ID   RACD_ENTFU              Reviewed;         243 AA.
AC   H8L901;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Aspartate racemase;
DE            EC=5.1.1.13;
DE   AltName: Full=Rac(fm);
GN   OrderedLocusNames=EFAU004_01689;
OS   Enterococcus faecium (strain Aus0004).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1155766;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Aus0004;
RX   PubMed=22366422; DOI=10.1128/jb.00259-12;
RA   Lam M.M., Seemann T., Bulach D.M., Gladman S.L., Chen H., Haring V.,
RA   Moore R.J., Ballard S., Grayson M.L., Johnson P.D., Howden B.P.,
RA   Stinear T.P.;
RT   "Comparative analysis of the first complete Enterococcus faecium genome.";
RL   J. Bacteriol. 194:2334-2341(2012).
RN   [2]
RP   FUNCTION IN D-ASP PRODUCTION, AND PATHWAY.
RC   STRAIN=D359;
RX   PubMed=16510449; DOI=10.1074/jbc.m600114200;
RA   Bellais S., Arthur M., Dubost L., Hugonnet J.E., Gutmann L.,
RA   van Heijenoort J., Legrand R., Brouard J.P., Rice L., Mainardi J.L.;
RT   "Aslfm, the D-aspartate ligase responsible for the addition of D-aspartic
RT   acid onto the peptidoglycan precursor of Enterococcus faecium.";
RL   J. Biol. Chem. 281:11586-11594(2006).
CC   -!- FUNCTION: Aspartate racemase that provides the D-aspartate required by
CC       the D-aspartate ligase to be added onto the lysine residue in the
CC       peptidoglycan precursor UDP-MurNAc-pentapeptide.
CC       {ECO:0000269|PubMed:16510449}.
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   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000269|PubMed:16510449}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P29079}.
CC   -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC       {ECO:0000305}.
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DR   EMBL; CP003351; AFC63773.1; -; Genomic_DNA.
DR   AlphaFoldDB; H8L901; -.
DR   SMR; H8L901; -.
DR   KEGG; efc:EFAU004_01689; -.
DR   HOGENOM; CLU_055360_2_2_9; -.
DR   OMA; CNTAHFF; -.
DR   BioCyc; EFAE1155766:G1H3H-1783-MON; -.
DR   BioCyc; MetaCyc:MON-15488; -.
DR   UniPathway; UPA00219; -.
DR   GO; GO:0047689; F:aspartate racemase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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   Cell shape; Cell wall biogenesis/degradation; Isomerase;
KW   Peptidoglycan synthesis.
FT   CHAIN           1..243
FT                   /note="Aspartate racemase"
FT                   /id="PRO_0000418974"
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;  27940 MW;  E6C0149F39638006 CRC64;
     MENFFSILGG MGTMATESFV RLINHRTKAT KDQEYLNYVL FNHATVPDRT AYILDRSEEN
     PMPFLLDDIE KQNLLRPNFI VLTCNTAHYF FEELQAATDI PILHMPREAA NELVRQHTTG
     RVAILGTEGS MKAGIYEREV KNLGFETVIP DTALQEKINY LIYHEIKESD YLNQELYYEI
     LEEAVERLNC EKVILGCTEL SLMHEFAEDN HYPVIDAQSI LADRTIERAL AERSEALDTA
     SEK