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glutarate dioxygenase GlaH [Escherichia coli].


LOCUS       WP_001301435             325 aa            linear   BCT 30-MAY-2022
ACCESSION   WP_001301435
VERSION     WP_001301435.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Knorr,S., Sinn,M., Galetskiy,D., Williams,R.M., Wang,C., Muller,N.,
            Mayans,O., Schleheck,D. and Hartig,J.S.
  TITLE     Widespread bacterial lysine degradation proceeding via glutarate
            and L-2-hydroxyglutarate
  JOURNAL   Nat Commun 9 (1), 5071 (2018)
   PUBMED   30498244
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Marschall,C., Labrousse,V., Kreimer,M., Weichart,D., Kolb,A. and
            Hengge-Aronis,R.
  TITLE     Molecular analysis of the regulation of csiD, a carbon
            starvation-inducible gene in Escherichia coli that is exclusively
            dependent on sigma s and requires activation by cAMP-CRP
  JOURNAL   J Mol Biol 276 (2), 339-353 (1998)
   PUBMED   9512707
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF002814.1
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK02963
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..325
                     /gene="glaH"
     Protein         1..325
                     /product="glutarate dioxygenase GlaH"
                     /EC_number="1.14.11.64"
                     /GO_function="GO:0050498 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, with 2-oxoglutarate as one donor, and
                     the other dehydrogenated [Evidence IEA]"
                     /calculated_mol_wt=37376
     Region          7..322
                     /region_name="PRK02963"
                     /note="carbon starvation induced protein CsiD"
                     /db_xref="CDD:235092"
     Site            order(130,163,165,170,217,309,311)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238154"
     Site            order(160,162,188,292,305)
                     /site_type="active"
                     /db_xref="CDD:238154"
     Site            order(160,162,292)
                     /site_type="other"
                     /note="iron coordination sites [ion binding]"
                     /db_xref="CDD:238154"
ORIGIN      
        1 mnaltavqnn avdsdqdysg ftlipsaqsp rlleltfteq ttkqfleqva ewpvqaleyk
       61 sflrfrvgki lddlcanqlq plllktllnr aegallinav gvddvkqade mvklatavah
      121 ligrsnfdam sgqyyarfvv knvdnsdsyl rqphrvmelh ndgtyveeit dyvlmmkide
      181 qnmqggnsll lhlddwehld hyfrhpmarr pmrfaappsk nvskdvfhpv fdvdqqgrpv
      241 mryidqfvqp kdfeegvwls elsdaieisk gilsvpvpvg kfllinnlfw lhgrdrftph
      301 pdlrrelmrq rgyfayathh yqthq