The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Cytochrome P450
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 29442: Cytochrome P450 monooxygenase PikC

There are 41 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Linalool 8-monooxygenase. [EC: 1.14.13.151]
Linalool + 2 NADH + 2 O(2) = (6E)-8-oxolinalool + 2 NAD(+) + 3 H(2)O.
  • The secondary electron donor is a specific [2Fe-2S] ferredoxin from the same bacterial strain.
  • Formerly EC 1.14.99.28.
504 A0A031JJ70 A0A031JJ70 A0A031JPC8 A0A031JPC8 A0A051TU92 A0A051TU92 A0A059MJY6 A0A059MJY6 A0A059MUY8 A0A059MUY8
(494 more...)
Cholest-4-en-3-one 26-monooxygenase ((25S)-3-oxocholest-4-en-26-oate forming). [EC: 1.14.13.141]
Cholest-4-en-3-one + 3 NADH + 3 O(2) = (25S)-3-oxocholest-4-en-26-oate + 3 NAD(+) + 4 H(2)O.
  • This enzyme, found in several bacterial pathogens, is involved in degradation of the host's cholesterol.
  • It catalyzes the hydroxylation of the C-26 carbon, followed by oxidation of the alcohol to the carboxylic acid via the aldehyde intermediate, initiating the degradation of the alkyl side-chain of cholesterol.
  • The products are exclusively in the (25S) conformation.
  • The enzyme also accepts cholesterol as a substrate.
  • Cf. EC 1.14.13.221.
170 A0A075V0B7 A0A075V0B7 A0A098BT96 A0A098BT96 A0A0C1LDE9 A0A0C1LDE9 A0A0E3VBC5 A0A0E3VBC5 A0A0E3VBM6 A0A0E3VBM6
(160 more...)
Pimeloyl-[acyl-carrier protein] synthase. [EC: 1.14.15.12]
A long-chain acyl-[acyl-carrier protein] + 2 reduced flavodoxin + 3 O(2) = pimeloyl-[acyl-carrier protein] + an n-alkanal + 2 oxidized flavodoxin + 3 H(2)O.
  • The enzyme catalyzes an oxidative C-C bond cleavage of long-chain acyl-[acyl-carrier protein]s of various lengths to generate pimeloyl- [acyl-carrier protein], an intermediate in the biosynthesis of biotin.
  • The preferred substrate of the enzyme from the bacterium Bacillus subtilis is palmitoyl-[acyl-carrier protein] which then gives heptanal as the alkanal.
  • The mechanism is similar to EC 1.14.15.6, followed by a hydroxylation step, which may occur spontaneously.
150 A0A0A0TXC5 A0A0A0TXC5 A0A0D1CR49 A0A0D1CR49 A0A0D8HEX4 A0A0D8HEX4 A0A0F7KRT8 A0A0F7KRT8 A0A0F7QM08 A0A0F7QM08
(140 more...)
Unspecific monooxygenase. [EC: 1.14.14.1]
RH + [reduced NADPH--hemoprotein reductase] + O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O.
  • Acts on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins; reactions catalyzed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S- and O-dealkylations, desulfation, deamination, and reduction of azo, nitro and N-oxide groups.
  • Together with EC 1.6.2.4, it forms a system in which two reducing equivalents are supplied by NADPH.
  • Some of the reactions attributed to EC 1.14.15.3 belong here.
  • Formerly EC 1.14.1.1, EC 1.14.14.2, EC 1.14.99.8 and EC 1.99.1.1.
130 A0A083ZRG8 A0A083ZRG8 A0A0D0QF07 A0A0D0QF07 A0A0D6HLK2 A0A0D6HLK2 A0A0D6J1N2 A0A0D6J1N2 A0A0E0UAU1 A0A0E0UAU1
(120 more...)
Peroxidase. [EC: 1.11.1.7]
2 phenolic donor + H(2)O(2) = 2 phenoxyl radical of the donor + 2 H(2)O.
    122 A0A0B9AWI8 A0A0B9AWI8 A0A0N0MQ14 A0A0N0MQ14 A0A0N0MRA5 A0A0N0MRA5 A0A0N0MRZ8 A0A0N0MRZ8 A0A0N0MTM0 A0A0N0MTM0
    (112 more...)
