Family Search for PF09995 (MPAB_Lcp_cat)

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PF09995 hits 38 sequences in PaperBLAST's database above the trusted cutoff. Showing hits to curated sequences only. Or see all hits or try another family.

Q1HUS3 endo-cleaving rubber dioxygenase (EC 1.13.11.87) from Nocardia farcinica (see 2 papers)
Aligns to 124:360 / 413 (57.4%), covers 89.1% of PF09995, 68.9 bits

A0A165QBG6 endo-cleaving rubber dioxygenase (EC 1.13.11.87) from Rhodococcus rhodochrous (see paper)
Aligns to 124:359 / 408 (57.8%), covers 89.1% of PF09995, 64.4 bits

lcp / Q3L8N0 endo-cleaving rubber dioxygenase Lcp (EC 1.13.11.87) from Streptomyces sp. (strain K30) (see 6 papers)
LCP_STRK3 / Q3L8N0 Rubber oxygenase; Latex clearing protein; b-type cytochrome Lcp; EC 1.13.-.- from Streptomyces sp. (strain K30) (see 5 papers)
Q3L8N0 exo-cleaving rubber dioxygenase (EC 1.13.11.85); endo-cleaving rubber dioxygenase (EC 1.13.11.87) from Streptomyces sp. K30 (see 9 papers)
Aligns to 127:361 / 407 (57.7%), covers 91.7% of PF09995, 56.0 bits

• function: Involved in the initial step of rubber degradation (PubMed:22950008, PubMed:15638519, PubMed:18606806). Catalyzes the oxidative C-C cleavage of poly(cis-1,4-isoprene) in synthetic as well as in natural rubber by the addition of oxygen (O2) to the double bonds, leading to a mixture of oligonucleotide-isoprenoids with terminal keto and aldehyde groups (endo-type cleavage) (PubMed:25819959, PubMed:24907333). The cleavage products are of different lengths, ranging from C20 (four isoprene units) to higher oligo-isoprenoids (PubMed:24907333). Is not able to cleave low- molecular-weight substrate analogs with isoprenoid structure such as squalene (1,4-trans-isoprenoid), carotenoids, or alpha-tocopherol (PubMed:24907333).
  cofactor: heme b (Binds 1 b-type heme group non-covalently per subunit.)
  disruption phenotype: Cells lacking this gene exhibit reduced growth in medium containing poly(cis-1,4-isoprene) as the sole carbon and energy source. Additionally, they show no detectable Lcp activity on latex overlay agar plates, being unable to form a clear zone and to produce aldehydes. Complementation with the wild-type lcp gene restores the wild-type phenotype.

H6N4Z1 endo-cleaving rubber dioxygenase (EC 1.13.11.87) from Gordonia polyisoprenivorans (see paper)
Aligns to 102:339 / 388 (61.3%), covers 91.3% of PF09995, 54.4 bits

MPAB_PENRF / W6R4H8 ER-bound oxygenase mpaB; Mycophenolic acid biosynthesis cluster protein B; EC 1.-.-.- from Penicillium roqueforti (strain FM164) (see paper)
Aligns to 81:296 / 298 (72.5%), covers 88.3% of PF09995, 33.5 bits

• function: ER-bound oxygenase; part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world obtained from a culture of Penicillium brevicompactum in 1893 (PubMed:26751579). MpaB catalyzes the oxidative cleavage the C19-C20 double bond in farnesyl-DHMP (FDHMP) to yield FDHMP-3C via a mycophenolic aldehyde intermediate (By similarity). The first step of the pathway is the synthesis of 5- methylorsellinic acid (5MOA) by the cytosolic polyketide synthase mpaC. 5MOA is then converted to the phthalide compound 5,7-dihydroxy-4,6- dimethylphthalide (DHMP) by the endoplasmic reticulum-bound cytochrome P450 monooxygenase mpaDE. MpaDE first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB). MpaDE then acts as a lactone synthase that catalyzes the ring closure to convert DHMB into DHMP. The next step is the prenylation of DHMP by the Golgi apparatus-associated prenyltransferase mpaA to yield farnesyl- DHMP (FDHMP). The ER-bound oxygenase mpaB then mediates the oxidative cleavage the C19-C20 double bond in FDHMP to yield FDHMP-3C via a mycophenolic aldehyde intermediate. The O-methyltransferase mpaG catalyzes the methylation of FDHMP-3C to yield MFDHMP-3C. After the cytosolic methylation of FDHMP-3C, MFDHMP-3C enters into peroxisomes probably via free diffusion due to its low molecular weight. Upon a peroxisomal CoA ligation reaction, catalyzed by a beta-oxidation component enzyme acyl-CoA ligase ACL891, MFDHMP-3C-CoA would then be restricted to peroxisomes for the following beta-oxidation pathway steps. The peroxisomal beta-oxidation machinery than converts MFDHMP- 3C-CoA into MPA_CoA, via a beta-oxidation chain-shortening process. Finally mpaH acts as a peroxisomal acyl-CoA hydrolase with high substrate specificity toward MPA-CoA to release the final product MPA (PubMed:26751579) (Probable).
  catalytic activity: 4-farnesyl-3,5-dihydroxy-6-methylphthalide + AH2 + 2 O2 = (4E,8E)-10-(4,6-dihydroxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5- yl)-4,8-dimethyldeca-4,8-dienoate + A + acetone + H(+) + H2O (RHEA:66688)
  disruption phenotype: Results in dramatic reduction in MPA production.

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