ID   HILA_PANAA              Reviewed;         296 AA.
AC   A0A0H3L1B8;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=L-isoleucine 3(1)-dioxygenase {ECO:0000305};
DE            EC=1.14.11.74 {ECO:0000269|PubMed:23554367};
DE   AltName: Full=L-isoleucine 4'-dioxygenase {ECO:0000305};
GN   Name=hilA {ECO:0000303|PubMed:23554367};
GN   OrderedLocusNames=PAJ_3036 {ECO:0000312|EMBL:BAK13116.1};
OS   Pantoea ananatis (strain AJ13355).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=932677;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AJ13355;
RX   PubMed=22159605; DOI=10.1007/s00253-011-3713-5;
RA   Hara Y., Kadotani N., Izui H., Katashkina J.I., Kuvaeva T.M.,
RA   Andreeva I.G., Golubeva L.I., Malko D.B., Makeev V.J., Mashko S.V.,
RA   Kozlov Y.I.;
RT   "The complete genome sequence of Pantoea ananatis AJ13355, an organism with
RT   great biotechnological potential.";
RL   Appl. Microbiol. Biotechnol. 93:331-341(2012).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC   STRAIN=AJ13355;
RX   PubMed=23554367; DOI=10.1002/mbo3.87;
RA   Smirnov S.V., Sokolov P.M., Kotlyarova V.A., Samsonova N.N., Kodera T.,
RA   Sugiyama M., Torii T., Hibi M., Shimizu S., Yokozeki K., Ogawa J.;
RT   "A novel L-isoleucine-4'-dioxygenase and L-isoleucine dihydroxylation
RT   cascade in Pantoea ananatis.";
RL   MicrobiologyOpen 2:471-481(2013).
CC   -!- FUNCTION: Catalyzes the hydroxylation of L-isoleucine at the C-4'
CC       position to form L-4'-hydroxyisoleucine (4'-HIL) (PubMed:23554367).
CC       Exhibits low activity with L-valine and L-methionine (PubMed:23554367).
CC       {ECO:0000269|PubMed:23554367}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-isoleucine + O2 = 3(1)-hydroxy-L-isoleucine
CC         + CO2 + succinate; Xref=Rhea:RHEA:63872, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:58045, ChEBI:CHEBI:149627; EC=1.14.11.74;
CC         Evidence={ECO:0000269|PubMed:23554367};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63873;
CC         Evidence={ECO:0000269|PubMed:23554367};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000269|PubMed:23554367};
CC       Note=Binds 1 ascorbate molecule per subunit.
CC       {ECO:0000250|UniProtKB:E2GIN1};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000269|PubMed:23554367};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:E2GIN1};
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AP012032; BAK13116.1; -; Genomic_DNA.
DR   RefSeq; WP_014594863.1; NC_017531.2.
DR   SMR; A0A0H3L1B8; -.
DR   STRING; 932677.PAJ_3036; -.
DR   EnsemblBacteria; BAK13116; BAK13116; PAJ_3036.
DR   KEGG; paj:PAJ_3036; -.
DR   PATRIC; fig|553.3.peg.223; -.
DR   eggNOG; ENOG502Z9CB; Bacteria.
DR   HOGENOM; CLU_080184_0_0_6; -.
DR   OMA; FATFRRW; -.
DR   BioCyc; MetaCyc:MON-21133; -.
DR   BioCyc; PANA932677:PAJ_RS16835-MON; -.
DR   Proteomes; UP000006690; Chromosome.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Vitamin C.
FT   CHAIN           1..296
FT                   /note="L-isoleucine 3(1)-dioxygenase"
FT                   /id="PRO_0000454109"
FT   BINDING         176
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q96323"
FT   BINDING         178
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q96323"
FT   BINDING         267
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q96323"
SQ   SEQUENCE   296 AA;  33019 MW;  2752933BFA748082 CRC64;
     MTDLLTLEPT QTILTGSKKT NFGYLESTDG VINFSIVKNI ILNGHHHGNV LYVIRNYASK
     AVCEKLAKNF DYRVTQSGGN RADDGFVLTN QIGATQFSRN GEQYIHEVNR VNQSVADLMK
     ATSAEDSESL FLNLTLEKEF LERGIHFGPA RFKNGYACFA TFRRWLDNGV MSLMPHEDMA
     QVDFAKEDGF EIANTQTVTA YNVCLEAAQG GGQLKIWNLI PDQVCRETLG VTRTGYPYPP
     HLLNETESLS VQLNAGDLYF MNACHLHGVS SVSEGSRLTA GRFIGKLNDR KVVYWT