LTHAD_PSESP
ID LTHAD_PSESP Reviewed; 319 AA.
AC A4F2N8;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=L-threo-3-hydroxyaspartate ammonia-lyase {ECO:0000305|PubMed:10481099};
DE EC=4.3.1.16 {ECO:0000269|PubMed:10481099, ECO:0000269|PubMed:19193709};
DE AltName: Full=L-threo-3-hydroxyaspartate dehydratase {ECO:0000303|PubMed:10481099, ECO:0000303|PubMed:19193709};
DE Short=L-THA DH {ECO:0000303|PubMed:19193709};
GN Name=thadh {ECO:0000312|EMBL:BAF48772.1};
OS Pseudomonas sp.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=306;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND MUTAGENESIS OF
RP LYS-53.
RC STRAIN=T62;
RX PubMed=19193709; DOI=10.1093/jb/mvp023;
RA Murakami T., Maeda T., Yokota A., Wada M.;
RT "Gene cloning and expression of pyridoxal 5'-phosphate-dependent L-threo-3-
RT hydroxyaspartate dehydratase from Pseudomonas sp. T62, and characterization
RT of the recombinant enzyme.";
RL J. Biochem. 145:661-668(2009).
RN [2]
RP PROTEIN SEQUENCE OF 1-32, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVITY REGULATION,
RP INDUCTION, AND SUBUNIT.
RC STRAIN=T62;
RX PubMed=10481099; DOI=10.1111/j.1574-6968.1999.tb08720.x;
RA Wada M., Matsumoto T., Nakamori S., Sakamoto M., Kataoka M., Liu J.Q.,
RA Itoh N., Yamada H., Shimizu S.;
RT "Purification and characterization of a novel enzyme, L-threo-3-
RT hydroxyaspartate dehydratase, from Pseudomonas sp. T62.";
RL FEMS Microbiol. Lett. 179:147-151(1999).
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,L-threo-3-phenylserine, D-serine, and L-serine, are not substrates
CC for this enzyme (PubMed:10481099, PubMed:19193709). Exhibits no
CC detectable serine and aspartate racemase activity (PubMed:19193709).
CC Might play a role in the detoxification of naturally occurring 3-
CC hydroxyaspartate in Pseudomonas sp. T62 cells (PubMed:19193709).
CC {ECO:0000269|PubMed:10481099, ECO:0000269|PubMed:19193709}.
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:10481099, ECO:0000269|PubMed:19193709};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:10481099, ECO:0000269|PubMed:19193709};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:10481099, ECO:0000269|PubMed:19193709};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10481099, ECO:0000269|PubMed:19193709};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:10481099, ECO:0000269|PubMed:19193709};
CC Note=Requires a divalent metal cation such as Mn(2+), Mg(2+), or
CC Ca(2+). {ECO:0000269|PubMed:10481099, ECO:0000269|PubMed:19193709};
CC -!- ACTIVITY REGULATION: Is strongly inhibited by hydroxylamine and EDTA in
CC vitro. {ECO:0000269|PubMed:10481099}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.54 mM for L-threo-3-hydroxyaspartate
CC {ECO:0000269|PubMed:19193709};
CC KM=0.74 mM for L-threo-3-hydroxyaspartate
CC {ECO:0000269|PubMed:10481099};
CC Vmax=39 umol/min/mg enzyme {ECO:0000269|PubMed:19193709};
CC Vmax=37.5 umol/min/mg enzyme {ECO:0000269|PubMed:10481099};
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:19193709};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:19193709};
CC -!- SUBUNIT: May be either a monomer or a homodimer.
CC {ECO:0000269|PubMed:19193709}.
CC -!- INDUCTION: By D,L-threo-3-hydroxyaspartate.
CC {ECO:0000269|PubMed:19193709}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB297468; BAF48772.1; -; Genomic_DNA.
DR AlphaFoldDB; A4F2N8; -.
DR SMR; A4F2N8; -.
DR KEGG; ag:BAF48772; -.
DR BioCyc; MetaCyc:MON-15941; -.
DR BRENDA; 4.3.1.16; 10694.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0030848; F:threo-3-hydroxyaspartate ammonia-lyase activity; IDA:UniProtKB.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR GO; GO:0042219; P:cellular modified amino acid catabolic process; IDA:UniProtKB.
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 Direct protein sequencing; Lyase; Magnesium; Manganese;
KW Pyridoxal phosphate.
FT CHAIN 1..319
FT /note="L-threo-3-hydroxyaspartate ammonia-lyase"
FT /id="PRO_0000441721"
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,
FT ECO:0000305|PubMed:19193709"
FT MUTAGEN 53
FT /note="K->A: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:19193709"
SQ SEQUENCE 319 AA; 34333 MW; 1C9C094154837090 CRC64;
MQLSSYHDVI KAAERLEGFA NRTPVFTSRT LDAETGAQVF IKCENLQRTG SFKFRGAFNA
LSRFDEAQRK AGVVAFSSGN HAQGIALAAR LLQMPATIVM PTDAPAAKVA ATREYGATVV
FYDRITEDRE QIGRTLAEQH GMTLIPSYDH PDVLAGQGTA AKELLEFTGP LDALFVGLGG
GGMLSGTALA TRALSPDCLL YGVEPEAGND GQRSFQTGSI VHIDTPATIA DGAQTQHLGN
HTFPIIRENV NDILTVSDAE LVESMRFFMQ RMKMVVEPTG CLGLAALRNL KQQFRGQRVG
IIVTGGNVDI EKYASLLKG
