HILB_PANAA
ID HILB_PANAA Reviewed; 247 AA.
AC A0A0H3L116;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=3(1)-hydroxy-L-isoleucine 4-dioxygenase {ECO:0000305};
DE EC=1.14.11.75 {ECO:0000269|PubMed:23554367};
DE AltName: Full=4'-hydroxy-L-isoleucine 4-dioxygenase {ECO:0000305};
GN Name=hilB {ECO:0000303|PubMed:23554367};
GN OrderedLocusNames=PAJ_3037 {ECO:0000312|EMBL:BAK13117.1};
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, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=AJ13355;
RX PubMed=22448874; DOI=10.1111/j.1574-6968.2012.02558.x;
RA Smirnov S.V., Sokolov P.M., Kodera T., Sugiyama M., Hibi M., Shimizu S.,
RA Yokozeki K., Ogawa J.;
RT "A novel family of bacterial dioxygenases that catalyse the hydroxylation
RT of free L-amino acids.";
RL FEMS Microbiol. Lett. 331:97-104(2012).
RN [3]
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-4'-hydroxyisoleucine (4'-
CC HIL) at the C-4 position to form L-4,4'-dihydroxyisoleucine (4,4'-
CC DIHIL) (PubMed:23554367). Together with HilA, catalyzes the two step
CC conversion of L-isoleucine into L-4,4'-dihydroxyisoleucine
CC (PubMed:23554367). In vitro, in the absence of HilA, can also catalyze
CC the oxidation of L-methionine and the C-4-hydroxylation of L-leucine
CC and L-isoleucine (PubMed:22448874). {ECO:0000269|PubMed:22448874,
CC ECO:0000269|PubMed:23554367}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 3(1)-hydroxy-L-isoleucine + O2 = (4S)-3(1),4-
CC dihydroxy-L-isoleucine + CO2 + succinate; Xref=Rhea:RHEA:63876,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:149627, ChEBI:CHEBI:149628;
CC EC=1.14.11.75; Evidence={ECO:0000269|PubMed:23554367};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63877;
CC Evidence={ECO:0000269|PubMed:23554367};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000269|PubMed:22448874, 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:22448874, ECO:0000269|PubMed:23554367};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:E2GIN1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 mM for L-methionine {ECO:0000269|PubMed:22448874};
CC KM=1.1 mM for L-leucine {ECO:0000269|PubMed:22448874};
CC KM=5.1 mM for L-isoleucine {ECO:0000269|PubMed:22448874};
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AP012032; BAK13117.1; -; Genomic_DNA.
DR RefSeq; WP_014594864.1; NC_017531.2.
DR SMR; A0A0H3L116; -.
DR STRING; 932677.PAJ_3037; -.
DR EnsemblBacteria; BAK13117; BAK13117; PAJ_3037.
DR KEGG; paj:PAJ_3037; -.
DR PATRIC; fig|932677.3.peg.3526; -.
DR eggNOG; COG4340; Bacteria.
DR HOGENOM; CLU_1140761_0_0_6; -.
DR OMA; KVFHAVT; -.
DR BioCyc; MetaCyc:MON-21132; -.
DR BioCyc; PANA932677:PAJ_RS16840-MON; -.
DR Proteomes; UP000006690; Chromosome.
DR GO; GO:0051213; F:dioxygenase activity; IDA:CACAO.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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 Dioxygenase; Iron; Metal-binding; Oxidoreductase; Vitamin C.
FT CHAIN 1..247
FT /note="3(1)-hydroxy-L-isoleucine 4-dioxygenase"
FT /id="PRO_0000454110"
FT BINDING 160
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q96323"
FT BINDING 162
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q96323"
FT BINDING 213
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q96323"
SQ SEQUENCE 247 AA; 28263 MW; 11604841C646DC9D CRC64;
MMEYATHLSR QGYAFIPGDY YRSTEAMQFS NKEDFLDELE ELKKGYENLL LDPYSPGNRW
RGYAQCKKNE KGELTFGKFN PYKQTKAFNP DTGDIIRDYP LLPEAITRNR LFQTLLHDDL
SLVDAYESIG PVDSLTIGIH FFRYQATENE PAYSSPVWLH KDDEDVVFVH MINASPNMLG
GDSLIASHPR SIDRVLRLEQ LFDTLVVNHD KLHAVTPVGA RENSGPAQRD IILITFQKNE
EKTACPV
