GenomeNet

Database: UniProt
Entry: Q9RER4
LinkDB: Q9RER4
Original site: Q9RER4 
ID   ALR_AQUPY               Reviewed;         341 AA.
AC   Q9RER4;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   05-DEC-2018, entry version 77.
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;
OS   Aquifex pyrophilus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=2714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   COFACTOR, AND PATHWAY.
RA   Kim S.S., Yu Y.G.;
RT   "Molecular cloning of an extremely thermostable alanine racemase from
RT   Aquifex pyrophilus and enzymatic characterization of the expressed
RT   protein.";
RL   J. Biochem. Mol. Biol. 33:82-88(2000).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. {ECO:0000269|Ref.1}.
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, ECO:0000269|Ref.1};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201, ECO:0000269|Ref.1};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01201, ECO:0000269|Ref.1}.
CC   -!- MISCELLANEOUS: Strong thermostability.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; AF212103; AAF23014.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q9RER4; -.
DR   SMR; Q9RER4; -.
DR   UniPathway; UPA00042; UER00497.
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   1: Evidence at protein level;
KW   Isomerase; Pyridoxal phosphate.
FT   CHAIN         1    341       Alanine racemase.
FT                                /FTId=PRO_0000114496.
FT   ACT_SITE     33     33       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    236    236       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     126    126       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     284    284       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   341 AA;  39014 MW;  B90B63A00C0EE1EF CRC64;
     MRRAVLEILE ERIIHNVKEI HRFSGKRIIA VVKANAYGIG VREVSRILEG LEEVDAFAVA
     CTQEGVELRE CGIKKKILIL GGILEEDVKL LEEYDLTPVI SDPEHLKVLK DRNIKFHVKY
     DTGMGRLGFT NEIIKDPRVE GVMSHFSSPA DRNFSKLQIK RFEEILKNYE KVKYIHLESS
     AGLIYRVPFT THVRVGLAIY GEKPLKDYPL EVKPALRLRA RLISVKELPE NYPVSYGRTY
     ITKRKTKLGV VAFGYADGLM KTLSNRSFLI FEGRKVPIIG NITMDMTMVD LSGTEARTGD
     WVYIVNEERS FTPLARDAGT IPYEIMCNLS RRVERLVIKK R
//
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