DTHAD_DELSH
ID DTHAD_DELSH Reviewed; 380 AA.
AC B2DFG5;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=D-threo-3-hydroxyaspartate dehydratase;
DE Short=D-THA DH;
DE Short=D-THA dehydratase;
DE EC=4.3.1.27;
DE AltName: Full=Threo-3-hydroxy-D-aspartate ammonia-lyase;
GN Name=dthadh;
OS Delftia sp. (strain HT23).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=518882;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25 AND 285-293,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF LYS-43.
RC STRAIN=HT23;
RX PubMed=20843822; DOI=10.1093/jb/mvq106;
RA Maeda T., Takeda Y., Murakami T., Yokota A., Wada M.;
RT "Purification, characterization and amino acid sequence of a novel enzyme,
RT D-threo-3-hydroxyaspartate dehydratase, from Delftia sp. HT23.";
RL J. Biochem. 148:705-712(2010).
CC -!- FUNCTION: Catalyzes the deamination of D-threo-3-hydroxyaspartate (D-
CC THA). Also exhibits dehydratase activity towards L-threo-3-
CC hydroxyaspartate (L-THA), L-erythro-3-hydroxyaspartate (L-EHA) and D-
CC serine. {ECO:0000269|PubMed:20843822}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-3-hydroxy-D-aspartate = NH4(+) + oxaloacetate;
CC Xref=Rhea:RHEA:27942, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:60898; EC=4.3.1.27;
CC Evidence={ECO:0000269|PubMed:20843822};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:20843822};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:20843822};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:20843822};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:20843822};
CC Note=Divalent metal ions, such as manganese, cobalt and nickel.
CC {ECO:0000269|PubMed:20843822};
CC -!- ACTIVITY REGULATION: Strongly inhibited by hydroxylamine. Modestly
CC inhibited by EDTA. {ECO:0000269|PubMed:20843822}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.42 mM for D-THA {ECO:0000269|PubMed:20843822};
CC KM=6.16 mM for L-THA {ECO:0000269|PubMed:20843822};
CC KM=0.16 mM for L-EHA {ECO:0000269|PubMed:20843822};
CC KM=0.15 mM for D-serine {ECO:0000269|PubMed:20843822};
CC Note=kcat is 10.93 sec(-1) for D-THA. kcat is 3.03 sec(-1) for L-THA.
CC kcat is 8.68 sec(-1) for L-EHA. kcat is 0.89 sec(-1) for D-serine.;
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:20843822};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:20843822};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20843822}.
CC -!- SIMILARITY: Belongs to the DSD1 family. {ECO:0000305}.
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DR EMBL; AB433986; BAG24498.1; -; Genomic_DNA.
DR PDB; 3WQC; X-ray; 1.50 A; A/B=1-380.
DR PDB; 3WQD; X-ray; 1.50 A; A/B=1-380.
DR PDB; 3WQE; X-ray; 1.60 A; A/B=1-380.
DR PDB; 3WQF; X-ray; 2.30 A; A/B=1-380.
DR PDB; 3WQG; X-ray; 1.55 A; A/B=1-380.
DR PDB; 4PB3; X-ray; 1.70 A; A/B=1-380.
DR PDB; 4PB4; X-ray; 1.80 A; A/B=1-380.
DR PDB; 4PB5; X-ray; 1.90 A; A/B=1-380.
DR PDBsum; 3WQC; -.
DR PDBsum; 3WQD; -.
DR PDBsum; 3WQE; -.
DR PDBsum; 3WQF; -.
DR PDBsum; 3WQG; -.
DR PDBsum; 4PB3; -.
DR PDBsum; 4PB4; -.
DR PDBsum; 4PB5; -.
DR AlphaFoldDB; B2DFG5; -.
DR SMR; B2DFG5; -.
DR KEGG; ag:BAG24498; -.
DR BioCyc; MetaCyc:MON-15942; -.
DR BRENDA; 4.3.1.27; 12512.
DR SABIO-RK; B2DFG5; -.
DR GO; GO:0016841; F:ammonia-lyase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IMP: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 3D-structure; Cobalt; Direct protein sequencing; Lyase; Manganese; Nickel;
KW Pyridoxal phosphate.
FT CHAIN 1..380
FT /note="D-threo-3-hydroxyaspartate dehydratase"
FT /id="PRO_0000418669"
FT MOD_RES 43
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000305"
FT MUTAGEN 43
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20843822"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:3WQC"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:3WQC"
FT HELIX 17..34
FT /evidence="ECO:0007829|PDB:3WQC"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:4PB5"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:3WQC"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:3WQC"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:3WQC"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:3WQC"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:3WQC"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:3WQC"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:3WQC"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:3WQC"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:3WQC"
FT STRAND 130..145
FT /evidence="ECO:0007829|PDB:3WQC"
FT HELIX 149..161
FT /evidence="ECO:0007829|PDB:3WQC"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:3WQC"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:3WQC"
FT HELIX 182..205
FT /evidence="ECO:0007829|PDB:3WQC"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:3WQC"
FT HELIX 218..223
FT /evidence="ECO:0007829|PDB:3WQC"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:4PB5"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:3WQC"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:3WQC"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:3WQC"
FT STRAND 258..268
FT /evidence="ECO:0007829|PDB:3WQC"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:3WQC"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:3WQC"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:3WQC"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:3WQC"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:3WQC"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:3WQC"
FT STRAND 308..317
FT /evidence="ECO:0007829|PDB:3WQC"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:3WQC"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:3WQC"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:3WQC"
FT HELIX 352..357
FT /evidence="ECO:0007829|PDB:3WQC"
FT STRAND 360..365
FT /evidence="ECO:0007829|PDB:3WQC"
FT STRAND 369..375
FT /evidence="ECO:0007829|PDB:3WQC"
SQ SEQUENCE 380 AA; 40329 MW; 916B18060E25BAAB CRC64;
MQDTLLTLDT PAAVIDLDRM QRNIARMQQR MDAQGVRLRP HVKTSKSVPV AAAQRAAGAS
GITVSTLKEA EQFFAAGTTD ILYAVSMAPH RLPQALQLRR RGCDLKLIVD SVAAAQAIAA
FGREQGEAFE VWIEIDTDGH RSGVGADDTP LLLAIGRTLH DGGMRLGGVL THAGSSYELD
TPEALQALAE RERAGCVQAA EALRAAGLPC PVVSVGSTPT ALAASRLDGV TEVRAGVYVF
FDLVMRNIGV CAAEDVALSV LATVIGHQAD KGWAIVDAGW MAMSRDRGTA RQKQDFGYGQ
VCDLQGRVMP GFVLTGANQE HGILARADGA AEADIATRFP LGTRLRILPN HACATGAQFP
AYQALAADGS VQTWERLHGW
