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hydrogenase maturation carbamoyl dehydratase HypE [Escherichia


LOCUS       WP_001059937             336 aa            linear   BCT 10-JUL-2019
            coli].
ACCESSION   WP_001059937
VERSION     WP_001059937.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Blokesch,M., Albracht,S.P., Matzanke,B.F., Drapal,N.M., Jacobi,A.
            and Bock,A.
  TITLE     The complex between hydrogenase-maturation proteins HypC and HypD
            is an intermediate in the supply of cyanide to the active site iron
            of [NiFe]-hydrogenases
  JOURNAL   J. Mol. Biol. 344 (1), 155-167 (2004)
   PUBMED   15504408
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Jones,A.K., Lenz,O., Strack,A., Buhrke,T. and Friedrich,B.
  TITLE     NiFe hydrogenase active site biosynthesis: identification of Hyp
            protein complexes in Ralstonia eutropha
  JOURNAL   Biochemistry 43 (42), 13467-13477 (2004)
   PUBMED   15491154
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Blokesch,M., Paschos,A., Bauer,A., Reissmann,S., Drapal,N. and
            Bock,A.
  TITLE     Analysis of the transcarbamoylation-dehydration reaction catalyzed
            by the hydrogenase maturation proteins HypF and HypE
  JOURNAL   Eur. J. Biochem. 271 (16), 3428-3436 (2004)
   PUBMED   15291820
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Schwartz,E., Henne,A., Cramm,R., Eitinger,T., Friedrich,B. and
            Gottschalk,G.
  TITLE     Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16
            megaplasmid encoding key enzymes of H(2)-based ithoautotrophy and
            anaerobiosis
  JOURNAL   J. Mol. Biol. 332 (2), 369-383 (2003)
   PUBMED   12948488
REFERENCE   5  (residues 1 to 336)
  AUTHORS   Reissmann,S., Hochleitner,E., Wang,H., Paschos,A., Lottspeich,F.,
            Glass,R.S. and Bock,A.
  TITLE     Taming of a poison: biosynthesis of the NiFe-hydrogenase cyanide
            ligands
  JOURNAL   Science 299 (5609), 1067-1070 (2003)
   PUBMED   12586941
REFERENCE   6  (residues 1 to 336)
  AUTHORS   Lenz,O., Schwartz,E., Dernedde,J., Eitinger,M. and Friedrich,B.
  TITLE     The Alcaligenes eutrophus H16 hoxX gene participates in hydrogenase
            regulation
  JOURNAL   J. Bacteriol. 176 (14), 4385-4393 (1994)
   PUBMED   8021224
REFERENCE   7  (residues 1 to 336)
  AUTHORS   Dernedde,J., Eitinger,M. and Friedrich,B.
  TITLE     Analysis of a pleiotropic gene region involved in formation of
            catalytically active hydrogenases in Alcaligenes eutrophus H16
  JOURNAL   Arch. Microbiol. 159 (6), 545-553 (1993)
   PUBMED   8352644
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  :: BlastRule
            Evidence Accession :: NBR008104
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..336
                     /gene="hypE"
     Protein         1..336
                     /product="hydrogenase maturation carbamoyl dehydratase
                     HypE"
                     /EC_number="4.2.1.-"
                     /calculated_mol_wt=35023
     Region          15..336
                     /region_name="hypE"
                     /note="hydrogenase expression/formation protein HypE;
                     TIGR02124"
                     /db_xref="CDD:273984"
ORIGIN      
        1 mnniqlahgs ggqamqqlin slfmeafanp wlaeqedqar ldlaqlvaeg drlafstdsy
       61 vidplffpgg nigklaicgt andvavsgai prylscgfil eeglpmetlk avvtsmaeta
      121 rtagiaivtg dtkvvqrgaa dklfintagm gaiptnihwg aqtltagdil lvsgtlgdhg
      181 atilnlreql gldgelvsdc avltpliqtl rdipgvkalr datrggvnav vhefaaacgc
      241 gieisesalp vkpavrgvce llgldalnfa negklviave rnaaeqvlaa lhshplgkda
      301 aligevverk gvrlaglygv krtldlphae plpric