ID   RACD_ANABR              Reviewed;          31 AA.
AC   P83989;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Aspartate racemase;
DE            EC=5.1.1.13;
DE   Flags: Fragment;
OS   Anadara broughtonii (Blood clam) (Scapharca broughtonii).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Arcoida; Arcoidea; Arcidae; Anadara.
OX   NCBI_TaxID=148819;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, COFACTOR, AND ACTIVITY REGULATION.
RC   TISSUE=Foot muscle {ECO:0000269|PubMed:12568809};
RX   PubMed=12568809; DOI=10.1016/s1096-4959(02)00267-1;
RA   Shibata K., Watanabe T., Yoshikawa H., Abe K., Takahashi S., Kera Y.,
RA   Yamada R.-H.;
RT   "Purification and characterization of aspartate racemase from the bivalve
RT   mollusk Scapharca broughtonii.";
RL   Comp. Biochem. Physiol. 134B:307-314(2003).
CC   -!- FUNCTION: Highly specific toward aspartate and entirely inactive on
CC       glutamate, alanine and serine. {ECO:0000269|PubMed:12568809}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate = D-aspartate; Xref=Rhea:RHEA:14973,
CC         ChEBI:CHEBI:29990, ChEBI:CHEBI:29991; EC=5.1.1.13;
CC         Evidence={ECO:0000269|PubMed:12568809};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:12568809};
CC   -!- ACTIVITY REGULATION: Inhibited by hydroxylamine, aminooxyacetate,
CC       phenylhydrazine and sodium borohydride. {ECO:0000269|PubMed:12568809}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8 for both directions of the reaction.;
CC       Temperature dependence:
CC         Optimum temperature is 25 degrees Celsius.;
CC   -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P83989; -.
DR   PRIDE; P83989; -.
DR   GO; GO:0047689; F:aspartate racemase activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Isomerase; Pyridoxal phosphate.
FT   CHAIN           1..>31
FT                   /note="Aspartate racemase"
FT                   /id="PRO_0000095539"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         31
FT                   /evidence="ECO:0000303|PubMed:12568809"
SQ   SEQUENCE   31 AA;  3487 MW;  8E775705BCD53DF0 CRC64;
     PVAPEYLFKK EEDKGANKEE EEVAPELGIR A