ID   GLAH_CITK8              Reviewed;         325 AA.
AC   A8ANL5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=CKO_04006;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000822; ABV15078.1; -; Genomic_DNA.
DR   RefSeq; WP_012134770.1; NC_009792.1.
DR   AlphaFoldDB; A8ANL5; -.
DR   SMR; A8ANL5; -.
DR   STRING; 290338.CKO_04006; -.
DR   EnsemblBacteria; ABV15078; ABV15078; CKO_04006.
DR   GeneID; 45137653; -.
DR   KEGG; cko:CKO_04006; -.
DR   HOGENOM; CLU_075277_0_0_6; -.
DR   OMA; HNDGTFV; -.
DR   OrthoDB; 837705at2; -.
DR   Proteomes; UP000008148; 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; Reference proteome.
FT   CHAIN           1..325
FT                   /note="Glutarate 2-hydroxylase"
FT                   /id="PRO_1000064805"
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;  37243 MW;  7E8E0193F28D4769 CRC64;
     MNALTAVKTN ADSVTRSDAG FTFAPSVQSP RLLELTFSAK TTAQFLQQVE QWPVQALEYK
     SFLRFKVGQI LDALCGNQLQ PLLIKTLLDR AEGALLINAE GIDNVEQADE MVKLATAVAH
     LIGRSNYDAM SGQYYARFVV KNVDNSDSYL RQPHRVMELH NDGTYVEEVT DYVLMMKIDE
     QNMAGGNSLL LHLDDWEHLE RFFSHPLARR SMRFAAPPSK NVSHDVYHPV FDVDQQGRPV
     MRYIDQFVQP KDFEEGVWLS DLSDALETSK NILSVPVPVG KFLLINNLFW LHGRDRFTPH
     PDLRRELMRQ RGYFAYSTRC YQTHQ