BARAC_PYRHO
ID BARAC_PYRHO Reviewed; 466 AA.
AC O57878;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Broad substrate specificity amino-acid racemase {ECO:0000303|PubMed:25963389};
DE Short=BAR {ECO:0000303|PubMed:25963389};
DE EC=5.1.1.10 {ECO:0000269|PubMed:25963389, ECO:0000269|PubMed:28343923};
GN OrderedLocusNames=PH0138 {ECO:0000312|EMBL:BAA29207.1};
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND COFACTOR.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=25963389; DOI=10.1007/s00726-015-2001-6;
RA Kawakami R., Ohmori T., Sakuraba H., Ohshima T.;
RT "Identification of a novel amino acid racemase from a hyperthermophilic
RT archaeon Pyrococcus horikoshii OT-3 induced by D-amino acids.";
RL Amino Acids 47:1579-1587(2015).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP SUBUNIT.
RX PubMed=28343923; DOI=10.1016/j.jbiosc.2017.02.004;
RA Kawakami R., Sakuraba H., Ohmori T., Ohshima T.;
RT "First characterization of an archaeal amino acid racemase with broad
RT substrate specificity from the hyperthermophile Pyrococcus horikoshii OT-
RT 3.";
RL J. Biosci. Bioeng. 124:23-27(2017).
CC -!- FUNCTION: Amino-acid racemase able to utilize a broad range of
CC substrates (PubMed:25963389). Can use Met, Leu, Phe, Ala, Ser, Ile,
CC Val, Trp, Tyr and Thr (PubMed:25963389, PubMed:28343923). Is mostly
CC active with Phe, Leu, Met and Tyr, followed by Ile, Thr and Trp. Has
CC weaker activity with Val, Ser and Ala (PubMed:28343923). Shows no
CC activity toward Pro, Asp, Glu, Arg, His, Gln and Asn (PubMed:25963389,
CC PubMed:28343923). {ECO:0000269|PubMed:25963389,
CC ECO:0000269|PubMed:28343923}.
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:0000269|PubMed:25963389,
CC ECO:0000269|PubMed:28343923};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-phenylalanine = D-phenylalanine; Xref=Rhea:RHEA:59804,
CC ChEBI:CHEBI:57981, ChEBI:CHEBI:58095;
CC Evidence={ECO:0000269|PubMed:28343923};
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:28343923};
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:28343923};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosine = D-tyrosine; Xref=Rhea:RHEA:59808,
CC ChEBI:CHEBI:58315, ChEBI:CHEBI:58570;
CC Evidence={ECO:0000269|PubMed:28343923};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-isoleucine = D-allo-isoleucine; Xref=Rhea:RHEA:45560,
CC ChEBI:CHEBI:58045, ChEBI:CHEBI:85306;
CC Evidence={ECO:0000269|PubMed:28343923};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonine = D-threonine; Xref=Rhea:RHEA:13913,
CC ChEBI:CHEBI:57757, ChEBI:CHEBI:57926;
CC Evidence={ECO:0000269|PubMed:28343923};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tryptophan = D-tryptophan; Xref=Rhea:RHEA:60516,
CC ChEBI:CHEBI:57719, ChEBI:CHEBI:57912;
CC Evidence={ECO:0000269|PubMed:28343923};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:25963389, ECO:0000269|PubMed:28343923};
CC -!- ACTIVITY REGULATION: Inhibited by hydroxylamine.
