzyme {ECO:0000269|PubMed:12951240};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12951240}.
-!- DISRUPTION PHENOTYPE: 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.
{ECO:0000269|PubMed:12951240}.
-!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
{ECO:0000305}.
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EMBL; X75951; CAA53555.1; -; Genomic_DNA.
EMBL; Z28218; CAA82063.1; -; Genomic_DNA.
EMBL; BK006944; DAA08951.1; -; Genomic_DNA.
PIR; S38061; S38061.
RefSeq; NP_012704.1; NM_001179783.1.
ProteinModelPortal; P36007; -.
SMR; P36007; -.
BioGrid; 33947; 134.
DIP; DIP-6523N; -.
IntAct; P36007; 3.
MINT; P36007; -.
STRING; 4932.YKL218C; -.
MaxQB; P36007; -.
PaxDb; P36007; -.
PRIDE; P36007; -.
EnsemblFungi; YKL218C; YKL218C; YKL218C.
GeneID; 853662; -.
KEGG; sce:YKL218C; -.
EuPathDB; FungiDB:YKL218C; -.
SGD; S000001701; SRY1.
GeneTree; ENSGT00550000075026; -.
HOGENOM; HOG000046974; -.
InParanoid; P36007; -.
OMA; LIHPFDH; -.
OrthoDB; EOG092C3P3F; -.
BioCyc; YEAST:YKL218C-MONOMER; -.
Reactome; R-SCE-977347; Serine biosynthesis.
PRO; PR:P36007; -.
Proteomes; UP000002311; Chromosome XI.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0030848; F:threo-3-hydroxyaspartate ammonia-lyase activity; IDA:SGD.
GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
GO; GO:0042219; P:cellular modified amino acid catabolic process; IDA:SGD.
InterPro; IPR001926; PLP-dep.
InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
InterPro; IPR036052; Trypto_synt_PLP_dependent.
Pfam; PF00291; PALP; 1.
SUPFAM; SSF53686; SSF53686; 1.
PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
1: Evidence at protein level;
Complete proteome; Lyase; Magnesium; Manganese; Pyridoxal phosphate;
Reference proteome.
CHAIN 1 326 L-threo-3-hydroxyaspartate ammonia-lyase.
/FTId=PRO_0000185589.
REGION 179 183 Pyridoxal phosphate binding.
{ECO:0000250|UniProtKB:P04968}.
BINDING 80 80 Pyridoxal phosphate.
{ECO:0000250|UniProtKB:P04968}.
BINDING 304 304 Pyridoxal phosphate.
{ECO:0000250|UniProtKB:P04968}.
MOD_RES 53 53 N6-(pyridoxal phosphate)lysine.
{ECO:0000250|UniProtKB:P04968}.
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


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19398-78-8 3,4_Diethyl_3_hexanol Threo + erythro 1g
19549-74-7 3,5_Dimethyl_3_heptanol Threo + erythro 1g


 

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