    Transferred entry: 1.14.13.151. [EC: 1.14.99.28]
      108 A0A1A9DRX9 A0A1A9DRX9 A0A1A9DTK4 A0A1A9DTK4 A0A1C4K283 A0A1C4K283 A0A1C4Q4N9 A0A1C4Q4N9 A0A1C4TTS1 A0A1C4TTS1
      (98 more...)
      Camphor 5-monooxygenase. [EC: 1.14.15.1]
      (+)-camphor + reduced putidaredoxin + O(2) = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H(2)O.
      • Also acts on (-)-camphor and 1,2-campholide, forming 5-exo-hydroxy- 1,2-campholide.
      102 A0A059MJ30 A0A059MJ30 A0A059MJ97 A0A059MJ97 A0A059MUU2 A0A059MUU2 A0A081RGT5 A0A081RGT5 A0A081RJT5 A0A081RJT5
      (92 more...)
      Pulcherriminic acid synthase. [EC: 1.14.15.13]
      Cyclo(L-leucyl-L-leucyl) + 6 reduced ferredoxin + 3 O(2) = pulcherriminic acid + 6 oxidized ferredoxin + 4 H(2)O.
      • A P450 enzyme from the bacterium Bacillus subtilis.
      • The order of events during the overall reaction is unknown.
      • Pulcherrimic acid spontaneously forms an iron chelate with Fe(3+) to form the red pigment pulcherrimin.
      60 A0A0C1P1N6 A0A0C1P1N6 A0A0D0TJI9 A0A0D0TJI9 A0A0D8BBV2 A0A0D8BBV2 A0A0K6JCX9 A0A0K6JCX9 A0A0K6JZZ2 A0A0K6JZZ2
      (50 more...)
      Pentalenic acid synthase. [EC: 1.14.15.11]
      1-deoxypentalenate + reduced ferredoxin + O(2) = pentalenate + oxidized ferredoxin + H(2)O.
      • Isolated from the bacterium Streptomyces avermitilis.
      • The product, pentalenate, is a co-metabolite from pentalenolactone biosynthesis.
      56 A0A0B8NDN6 A0A0B8NDN6 A0A0Q0HH78 A0A0Q0HH78 A0A0U5GZE5 A0A0U5GZE5 A0A0U5HHW4 A0A0U5HHW4 A0A0U5LBR7 A0A0U5LBR7
      (46 more...)
      Cholest-4-en-3-one 26-monooxygenase ((25R)-3-oxocholest-4-en-26-oate forming). [EC: 1.14.13.221]
      Cholest-4-en-3-one + 3 NADPH + 3 O(2) = (25R)-3-oxocholest-4-en-26-oate + 3 NADP(+) + 4 H(2)O.
      • This enzyme, found in several bacterial pathogens, is involved in degradation of the host cholesterol.
      • It catalyzes the hydroxylation of the C-26 carbon, followed by oxidation of the alcohol to the carboxylic acid via the aldehyde intermediate, initiating the degradation of the alkyl side-chain of cholesterol.
      • The products are exclusively in the (25R) conformation.
      • The enzyme also accepts cholesterol as a substrate.
      • Cf. EC 1.14.13.141.
      • The enzyme can receive electrons from ferredoxin reductase in vitro, its natural electron donor is not known yet.
      52 A0A045HBS7 A0A045HBS7 A0A045KDZ0 A0A045KDZ0 A0A083W380 A0A083W380 A0A0G4E3V7 A0A0G4E3V7 A0A0H3LC30 A0A0H3LC30
      (42 more...)
      Transferred entry: 1.14.15.15. [EC: 1.14.13.15]
        48 A0A075V335 A0A075V335 A0A076MB13 A0A076MB13 A0A0D6IDY5 A0A0D6IDY5 A0A0J6VK72 A0A0J6VK72 A0A0J6YLE7 A0A0J6YLE7
        (38 more...)
        Pentalenolactone synthase. [EC: 1.14.19.8]
        Pentalenolactone F + O(2) + 2 reduced ferredoxin + 2 H(+) = pentalenolactone + 2 oxidized ferredoxin + 2 H(2)O.
        • Isolated from the bacteria Streptomyces exfoliatus and Streptomyces arenae.
        • Formerly EC 1.3.7.10.
        40 A0A100J014 A0A100J014 A0A100JH85 A0A100JH85 A0A124C0R4 A0A124C0R4 A0A177HLF9 A0A177HLF9 A0A178X8W9 A0A178X8W9
        (30 more...)