CC {ECO:0000269|PubMed:25963389}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.94 mM for L-Ile {ECO:0000269|PubMed:28343923};
CC KM=9.54 mM for D-Ile {ECO:0000269|PubMed:28343923};
CC KM=4.95 mM for L-Leu {ECO:0000269|PubMed:28343923};
CC KM=4.19 mM for D-Leu {ECO:0000269|PubMed:28343923};
CC KM=4.28 mM for L-Met {ECO:0000269|PubMed:28343923};
CC KM=7.86 mM for D-Met {ECO:0000269|PubMed:28343923};
CC KM=8.23 mM for L-Phe {ECO:0000269|PubMed:28343923};
CC KM=2.78 mM for D-Phe {ECO:0000269|PubMed:28343923};
CC KM=2.23 mM for L-Tyr {ECO:0000269|PubMed:28343923};
CC KM=2.77 mM for D-Tyr {ECO:0000269|PubMed:28343923};
CC KM=5.84 mM for L-Trp {ECO:0000269|PubMed:28343923};
CC KM=1.68 mM for D-Trp {ECO:0000269|PubMed:28343923};
CC Vmax=14.3 umol/min/mg enzyme with L-Ile as substrate
CC {ECO:0000269|PubMed:28343923};
CC Vmax=25.9 umol/min/mg enzyme with D-Ile as substrate
CC {ECO:0000269|PubMed:28343923};
CC Vmax=38.9 umol/min/mg enzyme with L-Leu as substrate
CC {ECO:0000269|PubMed:28343923};
CC Vmax=50.9 umol/min/mg enzyme with D-Leu as substrate
CC {ECO:0000269|PubMed:28343923};
CC Vmax=23.3 umol/min/mg enzyme with L-Met as substrate
CC {ECO:0000269|PubMed:28343923};
CC Vmax=65.7 umol/min/mg enzyme with D-Met as substrate
CC {ECO:0000269|PubMed:28343923};
CC Vmax=59.9 umol/min/mg enzyme with L-Phe as substrate
CC {ECO:0000269|PubMed:28343923};
CC Vmax=36.4 umol/min/mg enzyme with D-Phe as substrate
CC {ECO:0000269|PubMed:28343923};
CC Vmax=16.8 umol/min/mg enzyme with L-Tyr as substrate
CC {ECO:0000269|PubMed:28343923};
CC Vmax=10.4 umol/min/mg enzyme with D-Tyr as substrate
CC {ECO:0000269|PubMed:28343923};
CC Vmax=9.23 umol/min/mg enzyme with L-Trp as substrate
CC {ECO:0000269|PubMed:28343923};
CC Vmax=1.45 umol/min/mg enzyme with D-Trp as substrate
CC {ECO:0000269|PubMed:28343923};
CC pH dependence:
CC Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:28343923};
CC Temperature dependence:
CC Shows extremely high thermostability. Retains full activity after
CC incubation at 80 degrees Celsius for at least 2 hours.
CC {ECO:0000269|PubMed:28343923};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:28343923}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; BA000001; BAA29207.1; -; Genomic_DNA.
DR PIR; H71234; H71234.
DR AlphaFoldDB; O57878; -.
DR SMR; O57878; -.
DR STRING; 70601.3256524; -.
DR EnsemblBacteria; BAA29207; BAA29207; BAA29207.
DR KEGG; pho:PH0138; -.
DR eggNOG; arCOG00915; Archaea.
DR OMA; FWGWQAH; -.
DR BRENDA; 5.1.1.10; 5244.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0018111; F:methionine racemase activity; IEA:RHEA.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0018114; F:threonine racemase activity; IEA:RHEA.
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.
FT CHAIN 1..466
FT /note="Broad substrate specificity amino-acid racemase"
FT /id="PRO_0000448758"
FT BINDING 129..130
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P22256"
FT BINDING 269
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P22256"
FT BINDING 324
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P22256"
FT MOD_RES 295
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P22256"
SQ SEQUENCE 466 AA; 52392 MW; 179C05F5E4086994 CRC64;
MVSMTKWDEI RKYTSKKIEK NLEIVKLDEK YIPRASGFKY YPMVIERSSG SRIWDKDGNE
YIDFLTSAAV FNVGHTHPGV VKAVEEQIKK FFNYTMGYLY VEPPVRLAEL LVEITPGNFE
KKVTYGFSGS DAVDSSIKAA RAYTKRVNII SFLHSYHGMT YGALSATGIL DPKLKKLLHP
MGNFHHVEFP DPYRNSWGID GYEDPSELAN RALDEIERKI KELNEDVAGI IIEPIQGDAG
VVIPPEEFVR DLKKLTEEYG IVFIDEEVQT GMGRTGRWWG IEHFGVTPDL IVSAKALGGG
MPISAVVGKA EIMDSVPVPF FVFTHIGHAV NASAAIATIN VIKEEKLVER SEKLGEYMLK
RLRELQETYP IIGDVRGKGL LIGVDIVKEG TREPDRSLAQ KISWRAWEKG LIMITFGKHG
NVLRIAPPLN IPQEDLDKGV EIIEESIKDA VEGKIPDEVL KFLRAW
