ID   ALR2_KLEAE              Reviewed;         356 AA.
AC   O30746;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Alanine racemase, catabolic;
DE            EC=5.1.1.1;
GN   Name=dadB;
OS   Klebsiella aerogenes (Enterobacter aerogenes).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=548;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=W70;
RX   PubMed=9457858; DOI=10.1128/jb.180.3.563-570.1998;
RA   Janes B.K., Bender R.A.;
RT   "Alanine catabolism in Klebsiella aerogenes: molecular characterization of
RT   the dadAB operon and its regulation by the nitrogen assimilation control
RT   protein.";
RL   J. Bacteriol. 180:563-570(1998).
CC   -!- FUNCTION: Isomerizes L-alanine to D-alanine which is then oxidized to
CC       pyruvate by DadA. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000305}.
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DR   EMBL; AF016253; AAC38140.1; -; Genomic_DNA.
DR   AlphaFoldDB; O30746; -.
DR   SMR; O30746; -.
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:0006522; P:alanine metabolic process; IEA:UniProtKB-UniRule.
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   Isomerase; Pyridoxal phosphate.
FT   CHAIN           1..356
FT                   /note="Alanine racemase, catabolic"
FT                   /id="PRO_0000114525"
FT   ACT_SITE        35
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        253
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         301
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         35
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   356 AA;  38788 MW;  45A7CD7E56855856 CRC64;
     MTRPVVASID LLALRQNLQI VRRAAPGSRL WAVDKDNAYG HGVARVWSAL SAADGFALLN
     LEEAILLREQ GWKGPILLLE GFFHADELAV LDQYRLPTSV HSNWQIKALQ QAKLRAPLDI
     YLKVNSGMNR LGFMPERVHT VWQQLRAISN VGEMTLMSHF AEAENPQGIV EPMRRIEQAA
     EGLDCPRSLA NSAATLWHPE AHFDWVRPGI VLYGASPSGQ WQDIANTGLK PVMTLRSEII
     GVQNLRPGEA IGYGGLYRTT QEQRIGIVAC GYADGYPRVA PSGTPVLVDG VRTTTVGRVS
     MDMLAVDLTP CPQAGIGAPV ELWGKEIKID DVAASSGTVG YELMCALAPR VPVVTL