ID   Q0SP05_BORAP            Unreviewed;       366 AA.
AC   Q0SP05;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   02-SEP-2026, entry version 146.
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:AEL69390.1};
GN   OrderedLocusNames=BafPKo_0157 {ECO:0000313|EMBL:AEL69390.1};
OS   Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC   Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia; Spirochaetales;
OC   Borreliaceae; Borreliella.
OX   NCBI_TaxID=390236 {ECO:0000313|EMBL:AEL69390.1, ECO:0000313|Proteomes:UP000005216};
RN   [1] {ECO:0000313|EMBL:AEL69390.1, ECO:0000313|Proteomes:UP000005216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo {ECO:0000313|EMBL:AEL69390.1,
RC   ECO:0000313|Proteomes:UP000005216};
RX   PubMed=22123755; DOI=10.1128/JB.05951-11;
RA   Casjens S.R., Mongodin E.F., Qiu W.-G., Dunn J.J., Luft B.J.,
RA   Fraser-Liggett C.M., Schutzer S.E.;
RT   "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT   Lyme disease agent isolates.";
RL   J. Bacteriol. 193:6995-6996(2011).
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|ARBA:ARBA00000316, ECO:0000256|HAMAP-
CC         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}.
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DR   EMBL; CP002933; AEL69390.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0SP05; -.
DR   STRING; 29518.BLA32_03505; -.
DR   KEGG; baf:BAPKO_0161; -.
DR   KEGG; bafz:BafPKo_0157; -.
DR   PATRIC; fig|390236.22.peg.155; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_2_2_12; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000005216; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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-UniRule.
DR   CDD; cd00430; PLPDE_III_AR; 1.
DR   FunFam; 3.20.20.10:FF:000002; Alanine racemase; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   Gene3D; 2.40.37.10; Lyase, Ornithine Decarboxylase, Chain A, domain 1; 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 {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:UP000005216}.
FT   DOMAIN          241..365
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        35
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        262
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         310
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         35
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   366 AA;  42300 MW;  DCD3E95D73B80FC3 CRC64;
     MSSNKTIIIN LNNLEHNLNL IKNKIGEKEI VATLKGDAYG HGLINIFKFF KAKKINYFGL
     SNIEDAKTLK KIDKSTKILM YIKVDKKEIK NLIKLELLPF VADFEYLFLI EKECALQKKK
     IKVHLKIDVG MNRYGIKIDS ALEIATYIQN SKFLELEGVC SHLPTTENFK ITQKQIEQFL
     FFLETLKQKN INPKFVHISN SGHIINYKLN PQFNMVRPGL ILYGYCPTLK NKKTTLNFKP
     VLNLFSKVVF IKNVKKGEKI SYSGTFQAKE DMKIGIIPIG YFDGIPQNIN NNFYFLINNK
     KCKIRGKVCM NLTIVEIPKD LKVETGSKVE IVSEKLSINE MSKFSKRSHY ELLCNIGKYE
     NRKYLD
//