ID   RACD_ENTFC              Reviewed;         243 AA.
AC   P29079;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Aspartate racemase;
DE            EC=5.1.1.13 {ECO:0000269|PubMed:1907199};
OS   Enterococcus faecium (Streptococcus faecium).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1352;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 51836 / IAM 10064;
RX   PubMed=2054383; DOI=10.1016/0167-4781(91)90013-c;
RA   Yohda M., Okada H., Kumagai H.;
RT   "Molecular cloning and nucleotide sequencing of the aspartate racemase gene
RT   from lactic acid bacteria Streptococcus thermophilus.";
RL   Biochim. Biophys. Acta 1089:234-240(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-19, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC
RP   ACTIVITY, AND SUBUNIT.
RC   STRAIN=ATCC 51836 / IAM 10064;
RX   PubMed=1907199; DOI=10.1016/0167-4838(91)90159-w;
RA   Okada H., Yohda M., Giga-Hama Y., Ueno Y., Ohdo S., Kumagai H.;
RT   "Distribution and purification of aspartate racemase in lactic acid
RT   bacteria.";
RL   Biochim. Biophys. Acta 1078:377-382(1991).
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:1907199};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.;
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius.;
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1907199}.
CC   -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC       {ECO:0000305}.
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DR   EMBL; X61301; CAA43598.1; -; Genomic_DNA.
DR   PIR; S16175; S16175.
DR   RefSeq; WP_038398745.1; NZ_SWBS01000003.1.
DR   AlphaFoldDB; P29079; -.
DR   SMR; P29079; -.
DR   STRING; 1352.AL014_07335; -.
DR   eggNOG; COG1794; Bacteria.
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; IPR018187; Asp/Glu_racemase_AS_1.
DR   InterPro; IPR033134; Asp/Glu_racemase_AS_2.
DR   InterPro; IPR004380; Asp_race.
DR   Pfam; PF01177; Asp_Glu_race; 1.
DR   SUPFAM; SSF53681; SSF53681; 2.
DR   TIGRFAMs; TIGR00035; asp_race; 1.
DR   PROSITE; PS00923; ASP_GLU_RACEMASE_1; 1.
DR   PROSITE; PS00924; ASP_GLU_RACEMASE_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Isomerase.
FT   CHAIN           1..243
FT                   /note="Aspartate racemase"
FT                   /id="PRO_0000095535"
FT   ACT_SITE        84
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O58403"
FT   ACT_SITE        197
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O58403"
FT   BINDING         48..50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O58403"
FT   BINDING         85..87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O58403"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O58403"
SQ   SEQUENCE   243 AA;  27946 MW;  6444569529768003 CRC64;
     MENFFSILGG MGTMATESFV RLINHRTKAT KDQEYLNYVL FNHATVPDRT AYILDRSEEN
     PMPFLLDDIE KQNLLRPNFI VLTCNTAHYF FEELQAATDI PILHMPREAA NELVRQHTTG
     RVAILGTEGS MKAGIYEREV KNLGFETVIP DTALQEKINY LIYHEIKESD HLNQELYYEI
     LEEAVERLNC EKVILGCTEL SLMNEFAEDN HYPVIDAQSI LADRTIERAL AERNEALDTV
     SEK