ID ALR_STRP3 Reviewed; 366 AA.
AC P0CZ56; Q8K5Z8;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=SpyM3_1563;
OS Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=198466;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-595 / MGAS315;
RX PubMed=12122206; DOI=10.1073/pnas.152298499;
RA Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT encoded toxins, the high-virulence phenotype, and clone emergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002).
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; AE014074; AAM80170.1; -; Genomic_DNA.
DR RefSeq; WP_002995397.1; NC_004070.1.
DR AlphaFoldDB; P0CZ56; -.
DR SMR; P0CZ56; -.
DR KEGG; spg:SpyM3_1563; -.
DR HOGENOM; CLU_028393_2_1_9; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000000564; 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.
FT CHAIN 1..366
FT /note="Alanine racemase"
FT /id="PRO_0000114584"
FT ACT_SITE 40
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT ACT_SITE 263
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT MOD_RES 40
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
SQ SEQUENCE 366 AA; 39891 MW; A68E7AF7E0AF9B95 CRC64;
MISSFHRPTV ARVNLQAIKE NVASVQKHIP LGVKTYAVVK ADAYGHGAVQ VSKALLPQVD
GYCVSNLDEA LQLRQAGIDK EILILGVLLP NELELAVANA ITVTIASLDW IALARLEKKE
CQGLKVHVKV DSGMGRIGLR SSKEVNLLID SLKELGADVE GIFTHFATAD EADDTKFNQQ
LQFFKKLIAG LEDKPRLVHA SNSATSIWHS DTIFNAVRLG IVSYGLNPSG SDLSLPFPLQ
EALSLESSLV HVKMISAGDT VGYGATYTAK KSEYVGTVPI GYADGWTRNM QGFSVLVDGQ
FCEIIGRVSM DQLTIRLSKA YPLGTKVTLI GSNQQKNIST TDIANYRNTI NYEVLCLLSD
RIPRIY
//
