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Database: UniProt/TrEMBL
Entry: A0A1B3MPT2_9SPHN
LinkDB: A0A1B3MPT2_9SPHN
Original site: A0A1B3MPT2_9SPHN 
ID   A0A1B3MPT2_9SPHN        Unreviewed;       372 AA.
AC   A0A1B3MPT2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-SEP-2017, entry version 8.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   Name=alr {ECO:0000313|EMBL:AOF95091.1};
GN   ORFNames=BSY17_3760 {ECO:0000313|EMBL:AOF95091.1};
OS   Sphingobium sp. RAC03.
OG   Plasmid pbsy17_1 {ECO:0000313|Proteomes:UP000094323}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1843368 {ECO:0000313|EMBL:AOF95091.1, ECO:0000313|Proteomes:UP000094323};
RN   [1] {ECO:0000313|EMBL:AOF95091.1, ECO:0000313|Proteomes:UP000094323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RAC03 {ECO:0000313|EMBL:AOF95091.1,
RC   ECO:0000313|Proteomes:UP000094323};
RC   PLASMID=Plasmid pbsy17_1 {ECO:0000313|Proteomes:UP000094323};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-2016) 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; CP016453; AOF95091.1; -; Genomic_DNA.
DR   RefSeq; WP_069064296.1; NZ_CP016453.1.
DR   EnsemblBacteria; AOF95091; AOF95091; BSY17_3760.
DR   KEGG; sphr:BSY17_3760; -.
DR   PATRIC; fig|1843368.3.peg.3836; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000094323; Plasmid pbsy17_1.
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:UP000094323};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:AOF95091.1};
KW   Plasmid {ECO:0000313|EMBL:AOF95091.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   DOMAIN      236    362       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     37     37       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    257    257       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     136    136       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     305    305       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      37     37       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   372 AA;  39082 MW;  00CBBDEBA0ED13BF CRC64;
     MDLQLAGNLR IDLAALVANY RLIAAQVAPA SVAGVVKANA YGLGAAEVSR ALLDAGCRHF
     FVAHLCEATA LHPHLPTDAT LYVLNGVQPG AEAACAAIGA LPVLNSLEQI DGWAATARRQ
     GHALPAVIQV DSGMSRLGLA SAELATLRDQ PDRLAGIDVR LVITHLACAD HPDDSFNPHQ
     RATFDAIARQ FPGVPRSIDN SGGAMTSGVT HGDIVRAGIA LYGGAPHGKP NPMHAVVALD
     AYIIQLRTVE AGAGVGYGLT HRFDRPSRIA TVSVGYADGW PRHLSNRGFA YIGGVRAPIV
     GRVSMDSLAL DVTDVPDYLL YPAAAVELIG PHQSIDDVAT QADTISYEIL TRLGPRYART
     YLPTPAAAIQ EQ
//
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