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L-isoleucine-4-hydroxylase (EC 1.14.11.45) (L-isoleucine dioxygenase) (IDO)

 IDO_BACTU               Reviewed;         240 AA.
E2GIN1;
29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 1.
18-JAN-2017, entry version 14.
RecName: Full=L-isoleucine-4-hydroxylase {ECO:0000303|PubMed:20665018};
EC=1.14.11.45 {ECO:0000269|PubMed:19850012, ECO:0000269|PubMed:20665018, ECO:0000269|PubMed:21821743};
AltName: Full=L-isoleucine dioxygenase {ECO:0000303|PubMed:19850012};
Short=IDO {ECO:0000303|PubMed:19850012};
Name=ido {ECO:0000303|PubMed:20665018};
Bacillus thuringiensis.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
Bacillus cereus group.
NCBI_TaxID=1428 {ECO:0000312|EMBL:ADJ94127.1};
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
BIOTECHNOLOGY.
STRAIN=2e2 {ECO:0000269|PubMed:20665018};
PubMed=20665018; DOI=10.1007/s00253-010-2772-3;
Smirnov S.V., Kodera T., Samsonova N.N., Kotlyarova V.A.,
Rushkevich N.Y., Kivero A.D., Sokolov P.M., Hibi M., Ogawa J.,
Shimizu S.;
"Metabolic engineering of Escherichia coli to produce (2S, 3R, 4S)-4-
hydroxyisoleucine.";
Appl. Microbiol. Biotechnol. 88:719-726(2010).
[2]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOTECHNOLOGY.
STRAIN=2e2;
PubMed=19850012; DOI=10.1016/j.bbrc.2009.09.126;
Kodera T., Smirnov S.V., Samsonova N.N., Kozlov Y.I., Koyama R.,
Hibi M., Ogawa J., Yokozeki K., Shimizu S.;
"A novel l-isoleucine hydroxylating enzyme, l-isoleucine dioxygenase
from Bacillus thuringiensis, produces (2S,3R,4S)-4-
hydroxyisoleucine.";
Biochem. Biophys. Res. Commun. 390:506-510(2009).
[3]
FUNCTION, AND CATALYTIC ACTIVITY.
STRAIN=2e2;
PubMed=21821743; DOI=10.1128/AEM.05035-11;
Hibi M., Kawashima T., Kodera T., Smirnov S.V., Sokolov P.M.,
Sugiyama M., Shimizu S., Yokozeki K., Ogawa J.;
"Characterization of Bacillus thuringiensis L-isoleucine dioxygenase
for production of useful amino acids.";
Appl. Environ. Microbiol. 77:6926-6930(2011).
-!- FUNCTION: Catalyzes the hydroxylation of L-isoleucine to produce
(4S)-4-hydroxy-L-isoleucine (PubMed:20665018, PubMed:19850012,
PubMed:21821743). Can also catalyze the hydroxylation of L-
leucine, L-norvaline, L-norleucine and L-allo-isoleucine, as well
as the sulfoxidation of L-methionine, L-ethionine, S-methyl-L-
cysteine, S-ethyl-L-cysteine, and S-allyl-L-cysteine
(PubMed:21821743). {ECO:0000269|PubMed:19850012,
ECO:0000269|PubMed:20665018, ECO:0000269|PubMed:21821743}.
-!- CATALYTIC ACTIVITY: L-isoleucine + 2-oxoglutarate + O(2) = (4S)-4-
hydroxy-L-isoleucine + succinate + CO(2).
{ECO:0000269|PubMed:19850012, ECO:0000269|PubMed:20665018,
ECO:0000269|PubMed:21821743}.
-!- COFACTOR:
Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
Evidence={ECO:0000305|PubMed:19850012};
Note=Binds 1 ascorbate molecule per subunit.
{ECO:0000305|PubMed:19850012};
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000305|PubMed:19850012};
Note=Binds 1 Fe(2+) ion per subunit.
{ECO:0000305|PubMed:19850012};
-!- BIOTECHNOLOGY: 4-Hydroxyisoleucine is a natural nonproteinogenic
amino acid that exhibits insulinotropic biological activity and
increases glucose-induced release of insulin.
{ECO:0000303|PubMed:19850012, ECO:0000303|PubMed:20665018}.
-!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
family. {ECO:0000305}.
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EMBL; HM358019; ADJ94127.1; -; Genomic_DNA.
SMR; E2GIN1; -.
KEGG; ag:ADJ94127; -.
KO; K20418; -.
BioCyc; MetaCyc:MONOMER-17595; -.
GO; GO:0051213; F:dioxygenase activity; IDA:CACAO.
GO; GO:0008198; F:ferrous iron binding; IDA:UniProtKB.
GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
InterPro; IPR018724; 2OG-Fe_dioxygenase.
Pfam; PF10014; 2OG-Fe_Oxy_2; 1.
1: Evidence at protein level;
Dioxygenase; Iron; Metal-binding; Oxidoreductase; Vitamin C.
CHAIN 1 240 L-isoleucine-4-hydroxylase.
/FTId=PRO_0000430784.
METAL 159 159 Iron; catalytic.
{ECO:0000250|UniProtKB:Q96323}.
METAL 161 161 Iron; catalytic.
{ECO:0000250|UniProtKB:Q96323}.
METAL 212 212 Iron; catalytic.
{ECO:0000250|UniProtKB:Q96323}.
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


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EIAAB43065 Epsilon-trimethyllysine 2-oxoglutarate dioxygenase,Mouse,Mus musculus,TML dioxygenase,TML hydroxylase,TML-alpha-ketoglutarate dioxygenase,TMLD,Tmlh,Tmlhe,Trimethyllysine dioxygenase, mitochondrial
40900012-1 L-Isoleucine 10 g
20330-15 L_ (+)_ Isoleucine 500 g
M25147827 L-Isoleucine CAS: [73-32-5] 100 g
20330-31 L_ (+)_ Isoleucine 1 g
IB0914 L-Isoleucine 250g
40900012-2 L-Isoleucine 25 g
20330-02 L_ (+)_ Isoleucine 25 g
M45157892 D-Isoleucine CAS: [319-78-8] 100 mg
20330-02 L‐(+)‐Isoleucine CAS: 73-32-5 25G
20330-31 L‐(+)‐Isoleucine CAS: 73-32-5 1G
M72521737 DL-Isoleucine CAS: [443-79-8] 5 g
M12370710 L-Isoleucine CAS: [73-32-5] 1 kg
40900012-3 L-Isoleucine 100 g
20330-15 L‐(+)‐Isoleucine CAS: 73-32-5 500G
20330-15 L‐(+)‐Isoleucine 500G


 

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