Family Search for PF10615 (DUF2470)

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PF10615 hits 37 sequences in PaperBLAST's database above the trusted cutoff. Showing hits to curated sequences only. Or see all hits or try another family.

HUGZ_HELPY / O25087 Heme oxygenase HugZ; EC 1.14.99.- from Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) (see 3 papers)
Aligns to 2:74 / 251 (29.1%), covers 98.7% of PF10615, 54.6 bits

• function: Involved in heme iron utilization (PubMed:19091096, PubMed:21030596). Catalyzes the degradation of heme to biliverdin, with the release of iron and carbon monoxide (PubMed:19091096, PubMed:21030596). Release of iron from heme may play a crucial role in the pathogenicity of H.pylori (PubMed:19091096).
  catalytic activity: 3 AH2 + 3 H(+) + heme b + 3 O2 = 3 A + biliverdin delta + CO + Fe(2+) + 3 H2O (RHEA:52224)
  subunit: Homodimer.
  disruption phenotype: Deletion mutant cannot utilize heme iron for normal growth.

GLUBP_ARATH / Q9LU39 Glutamyl-tRNA reductase-binding protein, chloroplastic; AtGluTRBP; GluTR-binding protein; Protein PROTON GRADIENT REGULATION 7 from Arabidopsis thaliana (Mouse-ear cress) (see 3 papers)
Aligns to 204:280 / 317 (24.3%), covers 93.5% of PF10615, 39.0 bits

• function: Involved in the regulation of glutamyl-tRNA reductase (GluTR) which is important for the synthesis and distribution of 5- aminolevulinate, a precursor in heme and chlorophyll biosynthesis (PubMed:22180625). Stimulates GluTR activity and regulates glutamate-1- semialdehyde release. May play a role in heme metabolism (PubMed:24753615). Necessary for efficient photosynthetic electron transport in chloroplasts (PubMed:20657737)
  subunit: Interacts with HEMA1 (PubMed:22180625, PubMed:24753615) and forms a heterotetramer of two GLUTRBP and two HEMA1 subunits (PubMed:24753615).
  disruption phenotype: Reduced growth, slightly pale green leaves, reduced levels of chlorophyll and heme, and low non-photochemical quenching (NPQ).

STR1_STRTC / A0A384XG60 Strobilurin A biosynthesis cluster protein r1 from Strobilurus tenacellus (see 3 papers)
Aligns to 19:89 / 207 (34.3%), covers 84.4% of PF10615, 38.8 bits

• function: Part of the gene cluster that mediates the biosynthesis of strobilurin A, an antifungal polyketide that contains a key beta- methoxyacrylate toxophore that targets the complex III of the mitochondrial electron transport chain (PubMed:30258052). Strobilurin biosynthesis begins with construction of benzoyl CoA by step-wise elimination of ammonia from phenylalanine by the phenylalanine ammonia- lyase str11, oxygenation by str8 and retro-Claisen reaction to form benzoic acid, which is activated to its CoA thiolester benzoyl CoA by the dedicated CoA ligase str10 (PubMed:30258052). Benzoyl CoA forms the starter unit for the highly reducing polyketide synthase stpks1 that produces the polyketide prestrobilutin A (PubMed:30258052). The FAD- dependent oxygenase str9 then catalyzes the key oxidative rearrangement responsible for the creation of the beta-methoxyacrylate toxophore (PubMed:30258052). Str9 performs epoxidation of the 2,3 olefin of prestrobilutin A, followed by Meinwald rearrangement to furnish the aldehyde intermediate (Probable). Rapid enolization of the aldehyde intermediate would give the beta-methoxyacrylate skeleton and methylations catalyzed by str2 and str3 complete the synthesis and lead to the production of strobilurin A (Probable). The short-chain dehydrogenase stl2 and the dehydrogenase str4 play a role in the shunt pathway leading to the production of bolineol (PubMed:30258052). The cluster encodes no obvious halogenase gene that could be involved in production of strobilurin B, nor any obvious dimethylallyl-transferase that could be involved in the production of strobilurin G (Probable). It is possible that unknown proteins encoded in, or near, the cluster (such as str1 or stl1) may form new classes of halogenases or dimethylally-transferases, or that the responsible genes are located elsewhere on the genome (Probable). Similarly, proteins encoded by str5/str6 hydrolases appear to have no chemical role in the biosynthesis of strobilurin A (Probable). Finally, no obvious self- resistance gene is found within the cluster (Probable).

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