ALR_PSETA
ID ALR_PSETA Reviewed; 357 AA.
AC B9WZ64;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN Name=alr {ECO:0000303|PubMed:19300994};
OS Pseudomonas taetrolens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=47884;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 4683 / DSM 21104 / JCM 20238 / CCUG 560 / NBRC 3460 / NCIMB
RC 9396 / NCTC 10697 / NRRL B-14;
RX PubMed=19300994; DOI=10.1007/s00253-009-1942-7;
RA Matsui D., Oikawa T., Arakawa N., Osumi S., Lausberg F., Stabler N.,
RA Freudl R., Eggeling L.;
RT "A periplasmic, pyridoxal-5'-phosphate-dependent amino acid racemase in
RT Pseudomonas taetrolens.";
RL Appl. Microbiol. Biotechnol. 83:1045-1054(2009).
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. Is
CC highly specific for alanine as substrate. May serve both anabolic and
CC catabolic purposes. {ECO:0000269|PubMed:19300994}.
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:19300994};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:19300994};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:19300994};
CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC from L-alanine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01201}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19300994}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000255|HAMAP-
CC Rule:MF_01201}.
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DR EMBL; AB296103; BAH23434.1; -; Genomic_DNA.
DR AlphaFoldDB; B9WZ64; -.
DR SMR; B9WZ64; -.
DR UniPathway; UPA00042; UER00497.
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.
FT CHAIN 1..357
FT /note="Alanine racemase"
FT /id="PRO_0000419112"
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; 38814 MW; 9CD988FF18E944DA CRC64;
MRPARALIDL QALRHNYRLA RELTGAKALA VIKADAYGHG AVRCALALEA EADGFAVACI
EEALELRAAG IKAPVLLLEG FFEASELALI AEHDLWCVVH SLWQLEAIER TQLHKPLTVW
LKLDSGMHRV GLHPKDYHEA YQRLLASGKV ARIVLMSHFA RADELDADAT AQQIAVFEAA
RQGLAAECSL RNSPGVLGWP QAPSDWVRPG LMLYGATPFE VAQAEAERLQ PVMTLQSRVI
SVRELPAGEP VGYGAKFVSP RPTRVGVVAM GYADGYPRQA PNGTPVLVAG KRTQLIGRVS
MDMLSIDLTD VPEATVGSPV ELWGKHVLAS EVAAHAGTIP YQIFCNLKRV PRDYIGE