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Database: UniProt/TrEMBL
Entry: B1M861_METRJ
LinkDB: B1M861_METRJ
Original site: B1M861_METRJ 
ID   B1M861_METRJ            Unreviewed;       377 AA.
AC   B1M861;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-SEP-2017, entry version 75.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   OrderedLocusNames=Mrad2831_4822 {ECO:0000313|EMBL:ACB26782.1};
OS   Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM
OS   2831).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=426355 {ECO:0000313|EMBL:ACB26782.1, ECO:0000313|Proteomes:UP000006589};
RN   [1] {ECO:0000313|EMBL:ACB26782.1, ECO:0000313|Proteomes:UP000006589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27329 / DSM 1819 / JCM 2831
RC   {ECO:0000313|Proteomes:UP000006589};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT   2831.";
RL   Submitted (MAR-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:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000256|HAMAP-
CC       Rule:MF_01201, ECO:0000256|SAAS:SAAS00630646}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201,
CC         ECO:0000256|PIRSR:PIRSR600821-50,
CC         ECO:0000256|SAAS:SAAS00758845};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|SAAS:SAAS00630654}.
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DR   EMBL; CP001001; ACB26782.1; -; Genomic_DNA.
DR   ProteinModelPortal; B1M861; -.
DR   STRING; 426355.Mrad2831_4822; -.
DR   EnsemblBacteria; ACB26782; ACB26782; Mrad2831_4822.
DR   KEGG; mrd:Mrad2831_4822; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031445; -.
DR   KO; K01775; -.
DR   OMA; ISHFACA; -.
DR   OrthoDB; POG091H022F; -.
DR   BioCyc; MRAD426355:GJB5-4815-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000006589; 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 {ECO:0000313|Proteomes:UP000006589};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:ACB26782.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006589}.
FT   DOMAIN      250    375       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     50     50       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    271    271       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     149    149       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     318    318       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      50     50       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   377 AA;  38655 MW;  7381EE7308F362FD CRC64;
     MSMIDRDLRP DAGPAGTASA LLTIDLAALA ENYRLLAARA GTATCAAVVK ADAYGLGADR
     VAPVLAAAGC RHFFVAQVGE GVALRSILGP GAVIAVLNGA APGSEATCAD HDLVPVLNDL
     SQLDGWQGLA RRRARRLPAI LQVDTGMARF GFAPDEVGAL LDRPDALAGL DLRLVMSHLA
     CAGEPDSPVN AAQLSVFRAV RRRLPAVPAS LAASSGIFLG PDFHFDLVRP GAALYGIAPQ
     EGAPNPMRPV IGLRARVMQT RSVPAGTPVG YGHAATVARD SRLATVAIGY ADGFFRSTAG
     GAAWFGGVRL PVVGRVSMDS LVLDVTDAAP GTLGPGALVD IVGPERDVDA AAAAAGTIGY
     EVLTNLGHRF HRVYLGA
//
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