GLAH_ECO81
ID GLAH_ECO81 Reviewed; 325 AA.
AC B7MYW1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Glutarate 2-hydroxylase {ECO:0000255|HAMAP-Rule:MF_01083};
DE Short=G-2-H {ECO:0000255|HAMAP-Rule:MF_01083};
DE EC=1.14.11.64 {ECO:0000255|HAMAP-Rule:MF_01083};
GN Name=glaH {ECO:0000255|HAMAP-Rule:MF_01083}; OrderedLocusNames=ECED1_3112;
OS Escherichia coli O81 (strain ED1a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585397;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ED1a;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- FUNCTION: Acts as an alpha-ketoglutarate-dependent dioxygenase
CC catalyzing hydroxylation of glutarate (GA) to L-2-hydroxyglutarate
CC (L2HG). Functions in a L-lysine degradation pathway that proceeds via
CC cadaverine, glutarate and L-2-hydroxyglutarate. {ECO:0000255|HAMAP-
CC Rule:MF_01083}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + glutarate + O2 = (S)-2-hydroxyglutarate + CO2
CC + succinate; Xref=Rhea:RHEA:13821, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16782, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:30921; EC=1.14.11.64;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13822;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01083};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01083};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01083};
CC -!- PATHWAY: Amino-acid degradation. {ECO:0000255|HAMAP-Rule:MF_01083}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01083}.
CC -!- SIMILARITY: Belongs to the glutarate hydroxylase family.
CC {ECO:0000255|HAMAP-Rule:MF_01083}.
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DR EMBL; CU928162; CAR09278.2; -; Genomic_DNA.
DR RefSeq; WP_000993121.1; NC_011745.1.
DR AlphaFoldDB; B7MYW1; -.
DR SMR; B7MYW1; -.
DR EnsemblBacteria; CAR09278; CAR09278; ECED1_3112.
DR KEGG; ecq:ECED1_3112; -.
DR HOGENOM; CLU_075277_0_0_6; -.
DR OMA; HNDGTFV; -.
DR Proteomes; UP000000748; Chromosome.
DR GO; GO:0008198; F:ferrous iron binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106343; F:glutarate dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050498; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, with 2-oxoglutarate as one donor, and the other dehydrogenated; IEA:UniProtKB-UniRule.
DR GO; GO:0019477; P:L-lysine catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.60.130.10; -; 1.
DR HAMAP; MF_01083; glutarate_hydroxylase; 1.
DR InterPro; IPR015038; GlaH.
DR InterPro; IPR042098; TauD-like_sf.
DR Pfam; PF08943; CsiD; 1.
PE 3: Inferred from homology;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..325
FT /note="Glutarate 2-hydroxylase"
FT /id="PRO_1000149852"
FT BINDING 160
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01083"
FT BINDING 162
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01083"
FT BINDING 292
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01083"
SQ SEQUENCE 325 AA; 37367 MW; 2AA147DF944B9198 CRC64;
MNALTAVQNN AVDSGQDYSG FTLIPSAQSP RLLELTFTEQ TTNRFLEQVA EWPVQALEYK
SFLRFRVGKI LDDLCANQLQ PLLLKTLLNR AEGALLINAV GIDDVAQADE MVKLATAVAH
LIGRSNFDAM SGQYYARFVV KNVDNSDSYL RQPHRVMELH NDGTYVEEIT DYVLMMKIDE
QNMQGGNSLL LHLDDWEHLD LFFRHPLARR PMRFAAPPSK NVSKDVFHPV FDVDQQGRPV
MRYIDQFVQP KDFEEGVWLS ELSDTIETSK GTLSVPVPVG KFLLINNLFW LHGRDRFTPH
PDLRRELMRQ RGYFAYATHH YQTHQ