GenomeNet

Database: UniProt
Entry: B3DWZ0
LinkDB: B3DWZ0
Original site: B3DWZ0 
ID   ALR_METI4               Reviewed;         387 AA.
AC   B3DWZ0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   13-FEB-2019, entry version 68.
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=Minf_0070;
OS   Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum
OS   (strain V4)).
OC   Bacteria; Verrucomicrobia; Methylacidiphilae; Methylacidiphilales;
OC   Methylacidiphilaceae; Methylacidiphilum.
OX   NCBI_TaxID=481448;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate V4;
RX   PubMed=18593465; DOI=10.1186/1745-6150-3-26;
RA   Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y.,
RA   Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N.,
RA   Koonin E.V., Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V.,
RA   Dunfield P.F., Feng L., Wang L., Alam M.;
RT   "Complete genome sequence of the extremely acidophilic methanotroph
RT   isolate V4, Methylacidiphilum infernorum, a representative of the
RT   bacterial phylum Verrucomicrobia.";
RL   Biol. Direct 3:26-26(2008).
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; CP000975; ACD82130.1; -; Genomic_DNA.
DR   RefSeq; WP_012462412.1; NC_010794.1.
DR   ProteinModelPortal; B3DWZ0; -.
DR   SMR; B3DWZ0; -.
DR   STRING; 481448.Minf_0070; -.
DR   PRIDE; B3DWZ0; -.
DR   EnsemblBacteria; ACD82130; ACD82130; Minf_0070.
DR   KEGG; min:Minf_0070; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; 859043at2; -.
DR   BioCyc; MINF481448:G1GBH-63-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000009149; 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.
FT   CHAIN         1    387       Alanine racemase.
FT                                /FTId=PRO_1000213837.
FT   ACT_SITE     48     48       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    267    267       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     146    146       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     315    315       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      48     48       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   387 AA;  43310 MW;  E1524C51658C076C CRC64;
     MTQETYPSCS FPAHPRSWVE IDGRALRFNI RVARERIPKK TKIIAVVKSE AYGHGLIPIA
     KELVHSGVEV LGINNIDEAI ELRQAGIRSA LLILCPILPS EASIIVSYNV GVVISSYNEA
     KWLSQAAERQ GKKAIVHIKI DTGMGRLGFI PSQFIQEMEK IKRLSSLSIA AICTHFSQAE
     TDIEATEKQW LELLKFRHYF KGLPIHVANS AALWRKSVYA CDYVRIGLAL YGIAPMPFLR
     RFLKPILTWK CKIVLIKELP RGHPISYGAT YKLKKPSRIA VLSVGYGDGY CRSLSNKASV
     LIKGKRCPVR GAITMNLLMV DITDLPSCKV GDEAVLLGTQ GKESITADEL AKLSQTISYE
     IITNIHSHIR RNYRHFLSHS NELSLYE
//
DBGET integrated database retrieval system