GenomeNet

Database: UniProt
Entry: Q163V1
LinkDB: Q163V1
Original site: Q163V1 
ID   ALR_ROSDO               Reviewed;         344 AA.
AC   Q163V1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   16-JAN-2019, entry version 86.
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=RD1_3240;
OS   Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter
OS   sp. (strain OCh 114)) (Roseobacter denitrificans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Roseobacter.
OX   NCBI_TaxID=375451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33942 / OCh 114;
RX   PubMed=17098896; DOI=10.1128/JB.01390-06;
RA   Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J.,
RA   Ramos H., Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C.,
RA   Shah M.K., O'Huallachain M.E., Lince M.T., Blankenship R.E.,
RA   Beatty J.T., Touchman J.W.;
RT   "The complete genome sequence of Roseobacter denitrificans reveals a
RT   mixotrophic rather than photosynthetic metabolism.";
RL   J. Bacteriol. 189:683-690(2007).
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; CP000362; ABG32742.1; -; Genomic_DNA.
DR   RefSeq; WP_011569358.1; NZ_FOOO01000004.1.
DR   ProteinModelPortal; Q163V1; -.
DR   SMR; Q163V1; -.
DR   STRING; 375451.RD1_3240; -.
DR   EnsemblBacteria; ABG32742; ABG32742; RD1_3240.
DR   KEGG; rde:RD1_3240; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031445; -.
DR   KO; K01775; -.
DR   OMA; VEILFIM; -.
DR   OrthoDB; 859043at2; -.
DR   BioCyc; RDEN375451:G1G6J-2990-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000007029; 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    344       Alanine racemase.
FT                                /FTId=PRO_1000138620.
FT   ACT_SITE     33     33       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    242    242       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     128    128       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     290    290       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      33     33       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   344 AA;  36340 MW;  95C727E56ADD6D14 CRC64;
     MSTAVLTIDL SALAANWRSL NALSDVETAA VVKANAYGLG VGTAASALAE AGARHFFVAV
     AEEGVALRQA LGAGPQISVF SGHMAGDTAL IRDAGLTPMI NSIDQMIRHV EALPEHDFGI
     QLDTGMNRLG MEDGEWRAVR EVATQRPPSL VMSHLACADE PSHQMNRQQL DCFVEMTQDI
     TAPRSLAATG GILMGPDYHF DLTRPGIGLY GGLPFVDALP VVQLDVPVIQ VRDVHPGETV
     GYANTWTATA PARIATISAG YADGLIRAMG AKARLHAGDT ALPVVGRVSM DLIGVDVTAL
     GSDPDSLQLI GRHQSVDTVA GFADTIGYEI LTSLGDRYKR VYTQ
//
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