BHCC_PARDE
ID BHCC_PARDE Reviewed; 387 AA.
AC Q8GRC8;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=3-hydroxy-D-aspartate aldolase {ECO:0000305|PubMed:12835921};
DE EC=4.1.3.41 {ECO:0000269|PubMed:12835921};
DE AltName: Full=D-3-hydroxyaspartate aldolase {ECO:0000303|PubMed:12835921};
DE Short=D-HAA {ECO:0000303|PubMed:12835921};
GN Name=dhaa;
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-23, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 19367 / NBRC 13301 / NCIMB 8944 / NRRL B-3785;
RX PubMed=12835921; DOI=10.1007/s00253-003-1238-2;
RA Liu J.Q., Dairi T., Itoh N., Kataoka M., Shimizu S.;
RT "A novel enzyme, D-3-hydroxyaspartate aldolase from Paracoccus
RT denitrificans IFO 13301: purification, characterization, and gene
RT cloning.";
RL Appl. Microbiol. Biotechnol. 62:53-60(2003).
CC -!- FUNCTION: Catalyzes the condensation of glyoxylate and glycine into
CC (2R,3S)-beta-hydroxyaspartate ((3S)-3-hydroxy-D-aspartate). Functions
CC in glyoxylate assimilation via the beta-hydroxyaspartate cycle (BHAC)
CC (By similarity). In vitro catalyzes the cleavage of both D-erythro- and
CC D-threo-3-hydroxyaspartate to glycine and glyoxylate. Also acts on D-
CC threonine, D-3-phenylserine and D-3-3,4-methylenedioxyphenylserine
CC (PubMed:12835921). {ECO:0000250|UniProtKB:A1B8Z1,
CC ECO:0000269|PubMed:12835921}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3-hydroxy-D-aspartate = glycine + glyoxylate;
CC Xref=Rhea:RHEA:27934, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:60894; EC=4.1.3.41;
CC Evidence={ECO:0000269|PubMed:12835921};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27936;
CC Evidence={ECO:0000250|UniProtKB:A1B8Z1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-3-hydroxy-D-aspartate = glycine + glyoxylate;
CC Xref=Rhea:RHEA:27938, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:60898; EC=4.1.3.41;
CC Evidence={ECO:0000269|PubMed:12835921};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:12835921};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12835921};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12835921};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:12835921};
CC Note=Divalent metal cation. Can use Mn(2+), Mg(2+) or Co(2+).
CC {ECO:0000269|PubMed:12835921};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 mM for D-erythro-3-hydroxyaspartate
CC {ECO:0000269|PubMed:12835921};
CC Vmax=30 umol/min/mg enzyme with D-erythro-3-hydroxyaspartate as
CC substrate {ECO:0000269|PubMed:12835921};
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:12835921};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:12835921};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12835921}.
CC -!- MISCELLANEOUS: Strictly D-specific as to the alpha-position, but does
CC not distinguish between threo and erythro forms at the beta-position.
CC {ECO:0000305|PubMed:12835921}.
CC -!- SIMILARITY: Belongs to the DSD1 family. {ECO:0000305}.
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DR EMBL; AB075600; BAC20179.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GRC8; -.
DR SMR; Q8GRC8; -.
DR KEGG; ag:BAC20179; -.
DR BioCyc; MetaCyc:MON-15943; -.
DR BRENDA; 4.1.3.41; 3341.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016833; F:oxo-acid-lyase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; 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 Cobalt; Direct protein sequencing; Lyase; Magnesium; Manganese;
KW Metal-binding; Pyridoxal phosphate.
FT CHAIN 1..387
FT /note="3-hydroxy-D-aspartate aldolase"
FT /id="PRO_0000418597"
FT REGION 199..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:A1B8Z1"
FT BINDING 238
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:A1B8Z1"
FT BINDING 256..257
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:A1B8Z1"
FT BINDING 265
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:A1B8Z1"
FT BINDING 355
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A1B8Z1"
FT BINDING 357
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A1B8Z1"
FT MOD_RES 62
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:A1B8Z1"
SQ SEQUENCE 387 AA; 41633 MW; 242954BAE9BA3C5F CRC64;
MNAKTDFSGY EVGYDIPALP GMDESEIQTP CLILDLDALE RNIRKMGDYA KAHGMRHRSH
GKMHKSVDVQ KLQESLGGSV GVCCQKVSEA EAFARGGIKD VLVTNEVREP AKIDRLARLP
KTGATVTVCV DDVQNIADLS AAAQKHGTEL GIFVEIDCGA GRCGVTTKEA VVEIAKAAAA
APNLTFKGIQ AYQGRDAAHG QLRGPQGQAG RRHCPGERGR GRAGGRGLAP EFVSGGGTGS
YYFESNSGIY NELQCGSYAF MDADYGRIHD AEGKRIDQGE WENALFILTS VMSHAKPHLA
VVDAGLKAQS VDSGLPFVYG RDDVKYIKCS DEHGVVEDKD GVLKVNDKLR LVPGHCDPTC
NVHDWYVGVR NGKVETVWPV SARGKGY
