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Database: UniProt
Entry: O30746
LinkDB: O30746
Original site: O30746 
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   05-DEC-2018, entry version 86.
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.
OX   NCBI_TaxID=548;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=W70;
RX   PubMed=9457858;
RA   Janes B.K., Bender R.A.;
RT   "Alanine catabolism in Klebsiella aerogenes: molecular
RT   characterization of the dadAB operon and its regulation by the
RT   nitrogen assimilation control protein.";
RL   J. Bacteriol. 180:563-570(1998).
CC   -!- FUNCTION: Isomerizes L-alanine to D-alanine which is then oxidized
CC       to 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}.
DR   EMBL; AF016253; AAC38140.1; -; Genomic_DNA.
DR   ProteinModelPortal; O30746; -.
DR   SMR; O30746; -.
DR   PRIDE; 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       Alanine racemase, catabolic.
FT                                /FTId=PRO_0000114525.
FT   ACT_SITE     35     35       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000250}.
FT   ACT_SITE    253    253       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000250}.
FT   BINDING     130    130       Substrate. {ECO:0000250}.
FT   BINDING     301    301       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   MOD_RES      35     35       N6-(pyridoxal phosphate)lysine.
FT                                {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
//
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