DTA_ARTSP
ID DTA_ARTSP Reviewed; 379 AA.
AC O82872;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=D-threonine aldolase {ECO:0000303|PubMed:9346293, ECO:0000303|PubMed:9642221};
DE EC=4.1.2.42;
OS Arthrobacter sp.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=1667;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA31547.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 50-62, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DK-38 {ECO:0000312|EMBL:BAA31547.1};
RX PubMed=9642221; DOI=10.1074/jbc.273.27.16678;
RA Liu J.-Q., Dairi T., Itoh N., Kataoka M., Shimizu S., Yamada H.;
RT "A novel metal-activated pyridoxal enzyme with a unique primary structure,
RT low specificity D-threonine aldolase from Arthrobacter sp. Strain DK-38.
RT Molecular cloning and cofactor characterization.";
RL J. Biol. Chem. 273:16678-16685(1998).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DK-38 {ECO:0000269|PubMed:9346293};
RX PubMed=9346293; DOI=10.1111/j.1432-1033.1997.00385.x;
RA Kataoka M., Ikemi M., Morikawa T., Miyoshi T., Nishi K., Wada M.,
RA Yamada H., Shimizu S.;
RT "Isolation and characterization of D-threonine aldolase, a pyridoxal-5'-
RT phosphate-dependent enzyme from Arthrobacter sp. DK-38.";
RL Eur. J. Biochem. 248:385-393(1997).
CC -!- FUNCTION: Catalyzes the reversible cleavage of D-threonine or D-
CC allothreonine into glycine and acetaldehyde. Can also cleave D-beta-
CC phenylserine, D-beta-hydroxy-alpha-aminovaleric acid, D-beta-3,4-
CC dihydroxyphenylserine and D-beta-3,4-methylenedioxyphenylserine into
CC glycine and the corresponding aldehyde compounds. Inactive towards D-
CC serine, beta-hydroxyaspartate and O-phospho-DL-threonine.
CC {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threonine = acetaldehyde + glycine; Xref=Rhea:RHEA:15257,
CC ChEBI:CHEBI:15343, ChEBI:CHEBI:57305, ChEBI:CHEBI:57757; EC=4.1.2.42;
CC Evidence={ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-allothreonine = acetaldehyde + glycine;
CC Xref=Rhea:RHEA:20073, ChEBI:CHEBI:15343, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:58645; EC=4.1.2.42; Evidence={ECO:0000269|PubMed:9346293,
CC ECO:0000269|PubMed:9642221};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC Note=Binds 1 pyridoxal phosphate per subunit.
CC {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC Note=Binds 1 Mn(2+) ion per subunit. Can also use Co(2+), Ni(2+) and
CC Mg(2+). {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC -!- ACTIVITY REGULATION: Inhibited by the carbonyl reagents hydroxylamine,
CC phenylhydrazine and semicarbazide. Inhibited by the chelating agent
CC EDTA. Inhibited by the sulfhydryl reagent p-chloromercuribenzoic acid,
CC and by sodium cyanide. Inhibited by iodoacetate, Ag(2)SO(4), HgCl(2)
CC and CdCl(2). Competitively inhibited by beta-hydroxyaspartate and O-
CC phospho-DL-threonine. {ECO:0000269|PubMed:9346293}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.81 mM for D-threonine (at pH 7.5, in the presence of 0.5 mM
CC MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC KM=14.0 mM for D-allothreonine (at pH 7.5, in the presence of 0.5 mM
CC MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC KM=1.75 mM for D-threo-beta-hydroxy-alpha-aminovaleric acid (at pH
CC 7.5, in the presence of 0.5 mM MnCl(2)) {ECO:0000269|PubMed:9346293,
CC ECO:0000269|PubMed:9642221};
CC KM=46.8 mM for D-threo-beta-phenylserine (at pH 7.5, in the presence
CC of 0.5 mM MnCl(2)) {ECO:0000269|PubMed:9346293,
CC ECO:0000269|PubMed:9642221};
CC KM=8.4 mM for D-threonine (at pH 8.0, in the presence of 0.1 uM
