DADX_PSEPK
ID DADX_PSEPK Reviewed; 357 AA.
AC Q88CB2;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Alanine racemase, catabolic {ECO:0000305|PubMed:23995642};
DE EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201, ECO:0000269|PubMed:23995642};
GN Name=dadX {ECO:0000303|PubMed:23995642, ECO:0000312|EMBL:AAN70834.1};
GN OrderedLocusNames=PP_5269 {ECO:0000312|EMBL:AAN70834.1};
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=23995642; DOI=10.1128/jb.00761-13;
RA Radkov A.D., Moe L.A.;
RT "Amino acid racemization in Pseudomonas putida KT2440.";
RL J. Bacteriol. 195:5016-5024(2013).
CC -!- FUNCTION: Isomerizes L-alanine to D-alanine which is then likely
CC oxidized to pyruvate by DadA. Shows racemase activity with both alanine
CC stereoisomers, negligible activity with D-cysteine and L-serine, and
CC exhibits no activity with the remaining natural chiral amino acids.
CC {ECO:0000269|PubMed:23995642}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01201,
CC ECO:0000269|PubMed:23995642};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.73 mM for D-alanine {ECO:0000269|PubMed:23995642};
CC KM=24.57 mM for L-alanine {ECO:0000269|PubMed:23995642};
CC Note=kcat is 37.47 sec(-1) with D-alanine as substrate. kcat is 92.0
CC sec(-1) with L-alanine as substrate. {ECO:0000269|PubMed:23995642};
CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC from L-alanine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01201}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000255|HAMAP-
CC Rule:MF_01201}.
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DR EMBL; AE015451; AAN70834.1; -; Genomic_DNA.
DR RefSeq; NP_747370.1; NC_002947.4.
DR RefSeq; WP_010955779.1; NC_002947.4.
DR AlphaFoldDB; Q88CB2; -.
DR SMR; Q88CB2; -.
DR STRING; 160488.PP_5269; -.
DR EnsemblBacteria; AAN70834; AAN70834; PP_5269.
DR KEGG; ppu:PP_5269; -.
DR PATRIC; fig|160488.4.peg.5622; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_1_0_6; -.
DR OMA; WEILCGF; -.
DR PhylomeDB; Q88CB2; -.
DR BioCyc; MetaCyc:G1G01-5627-MON; -.
DR BioCyc; PPUT160488:G1G01-5627-MON; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000000556; 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:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
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 1: Evidence at protein level;
KW Isomerase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..357
FT /note="Alanine racemase, catabolic"
FT /id="PRO_0000446938"
FT ACT_SITE 33
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT ACT_SITE 253
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT MOD_RES 33
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
SQ SEQUENCE 357 AA; 38766 MW; ED4D7DE7CAE5684B CRC64;
MRPARALIDL QALRHNYRLA RELTGAKALA VIKADAYGHG AVRCALALEA EADGFAVACI
EEALELRAAG IKAPVLLLEG FFEASELALI AEHDLWCVVH SLWQLEAIEK TPLHKPLNVW
LKLDSGMHRV GLHPKDYHDA YQRLLASGKV SRIVLMTHFA RADELDADAT SQQIAVFEAA
RQGLAAECSL RNSPGVLGWP QAPSDWVRPG LMLYGATPFE VAQAEAARLQ PVMTLQSRVI
SVRELPAGEP VGYGAKFVSP RPTRVGVVAM GYADGYPRQA PNGTPVLVAG KRTQLIGRVS
MDMLSIDLTD VPQATVGSPV EFWGKQVLAS EVAAHAGTIP YQIFCNLKRV PRDYIGE