        Methyl-branched lipid omega-hydroxylase. [EC: 1.14.15.14]
        A methyl-branched lipid + O(2) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) = an omega-hydroxy-methyl-branched lipid + H(2)O + 2 oxidized ferredoxin [iron-sulfur] cluster.
        • The enzyme, found in pathogenic and nonpathogenic mycobacteria species, actinomycetes, and some proteobacteria, hydroxylates the omega-carbon of a number of methyl-branched lipids, including (2E,6E)-farnesol, phytanate, geranylgeraniol, 15-methylpalmitate and (2E,6E)-farnesyl diphosphate.
        38 A0A045HBS7 A0A045HBS7 A0A083W380 A0A083W380 A0A0G4E3V7 A0A0G4E3V7 A0A0H3LC30 A0A0H3LC30 A0A0H3M6W3 A0A0H3M6W3
        (28 more...)
        Alkane 1-monooxygenase. [EC: 1.14.15.3]
        Octane + 2 reduced rubredoxin + O(2) + 2 H(+) = 1-octanol + 2 oxidized rubredoxin + H(2)O.
        • Some enzyme of this group are heme-thiolated proteins (P450).
        • Also hydroxylates fatty acids in the omega-position.
        36 A0A095CYT9 A0A095CYT9 A0A0L1KAC6 A0A0L1KAC6 A0A0M4MXM3 A0A0M4MXM3 A0A0W1ESB1 A0A0W1ESB1 A0A0W1G762 A0A0W1G762
        (26 more...)
        Cholestanetriol 26-monooxygenase. [EC: 1.14.15.15]
        5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol + 6 reduced adrenodoxin + 6 H(+) + 3 O(2) = (25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta- cholestan-26-oate + 6 oxidized adrenodoxin + 4 H(2)O.
        • Catalyzes the first three sterol side chain oxidations in bile acid biosynthesis via the neutral (classic) pathway.
        • Can also act on cholesterol, cholest-5-en-3-beta,7-alpha-diol, 7-alpha-hydroxycholest-4-en-3-one, and 5-beta-cholestane-3-alpha,7- alpha-diol.
        • The enzyme can also hydroxylate cholesterol at positions 24 and 25.
        • The initial source of the electrons is NADPH, which transfers the electrons to the adrenodoxin via EC 1.18.1.6.
        • Formerly EC 1.14.13.15.
        36 A0A178WNY5 A0A178WNY5 A0A178WYC7 A0A178WYC7 A0A178WZ95 A0A178WZ95 A0A178WZE6 A0A178WZE6 A0A1D8BYZ1 A0A1D8BYZ1
        (26 more...)
        Erythromycin 12 hydroxylase. [EC: 1.14.13.154]
        Erythromycin D + NADPH + O(2) = erythromycin C + NADP(+) + H(2)O.
        • The enzyme is responsible for the C-12 hydroxylation of the macrolactone ring, one of the last steps in erythromycin biosynthesis.
        • It shows 1200-1900-fold preference for erythromycin D over the alternative substrate erythromycin B.
        28 A0A011P4G0 A0A011P4G0 A0A075UN13 A0A075UN13 A0A089XDU0 A0A089XDU0 A0A0U5LDT4 A0A0U5LDT4 A0A0V8SRF5 A0A0V8SRF5
        (18 more...)
        Mycocyclosin synthase. [EC: 1.14.21.9]
        Cyclo(L-tyrosyl-L-tyrosyl) + NADPH + O(2) = mycocyclosin + NADP(+) + 2 H(2)O.
        • A P450 enzyme from the bacterium Mycobacterium tuberculosis catalyzing an oxidative reaction that does not incorporate oxygen into the product.
        28 A0A083W388 A0A083W388 A0A0G4E442 A0A0G4E442 A0A0H3M6X2 A0A0H3M6X2 A0A0T9WNE5 A0A0T9WNE5 A0A0U5LGE7 A0A0U5LGE7
        (18 more...)
        Pikromycin synthase. [EC: 1.14.13.185]
        (1) Narbomycin + NADPH + O(2) = pikromycin + NADP(+) + H(2)O. (2) Narbomycin + NADPH + O(2) = neopikromycin + NADP(+) + H(2)O. (3) Narbomycin + 2 NADPH + 2 O(2) = novapikromyin + 2 NADP(+) + 2 H(2)O. (4) 10-deoxymethymycin + NADPH + O(2) = methymycin + NADP(+) + H(2)O. (5) 10-deoxymethymycin + NADPH + O(2) = neomethymycin + NADP(+) + H(2)O. (6) 10-deoxymethymycin + 2 NADPH + 2 O(2) = novamethymycin + 2 NADP(+) + 2 H(2)O.
