ID   K0AEU4_EXIAB            Unreviewed;       357 AA.
AC   K0AEU4;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 61.
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=alr2 {ECO:0000313|EMBL:AFS71704.1};
GN   OrderedLocusNames=Eab7_2619 {ECO:0000313|EMBL:AFS71704.1};
OS   Exiguobacterium antarcticum (strain B7).
OC   Bacteria; Bacillota; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=1087448 {ECO:0000313|EMBL:AFS71704.1, ECO:0000313|Proteomes:UP000006274};
RN   [1] {ECO:0000313|EMBL:AFS71704.1, ECO:0000313|Proteomes:UP000006274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B7 {ECO:0000313|Proteomes:UP000006274};
RX   PubMed=23144424; DOI=10.1128/JB.01791-12;
RA   Carneiro A.R., Ramos R.T., Dall'Agnol H., Pinto A.C., de Castro Soares S.,
RA   Santos A.R., Guimaraes L.C., Almeida S.S., Barauna R.A., das Gracas D.A.,
RA   Franco L.C., Ali A., Hassan S.S., Nunes C.I., Barbosa M.S., Fiaux K.K.,
RA   Aburjaile F.F., Barbosa E.G., Bakhtiar S.M., Vilela D., Nobrega F.,
RA   Dos Santos A.L., Carepo M.S., Azevedo V., Schneider M.P., Pellizari V.H.,
RA   Silva A.;
RT   "Genome sequence of Exiguobacterium antarcticum B7, isolated from a biofilm
RT   in Ginger Lake, King George Island, Antarctica.";
RL   J. Bacteriol. 194:6689-6690(2012).
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; CP003063; AFS71704.1; -; Genomic_DNA.
DR   RefSeq; WP_014971521.1; NC_018665.1.
DR   AlphaFoldDB; K0AEU4; -.
DR   STRING; 1087448.Eab7_2619; -.
DR   KEGG; ean:Eab7_2619; -.
DR   PATRIC; fig|1087448.3.peg.2689; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_2_1_9; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000006274; 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          238..357
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        259
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         306
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   357 AA;  39657 MW;  D19F9829E9489A4F CRC64;
     MYRPTWIEID REAIAHNVRE IKARMGHQSM MAVVKADGYG HGAITVAEIA LANGAEMLAV
     ALLEEAIELR EAGIQAPILM LEALLPEHAP IASNYDVAVP VFSAEWLREA KQHLTEIDHL
     RLHIKVDSGM GRLGLQTLDE LDAVLKELDP DLMELDGIYT HFATADELTS RLFEKQQTVF
     LRFVERVPGI RYIHASNSAA AIRLAGQEPC NVVRIGIALY GALPSDEMSS YYDFLQPAFS
     LKSRLMQVKH VEPGQTISYG ATYTAPTDEW IGTVPIGYAD GWSRKFQGYA LIVDGTPCEI
     VGRVCMDRLM IRLPRAYPVG TEVTLIGRGA PIDEAAHWLG TINYEVLCQF SKRVPRI
//