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Literature summary extracted from

  • Dailey, T.A.; Boynton, T.O.; Albetel, A.N.; Gerdes, S.; Johnson, M.K.; Dailey, H.A.
    Discovery and characterization of HemQ an essential heme biosynthetic pathway component (2010), J. Biol. Chem., 285, 25978-25986 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.98.5 expressed in Escherichia coli Bacillus subtilis
1.3.98.5 expressed in Escherichia coli Mycobacterium tuberculosis
1.3.98.5 expressed in Escherichia coli Streptomyces coelicolor
1.3.98.5 expressed in Escherichia coli Cutibacterium acnes
1.3.98.5 expression in Escherichia coli Bacillus subtilis
1.3.98.5 expression in Escherichia coli Mycobacterium tuberculosis
1.3.98.5 expression in Escherichia coli Streptomyces coelicolor

Protein Variants

EC Number Protein Variants Comment Organism
1.3.98.5 H156A the mutant shows less than 10% of wild type activity Mycobacterium tuberculosis
1.3.98.5 H156C the mutant shows less than 10% of wild type activity Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.98.5 Fe-coproporphyrin III + H2O2 Bacillus subtilis
-
 harderoheme III + CO2 + H2O
-
 ?
1.3.98.5 Fe-coproporphyrin III + H2O2 Mycobacterium tuberculosis
-
 harderoheme III + CO2 + H2O
-
 ?
1.3.98.5 Fe-coproporphyrin III + H2O2 Streptomyces coelicolor
-
 harderoheme III + CO2 + H2O
-
 ?
1.3.98.5 Fe-coproporphyrin III + H2O2 Cutibacterium acnes
-
 harderoheme III + CO2 + H2O
-
 ?
1.3.98.5 Fe-coproporphyrin III + H2O2 Bacillus subtilis overall reaction protoheme + CO2 + H2O
-
 ?
1.3.98.5 Fe-coproporphyrin III + H2O2 Mycobacterium tuberculosis overall reaction protoheme + CO2 + H2O
-
 ?
1.3.98.5 Fe-coproporphyrin III + H2O2 Streptomyces coelicolor overall reaction protoheme + CO2 + H2O
-
 ?
1.3.98.5 Fe-coproporphyrin III + H2O2 Cutibacterium acnes overall reaction protoheme + CO2 + H2O
-
 ?
1.3.98.5 harderoheme III + H2O2 Bacillus subtilis
-
 protoheme + CO2 + H2O
-
 ?
1.3.98.5 harderoheme III + H2O2 Mycobacterium tuberculosis
-
 protoheme + CO2 + H2O
-
 ?
1.3.98.5 harderoheme III + H2O2 Streptomyces coelicolor
-
 protoheme + CO2 + H2O
-
 ?
1.3.98.5 harderoheme III + H2O2 Cutibacterium acnes
-
 protoheme + CO2 + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.98.5 Bacillus subtilis
-
-
-
1.3.98.5 Cutibacterium acnes
-
-
-
1.3.98.5 Mycobacterium tuberculosis
-
-
-
1.3.98.5 Streptomyces coelicolor
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.98.5 HisPur metal chelate column chromatography and Sephacryl S-300 gel filtration Bacillus subtilis
1.3.98.5 HisPur metal chelate column chromatography and Sephacryl S-300 gel filtration Mycobacterium tuberculosis
1.3.98.5 HisPur metal chelate column chromatography and Sephacryl S-300 gel filtration Streptomyces coelicolor
1.3.98.5 HisPur metal chelate column chromatography and Sephacryl S-300 gel filtration Cutibacterium acnes

