BSR_PSETA
ID BSR_PSETA Reviewed; 409 AA.
AC I0J1I6;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Broad specificity amino-acid racemase {ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000305|PubMed:19300994};
DE EC=5.1.1.10 {ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000269|PubMed:19300994, ECO:0000269|PubMed:20564572};
DE AltName: Full=Arginine racemase {ECO:0000303|PubMed:20564572};
DE AltName: Full=Broad substrate specificity racemase {ECO:0000303|PubMed:19300994};
DE Flags: Precursor;
GN Name=argR {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], PROTEIN SEQUENCE OF 24-33, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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).
RN [2]
RP DISULFIDE BOND, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-70 AND CYS-96.
RC STRAIN=ATCC 4683 / DSM 21104 / JCM 20238 / CCUG 560 / NBRC 3460 / NCIMB
RC 9396 / NCTC 10697 / NRRL B-14;
RX PubMed=20564572; DOI=10.1002/cbdv.200900258;
RA Matsui D., Oikawa T.;
RT "Detection and function of the intramolecular disulfide bond in arginine
RT racemase: an enzyme with broad substrate specificity.";
RL Chem. Biodivers. 7:1591-1602(2010).
CC -!- FUNCTION: Amino-acid racemase able to utilize a broad range of
CC substrates. Is mostly active with lysine and arginine and, to a lesser
CC extent, with ornithine, whereas is about 10 times less active with
CC alanine, methionine and ethionine. With phenylalanine as substrate only
CC a trace activity is detectable, and is inactive with glutamate. Plays a
CC key role in the catabolism of D-arginine and D-lysine, that allows
CC P.taetrolens strain NBRC 3460 to grow on these basic D-amino acids as a
CC sole carbon source. {ECO:0000269|PubMed:19300994}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an L-alpha-amino acid = a D-alpha-amino acid;
CC Xref=Rhea:RHEA:18317, ChEBI:CHEBI:59869, ChEBI:CHEBI:59871;
CC EC=5.1.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_02212,
CC ECO:0000269|PubMed:19300994, ECO:0000269|PubMed:20564572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysine = D-lysine; Xref=Rhea:RHEA:22864, ChEBI:CHEBI:32551,
CC ChEBI:CHEBI:32557; Evidence={ECO:0000255|HAMAP-Rule:MF_02212,
CC ECO:0000269|PubMed:19300994, ECO:0000269|PubMed:20564572};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22866;
CC Evidence={ECO:0000269|PubMed:19300994};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginine = D-arginine; Xref=Rhea:RHEA:18069,
CC ChEBI:CHEBI:32682, ChEBI:CHEBI:32689; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02212, ECO:0000269|PubMed:19300994,
CC ECO:0000269|PubMed:20564572};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18071;
CC Evidence={ECO:0000269|PubMed:19300994};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ornithine = D-ornithine; Xref=Rhea:RHEA:11584,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:57668;
CC Evidence={ECO:0000269|PubMed:19300994, ECO:0000269|PubMed:20564572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC ChEBI:CHEBI:57416, ChEBI:CHEBI:57972;
CC Evidence={ECO:0000269|PubMed:19300994, ECO:0000269|PubMed:20564572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-methionine = D-methionine; Xref=Rhea:RHEA:12492,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:57932;
CC Evidence={ECO:0000269|PubMed:19300994};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02212,
CC ECO:0000269|PubMed:19300994};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.4 mM for L-lysine {ECO:0000269|PubMed:20564572};
CC KM=2.4 mM for D-lysine {ECO:0000269|PubMed:20564572};
CC KM=1.2 mM for L-arginine {ECO:0000269|PubMed:20564572};
CC KM=1.2 mM for D-arginine {ECO:0000269|PubMed:20564572};
CC KM=3.7 mM for L-ornithine {ECO:0000269|PubMed:20564572};
CC KM=3.6 mM for D-ornithine {ECO:0000269|PubMed:20564572};
CC KM=15.7 mM for L-alanine {ECO:0000269|PubMed:20564572};
CC KM=15.0 mM for D-alanine {ECO:0000269|PubMed:20564572};
CC Note=kcat is 109.0 sec(-1) with L-lysine as substrate. kcat is 104.0
CC sec(-1) with D-lysine as substrate. kcat is 119.0 sec(-1) with L-
CC arginine as substrate. kcat is 119.0 sec(-1) with D-arginine as
CC substrate. kcat is 87.7 sec(-1) with L-ornithine as substrate. kcat
CC is 87.3 sec(-1) with D-ornithine as substrate. kcat is 2.4 sec(-1)
CC with L-alanine as substrate. kcat is 2.6 sec(-1) with D-alanine as
CC substrate. {ECO:0000269|PubMed:20564572};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:19300994};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius.
