ID   B3DT83_BIFLD            Unreviewed;       450 AA.
AC   B3DT83;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 89.
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:ACD98352.1};
GN   OrderedLocusNames=BLD_0906 {ECO:0000313|EMBL:ACD98352.1};
OS   Bifidobacterium longum (strain DJO10A).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=205913 {ECO:0000313|EMBL:ACD98352.1, ECO:0000313|Proteomes:UP000002419};
RN   [1] {ECO:0000313|EMBL:ACD98352.1, ECO:0000313|Proteomes:UP000002419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJO10A {ECO:0000313|EMBL:ACD98352.1,
RC   ECO:0000313|Proteomes:UP000002419};
RX   PubMed=16391088; DOI=10.1128/AEM.72.1.527-535.2006;
RA   Lee J.H., O'Sullivan D.J.;
RT   "Sequence analysis of two cryptic plasmids from Bifidobacterium longum
RT   DJO10A and construction of a shuttle cloning vector.";
RL   Appl. Environ. Microbiol. 72:527-535(2006).
RN   [2] {ECO:0000313|EMBL:ACD98352.1, ECO:0000313|Proteomes:UP000002419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJO10A {ECO:0000313|EMBL:ACD98352.1,
RC   ECO:0000313|Proteomes:UP000002419};
RX   PubMed=18505588; DOI=10.1186/1471-2164-9-247;
RA   Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R.,
RA   Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V.,
RA   Slesarev A.I., Weimer B., O'Sullivan D.J.;
RT   "Comparative genomic analysis of the gut bacterium Bifidobacterium longum
RT   reveals loci susceptible to deletion during pure culture growth.";
RL   BMC Genomics 9:247-247(2008).
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|HAMAP-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; CP000605; ACD98352.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3DT83; -.
DR   KEGG; blj:BLD_0906; -.
DR   HOGENOM; CLU_028393_0_0_11; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002419; 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 {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_01201}.
FT   DOMAIN          280..430
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        61
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        301
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         365
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         61
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   450 AA;  48055 MW;  5C48192B290E7B17 CRC64;
     MNAAPEIAFS SEQGKANYAA ARRQYPAQAI VDLKTMRDNM AHLVSVVGGP ASGTAVMGVV
     KADAYGHGLL PAALAALAGG ATWLGTAQSH EALLLRKLGI GPDRCHILTW VYNGTEVPFD
     ELIAADIDVS VGSLPGIDAV AAAARKLGKP ARVHVKVDSG FGRNGFTPAG FDAALAKLVP
     LAKEGVLHIV GQWSHLAVAD SPDVSEFVSS TDRQIETFKD FTRRMEQAGI PPEIRHLANT
     AATLDRPEIH FELTRPGIGL YGYEPDPAMG TPRDWHLTPA MRLQAQLGTV KDVEAGHGIS
     YGRTYLTLDN TSTAIVPLGY ADGIHRSASG FDMEGAKHVE KPGGPVRIMT TEGPKIYRVC
     GRVCMDQFIV DLHGSAAELG VHEGDTVELF GPGRGEDYVE PTADDWARAA DTISYEIFTC
     LRNRIPRLYE HAAEVLPAAD LAKLDPATLL
//