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Database: UniProt/TrEMBL
Entry: A0A1P8K5M1_9BURK
LinkDB: A0A1P8K5M1_9BURK
Original site: A0A1P8K5M1_9BURK 
ID   A0A1P8K5M1_9BURK        Unreviewed;       363 AA.
AC   A0A1P8K5M1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-SEP-2017, entry version 5.
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=RS694_01220 {ECO:0000313|EMBL:APW41298.1};
OS   Rhodoferax saidenbachensis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=1484693 {ECO:0000313|EMBL:APW41298.1, ECO:0000313|Proteomes:UP000186110};
RN   [1] {ECO:0000313|EMBL:APW41298.1, ECO:0000313|Proteomes:UP000186110}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22694 {ECO:0000313|EMBL:APW41298.1,
RC   ECO:0000313|Proteomes:UP000186110};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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; CP019239; APW41298.1; -; Genomic_DNA.
DR   RefSeq; WP_029707880.1; NZ_CP019239.1.
DR   KEGG; rsb:RS694_01220; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000186110; 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:UP000186110};
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:UP000186110}.
FT   DOMAIN      234    363       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    255    255       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     303    303       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   363 AA;  38932 MW;  A825AB6F77C4DEE2 CRC64;
     MPRPIQATIH IQSLRHNLAQ ARLRAPDAKV WAVVKANAYG HGIEHVFDGL RGADGFALLD
     FAEAKRVRDL GWRGPILMLE GAFELRDLEL CSRLDLWHTV HSEAQIDMLA AHKTNVPQRV
     FLKMNSGMNR LGFAPSQMRA AWTRLNALPQ VDEISLMTHF SDADGPRGVA TQMALFAQAT
     DDLPGERSLA NSAATLRHPD SVAASDWVRP GIAIYGSAPD YPEHDAAHWG LQPTMTLAAK
     IIAVQALSTG ATVGYGSNFV ADAPMRIGVV ACGYADGYPR ICPSGTPVLV NGVRTRTVGR
     VSMDMLTVDL GPVPDADVGS EVTLWGRATN GAWLTIDEVA ALAGTVGYEL MCALAARVPV
     VVA
//
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