ID   Q837J0_ENTFA            Unreviewed;       371 AA.
AC   Q837J0;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 148.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   Name=alr {ECO:0000313|EMBL:AAO80661.1};
GN   OrderedLocusNames=EF_0849 {ECO:0000313|EMBL:AAO80661.1};
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185 {ECO:0000313|EMBL:AAO80661.1, ECO:0000313|Proteomes:UP000001415};
RN   [1] {ECO:0000313|EMBL:AAO80661.1, ECO:0000313|Proteomes:UP000001415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583 {ECO:0000313|Proteomes:UP000001415};
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D.,
RA   Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L., Brinkac L., Beanan M., Daugherty S., DeBoy R.T.,
RA   Durkin S., Kolonay J., Madupu R., Nelson W., Vamathevan J., Tran B.,
RA   Upton J., Hansen T., Shetty J., Khouri H., Utterback T., Radune D.,
RA   Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
RN   [2] {ECO:0007829|PDB:3E5P, ECO:0007829|PDB:3E6E}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), AND PYRIDOXAL PHOSPHATE AT LYS-40.
RX   PubMed=19328247; DOI=10.1016/j.bbapap.2009.03.006;
RA   Priyadarshi A., Lee E.H., Sung M.W., Nam K.H., Lee W.H., Kim E.E.,
RA   Hwang K.Y.;
RT   "Structural insights into the alanine racemase from Enterococcus
RT   faecalis.";
RL   Biochim. Biophys. Acta 1794:1030-1040(2009).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC       also act on other amino acids. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933, ECO:0000256|HAMAP-
CC         Rule:MF_01201, ECO:0000256|PIRSR:PIRSR600821-50};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC       from L-alanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016830; AAO80661.1; -; Genomic_DNA.
DR   RefSeq; NP_814591.1; NC_004668.1.
DR   RefSeq; WP_002355728.1; NZ_KE136527.1.
DR   PDB; 3E5P; X-ray; 2.50 A; A/B/C=1-371.
DR   PDB; 3E6E; X-ray; 2.50 A; A/B/C=1-371.
DR   PDBsum; 3E5P; -.
DR   PDBsum; 3E6E; -.
DR   AlphaFoldDB; Q837J0; -.
DR   SMR; Q837J0; -.
DR   STRING; 226185.EF_0849; -.
DR   EnsemblBacteria; AAO80661; AAO80661; EF_0849.
DR   KEGG; efa:EF0849; -.
DR   PATRIC; fig|226185.46.peg.1254; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_2_1_9; -.
DR   UniPathway; UPA00042; UER00497.
DR   EvolutionaryTrace; Q837J0; -.
DR   Proteomes; UP000001415; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00430; PLPDE_III_AR; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   HAMAP; MF_01201; Ala_racemase; 1.
DR   InterPro; IPR000821; Ala_racemase.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   NCBIfam; TIGR00492; alr; 1.
DR   PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR   PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3E5P, ECO:0007829|PDB:3E6E};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_01201}; Reference proteome {ECO:0000313|Proteomes:UP000001415}.
FT   DOMAIN          246..371
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        40
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        267
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         40
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="covalent"
FT                   /evidence="ECO:0007829|PDB:3E5P"
FT   BINDING         44
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:3E5P"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         207
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:3E5P"
FT   BINDING         222
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:3E5P"
FT   BINDING         224
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:3E5P"
FT   BINDING         225
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:3E5P"
FT   BINDING         314
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         356
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:3E5P"
FT   MOD_RES         40
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   371 AA;  40980 MW;  4DE356FE62478E0B CRC64;
     MVVGWHRPTR LHIDTQAITE NVQKECQRLP EGTALFAVVK ANGYGHGAVE SAKAAKKGGA
     TGFCVALLDE AIELREAGVQ DPILILSVVD LAYVPLLIQY DLSVTVATQE WLEAALQQLT
     PESNTPLRVH LKVDTGMGRI GFLTPEETKQ AVRFVQSHKE FLWEGIFTHF STADEIDTSY
     FEKQAGRFKA VLAVLEELPR YVHVSNSATA LWHPDVPGNM IRYGVAMYGL NPSGNKLAPS
     YALKPALRLT SELIHVKRLA AGEGIGYGET YVTEAEEWIG TVPIGYADGW LRHLQGFTVL
     VNGKRCEIVG RVCMDQCMIR LAEEVPVGSV VTLVGKDGNE ENTLQMVAEK LETIHYEVAC
     TFSQRIPREY N
//