ID   GLAH_ECO8A              Reviewed;         325 AA.
AC   B7M9A2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=ECIAI1_2755;
OS   Escherichia coli O8 (strain IAI1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI1;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU928160; CAQ99581.1; -; Genomic_DNA.
DR   RefSeq; WP_000993087.1; NC_011741.1.
DR   AlphaFoldDB; B7M9A2; -.
DR   SMR; B7M9A2; -.
DR   GeneID; 66673471; -.
DR   KEGG; ecr:ECIAI1_2755; -.
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_1000136866"
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;  37384 MW;  E065615720D6EA20 CRC64;
     MNALTAVHNN AVDSGQDYSG FTLIPSAQSP RLLELTFTEQ TTKQFLEQVA EWPVQALEYK
     SFLRFRVGKI LDDLCANQLQ PLLLKTLLNR AEGALLINAV GIDDVAQADE MVKLATAVAH
     LIGRSNFDAM SGQYYARFVV KNVDNSDSYL RQPHRVMELH NDGTYVEEIT DYVLMMKIDE
     QNMQGGNSLL LHLDDWEHLD HYFRHPLARR PMRFAAPPSK NVSKDVFHPV FDVDQQGRPV
     MRYIDQFVQP KDFEEGVWLS ELSDAIETSK GILSVPVPVG KFLLINNLFW LHGRDRFTPH
     PDLRRELMRQ RGYFAYATHH YQTHQ