ID   LMRAC_THEKO             Reviewed;         443 AA.
AC   Q5JGG6;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Leucine/methionine racemase {ECO:0000305};
DE            Short=Leu/Met racemase {ECO:0000305};
DE            EC=5.1.1.- {ECO:0000269|PubMed:33468590};
DE            EC=5.1.1.2 {ECO:0000269|PubMed:33468590};
GN   OrderedLocusNames=TK1211 {ECO:0000312|EMBL:BAD85400.1};
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC   STRAIN=KU216;
RX   PubMed=33468590; DOI=10.1128/jb.00617-20;
RA   Zheng R.C., Lu X.F., Tomita H., Hachisuka S.I., Zheng Y.G., Atomi H.;
RT   "TK1211 encodes an amino acid racemase towards leucine and methionine in
RT   the hyperthermophilic archaeon Thermococcus kodakarensis.";
RL   J. Bacteriol. 203:0-0(2021).
CC   -!- FUNCTION: Amino acid racemase that shows relatively high activity
CC       toward leucine, which is the preferred substrate, and methionine
CC       (PubMed:33468590). Also exhibits lower levels of activity toward
CC       phenylalanine and alanine, and trace activities toward isoleucine and
CC       valine (PubMed:33468590). {ECO:0000269|PubMed:33468590}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-leucine = D-leucine; Xref=Rhea:RHEA:59396,
CC         ChEBI:CHEBI:57427, ChEBI:CHEBI:143079;
CC         Evidence={ECO:0000269|PubMed:33468590};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-methionine = D-methionine; Xref=Rhea:RHEA:12492,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:57932; EC=5.1.1.2;
CC         Evidence={ECO:0000269|PubMed:33468590};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:33468590};
CC   -!- ACTIVITY REGULATION: Activity is completely abolished in the presence
CC       of hydroxylamine, a known specific pyridoxal-phosphate inhibitor.
CC       {ECO:0000269|PubMed:33468590}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=16.3 mM for D-leucine {ECO:0000269|PubMed:33468590};
CC         KM=6.98 mM for L-leucine {ECO:0000269|PubMed:33468590};
CC         KM=26.8 mM for D-methionine {ECO:0000269|PubMed:33468590};
CC         KM=18.0 mM for L-methionine {ECO:0000269|PubMed:33468590};
CC         Vmax=133 umol/min/mg enzyme with D-leucine as substrate
CC         {ECO:0000269|PubMed:33468590};
CC         Vmax=53 umol/min/mg enzyme with L-leucine as substrate
CC         {ECO:0000269|PubMed:33468590};
CC         Vmax=105 umol/min/mg enzyme with D-methionine as substrate
CC         {ECO:0000269|PubMed:33468590};
CC         Vmax=66.6 umol/min/mg enzyme with L-methionine as substrate
CC         {ECO:0000269|PubMed:33468590};
CC         Note=kcat is 108 sec(-1) with D-leucine as substrate. kcat is 43.3
CC         sec(-1) with L-leucine as substrate. kcat is 86.0 sec(-1) with D-
CC         methionine as substrate. kcat is 54.4 sec(-1) with L-methionine as
CC         substrate. {ECO:0000269|PubMed:33468590};
CC       pH dependence:
CC         Optimum pH is 5.0 for leucine racemase activity.
CC         {ECO:0000269|PubMed:33468590};
CC       Temperature dependence:
CC         Optimum temperature is 70 degrees Celsius for D-leucine to L-leucine
CC         reaction. Optimum temperature is 75 degrees Celsius for L-leucine to
CC         D-leucine reaction. {ECO:0000269|PubMed:33468590};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:33468590}.
CC   -!- DISRUPTION PHENOTYPE: The disruption mutant displays growth in medium
CC       with L-leucine but cannot grow with D-leucine.
CC       {ECO:0000269|PubMed:33468590}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AP006878; BAD85400.1; -; Genomic_DNA.
DR   RefSeq; WP_011250162.1; NC_006624.1.
DR   SMR; Q5JGG6; -.
DR   STRING; 69014.TK1211; -.
DR   EnsemblBacteria; BAD85400; BAD85400; TK1211.
DR   GeneID; 3235094; -.
DR   KEGG; tko:TK1211; -.
DR   PATRIC; fig|69014.16.peg.1186; -.
DR   eggNOG; arCOG00916; Archaea.
DR   HOGENOM; CLU_016922_10_0_2; -.
DR   InParanoid; Q5JGG6; -.
DR   OMA; GMTTQIY; -.
DR   OrthoDB; 20774at2157; -.
DR   PhylomeDB; Q5JGG6; -.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   1: Evidence at protein level;
KW   Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..443
FT                   /note="Leucine/methionine racemase"
FT                   /id="PRO_0000453288"
FT   BINDING         110..111
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P22256"
FT   BINDING         247
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P22256"
FT   BINDING         302
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P22256"
FT   MOD_RES         273
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P22256"
SQ   SEQUENCE   443 AA;  48981 MW;  C2FE1179B795EDA8 CRC64;
     MTPEEVVERY SQVISRASHV TYVPIVPSRA ENALVWDIEG RAYIDFLADA AVQNVGHNNP
     RVVEAVKKTA DRLLHFTFIY GFPVEPLLLA EKLREIAPLE GAKVAFGLSG SDANDGAIKF
     ARAYTGRRSI IGYLRSYYGS TYGAMSVTGL DFEVRSKVGQ LSDVHFIPFP NCYRCPFGKE
     PGKCRMECVS FLKEKFEGEV HAEGTAALIA EAIQGDAGMV VPPENYFKKL KRILDEHGIL
     LVVDEVQSGL GRTGKWFAIE HFGVEPEIIT LAKPLGGGLP ISAIVGRGEI MDSLPPLGHA
     FTMSGNPVAS AAALAVIEEI EEKELLKRAQ ILGERAKRRL EKMKKKHELI GDVRGLGLML
     GVDLVKDRET KERAYDEAKK VVWRAYELGL IVAFLQGNVL RIEPPLTIEE EVLDEGLDKL
     EEAIEDVEEG RVPDEVIEKV QGW