GLAH_ECOBW
ID GLAH_ECOBW Reviewed; 325 AA.
AC C4ZYR1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=BWG_2402;
OS Escherichia coli (strain K12 / MC4100 / BW2952).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=595496;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MC4100 / BW2952;
RX PubMed=19376874; DOI=10.1128/jb.00118-09;
RA Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA Wang L.;
RT "Genomic sequencing reveals regulatory mutations and recombinational events
RT in the widely used MC4100 lineage of Escherichia coli K-12.";
RL J. Bacteriol. 191:4025-4029(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; CP001396; ACR65010.1; -; Genomic_DNA.
DR RefSeq; WP_000993126.1; NC_012759.1.
DR AlphaFoldDB; C4ZYR1; -.
DR SMR; C4ZYR1; -.
DR KEGG; ebw:BWG_2402; -.
DR HOGENOM; CLU_075277_0_0_6; -.
DR OMA; HNDGTFV; -.
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_1000213519"
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; 37360 MW; AF403B3029E0B7F4 CRC64;
MNALTAVQNN AVDSGQDYSG FTLTPSAQSP RLLELTFTEQ TTKQFLEQVA EWPVQALEYK
SFLRFRVAKI LDDLCANQLQ PLLLKTLLNR AEGALLINAV GVDDVKQADE MVKLATAVAH
LIGRSNFDAM SGQYYARFVV KNVDNSDSYL RQPHRVMELH NDGTYVEEIT DYVLMMKIDE
QNMQGGNSLL LHLDDWEHLD NYFRHPLARR PMRFAAPPSK NVSKDVFHPV FDVDQQGRPV
MRYIDQFVQP KDFEEGVWLS ELSDAIETSK GILSVPVPVG KFLLINNLFW LHGRDRFTPH
PDLRRELMRQ RGYFAYASNH YQTHQ