CC {ECO:0000269|PubMed:19300994};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19300994}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_02212,
CC ECO:0000269|PubMed:19300994}. Note=Is translocated into the periplasm
CC via a Tat-independent protein translocation pathway and, therefore,
CC must have been translocated via the Sec route.
CC {ECO:0000269|PubMed:19300994}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are no longer able to
CC utilize D-Lys as a sole carbon source for growth, and also the
CC utilization of D-Arg is strongly reduced. The growth of the deletion
CC mutant strain on LB medium is slightly retarded as compared to the wild
CC type, which might indicate that ArgR is also generally involved in
CC amino acid degradation. {ECO:0000269|PubMed:19300994}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. Bsr subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000305}.
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DR EMBL; AB096176; BAM13386.1; -; Genomic_DNA.
DR AlphaFoldDB; I0J1I6; -.
DR SMR; I0J1I6; -.
DR STRING; 47884.SAMN04490203_2786; -.
DR BRENDA; 5.1.1.10; 5196.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0008784; F:alanine racemase activity; IEA:InterPro.
DR GO; GO:0047679; F:arginine racemase activity; IEA:RHEA.
DR GO; GO:0018113; F:lysine racemase activity; IEA:RHEA.
DR GO; GO:0018111; F:methionine racemase activity; IEA:RHEA.
DR GO; GO:0050157; F:ornithine racemase activity; IEA:RHEA.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR CDD; cd06826; PLPDE_III_AR2; 1.
DR Gene3D; 2.40.37.10; -; 1.
DR Gene3D; 3.20.20.10; -; 1.
DR HAMAP; MF_02212; Bsr_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 InterPro; IPR043698; Racemase_Bsr/Lyr.
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 Direct protein sequencing; Disulfide bond; Isomerase; Periplasm;
KW Pyridoxal phosphate; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212,
FT ECO:0000269|PubMed:19300994"
FT CHAIN 24..409
FT /note="Broad specificity amino-acid racemase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT /id="PRO_0000419111"
FT ACT_SITE 74
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT ACT_SITE 300
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT MOD_RES 74
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT DISULFID 70..96
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212,
FT ECO:0000269|PubMed:20564572"
FT MUTAGEN 70
FT /note="C->A: The catalytic efficiency with arginine,
FT lysine, and ornithine is very similar to that of wild-type,
FT and that with both L-alanine and D-alanine increases
FT approximately five times; when associated with A-96."
FT /evidence="ECO:0000269|PubMed:20564572"
FT MUTAGEN 96
FT /note="C->A: The catalytic efficiency with arginine,
FT lysine, and ornithine is very similar to that of wild-type,
FT and that with both L-alanine and D-alanine increases
FT approximately five times; when associated with A-70."
FT /evidence="ECO:0000269|PubMed:20564572"
SQ SEQUENCE 409 AA; 43976 MW; 8AE24501C32309E8 CRC64;
MPFSRTLLAL SLGMALLQNP AFAAPPLSMT DGVAQVNTQD SNAWVEINKA AFEHNIRTLQ
TALAGKSQIC AVLKADAYGH GIGLLMPSVI AMGVPCVGVA SNEEARVVRE SGFKGQLIRV
RTAALSELEA ALPYNMEELV GNLDFAVKAS LIAEDHGRPL VVHLGLNSSG MSRNGVDMTT
AQGRRDAVAI TKVPNLEVRA IMTHFAVEDA ADVRAGLKAF NQQAQWLMNV AQLDRSKITL
HAANSFATLE VPESHLDMVR PGGALFGDTV PSHTEYKRVM QFKSHVASVN SYPKGNTVGY
GRTYTLGRDS RLANITVGYS DGYRRAFTNK GIVLINGHRV PVVGKVSMNT LMVDVTDAPD
VKSGDEVVLF GHQGKAEITQ AEIEDINGAL LADLYTVWGN SNPKILKDQ