        • Involved in the biosynthesis of a number of bacterial macrolide antibiotics containing a desosamine glycoside unit.
        • With 10-deoxymethymycin it hydroxylates at either C-10 to give methymycin or C-12 to give neomethymycin.
        18 A0A0S2HKV8 A0A0S2HKV8 A0A143QBX2 A0A143QBX2 A0A1K2FHE5 A0A1K2FHE5 A0A1K2FMS5 A0A1K2FMS5 A0A1K2FP19 A0A1K2FP19
        (8 more...)
        Phthalate 4,5-dioxygenase. [EC: 1.14.12.7]
        Phthalate + NADH + O(2) = cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2- dicarboxylate + NAD(+).
        • A system, containing a reductase which is an iron-sulfur flavoprotein (FMN), an iron-sulfur oxygenase, and no independent ferredoxin.
        14 A0A031I935 A0A031I935 A0A0C1Z2F1 A0A0C1Z2F1 A0A158GIZ6 A0A158GIZ6 F6APX6 F6APX6 I4EXP4 I4EXP4
        (4 more...)
        Biflaviolin synthase. [EC: 1.14.21.7]
        (1) 2 flaviolin + NADPH + O(2) = 3,3'-biflaviolin + NADP(+) + 2 H(2)O. (2) 2 flaviolin + NADPH + O(2) = 3,8'-biflaviolin + NADP(+) + 2 H(2)O.
        • This cytochrome-P450 enzyme, from the soil-dwelling bacterium Streptomyces coelicolor A3(2), catalyzes a phenol oxidation C-C coupling reaction, which results in the polymerization of flaviolin to form biflaviolin or triflaviolin without the incorporation of oxygen into the product.
        • The products are highly conjugated pigments that protect the bacterium from the deleterious effects of UV irradiation.
        12 A0A1I9Z4C8 A0A1I9Z4C8 A0A1K2FQT0 A0A1K2FQT0 A0A1K2FW45 A0A1K2FW45 D6ESE9 D6ESE9 Q9FCA6 Q9FCA6
        (2 more...)
        Ribonuclease P. [EC: 3.1.26.5]
        Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
        • Essential for tRNA processing; generates 5'-termini of mature tRNA molecules.
        12 A0A081I0R0 A0A081I0R0 D5PEF5 D5PEF5 H8IRW0 H8IRW0 S4Z6A9 S4Z6A9 X8A2L1 X8A2L1
        (2 more...)
        1,8-cineole 2-endo-monooxygenase. [EC: 1.14.13.156]
        1,8-cineole + NADPH + O(2) = 2-endo-hydroxy-1,8-cineole + NADP(+) + H(2)O.
        • Isolated from the bacterium Citrobacter braakii, which can use 1,8- cineole as the sole source of carbon.
        10 A0A0J6VEL6 A0A0J6VEL6 A0A0J6Z7L8 A0A0J6Z7L8 A0A1J5P221 A0A1J5P221 A0A1L8QBN0 A0A1L8QBN0 Q8VQF6 Q8VQF6
        4-methoxybenzoate monooxygenase (O-demethylating). [EC: 1.14.99.15]
        4-methoxybenzoate + AH(2) + O(2) = 4-hydroxybenzoate + formaldehyde + A + H(2)O.
        • The bacterial enzyme consists of a ferredoxin-type protein and an iron-sulfur flavoprotein (FMN).
        • Also acts on 4-ethoxybenzoate, N-methyl-4-aminobenzoate and toluate.
        • The fungal enzyme acts best on veratrate.
        10 A0A143QDV9 A0A143QDV9 A0A143QJX9 A0A143QJX9 A0A165LED9 A0A165LED9 B3QAR3 B3QAR3 Q6N8N2 Q6N8N2
        6-deoxyerythronolide B hydroxylase. [EC: 1.14.13.188]
        6-deoxyerythronolide B + NADPH + O(2) = erythronolide B + NADP(+) + H(2)O.
        • Isolated from the bacterium Saccharopolyspora erythraea.
        • The enzyme is involved in the biosynthesis of the antibiotic erythromycin.
