ID   ALR_MYCSM               Reviewed;         389 AA.
AC   P94967;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 106.
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; Synonyms=alrA;
OS   Mycolicibacterium smegmatis (Mycobacterium smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=9260945; DOI=10.1128/jb.179.16.5046-5055.1997;
RA   Caceres N.E., Harris N.B., Wellehan J.F., Feng Z., Kapur V., Barletta R.G.;
RT   "Overexpression of the D-alanine racemase gene confers resistance to D-
RT   cycloserine in Mycobacterium smegmatis.";
RL   J. Bacteriol. 179:5046-5055(1997).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine.
CC       Overexpression due to a natural mutation in the promoter is responsible
CC       for mediating resistance to D-cycloserine (DCS) in mycobacteria.
CC       {ECO:0000269|PubMed:9260945}.
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; U70872; AAC45589.1; -; Genomic_DNA.
DR   RefSeq; WP_011727747.1; NZ_UGQO01000001.1.
DR   AlphaFoldDB; P94967; -.
DR   SMR; P94967; -.
DR   GeneID; 66733029; -.
DR   OMA; HMTHFSD; -.
DR   UniPathway; UPA00042; UER00497.
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   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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   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; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Isomerase; Pyridoxal phosphate.
FT   CHAIN           1..389
FT                   /note="Alanine racemase"
FT                   /id="PRO_0000114538"
FT   ACT_SITE        46
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   ACT_SITE        275
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         323
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   MOD_RES         46
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
SQ   SEQUENCE   389 AA;  41056 MW;  A53F326029904830 CRC64;
     MQTTEPMTPP APLASAQTVI DLGAIDHNVR VLRELAGSAD VMAVVKADAY GHGALPVART
     ALAAGAAALG VATIPEALAL REGGITAPVL AWLHPPGTDF APAIAADVEV AVSSRRQLEQ
     VTAAAAEVGR TATVTVKVDT GLSRNGVGAA DYPEVLDVLR RAQADGAIRV RGLMSHLVHG
     DDPENPFNGL QGQRLADMRV YAREHGVDYE VAHLCNSPAA MTRPDLAFEM VRPGISLYGL
     SPIPERGDMG LRPAMTLKCP VALVRSVHAG DGVSYGHRWV ADRDTTLGLL PIGYADGVYR
     ALSGRIDVLI KGRRRRAVGR ICMDQFVVDL GPDADDVAVG DDAILFGPGA NGEPTAQDWA
     ELLDTIHYEV VTSPRGRVTR TYLPAGQQD