ID   RACD_THEK8              Reviewed;         232 AA.
AC   O93779;
DT   27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Aspartate racemase {ECO:0000303|PubMed:10515953};
DE            EC=5.1.1.13 {ECO:0000269|PubMed:10515953};
OS   Thermococcus sp. (strain KS-8).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus; unclassified Thermococcus.
OX   NCBI_TaxID=79680 {ECO:0000312|EMBL:BAA35091.1};
RN   [1] {ECO:0000312|EMBL:BAA35091.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC   STRAIN=KS-8 {ECO:0000312|EMBL:BAA35091.1};
RX   PubMed=10515953; DOI=10.1128/jb.181.20.6560-6563.1999;
RA   Matsumoto M., Homma H., Long Z., Imai K., Iida T., Maruyama T., Aikawa Y.,
RA   Endo I., Yohda M.;
RT   "Occurrence of free D-amino acids and aspartate racemases in
RT   hyperthermophilic archaea.";
RL   J. Bacteriol. 181:6560-6563(1999).
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:10515953};
CC   -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC       {ECO:0000305}.
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DR   EMBL; AB015880; BAA35091.1; -; Genomic_DNA.
DR   AlphaFoldDB; O93779; -.
DR   SMR; O93779; -.
DR   GO; GO:0047689; F:aspartate racemase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   InterPro; IPR015942; Asp/Glu/hydantoin_racemase.
DR   InterPro; IPR001920; Asp/Glu_race.
DR   InterPro; IPR004380; Asp_race.
DR   PANTHER; PTHR21198:SF7; PTHR21198:SF7; 1.
DR   Pfam; PF01177; Asp_Glu_race; 1.
DR   SUPFAM; SSF53681; SSF53681; 2.
DR   TIGRFAMs; TIGR00035; asp_race; 1.
PE   1: Evidence at protein level;
KW   Isomerase.
FT   CHAIN           1..232
FT                   /note="Aspartate racemase"
FT                   /id="PRO_0000433136"
FT   ACT_SITE        84
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O58403"
FT   ACT_SITE        195
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O58403"
FT   BINDING         49..51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O58403"
FT   BINDING         85..87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O58403"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O58403"
SQ   SEQUENCE   232 AA;  25428 MW;  5115EC43F9D730E1 CRC64;
     MPERVIGILG GMGPLATADL FRRIVEKTPA KRDQDHPRII IYNNPKIPDR TAFILGNGPD
     PRPELITSAR KLEECGADFI IMPCNTAHFF AGTIQSSVIY PLVSMIEETA KRIEEMGLRK
     VGLLATDGTI KGMVYHRALL KRGIHIAVPN KKDQGLVMKA IYEGVKAGNL ELGRELLLKV
     AKKLERRSEG IIAGCTEVSV VLKPGDLTVP LIDPMDVIAE RAVKLALGVE DF