GLAH_ECO57
ID GLAH_ECO57 Reviewed; 325 AA.
AC Q8X954;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 94.
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};
GN OrderedLocusNames=Z3956, ECs3520;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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=AAG57766.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB36943.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG57766.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB36943.1; ALT_INIT; Genomic_DNA.
DR PIR; B85913; B85913.
DR PIR; H91068; H91068.
DR RefSeq; NP_311547.2; NC_002695.1.
DR RefSeq; WP_001301435.1; NZ_SEKU01000002.1.
DR AlphaFoldDB; Q8X954; -.
DR SMR; Q8X954; -.
DR STRING; 155864.EDL933_3822; -.
DR EnsemblBacteria; AAG57766; AAG57766; Z3956.
DR EnsemblBacteria; BAB36943; BAB36943; ECs_3520.
DR GeneID; 914764; -.
DR KEGG; ece:Z3956; -.
DR KEGG; ecs:ECs_3520; -.
DR PATRIC; fig|386585.9.peg.3674; -.
DR eggNOG; ENOG502Z8GB; Bacteria.
DR HOGENOM; CLU_075277_0_0_6; -.
DR OMA; HNDGTFV; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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_0000218179"
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; 37507 MW; B284FD758275CCF6 CRC64;
MNALTAVQNN AVDSDQDYSG FTLIPSAQSP RLLELTFTEQ TTKQFLEQVA EWPVQALEYK
SFLRFRVGKI LDDLCANQLQ PLLLKTLLNR AEGALLINAV GVDDVKQADE MVKLATAVAH
LIGRSNFDAM SGQYYARFVV KNVDNSDSYL RQPHRVMELH NDGTYVEEIT DYVLMMKIDE
QNMQGGNSLL LHLDDWEHLD HYFRHPMARR PMRFAAPPSK NVSKDVFHPV FDVDQQGRPV
MRYIDQFVQP KDFEEGVWLS ELSDAIEISK GILSVPVPVG KFLLINNLFW LHGRDRFTPH
PDLRRELMRQ RGYFAYATHH YQTHQ
