IDO_BACTU
ID IDO_BACTU Reviewed; 240 AA.
AC E2GIN1;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=L-isoleucine-4-hydroxylase {ECO:0000303|PubMed:20665018};
DE EC=1.14.11.45 {ECO:0000269|PubMed:19850012, ECO:0000269|PubMed:20665018, ECO:0000269|PubMed:21821743};
DE AltName: Full=L-isoleucine dioxygenase {ECO:0000303|PubMed:19850012};
DE Short=IDO {ECO:0000303|PubMed:19850012};
GN Name=ido {ECO:0000303|PubMed:20665018};
OS Bacillus thuringiensis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1428 {ECO:0000312|EMBL:ADJ94127.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOTECHNOLOGY.
RC STRAIN=2e2 {ECO:0000269|PubMed:20665018};
RX PubMed=20665018; DOI=10.1007/s00253-010-2772-3;
RA Smirnov S.V., Kodera T., Samsonova N.N., Kotlyarova V.A., Rushkevich N.Y.,
RA Kivero A.D., Sokolov P.M., Hibi M., Ogawa J., Shimizu S.;
RT "Metabolic engineering of Escherichia coli to produce (2S, 3R, 4S)-4-
RT hydroxyisoleucine.";
RL Appl. Microbiol. Biotechnol. 88:719-726(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOTECHNOLOGY.
RC STRAIN=2e2;
RX PubMed=19850012; DOI=10.1016/j.bbrc.2009.09.126;
RA Kodera T., Smirnov S.V., Samsonova N.N., Kozlov Y.I., Koyama R., Hibi M.,
RA Ogawa J., Yokozeki K., Shimizu S.;
RT "A novel l-isoleucine hydroxylating enzyme, l-isoleucine dioxygenase from
RT Bacillus thuringiensis, produces (2S,3R,4S)-4-hydroxyisoleucine.";
RL Biochem. Biophys. Res. Commun. 390:506-510(2009).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=2e2;
RX PubMed=21821743; DOI=10.1128/aem.05035-11;
RA Hibi M., Kawashima T., Kodera T., Smirnov S.V., Sokolov P.M., Sugiyama M.,
RA Shimizu S., Yokozeki K., Ogawa J.;
RT "Characterization of Bacillus thuringiensis L-isoleucine dioxygenase for
RT production of useful amino acids.";
RL Appl. Environ. Microbiol. 77:6926-6930(2011).
CC -!- FUNCTION: Catalyzes the hydroxylation of L-isoleucine to produce (4S)-
CC 4-hydroxy-L-isoleucine (PubMed:20665018, PubMed:19850012,
CC PubMed:21821743). Can also catalyze the hydroxylation of L-leucine, L-
CC norvaline, L-norleucine and L-allo-isoleucine, as well as the
CC sulfoxidation of L-methionine, L-ethionine, S-methyl-L-cysteine, S-
CC ethyl-L-cysteine, and S-allyl-L-cysteine (PubMed:21821743).
CC {ECO:0000269|PubMed:19850012, ECO:0000269|PubMed:20665018,
CC ECO:0000269|PubMed:21821743}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-isoleucine + O2 = (4S)-4-hydroxy-L-
CC isoleucine + CO2 + succinate; Xref=Rhea:RHEA:41448,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:58045, ChEBI:CHEBI:78247;
CC EC=1.14.11.45; Evidence={ECO:0000269|PubMed:19850012,
CC ECO:0000269|PubMed:20665018, ECO:0000269|PubMed:21821743};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000305|PubMed:19850012};
CC Note=Binds 1 ascorbate molecule per subunit.
CC {ECO:0000305|PubMed:19850012};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000305|PubMed:19850012};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000305|PubMed:19850012};
CC -!- BIOTECHNOLOGY: 4-Hydroxyisoleucine is a natural nonproteinogenic amino
CC acid that exhibits insulinotropic biological activity and increases
CC glucose-induced release of insulin. {ECO:0000303|PubMed:19850012,
CC ECO:0000303|PubMed:20665018}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; HM358019; ADJ94127.1; -; Genomic_DNA.
DR PDB; 6LNH; X-ray; 2.34 A; A/B/C/D=1-240.
DR PDBsum; 6LNH; -.
DR AlphaFoldDB; E2GIN1; -.
DR SMR; E2GIN1; -.
DR KEGG; ag:ADJ94127; -.
DR BioCyc; MetaCyc:MON-17595; -.
DR BRENDA; 1.14.11.45; 711.
DR GO; GO:0051213; F:dioxygenase activity; IDA:CACAO.
DR GO; GO:0008198; F:ferrous iron binding; IDA:UniProtKB.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR InterPro; IPR018724; 2OG-Fe_dioxygenase.
DR Pfam; PF10014; 2OG-Fe_Oxy_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase; Vitamin C.
FT CHAIN 1..240
FT /note="L-isoleucine-4-hydroxylase"
FT /id="PRO_0000430784"
FT BINDING 159
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q96323"
FT BINDING 161
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q96323"
FT BINDING 212
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q96323"
FT HELIX 8..18
FT /evidence="ECO:0007829|PDB:6LNH"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:6LNH"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:6LNH"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:6LNH"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:6LNH"
FT STRAND 56..66
FT /evidence="ECO:0007829|PDB:6LNH"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:6LNH"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:6LNH"
FT HELIX 109..123
FT /evidence="ECO:0007829|PDB:6LNH"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:6LNH"
FT STRAND 134..145
FT /evidence="ECO:0007829|PDB:6LNH"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:6LNH"
FT STRAND 162..174
FT /evidence="ECO:0007829|PDB:6LNH"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:6LNH"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:6LNH"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:6LNH"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:6LNH"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:6LNH"
FT STRAND 225..236
FT /evidence="ECO:0007829|PDB:6LNH"
SQ SEQUENCE 240 AA; 27838 MW; C0A4F38F13929E9E CRC64;
MKMSGFSIEE KVHEFESKGF LEISNEIFLQ EEENHSLLTQ AQLDYYNLED DAYGECRARS
YSRYIKYVDS PDYILDNSND YFQSKEYNYD DGGKVRQFNS INDSFLCNPL IQNIVRFDTE
FAFKTNIIDK SKDLIIGLHQ VRYKATKERP SFSSPIWLHK DDEPVVFLHL MNLSNTAIGG
DNLIANSPRE INQFISLKEP LETLVFGQKV FHAVTPLGTE CSTEAFRDIL LVTFSYKETK