        8 A0A1B2GN10 A0A1B2GN10 A0A1B2GN54 A0A1B2GN54 Q00441 Q00441 T2S317 T2S317
        13-deoxydaunorubicin hydroxylase. [EC: 1.14.13.181]
        (1) 13-deoxydaunorubicin + NADPH + O(2) = 13-dihydrodaunorubicin + NADP(+) + H(2)O. (2) 13-dihydrodaunorubicin + NADPH + O(2) = daunorubicin + NADP(+) + 2 H(2)O.
        • The enzymes from the Gram-positive bacteria Streptomyces sp. C5 and Streptomyces peucetius show broad substrate specificity for structures based on an anthracycline aglycone, but have a strong preference for 4-methoxy anthracycline intermediates (13-deoxydaunorubicin and 13-dihydrodaunorubicin) over their 4-hydroxy analogs (13-deoxycarminomycin and 13-dihydrocarminomycin), as well as a preference for substrates hydroxylated at the C-13 rather than the C-14 position.
        6 Q59971 Q59971 Q93MI2 Q93MI2 Q9ZAU3 Q9ZAU3
        Sterol 14-alpha-demethylase. [EC: 1.14.13.70]
        A 14-alpha-methylsteroid + 3 O(2) + 3 NADPH = a Delta(14)-steroid + formate + 3 NADP(+) + 4 H(2)O.
        • This heme-thiolate (P450) enzyme acts on a range of steroids with a 14-alpha-methyl group, such as obtusifoliol and lanosterol.
        • The enzyme catalyzes two successive hydroxylations of the 14-alpha- methyl group, followed by elimination as formate, leaving a 14(15) double bond.
        4 A0A0T7PAW9 A0A0T7PAW9 A0A0U0S9P1 A0A0U0S9P1
        Ferredoxin--NAD(+) reductase. [EC: 1.18.1.3]
        Reduced ferredoxin + NAD(+) = oxidized ferredoxin + NADH.
        • The reaction is written for a [2Fe-2S] ferredoxin, which is characteristic of some mono- and dioxygenase systems.
        • some anaerobic bacteria have a 2[4Fe-4S] ferredoxin, which transfers two electrons.
        4 A0A085I0G9 A0A085I0G9 W6WGD6 W6WGD6
        Nitric oxide reductase (NAD(P)(+), nitrous oxide-forming). [EC: 1.7.1.14]
        Nitrous oxide + NAD(P)(+) + H(2)O = 2 nitric oxide + NAD(P)H.
        • The enzyme from Fusarium oxysporum utilizes only NADH, but the isozyme from Trichosporon cutaneum utilizes both NADH and NADPH.
        • The electron transfer from NAD(P)H to heme occurs directly, not requiring flavin or other redox cofactors.
        4 A0A084G7X3 A0A084G7X3 P23295 P23295
        Calcidiol 1-monooxygenase. [EC: 1.14.15.18]
        (1) Calcidiol + 2 reduced adrenodoxin + 2 H(+) + O(2) = calcitriol + 2 oxidized adrenodoxin + H(2)O. (2) Secalciferol + 2 reduced adrenodoxin + 2 H(+) + O(2) = calcitetrol + 2 oxidized adrenodoxin + H(2)O.
        • Formerly EC 1.14.13.13.
        4 A0A1K2FP09 A0A1K2FP09 A0A1K2G1B3 A0A1K2G1B3
        Vitamin D 1,25-hydroxylase. [EC: 1.14.15.22]
        (1) Calciol + O(2) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) = calcidiol + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O. (2) Calcidiol + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) + O(2) = calcitriol + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O.
        • An enzyme found in the bacterium Streptomyces griseolus.
        • Cf. EC 1.14.14.24 and EC 1.14.15.18.
        2 P18326 P18326
        UDP-N-acetylglucosamine 1-carboxyvinyltransferase. [EC: 2.5.1.7]
        Phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP- N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine.
          2 U2XTP1 U2XTP1
          Epi-isozizaene 5-monooxygenase. [EC: 1.14.13.106]
          (+)-epi-isozizaene + 2 NADPH + 2 O(2) = albaflavenone + 2 NADP(+) + 3 H(2)O.
          • This enzyme, from the soil-dwelling bacterium Streptomyces coelicolor A3(2), catalyzes two sequential allylic oxidation reactions.
          • The substrate epi-isozizaene, which is formed by the action of EC 4.2.3.37 is first oxidized to yield the epimeric intermediates (5R)-albaflavenol and (5S)-albaflavenol, which can be further oxidized to yield the sesquiterpenoid antibiotic albaflavenone.
