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Database: UniProt/TrEMBL
Entry: A0A0D4DRY2_9ACTN
LinkDB: A0A0D4DRY2_9ACTN
Original site: A0A0D4DRY2_9ACTN 
ID   A0A0D4DRY2_9ACTN        Unreviewed;       406 AA.
AC   A0A0D4DRY2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-SEP-2017, entry version 17.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   ORFNames=T261_4708 {ECO:0000313|EMBL:AJT66347.1};
OS   Streptomyces lydicus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=47763 {ECO:0000313|EMBL:AJT66347.1, ECO:0000313|Proteomes:UP000032413};
RN   [1] {ECO:0000313|Proteomes:UP000032413}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A02 {ECO:0000313|Proteomes:UP000032413};
RA   Wu H., Yan J., Liu W., Liu T., Dong D., Li J., Liu H., Lu C.,
RA   Zhang D., Zhang T., Tian Z.;
RT   "Complete genome sequence of the natamycin-producing actinomycete
RT   Streptomyces lydicus A02.";
RL   Submitted (MAY-2014) 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; CP007699; AJT66347.1; -; Genomic_DNA.
DR   EnsemblBacteria; AJT66347; AJT66347; T261_4708.
DR   KEGG; sld:T261_4708; -.
DR   PATRIC; fig|1403539.3.peg.4850; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000032413; 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:UP000032413};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   DOMAIN      249    376       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     38     38       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    270    270       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     318    318       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      38     38       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   406 AA;  41974 MW;  39E3497384AEFF0F CRC64;
     MNETAKRARA TIDVAAVRSN VRALRDRAPR AELMAVVKAD GYGHGAVPCA RAARQAGASW
     LGTALPEEAF ALRAAGDTGR LLCWLWTPGG PWGKAVEQDI DVSVSGLWAL REVTEAARAC
     GRPARVQLKA DTGLGRNGCQ PADWPELTAA AAKAEADGAV KVTGLWSHFA CADEPGHPSI
     PLQTAAFEEA LEVAGAAGLR PEVRHIANTA ALLTLPDAHY DLVRGGIGIY GVSPSPELGT
     PHDFGLRPAM TLEASLASVK RAPGGHGVSY GHHYTTAGDT TLALIPLGYA DGIPRNASGR
     GPVLVAGRRR TVAGRIAMDQ FVVDLDGDRA GAGDPAVLFG PGDRGEPLAE DWAEAAGTIG
     YEIVTRIGTR VPRVYVDTDA GKGGVVTTGA EDTGGEADPT RTGGGR
//
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