AC MF_02212; DC Protein; auto TR HAMAP; MF_02212; -; 1; level=0 XX Names: Bsr_racemase XX ID BSR DE RecName: Full=Broad specificity amino-acid racemase; DE EC=5.1.1.10; DE Flags: Precursor; XX CC -!- FUNCTION: Amino-acid racemase able to utilize a broad range of CC substrates. CC -!- CATALYTIC ACTIVITY: CC Reaction=an L-alpha-amino acid = a D-alpha-amino acid; CC Xref=Rhea:RHEA:18317, ChEBI:CHEBI:59869, ChEBI:CHEBI:59871; CC EC=5.1.1.10; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysine = D-lysine; Xref=Rhea:RHEA:22864, ChEBI:CHEBI:32551, CC ChEBI:CHEBI:32557; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-arginine = D-arginine; Xref=Rhea:RHEA:18069, CC ChEBI:CHEBI:32682, ChEBI:CHEBI:32689; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC -!- SUBCELLULAR LOCATION: Periplasm. CC -!- SIMILARITY: Belongs to the alanine racemase family. Bsr subfamily. XX DR Pfam; PF00842; Ala_racemase_C; 1; trigger=no DR Pfam; PF01168; Ala_racemase_N; 1; trigger=no DR PRINTS; PR00992; ALARACEMASE; 1; trigger=no DR NCBIfam; TIGR00492; alr; 1; trigger=no DR PROSITE; PS00395; ALANINE_RACEMASE; 1; trigger=no DR General; Signal; -; 1; trigger=yes XX KW Isomerase KW Periplasm KW Pyridoxal phosphate KW Signal case KW Disulfide bond end case XX GO GO:0047661; F:amino-acid racemase activity GO GO:0030170; F:pyridoxal phosphate binding GO GO:0042597; C:periplasmic space XX FT From: BSR_PSEPU (I6LNY0) FT ACT_SITE 75 FT /note="Proton acceptor" FT Condition: K FT ACT_SITE 301 FT /note="Proton acceptor" FT Condition: Y FT BINDING 174 FT /ligand="substrate" FT Condition: R FT BINDING 349 FT /ligand="substrate" FT Condition: M FT MOD_RES 75 FT /note="N6-(pyridoxal phosphate)lysine" FT Condition: K FT DISULFID 71..97 FT Tag: Disulfide; Condition: C-x*-C XX Size: 380-445; Related: None; Template: I6LNY0; A0KLG5; Q88GJ9; I0J1I6; Q9KSE5; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.5 2023/06/01 //