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Database: UniProt/TrEMBL
Entry: R4WPW1_9BURK
LinkDB: R4WPW1_9BURK
Original site: R4WPW1_9BURK 
ID   R4WPW1_9BURK            Unreviewed;       356 AA.
AC   R4WPW1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-SEP-2017, entry version 30.
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=BRPE64_ACDS11660 {ECO:0000313|EMBL:BAN22920.1};
OS   Burkholderia sp. RPE64.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=758793 {ECO:0000313|EMBL:BAN22920.1, ECO:0000313|Proteomes:UP000013966};
RN   [1] {ECO:0000313|EMBL:BAN22920.1, ECO:0000313|Proteomes:UP000013966}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Shibata T.F., Maeda T., Nikoh N., Yamaguchi K., Oshima K., Hattori M.,
RA   Nishiyama T., Hasebe M., Fukatsu T., Kikuchi Y., Shigenobu S.;
RT   "Complete Genome Sequence of Burkholderia sp. Strain RPE64, Bacterial
RT   Symbiont of the Bean Bug Riptortus pedestris.";
RL   Genome Announc. 1:e00441-13(2013).
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; AP013058; BAN22920.1; -; Genomic_DNA.
DR   RefSeq; WP_016345075.1; NC_021287.1.
DR   EnsemblBacteria; BAN22920; BAN22920; BRPE64_ACDS11660.
DR   KEGG; buo:BRPE64_ACDS11660; -.
DR   PATRIC; fig|758793.3.peg.1166; -.
DR   KO; K01775; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000013966; Chromosome 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:UP000013966};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013966}.
FT   DOMAIN      232    356       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     35     35       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    253    253       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     130    130       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     301    301       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      35     35       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   356 AA;  38059 MW;  E0B4A84D4DC03F6B CRC64;
     MPRPLSATIH TAALANNLAI ARKHAPKSKI WAVVKANAYG HGLARAFPGL RATDGFGLLD
     LEEAVKLREL GWAGPILLLE GFFRPTDIDV IDRYSLTTAV HCDEQLRMLE MARLSKPVNI
     QLKMNSGMNR LGYTPERYRA AWERARAVQG VGQITLMTHF SDADGPRGIA HQLEAFERGA
     EGISGARSLA NSAAVLWHPD SHVDWVRPGI MLYGASPSGV TADIADIGLK PAMTLHSELI
     AVQTVPAGHS IGYGSTFTAG KPMRIGVVAC GYADGYPRVA PEGTPVIVDG VRTKLVGRVS
     MDMLTVDLTP CPGAGIGSRV ELWGTHLPID DVASSAGTIG YELMCAIAQR VPVRAE
//
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