ALR2_ECOLI
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 03-AUG-2022, entry version 168.
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., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT 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., Mau B.,
RA 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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
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 -!- INDUCTION: By alanine. {ECO:0000269|PubMed:7906689}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000305}.
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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_SSZK01000010.1.
DR AlphaFoldDB; P29012; -.
DR SMR; P29012; -.
DR BioGRID; 4260105; 648.
DR DIP; DIP-9395N; -.
DR IntAct; P29012; 2.
DR STRING; 511145.b1190; -.
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 eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_1_0_6; -.
DR InParanoid; P29012; -.
DR OMA; HMTHFSD; -.
DR PhylomeDB; P29012; -.
DR BioCyc; EcoCyc:ALARACECAT-MON; -.
DR BioCyc; MetaCyc:ALARACECAT-MON; -.
DR SABIO-RK; P29012; -.
DR PRO; PR:P29012; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008784; F:alanine racemase activity; IDA:EcoCyc.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0030632; P:D-alanine biosynthetic process; IBA:GO_Central.
DR GO; GO:0019480; P:L-alanine oxidation to pyruvate via D-alanine; IMP:EcoCyc.
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 Isomerase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..356
FT /note="Alanine racemase, catabolic"
FT /id="PRO_0000114517"
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"
FT CONFLICT 172
FT /note="A -> R (in Ref. 1; AAC36881)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="A -> R (in Ref. 1; AAC36881)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="P -> L (in Ref. 1; AAC36881)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="L -> V (in Ref. 1; AAC36881)"
FT /evidence="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