CC MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC KM=8.8 mM for D-threonine (at pH 8.0, in the absence of MnCl(2))
CC {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC KM=4.4 mM for D-allothreonine (at pH 8.0, in the presence of 0.1 uM
CC MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC KM=4.3 mM for D-allothreonine (at pH 8.0, in the absence of MnCl(2))
CC {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC KM=5.4 mM for DL-threo-phenylserine (at pH 8.0, in the presence of
CC 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293,
CC ECO:0000269|PubMed:9642221};
CC KM=5.9 mM for DL-threo-phenylserine (at pH 8.0, in the absence of
CC MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC KM=5.3 mM for DL-erythro-phenylserine (at pH 8.0, in the presence of
CC 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293,
CC ECO:0000269|PubMed:9642221};
CC KM=4.9 mM for DL-erythro-phenylserine (at pH 8.0, in the absence of
CC MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC KM=1.8 mM for DL-threo-beta-3,4-methylenedioxyphenylserine (at pH
CC 8.0, in the presence of 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293,
CC ECO:0000269|PubMed:9642221};
CC KM=1.8 mM for DL-threo-beta-3,4-methylenedioxyphenylserine (at pH
CC 8.0, in the absence of MnCl(2)) {ECO:0000269|PubMed:9346293,
CC ECO:0000269|PubMed:9642221};
CC KM=2.5 mM for DL-erythro-beta-3,4-methylenedioxyphenylserine (at pH
CC 8.0, in the presence of 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293,
CC ECO:0000269|PubMed:9642221};
CC KM=2.0 mM for DL-erythro-beta-3,4-methylenedioxyphenylserine (at pH
CC 8.0, in the absence of MnCl(2)) {ECO:0000269|PubMed:9346293,
CC ECO:0000269|PubMed:9642221};
CC KM=1.2 mM for DL-threo-beta-3,4-dihydroxyphenylserine (at pH 8.0, in
CC the presence of 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293,
CC ECO:0000269|PubMed:9642221};
CC KM=1.4 mM for DL-threo-beta-3,4-dihydroxyphenylserine (at pH 8.0, in
CC the absence of MnCl(2)) {ECO:0000269|PubMed:9346293,
CC ECO:0000269|PubMed:9642221};
CC Vmax=38.8 umol/min/mg enzyme with D-threonine as substrate (at pH
CC 7.5, in the presence of 0.5 mM MnCl(2)) {ECO:0000269|PubMed:9346293,
CC ECO:0000269|PubMed:9642221};
CC Vmax=102 umol/min/mg enzyme with D-allothreonine as substrate (at pH
CC 7.5, in the presence of 0.5 mM MnCl(2)) {ECO:0000269|PubMed:9346293,
CC ECO:0000269|PubMed:9642221};
CC Vmax=9.01 umol/min/mg enzyme with D-threo-beta-hydroxy-alpha-
CC aminovaleric acid as substrate (at pH 7.5, in the presence of 0.5 mM
CC MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC Vmax=59.9 umol/min/mg enzyme with D-threo-beta-phenylserine as
CC substrate (at pH 7.5, in the presence of 0.5 mM MnCl(2))
CC {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC Vmax=32.1 umol/min/mg enzyme with D-threonine as substrate (at pH
CC 8.0, in the presence of 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293,
CC ECO:0000269|PubMed:9642221};
CC Vmax=3.0 umol/min/mg enzyme with D-threonine as substrate (at pH 8.0,
CC in absence of MnCl(2)) {ECO:0000269|PubMed:9346293,
CC ECO:0000269|PubMed:9642221};
CC Vmax=34.9 umol/min/mg enzyme with D-allothreonine as substrate (at pH
CC 8.0, in the presence of 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293,
CC ECO:0000269|PubMed:9642221};
CC Vmax=2.8 umol/min/mg enzyme with D-allothreonine as substrate (at pH
CC 8.0, in absence of MnCl(2)) {ECO:0000269|PubMed:9346293,
CC ECO:0000269|PubMed:9642221};
CC Vmax=209.8 umol/min/mg enzyme with DL-threo-phenylserine as substrate
CC (at pH 8.0, in the presence of 0.1 uM MnCl(2))
