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Database: UniProt
Entry: P29012
LinkDB: P29012
Original site: P29012 
ID   ALR2_ECOLI              Reviewed;         356 AA.
AC   P29012; O87498; P78246;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   13-FEB-2019, entry version 154.
DE   RecName: Full=Alanine racemase, catabolic;
DE            EC=5.1.1.1;
GN   Name=dadX; Synonyms=alnB, dadB; OrderedLocusNames=b1190, JW1179;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=K12;
RX   PubMed=7906689; DOI=10.1128/jb.176.5.1500-1510.1994;
RA   Lobocka M., Hennig J., Wild J., Klopotowski T.;
RT   "Organization and expression of the Escherichia coli K-12 dad operon
RT   encoding the smaller subunit of D-amino acid dehydrogenase and the
RT   catabolic alanine racemase.";
RL   J. Bacteriol. 176:1500-1510(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
RA   Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA   Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA   Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA   Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA   Yano M., Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
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   -!- INDUCTION: By alanine. {ECO:0000269|PubMed:7906689}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000305}.
DR   EMBL; L02948; AAC36881.1; -; Unassigned_DNA.
DR   EMBL; U00096; AAC74274.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA36045.1; -; Genomic_DNA.
DR   PIR; C64865; C53383.
DR   RefSeq; NP_415708.1; NC_000913.3.
DR   RefSeq; WP_000197881.1; NZ_LN832404.1.
DR   ProteinModelPortal; P29012; -.
DR   SMR; P29012; -.
DR   BioGrid; 4260105; 648.
DR   DIP; DIP-9395N; -.
DR   IntAct; P29012; 2.
DR   STRING; 316385.ECDH10B_1243; -.
DR   EPD; P29012; -.
DR   jPOST; P29012; -.
DR   PaxDb; P29012; -.
DR   PRIDE; P29012; -.
DR   EnsemblBacteria; AAC74274; AAC74274; b1190.
DR   EnsemblBacteria; BAA36045; BAA36045; BAA36045.
DR   GeneID; 945754; -.
DR   KEGG; ecj:JW1179; -.
DR   KEGG; eco:b1190; -.
DR   PATRIC; fig|1411691.4.peg.1097; -.
DR   EchoBASE; EB1380; -.
DR   EcoGene; EG11408; dadX.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031446; -.
DR   InParanoid; P29012; -.
DR   KO; K01775; -.
DR   PhylomeDB; P29012; -.
DR   BioCyc; EcoCyc:ALARACECAT-MONOMER; -.
DR   BioCyc; ECOL316407:JW1179-MONOMER; -.
DR   BioCyc; MetaCyc:ALARACECAT-MONOMER; -.
DR   SABIO-RK; P29012; -.
DR   PRO; PR:P29012; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
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   2: Evidence at transcript level;
KW   Complete proteome; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    356       Alanine racemase, catabolic.
FT                                /FTId=PRO_0000114517.
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}.
FT   CONFLICT    172    172       A -> R (in Ref. 1; AAC36881).
FT                                {ECO:0000305}.
FT   CONFLICT    215    215       A -> R (in Ref. 1; AAC36881).
FT                                {ECO:0000305}.
FT   CONFLICT    281    281       P -> L (in Ref. 1; AAC36881).
FT                                {ECO:0000305}.
FT   CONFLICT    349    349       L -> V (in Ref. 1; AAC36881).
FT                                {ECO:0000305}.
SQ   SEQUENCE   356 AA;  38845 MW;  FFF3226B47E5AAB3 CRC64;
     MTRPIQASLD LQALKQNLSI VRQAATHARV WSVVKANAYG HGIERIWSAI GATDGFALLN
     LEEAITLRER GWKGPILMLE GFFHAQDLEI YDQHRLTTCV HSNWQLKALQ NARLKAPLDI
     YLKVNSGMNR LGFQPDRVLT VWQQLRAMAN VGEMTLMSHF AEAEHPDGIS GAMARIEQAA
     EGLECRRSLS NSAATLWHPE AHFDWVRPGI ILYGASPSGQ WRDIANTGLR PVMTLSSEII
     GVQTLKAGER VGYGGRYTAR DEQRIGIVAA GYADGYPRHA PTGTPVLVDG VRTMTVGTVS
     MDMLAVDLTP CPQAGIGTPV ELWGKEIKID DVAAAAGTVG YELMCALALR VPVVTV
//
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