Family Search for PF10615 (DUF2470)

PF10615 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.

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 IXdelta + 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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