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.98.5 Fe-coproporphyrin III + H2O2
-
 Bacillus subtilis harderoheme III + CO2 + H2O
-
 ?
1.3.98.5 Fe-coproporphyrin III + H2O2
-
 Mycobacterium tuberculosis harderoheme III + CO2 + H2O
-
 ?
1.3.98.5 Fe-coproporphyrin III + H2O2
-
 Streptomyces coelicolor harderoheme III + CO2 + H2O
-
 ?
1.3.98.5 Fe-coproporphyrin III + H2O2
-
 Cutibacterium acnes harderoheme III + CO2 + H2O
-
 ?
1.3.98.5 Fe-coproporphyrin III + H2O2 overall reaction Bacillus subtilis protoheme + CO2 + H2O
-
 ?
1.3.98.5 Fe-coproporphyrin III + H2O2 overall reaction Mycobacterium tuberculosis protoheme + CO2 + H2O
-
 ?
1.3.98.5 Fe-coproporphyrin III + H2O2 overall reaction Streptomyces coelicolor protoheme + CO2 + H2O
-
 ?
1.3.98.5 Fe-coproporphyrin III + H2O2 overall reaction Cutibacterium acnes protoheme + CO2 + H2O
-
 ?
1.3.98.5 harderoheme III + H2O2
-
 Bacillus subtilis protoheme + CO2 + H2O
-
 ?
1.3.98.5 harderoheme III + H2O2
-
 Mycobacterium tuberculosis protoheme + CO2 + H2O
-
 ?
1.3.98.5 harderoheme III + H2O2
-
 Streptomyces coelicolor protoheme + CO2 + H2O
-
 ?
1.3.98.5 harderoheme III + H2O2
-
 Cutibacterium acnes protoheme + CO2 + H2O
-
 ?
1.3.98.5 additional information HemQ additionally possesses minimal peroxidase activity, and as a catalase it has a turnover of over 10000 per min Bacillus subtilis ?
-
 ?
1.3.98.5 additional information HemQ additionally possesses minimal peroxidase activity, and as a catalase it has a turnover of over 10000 per min Mycobacterium tuberculosis ?
-
 ?
1.3.98.5 additional information HemQ additionally possesses minimal peroxidase activity, and as a catalase it has a turnover of over 10000 per min Streptomyces coelicolor ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.98.5 ? x * 26000, SDS-PAGE Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
1.3.98.5 HemQ
-
 Bacillus subtilis
1.3.98.5 HemQ
-
 Mycobacterium tuberculosis
1.3.98.5 HemQ
-
 Streptomyces coelicolor
1.3.98.5 HemQ
-
 Cutibacterium acnes

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.98.5 heme
-
 Bacillus subtilis
1.3.98.5 heme
-
 Mycobacterium tuberculosis
1.3.98.5 heme
-
 Streptomyces coelicolor
1.3.98.5 heme
-
 Cutibacterium acnes
1.3.98.5 heme heme is a high spin ferric iron and is ligated by a conserved histidine with the sixth coordination site available for binding a small molecule Bacillus subtilis
1.3.98.5 heme heme is a high spin ferric iron and is ligated by a conserved histidine with the sixth coordination site available for binding a small molecule Mycobacterium tuberculosis
1.3.98.5 heme heme is a high spin ferric iron and is ligated by a conserved histidine with the sixth coordination site available for binding a small molecule Streptomyces coelicolor

General Information

EC Number General Information Comment Organism
1.3.98.5 metabolism the enzyme, along with the terminal two pathway enzymes protoporphyrinogen oxidase HemY and ferrochelatase is required to synthesize heme in vivo and in vitro Bacillus subtilis
1.3.98.5 metabolism the enzyme, along with the terminal two pathway enzymes protoporphyrinogen oxidase HemY and ferrochelatase is required to synthesize heme in vivo and in vitro Mycobacterium tuberculosis
1.3.98.5 metabolism the enzyme, along with the terminal two pathway enzymes protoporphyrinogen oxidase HemY and ferrochelatase is required to synthesize heme in vivo and in vitro Streptomyces coelicolor
1.3.98.5 metabolism the enzyme, along with the terminal two pathway enzymes protoporphyrinogen oxidase HemY and ferrochelatase is required to synthesize heme in vivo and in vitro Cutibacterium acnes
1.3.98.5 physiological function the presence of HemQ along with the terminal two pathway enzymes, protoporphyrinogen oxidase (HemY) and ferrochelatase, is required to synthesize heme in vivo and in vitro. To be fully functional in vitro, HemQ requires the presence of a bound heme Bacillus subtilis
1.3.98.5 physiological function the presence of HemQ along with the terminal two pathway enzymes, protoporphyrinogen oxidase (HemY) and ferrochelatase, is required to synthesize heme in vivo and in vitro. To be fully functional in vitro, HemQ requires the presence of a bound heme Mycobacterium tuberculosis
1.3.98.5 physiological function the presence of HemQ along with the terminal two pathway enzymes, protoporphyrinogen oxidase (HemY) and ferrochelatase, is required to synthesize heme in vivo and in vitro. To be fully functional in vitro, HemQ requires the presence of a bound heme Streptomyces coelicolor