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Database: UniProt
Entry: B5Y9T8
LinkDB: B5Y9T8
Original site: B5Y9T8 
ID   ALR_COPPD               Reviewed;         348 AA.
AC   B5Y9T8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   16-JAN-2019, entry version 63.
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=COPRO5265_1229;
OS   Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / BT).
OC   Bacteria; Coprothermobacterota; Coprothermobacteria;
OC   Coprothermobacterales; Coprothermobacteraceae; Coprothermobacter.
OX   NCBI_TaxID=309798;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35245 / DSM 5265 / BT;
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Coprothermobacter proteolyticus
RT   strain ATCC 5245 / DSM 5265 / BT.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000255|HAMAP-
CC       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-
CC       alanine from L-alanine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; CP001145; ACI17536.1; -; Genomic_DNA.
DR   RefSeq; WP_012544188.1; NC_011295.1.
DR   ProteinModelPortal; B5Y9T8; -.
DR   SMR; B5Y9T8; -.
DR   STRING; 309798.COPRO5265_1229; -.
DR   EnsemblBacteria; ACI17536; ACI17536; COPRO5265_1229.
DR   KEGG; cpo:COPRO5265_1229; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; RDLELCS; -.
DR   OrthoDB; 859043at2; -.
DR   BioCyc; CPRO309798:G1GCO-1176-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001732; 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   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   Complete proteome; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    348       Alanine racemase.
FT                                /FTId=PRO_1000138590.
FT   ACT_SITE     34     34       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    243    243       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     127    127       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     291    291       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      34     34       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   348 AA;  38878 MW;  848E6471C8D0CF1F CRC64;
     MWNKWAEVSR MNLKNNVELI RQKLPDLEPI AVVKDDAYGH DAAVVVPELL KNGITKFAVV
     YAKDALMLSE FGAEWILVLD DPPLSNMCSE YEKRGIRFCI TDSKWLSDGL LELPIKFHLF
     VDVGMHREGV PWYETNTIRE ICKVVGNRLE GICSHLSNGL SDSQALATEE ERFREVLSIA
     PEGLMVHLSN SASLYNAKFP YATHFRPGIS LYGYGYPGLK PVLSLKARVI HEHILEPGEG
     LSYGWTWRAT EPTHVVTVPV GYGDGYNRKL SNKAIAGSKA GNLQQIGTVT MDFTMFEAPK
     NVTVGDEIVL MGEWEGGHFW ADEMAQLVGT IPYEVLTSIN PRVPRVLV
//
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