GenomeNet

Database: UniProt
Entry: B8DRL1
LinkDB: B8DRL1
Original site: B8DRL1 
ID   ALR_DESVM               Reviewed;         372 AA.
AC   B8DRL1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   16-JAN-2019, entry version 62.
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=DvMF_1349;
OS   Desulfovibrio vulgaris (strain Miyazaki F / DSM 19637).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=883;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Miyazaki F / DSM 19637;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Hazen T.C., Richardson P.;
RT   "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL   Submitted (OCT-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; CP001197; ACL08298.1; -; Genomic_DNA.
DR   RefSeq; WP_012612482.1; NC_011769.1.
DR   ProteinModelPortal; B8DRL1; -.
DR   SMR; B8DRL1; -.
DR   STRING; 883.DvMF_1349; -.
DR   EnsemblBacteria; ACL08298; ACL08298; DvMF_1349.
DR   KEGG; dvm:DvMF_1349; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; SGAAMYH; -.
DR   OrthoDB; 859043at2; -.
DR   BioCyc; DVUL883:G1GTY-1381-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001361; 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    372       Alanine racemase.
FT                                /FTId=PRO_1000164593.
FT   ACT_SITE     36     36       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    266    266       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     134    134       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     314    314       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      36     36       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   372 AA;  39146 MW;  F3F87E89E14A81FD CRC64;
     MSIAYNKIAV RVRLGALRRN FETLRRMSPA AMPVIKSDAY GHGLLPVART LEAAGADAFA
     AGTVGECAQL RDGGIPGRIV ALLGATDAAD AECCVARSIV PAVYSADQLE MLAGRAAPGQ
     QVDIALKFDT GMARLGFSEA DLPALLDRLH ARPMLRPVLV MSHLAVSDDP SRSDFTRQQG
     EAFGRILAGV RADWPAAQGS LANSAALLAH PELHFDVQRP GIALYGANPL RGTAQEHLGD
     GLQPAMDVAA PILQVHPLPA GRSISYGRTF TAPRDMTVAI VATGYADAYS RGLSGKGAMT
     VHGRRVPILG RVCMQMTAVD VTDVPGVAAG DDAYLLGGPG EALTPDELAD LWGTISYEVL
     CLLGMNPRTH RE
//
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