ID   GLAH_SALPA              Reviewed;         325 AA.
AC   Q5PEY3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=SPA2646;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV78510.1; -; Genomic_DNA.
DR   RefSeq; WP_000993100.1; NC_006511.1.
DR   AlphaFoldDB; Q5PEY3; -.
DR   SMR; Q5PEY3; -.
DR   EnsemblBacteria; AAV78510; AAV78510; SPA2646.
DR   KEGG; spt:SPA2646; -.
DR   HOGENOM; CLU_075277_0_0_6; -.
DR   OMA; HNDGTFV; -.
DR   Proteomes; UP000008185; 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_1000064812"
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;  37261 MW;  19D0C6D45589C416 CRC64;
     MNALTAVKAN TDDLAQRHTG FTLAPSAQSP RLLALTFTAD TTRQFLHQVA QWPVQALEYK
     SFLRFKIGKI LDDLCGNQLQ PLLIKTLLNR AQGALLISAE GIDDVAQAEE MVKLATAVAH
     LIGRSNYDAM SGQYYARFVV KNVDNSDSYL RQPHRVMELH NDGTYVEEVT DYVLMMKIDE
     QNMEGGNSLL LHLDDWEHLE SFFTHPLARR VMRWAAPPSK NVSHDVWHPV FDVDQQGRPV
     MRYIDQFVQP KDFEEGVWLS ELSDALETSQ NILSVPVPVG KFLLINNLFW LHGRDRFTPH
     PDLRRELMRQ RGYFAYAASH YQTHQ