CC {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC Vmax=4.9 umol/min/mg enzyme with DL-threo-phenylserine as substrate
CC (at pH 8.0, in absence of MnCl(2)) {ECO:0000269|PubMed:9346293,
CC ECO:0000269|PubMed:9642221};
CC Vmax=164.4 umol/min/mg enzyme with DL-erythro-phenylserine as
CC substrate (at pH 8.0, in the presence of 0.1 uM MnCl(2))
CC {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC Vmax=1.9 umol/min/mg enzyme with DL-erythro-phenylserine as substrate
CC (at pH 8.0, in absence of MnCl(2)) {ECO:0000269|PubMed:9346293,
CC ECO:0000269|PubMed:9642221};
CC Vmax=129.3 umol/min/mg enzyme with DL-threo-beta-3,4-
CC methylenedioxyphenylserine as substrate (at pH 8.0, in the presence
CC of 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293,
CC ECO:0000269|PubMed:9642221};
CC Vmax=9.2 umol/min/mg enzyme with DL-threo-beta-3,4-
CC methylenedioxyphenylserine as substrate (at pH 8.0, in absence of
CC MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC Vmax=16.0 umol/min/mg enzyme with DL-erythro-beta-3,4-
CC methylenedioxyphenylserine as substrate (at pH 8.0, in the presence
CC of 0.1 uM MnCl(2)) {ECO:0000269|PubMed:9346293,
CC ECO:0000269|PubMed:9642221};
CC Vmax=1.9 umol/min/mg enzyme with DL-erythro-beta-3,4-
CC methylenedioxyphenylserine as substrate (at pH 8.0, in absence of
CC MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC Vmax=84.6 umol/min/mg enzyme with DL-threo-beta-3,4-
CC dihydroxyphenylserine as substrate (at pH 8.0, in the presence of 0.1
CC uM MnCl(2)) {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC Vmax=8.4 umol/min/mg enzyme with DL-threo-beta-3,4-
CC dihydroxyphenylserine as substrate (at pH 8.0, in absence of MnCl(2))
CC {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC pH dependence:
CC Optimum pH is 8.0-9.0. Stable between pH 7.0 and 8.5.
CC {ECO:0000269|PubMed:9346293, ECO:0000269|PubMed:9642221};
CC Temperature dependence:
CC Stable below 55 degrees Celsius. {ECO:0000269|PubMed:9346293,
CC ECO:0000269|PubMed:9642221};
CC -!- SIMILARITY: Belongs to the DSD1 family. {ECO:0000305}.
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DR EMBL; AB010956; BAA31547.1; -; Genomic_DNA.
DR AlphaFoldDB; O82872; -.
DR SMR; O82872; -.
DR PRIDE; O82872; -.
DR KEGG; ag:BAA31547; -.
DR BRENDA; 4.1.2.42; 457.
DR GO; GO:0016832; F:aldehyde-lyase activity; IDA:UniProtKB.
DR GO; GO:0043876; F:D-threonine aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0019478; P:D-amino acid catabolic process; IDA:UniProtKB.
DR Gene3D; 2.40.37.20; -; 1.
DR Gene3D; 3.20.20.10; -; 1.
DR InterPro; IPR001608; Ala_racemase_N.
DR InterPro; IPR026956; D-ser_dehydrat-like_dom.
DR InterPro; IPR042208; D-ser_dehydrat-like_sf.
DR InterPro; IPR029066; PLP-binding_barrel.
DR Pfam; PF01168; Ala_racemase_N; 1.
DR Pfam; PF14031; D-ser_dehydrat; 1.
DR SMART; SM01119; D-ser_dehydrat; 1.
DR SUPFAM; SSF51419; SSF51419; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Lyase; Pyridoxal phosphate.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9346293"
FT CHAIN 2..379
FT /note="D-threonine aldolase"
FT /evidence="ECO:0000269|PubMed:9346293"
FT /id="PRO_0000403997"
FT MOD_RES 59
FT /note="N6-(pyridoxal phosphate)lysine"
SQ SEQUENCE 379 AA; 40031 MW; A5B6A3C2877CD2EB CRC64;
MSQEVIRGIA LPPPAQPGDP LARVDTPSLV LDLAPFEANL RAMQAWADRH DVALRPHAKA
HKCPEIALRQ LALGARGICC QKVSEALPFV AAGIQDIHIS NEVVGPAKLA LLGQLARVAK
ISVCVDNAHN LSQVSQAMVQ AGAQIDVLVE VDVGQGRCGV SDDALVLALA QQARDLPGVN
FAGLQAYHGS VQHYRTREER AEVCRQAARI AASYAQLLRE SGIACDTITG GGTGSAEFDA
ASGVYTELQA GSYAFMDGDY GANEWDGPLA FENSLFVLAT VMSKPAPDRV ILDAGLKSTT
AECGPPAIFG EPGLTYTAIN DEHGVVRVEP GAQAPDLGAV LRLVPSHVDP TFNLHDGLVV
VRDGVVEDIW EISARGFSR
