ID   ALR_DESRM               Reviewed;         370 AA.
AC   A4J8G6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr; OrderedLocusNames=Dred_2865;
OS   Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS   (Desulfotomaculum reducens).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=349161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT   "Complete sequence of Desulfotomaculum reducens MI-1.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC       also act on other amino acids. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC       from L-alanine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
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DR   EMBL; CP000612; ABO51369.1; -; Genomic_DNA.
DR   RefSeq; WP_011879162.1; NC_009253.1.
DR   AlphaFoldDB; A4J8G6; -.
DR   SMR; A4J8G6; -.
DR   STRING; 349161.Dred_2865; -.
DR   KEGG; drm:Dred_2865; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_2_2_9; -.
DR   OrthoDB; 9813814at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001556; 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   3: Inferred from homology;
KW   Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..370
FT                   /note="Alanine racemase"
FT                   /id="PRO_1000138595"
FT   ACT_SITE        36
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   ACT_SITE        265
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         313
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   MOD_RES         36
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
SQ   SEQUENCE   370 AA;  40808 MW;  3D3D552D57529C0E CRC64;
     MKEPIWAEIN LEAIRHNIKE IRKMVGPNRE IMAVVKANGY GHGAVPVARV ALEAGATRLA
     VARLSEAQEL RRAGLKVPIL LLGYISPDQI GDALEYNVTL TVFRFDLAKK IAAIAQGRGQ
     RATVHLKVDT GMGRIGFTPD EEGLAEITAV CALNGLDVEG IYTHFATADE QDKSYTRWQF
     KRFMLVLNRL EEQGITFSLR HCANSAAIME FPETYLDLVR PGIILYGLYP SEEVDKGKLL
     LQPAMTLKAR ITHVKKVNSG TKISYGCTYT VPQETDIASL PLGYADGYPR LLSSKGQVLV
     KGKRARVVGR VCMDQCMVDV GHIAEVKVHD EVIIFGGAEL PVEEVATWLG TINYEVVCWV
     GSRVPRVYIG
//