GLAH_SALTS
ID GLAH_SALTS Reviewed; 325 AA.
AC E1WA38; Q9FA43;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 03-AUG-2022, entry version 53.
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}; Synonyms=csiD;
GN OrderedLocusNames=SL1344_2773;
OS Salmonella typhimurium (strain SL1344).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=216597;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL1344;
RX PubMed=22538806; DOI=10.1073/pnas.1201061109;
RA Kroger C., Dillon S.C., Cameron A.D., Papenfort K., Sivasankaran S.K.,
RA Hokamp K., Chao Y., Sittka A., Hebrard M., Handler K., Colgan A.,
RA Leekitcharoenphon P., Langridge G.C., Lohan A.J., Loftus B., Lucchini S.,
RA Ussery D.W., Dorman C.J., Thomson N.R., Vogel J., Hinton J.C.;
RT "The transcriptional landscape and small RNAs of Salmonella enterica
RT serovar Typhimurium.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E1277-E1286(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-293.
RC STRAIN=SL1344;
RX PubMed=11083839; DOI=10.1128/iai.68.12.7126-7131.2000;
RA Valdivia R.H., Cirillo D.M., Lee A.K., Bouley D.M., Falkow S.;
RT "mig-14 is a horizontally acquired, host-induced gene required for
RT Salmonella enterica lethal infection in the murine model of typhoid
RT fever.";
RL Infect. Immun. 68:7126-7131(2000).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAG31208.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CBW18871.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; FQ312003; CBW18871.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF020810; AAG31208.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000993096.1; NZ_QASL01000009.1.
DR AlphaFoldDB; E1WA38; -.
DR SMR; E1WA38; -.
DR EnsemblBacteria; CBW18871; CBW18871; SL1344_2773.
DR KEGG; sey:SL1344_2773; -.
DR PATRIC; fig|216597.6.peg.3086; -.
DR HOGENOM; CLU_075277_0_0_6; -.
DR OMA; HNDGTFV; -.
DR BioCyc; SENT216597:SL1344_RS14440-MON; -.
DR Proteomes; UP000008962; 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_0000405413"
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"
FT CONFLICT 110
FT /note="E -> Q (in Ref. 2; AAG31208)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 325 AA; 37233 MW; 910DC08AE064CAC5 CRC64;
MNALTAVKAN TDDLAQRHTG FTLAPSAQSP RLLALTFTAD TTKQFLHQVA 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
