ID   ALR2_RHIL3              Reviewed;         377 AA.
AC   Q9RAE7; Q1M447;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 3.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Alanine racemase, catabolic;
DE            EC=5.1.1.1;
GN   Name=dadX; OrderedLocusNames=pRL120416;
OS   Rhizobium leguminosarum bv. viciae (strain 3841).
OG   Plasmid pRL12.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=216596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10792736; DOI=10.1046/j.1365-2958.2000.01884.x;
RA   Allaway D.A., Lodwig E.M., Crompton L.A., Wood M., Parsons R.,
RA   Wheeler T.R., Poole P.S.;
RT   "Identification of alanine dehydrogenase and its role in mixed secretion of
RT   ammonium and alanine by pea bacteroids.";
RL   Mol. Microbiol. 36:508-515(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3841; PLASMID=pRL12;
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA   Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA   East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA   Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT   components.";
RL   Genome Biol. 7:R34.1-R34.20(2006).
CC   -!- FUNCTION: Isomerizes L-alanine to D-alanine which is then oxidized to
CC       pyruvate by DadA.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB53547.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ249196; CAB53547.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AM236086; CAK12125.1; -; Genomic_DNA.
DR   RefSeq; WP_011649181.1; NC_008378.1.
DR   AlphaFoldDB; Q9RAE7; -.
DR   SMR; Q9RAE7; -.
DR   STRING; 216596.pRL120416; -.
DR   EnsemblBacteria; CAK12125; CAK12125; pRL120416.
DR   KEGG; rle:pRL120416; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_1_1_5; -.
DR   OMA; HMTHFSD; -.
DR   OrthoDB; 859043at2; -.
DR   Proteomes; UP000006575; Plasmid pRL12.
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; Plasmid; Pyridoxal phosphate.
FT   CHAIN           1..377
FT                   /note="Alanine racemase, catabolic"
FT                   /id="PRO_0000114554"
FT   ACT_SITE        51
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        272
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         320
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         51
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   377 AA;  40548 MW;  BB38DAC35BD3DBF2 CRC64;
     MDSDILVSRT RTATIAQGAT GYLMIDLAAL GRNYRKLVSM LAPVRAGAVV KADAYGLGAE
     RVARTLYSEG CRHFFVAQFV EAVRLRPALA HDAQIFVLNG LQPGNEIACA EMGIVPVLNS
     LAQWRQWSAA ARILKRCLPA VLQFDTGMSR LGFPREERRE LAAALRDGSN VEILFIMSHL
     ASADDMGSEQ NGEQFAEMSR IADEFPGFDI SFANSGGVFL GEAYYGVLAR PGIALYGGAP
     NAGEKNPMEP VVSLNVAVVQ TRTVPAGAKV GYGGAHVTQR ETRLATIAAG YADGLPRCLS
     DRGAVYFKGV RLPIVGRVSM DSTTVDITAL PEGALTFGSL VEVLGRHQTL EDIARDAGTI
     SYEILTGLGD RYDRQYR