KEGG   ORTHOLOGY: K14366Help
Entry
K14366                      KO                                     

Name
eryF, CYP107A
Definition
6-deoxyerythronolide B hydroxylase [EC:1.14.15.35]
Pathway
ko00522  Biosynthesis of 12-, 14- and 16-membered macrolides
ko01052  Type I polyketide structures
ko01100  Metabolic pathways
ko01130  Biosynthesis of antibiotics
Module
M00774  Erythromycin biosynthesis, propanoyl-CoA + methylmalonyl-CoA => deoxyerythronolide B => erythromycin A/B
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09109 Metabolism of terpenoids and polyketides
   01052 Type I polyketide structures
    K14366  eryF, CYP107A; 6-deoxyerythronolide B hydroxylase
   00522 Biosynthesis of 12-, 14- and 16-membered macrolides
    K14366  eryF, CYP107A; 6-deoxyerythronolide B hydroxylase
 09180 Brite Hierarchies
  09181 Protein families: metabolism
   01008 Polyketide biosynthesis proteins
    K14366  eryF, CYP107A; 6-deoxyerythronolide B hydroxylase
   00199 Cytochrome P450
    K14366  eryF, CYP107A; 6-deoxyerythronolide B hydroxylase
Enzymes [BR:ko01000]
 1. Oxidoreductases
  1.14  Acting on paired donors, with incorporation or reduction of molecular oxygen
   1.14.15  With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
    1.14.15.35  6-deoxyerythronolide B hydroxylase
     K14366  eryF, CYP107A; 6-deoxyerythronolide B hydroxylase
Polyketide biosynthesis proteins [BR:ko01008]
 Polyketide tailoring proteins
  Oxygenase
   K14366  eryF, CYP107A; 6-deoxyerythronolide B hydroxylase
Cytochrome P450 [BR:ko00199]
 Cytochrome P450, bacteria type
  CYP107 family
   K14366  eryF, CYP107A; 6-deoxyerythronolide B hydroxylase
BRITE hierarchy
Other DBs
RN: R05270
COG: COG2124
Genes
AER: AERYTH_15880
SEN: SACE_0730(eryF)
AEY: CDG81_13145
TaxonomyKoalaUniProt
Reference
PMID:2011746
  Authors
Weber JM, Leung JO, Swanson SJ, Idler KB, McAlpine JB
  Title
An erythromycin derivative produced by targeted gene disruption in Saccharopolyspora erythraea.
  Journal
Science 252:114-7 (1991)
DOI:10.1126/science.2011746
  Sequence
[sen:SACE_0730]
Reference
  Authors
Savino C, Montemiglio LC, Sciara G, Miele AE, Kendrew SG, Jemth P, Gianni S, Vallone B
  Title
Investigating the structural plasticity of a cytochrome P450: three-dimensional structures of P450 EryK and binding to its physiological substrate.
  Journal
J Biol Chem 284:29170-9 (2009)
DOI:10.1074/jbc.M109.003590

KEGG   ENZYME: 1.14.15.35Help
Entry
EC 1.14.15.35               Enzyme                                 

Name
6-deoxyerythronolide B hydroxylase;
DEB hydroxylase;
eryF (gene name);
P450(eryF);
CYP107A1
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
6-deoxyerythronolide-B,reduced ferredoxin:oxygen oxidoreductase
Reaction(IUBMB)
6-deoxyerythronolide B + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = erythronolide B + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O [RN:R05270]
Reaction(KEGG)
Substrate
6-deoxyerythronolide B [CPD:C03240];
reduced ferredoxin [iron-sulfur] cluster [CPD:C00138];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
erythronolide B [CPD:C06635];
oxidized ferredoxin [iron-sulfur] cluster [CPD:C00139];
H2O [CPD:C00001]
Comment
A cytochrome P-450 (heme-thiolate) protein isolated from the bacterium Saccharopolyspora erythraea. The enzyme is involved in the biosynthesis of the antibiotic erythromycin.
History
EC 1.14.15.35 created 2014 as EC 1.14.13.188, transferred 2018 to EC 1.14.15.35
Pathway
ec00522  Biosynthesis of 12-, 14- and 16-membered macrolides
ec01100  Metabolic pathways
ec01130  Biosynthesis of antibiotics
Orthology
K14366  6-deoxyerythronolide B hydroxylase
Genes
AER: AERYTH_15880
SEN: SACE_0730(eryF)
AEY: CDG81_13145
Taxonomy
Reference
1  [PMID:2011746]
  Authors
Weber JM, Leung JO, Swanson SJ, Idler KB, McAlpine JB
  Title
An erythromycin derivative produced by targeted gene disruption in Saccharopolyspora erythraea.
  Journal
Science 252:114-7 (1991)
DOI:10.1126/science.2011746
  Sequence
[sen:SACE_0730]
Reference
2  [PMID:2446657]
  Authors
Shafiee A, Hutchinson CR
  Title
Macrolide antibiotic biosynthesis: isolation and properties of two forms of 6-deoxyerythronolide B hydroxylase from Saccharopolyspora erythraea (Streptomyces erythreus).
  Journal
Biochemistry 26:6204-10 (1987)
Reference
3  [PMID:7846029]
  Authors
Cupp-Vickery JR, Li H, Poulos TL
  Title
Preliminary crystallographic analysis of an enzyme involved in erythromycin biosynthesis: cytochrome P450eryF.
  Journal
Proteins 20:197-201 (1994)
DOI:10.1002/prot.340200210
Reference
4  [PMID:15824115]
  Authors
Nagano S, Cupp-Vickery JR, Poulos TL
  Title
Crystal structures of the ferrous dioxygen complex of wild-type cytochrome P450eryF and its mutants, A245S and A245T: investigation of the proton transfer system in P450eryF.
  Journal
J Biol Chem 280:22102-7 (2005)
DOI:10.1074/jbc.M501732200
  Sequence
[sen:SACE_0730]
Other DBs
ExplorEnz - The Enzyme Database: 1.14.15.35
IUBMB Enzyme Nomenclature: 1.14.15.35
ExPASy - ENZYME nomenclature database: 1.14.15.35
BRENDA, the Enzyme Database: 1.14.15.35

KEGG   REACTION: R05270Help
Entry
R05270                      Reaction                               

Name
6-deoxyerythronolide-B,reduced ferredoxin:oxygen oxidoreductase
Definition
6-Deoxyerythronolide B + 2 Reduced ferredoxin + 2 H+ + Oxygen <=> Erythronolide B + 2 Oxidized ferredoxin + H2O
Equation
Reaction class
RC01315  C03240_C06635
Enzyme
Pathway
rn00522  Biosynthesis of 12-, 14- and 16-membered macrolides
rn01100  Metabolic pathways
rn01130  Biosynthesis of antibiotics
Module
M00774  Erythromycin biosynthesis, propanoyl-CoA + methylmalonyl-CoA => deoxyerythronolide B => erythromycin A/B
Orthology
K14366  6-deoxyerythronolide B hydroxylase [EC:1.14.15.35]
Other DBs
RHEA: 40302

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