ID   ALR_DEIRA               Reviewed;         351 AA.
AC   Q9RVE3;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 2.
DT   27-MAR-2024, entry version 145.
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=DR_1086;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS   27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 /
RC   NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF10657.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000513; AAF10657.1; ALT_INIT; Genomic_DNA.
DR   PIR; H75440; H75440.
DR   RefSeq; NP_294810.1; NC_001263.1.
DR   RefSeq; WP_027479629.1; NZ_JMLF01000002.1.
DR   AlphaFoldDB; Q9RVE3; -.
DR   SMR; Q9RVE3; -.
DR   STRING; 243230.DR_1086; -.
DR   PaxDb; 243230-DR_1086; -.
DR   EnsemblBacteria; AAF10657; AAF10657; DR_1086.
DR   GeneID; 69517332; -.
DR   KEGG; dra:DR_1086; -.
DR   PATRIC; fig|243230.17.peg.1281; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_0_0_0; -.
DR   InParanoid; Q9RVE3; -.
DR   OrthoDB; 9813814at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008784; F:alanine racemase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IBA:GO_Central.
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..351
FT                   /note="Alanine racemase"
FT                   /id="PRO_0000114513"
FT   ACT_SITE        34
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   ACT_SITE        248
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   MOD_RES         34
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
SQ   SEQUENCE   351 AA;  37193 MW;  F924ABD66E2FFA05 CRC64;
     MLPRAVAHIS AAALDHNLSA LAQRSGTRLL LPVKADAYGH GMELVGRLAA AHPDVWGLAV
     ATPQEAETLA RLDLGKPLLL LTPPAPEELG ALADLGVRLP VSTLAEVEAL PAHAQAHLKV
     DTGMNRLGAR PADAVAVGRA LAERGQLEGV YTHFATADEP DLSFALTQLV RFRSVLDALP
     PVLAHCANGG GVLSFGRIEG MSLARPGLAA YGYVPEHLRH VCALRPVMTV RARVNQLHTA
     YPGETVSYGA LWRAERETGV AVVGMGYADG YPRNATGRAA VLIGGERRPV LGRICMDQMM
     VDVTGLDVGV GDWAELWGEG DLSVTDVARW GDTIEYEVLT GLGSRVERRV G
//