ID   ALR_RICPR               Reviewed;         404 AA.
AC   Q9ZE52;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 127.
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=RP095;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
RN   [2]
RP   DOMAIN RPE1.
RX   PubMed=11030655; DOI=10.1126/science.290.5490.347;
RA   Ogata H., Audic S., Barbe V., Artiguenave F., Fournier P.-E., Raoult D.,
RA   Claverie J.-M.;
RT   "Selfish DNA in protein-coding genes of Rickettsia.";
RL   Science 290:347-350(2000).
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; AJ235270; CAA14565.1; -; Genomic_DNA.
DR   PIR; F71718; F71718.
DR   RefSeq; NP_220488.1; NC_000963.1.
DR   RefSeq; WP_004599740.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZE52; -.
DR   SMR; Q9ZE52; -.
DR   STRING; 272947.RP095; -.
DR   EnsemblBacteria; CAA14565; CAA14565; CAA14565.
DR   KEGG; rpr:RP095; -.
DR   PATRIC; fig|272947.5.peg.95; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_1_1_5; -.
DR   OMA; ELMAVQH; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002480; 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   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 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   InterPro; IPR005728; Rickett_RPE.
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; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR01045; RPE1; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..404
FT                   /note="Alanine racemase"
FT                   /id="PRO_0000114557"
FT   DOMAIN          226..273
FT                   /note="RPE1 insert"
FT   ACT_SITE        34
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   ACT_SITE        298
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         346
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   404 AA;  44730 MW;  FEA23D86698256DA CRC64;
     MSLCTLEINL SAIKNNYRLL QDICKTALVG AVVKANGYGL GAMQIAKALI KENCQYFFVA
     TSEEGINLRK VLNNDITILV LNGVFTHDAL ELIQYNLTPV LNNLSQIEIW QKFSNLKGKI
     LPCYLHFNTG LNRFGLNSDE IEQLINDRDL LKGLDLQYII SHLAASEETG NPYNLIQLNR
     FKVYLEYFPN VKASFANSGG IFLGQDYHFD LARPGAALYG LNSLIEVSSN LSYTEEFESN
     TAALTTTACI NKCPDVSVRL TPKLPLKGSY TVRLQNPVTL KAPIIDLQNL TLDSHIGYNM
     TFTTKRDSVI ATLPLGYADG FSRNFSSQGE VFINSCSVPI VGRVSMDLIN IDVTDLPPSE
     VFLGQEAEII GNYCTPDKIA SIIGTIGYEV LTSLGSRYKR KYIS