glutarate dioxygenase GlaH [Klebsiella pneumoniae].

LOCUS       WP_004147195             338 aa            linear   BCT 30-MAY-2022
ACCESSION   WP_004147195
VERSION     WP_004147195.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group;
            Klebsiella; Klebsiella pneumoniae complex.
REFERENCE   1  (residues 1 to 338)
  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 338)
  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..338
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     gene            1..338
                     /gene="glaH"
     Protein         1..338
                     /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=38679
     Region          20..335
                     /region_name="PRK02963"
                     /note="carbon starvation induced protein CsiD"
                     /db_xref="CDD:235092"
     Site            order(143,176,178,183,230,322,324)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238154"
     Site            order(173,175,201,305,318)
                     /site_type="active"
                     /db_xref="CDD:238154"
     Site            order(173,175,305)
                     /site_type="other"
                     /note="iron coordination sites [ion binding]"
                     /db_xref="CDD:238154"
ORIGIN      
        1 mnitltlqrg tilmnaltav kptpapvaqq ypgfsftpsa qsprlleltf saetttqflq
       61 qvaqwpvqal eyksflrfqv gkilddlcgn qlqplliktl ldraegalli ngegidhvsq
      121 aeemvklata vahligrsnf damsgqyyar fvvknvdnsd sylrqphrvm elhndgtyve
      181 eqtdyvlmmk ideqnmqggn slllhlddwe hldeffrdpl arrpmrwaap psknvskdvf
      241 hpvfdvdslg rpvmryidqf vqpkdfeegt wlsrlsdale tsknilsipv pvgkfllinn
      301 lfwlhgrdrf tphpdlrrel mrqrgyfays tnhyqthq