ILE2E_LENBU
ID ILE2E_LENBU Reviewed; 450 AA.
AC M1GRN3;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Isoleucine 2-epimerase {ECO:0000303|PubMed:24039265};
DE EC=5.1.1.21 {ECO:0000269|PubMed:24039265};
DE AltName: Full=BCAA racemase {ECO:0000303|PubMed:24039265};
OS Lentilactobacillus buchneri (Lactobacillus buchneri).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=1581;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=JCM 1115;
RX PubMed=24039265; DOI=10.1128/jb.00709-13;
RA Mutaguchi Y., Ohmori T., Wakamatsu T., Doi K., Ohshima T.;
RT "Identification, purification, and characterization of a novel amino acid
RT racemase, isoleucine 2-epimerase, from lactobacillus species.";
RL J. Bacteriol. 195:5207-5215(2013).
CC -!- FUNCTION: Catalyzes the epimerization of L-isoleucine to D-allo-
CC isoleucine and D-allo-isoleucine to L-isoleucine. Can also catalyze the
CC racemization of many nonpolar amino acids, including leucine and
CC valine. Does not have GABA aminotransferase activity.
CC {ECO:0000269|PubMed:24039265}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-isoleucine = D-allo-isoleucine; Xref=Rhea:RHEA:45560,
CC ChEBI:CHEBI:58045, ChEBI:CHEBI:85306; EC=5.1.1.21;
CC Evidence={ECO:0000269|PubMed:24039265};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:24039265};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.0 mM for L-isoleucine {ECO:0000269|PubMed:24039265};
CC KM=13.2 mM for D-allo-isoleucine {ECO:0000269|PubMed:24039265};
CC Vmax=153 umol/min/mg enzyme for the forward reaction
CC {ECO:0000269|PubMed:24039265};
CC Vmax=286 umol/min/mg enzyme for the reverse reaction
CC {ECO:0000269|PubMed:24039265};
CC Note=kcat is 502 sec(-1) with L-isoleucine as substrate. kcat is 939
CC sec(-1) with D-allo-isoleucine as substrate.
CC {ECO:0000269|PubMed:24039265};
CC pH dependence:
CC Optimum pH is 5.0 for the forward reaction, and 6.0 for the reverse
CC reaction. {ECO:0000269|PubMed:24039265};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius for the forward reaction,
CC and 45 degrees Celsius for the reverse reaction.
CC {ECO:0000269|PubMed:24039265};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:24039265}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; KC413940; AGE45209.1; -; Genomic_DNA.
DR PDB; 4YSN; X-ray; 1.94 A; A/B/C/D=1-450.
DR PDB; 4YSV; X-ray; 2.77 A; A=1-450.
DR PDB; 5LL2; X-ray; 2.60 A; A/B/C/D=1-450.
DR PDB; 5LL3; X-ray; 2.15 A; A/B/C/D=1-450.
DR PDB; 5WYA; X-ray; 2.65 A; A/B/C/D=1-450.
DR PDB; 5WYF; X-ray; 2.12 A; A/B/C/D=1-450.
DR PDBsum; 4YSN; -.
DR PDBsum; 4YSV; -.
DR PDBsum; 5LL2; -.
DR PDBsum; 5LL3; -.
DR PDBsum; 5WYA; -.
DR PDBsum; 5WYF; -.
DR AlphaFoldDB; M1GRN3; -.
DR SMR; M1GRN3; -.
DR KEGG; ag:AGE45209; -.
DR BRENDA; 5.1.1.21; 2852.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Pyridoxal phosphate.
FT CHAIN 1..450
FT /note="Isoleucine 2-epimerase"
FT /id="PRO_0000434753"
FT BINDING 115..116
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P22256"
FT BINDING 142
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P22256"
FT BINDING 250..253
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P22256"
FT BINDING 309
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P22256"
FT MOD_RES 280
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P22256"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:4YSN"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:4YSN"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:4YSN"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:4YSN"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:4YSN"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:4YSN"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:4YSN"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:4YSN"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:4YSN"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:4YSN"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:4YSN"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:4YSN"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:4YSN"
FT HELIX 115..130
FT /evidence="ECO:0007829|PDB:4YSN"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:4YSN"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:4YSN"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:4YSN"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:4YSN"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:4YSN"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:4YSN"
FT HELIX 187..202
FT /evidence="ECO:0007829|PDB:4YSN"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:4YSN"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:4YSN"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:4YSN"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:4YSN"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:4YSN"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:4YSN"
FT HELIX 230..243
FT /evidence="ECO:0007829|PDB:4YSN"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:4YSN"
FT TURN 252..259
FT /evidence="ECO:0007829|PDB:4YSN"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:4YSN"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:4YSN"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:4YSN"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:4YSN"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:4YSN"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:4YSN"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:4YSN"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:5LL3"
FT TURN 309..312
FT /evidence="ECO:0007829|PDB:4YSN"
FT HELIX 314..329
FT /evidence="ECO:0007829|PDB:4YSN"
FT HELIX 332..353
FT /evidence="ECO:0007829|PDB:4YSN"
FT STRAND 357..365
FT /evidence="ECO:0007829|PDB:4YSN"
FT STRAND 367..373
FT /evidence="ECO:0007829|PDB:4YSN"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:4YSN"
FT HELIX 382..394
FT /evidence="ECO:0007829|PDB:4YSN"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:4YSN"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:4YSN"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:4YSN"
FT HELIX 417..435
FT /evidence="ECO:0007829|PDB:4YSN"
SQ SEQUENCE 450 AA; 49424 MW; EE4976BE90FCB976 CRC64;
MGKLDKASKL IDEENKYYAR SARINYYNLV IDHAHGATLV DVDGNKYIDL LASASAINVG
HTHEKVVKAI ADQAQKLIHY TPAYFHHVPG MELSEKLAKI APGNSPKMVS FGNSGSDAND
AIIKFARAYT GRQYIVSYMG SYHGSTYGSQ TLSGSSLNMT RKIGPMLPSV VHVPYPDSYR
TYPGETEHDV SLRYFNEFKK PFESFLPADE TACVLIEPIQ GDGGIIKAPE EYMQLVYKFC
HEHGILFAID EVNQGLGRTG KMWAIQQFKD IEPDLMSVGK SLASGMPLSA VIGKKEVMQS
LDAPAHLFTT AGNPVCSAAS LATLDVIEYE GLVEKSATDG AYAKQRFLEM QQRHPMIGDV
RMWGLNGGIE LVKDPKTKEP DSDAATKVIY YAFAHGVVII TLAGNILRFQ PPLVIPREQL
DQALQVLDDA FTAVENGEVT IPKDTGKIGW
