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   16-JAN-2019, entry version 111.
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; Rhizobiales;
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
RT   secretion of 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.,
RA   Ghazoui Z.F., Hull K.H., Wexler M., Curson A.R.J., Todd J.D.,
RA   Poole P.S., Mauchline T.H., East A.K., Quail M.A., Churcher C.,
RA   Arrowsmith C., Cherevach I., Chillingworth T., Clarke K., Cronin A.,
RA   Davis P., Fraser A., Hance Z., Hauser H., Jagels K., Moule S.,
RA   Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA   Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and
RT   accessory components.";
RL   Genome Biol. 7:R34.1-R34.20(2006).
CC   -!- FUNCTION: Isomerizes L-alanine to D-alanine which is then oxidized
CC       to 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};
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   ProteinModelPortal; Q9RAE7; -.
DR   SMR; Q9RAE7; -.
DR   EnsemblBacteria; CAK12125; CAK12125; pRL120416.
DR   KEGG; rle:pRL120416; -.
DR   HOGENOM; HOG000031445; -.
DR   KO; K01775; -.
DR   OMA; VEILFIM; -.
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   Complete proteome; Isomerase; Plasmid; Pyridoxal phosphate.
FT   CHAIN         1    377       Alanine racemase, catabolic.
FT                                /FTId=PRO_0000114554.
FT   ACT_SITE     51     51       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000250}.
FT   ACT_SITE    272    272       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000250}.
FT   BINDING     150    150       Substrate. {ECO:0000250}.
FT   BINDING     320    320       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   MOD_RES      51     51       N6-(pyridoxal phosphate)lysine.
FT                                {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
//