          2 A0A1H8WHL0 A0A1H8WHL0
          [Acyl-carrier-protein] S-malonyltransferase. [EC: 2.3.1.39]
          Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier- protein].
          • Essential, along with EC 2.3.1.38, for the initiation of fatty-acid biosynthesis in bacteria.
          • Also provides the malonyl groups for polyketide biosynthesis.
          • The product of the reaction, malonyl-ACP, is an elongation substrate in fatty-acid biosynthesis.
          • In Mycobacterium tuberculosis, holo-ACP (the product of EC 2.7.8.7) is the preferred substrate.
          • This enzyme also forms part of the multienzyme complexes EC 4.1.1.88 and EC 4.1.1.89.
          • Malonylation of ACP is immediately followed by decarboxylation within the malonate-decarboxylase complex to yield acetyl-ACP, the catalytically active species of the decarboxylase.
          • In the enzyme from Klebsiella pneumoniae, methylmalonyl-CoA can also act as a substrate but acetyl-CoA cannot whereas the enzyme from Pseudomonas putida can use both as substrates.
          • The ACP subunit found in fatty-acid biosynthesis contains a pantetheine-4'-phosphate prosthetic group; that from malonate decarboxylase also contains pantetheine-4'-phosphate but in the form of a 2'-(5-triphosphoribosyl)-3'-dephospho-CoA prosthetic group.
          2 A0A0K3BQV0 A0A0K3BQV0
          2-hydroxy-5-methyl-1-naphthoate 7-hydroxylase. [EC: 1.14.99.49]
          2-hydroxy-5-methyl-1-naphthoate + reduced acceptor + O(2) = 2,7- dihydroxy-5-methyl-1-naphthoate + acceptor + H(2)O.
          • An enzyme involved in the synthesis of neocarzinostatin in the bacterium Streptomyces carzinostaticus.
          2 Q84HB6 Q84HB6
          Transferred entry: 1.7.2.5. [EC: 1.7.99.7]
            2 A2QPC1 A2QPC1
            Steroid 15-beta-monooxygenase. [EC: 1.14.15.8]
            Progesterone + 2 reduced [2Fe-2S] ferredoxin + O(2) = 15-beta- hydroxyprogesterone + 2 oxidized [2Fe-2S] ferredoxin + H(2)O.
            • The enzyme from Bacillus megaterium hydroxylates a variety of 3-oxo- Delta-4-steroids in position 15-beta.
            • Ring A-reduced, aromatic, and 3-beta-hydroxy-Delta-4-steroids do not serve as substrates.
            2 Q06069 Q06069
            5-methyl-1-naphthoate 3-hydroxylase. [EC: 1.14.13.189]
            5-methyl-1-naphthoate + NADPH + O(2) = 3-hydroxy-5-methyl-1-naphthoate + NADP(+) + H(2)O.
            • The enzyme from the bacterium Streptomyces sahachiroi is involved in the biosynthesis of 3-methoxy-5-methyl-1-naphthoate, a component of of the the antitumor antibiotic azinomycin B.
            2 B4XY99 B4XY99
            (2E,6E)-farnesyl diphosphate synthase. [EC: 2.5.1.10]
            Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)- farnesyl diphosphate.
            • Some forms of this enzyme will also use dimethylallyl diphosphate as a substrate.
            • The enzyme will not accept larger prenyl diphosphates as efficient donors.
            2 A0A0B7MLW9 A0A0B7MLW9
            Dephospho-CoA kinase. [EC: 2.7.1.24]
            ATP + 3'-dephospho-CoA = ADP + CoA.
              2 U2XUV4 U2XUV4
              3-deoxy-7-phosphoheptulonate synthase. [EC: 2.5.1.54]
              Phosphoenolpyruvate + D-erythrose 4-phosphate + H(2)O = 3-deoxy-D- arabino-hept-2-ulosonate 7-phosphate + phosphate.
              • Formerly EC 4.1.2.15.
              2 V6KL97 V6KL97
              20-oxo-5-O-mycaminosyltylactone 23-monooxygenase. [EC: 1.14.13.186]
              20-oxo-5-O-beta-mycaminosyltylactone + NADPH + O(2) = 5-O-beta- mycaminosyltylonolide + NADP(+) + H(2)O.
              • Involved in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria.
              2 Q9ZHQ1 Q9ZHQ1