Family Search for PF09910 (DUF2139)
PF09910 hits 6 sequences in PaperBLAST's database above the trusted cutoff. Showing all hits. Or show only hits to curated sequences or try another family.
Q8U4F6 sucrose alpha-glucosidase (EC 3.2.1.48) from Pyrococcus furiosus (see paper)
AAL80256.1 α-glucosidase (PF0132) (EC 3.2.1.20) (see protein)
Aligns to 28:362 / 487 (68.8%), covers 99.7% of PF09910, 532.3 bits
PF0132 hypothetical protein from Pyrococcus furiosus DSM 3638
Aligns to 30:364 / 489 (68.5%), covers 99.7% of PF09910, 532.2 bits
- Genome-wide binding analysis of the transcriptional regulator TrmBL1 in Pyrococcus furiosus
Reichelt, BMC genomics 2016 - “...organisation Gene Gene product (Refseq) Additional information Position TGM relative to the promoter elements operon PF0132 PF0133 hypothetical protein hypothetical protein putative isomaltase - downstream singleton PF0196 glucose-6-phosphate isomerase - downstream singleton PF0272 alpha-amylase - downstream singleton PF0464 glyceraldehyde-3-phosphate: ferredoxin oxidoreductase - downstream singleton PF0477 alpha-amylase...”
- “...of P. furiosus grown on maltose or peptides are underlined [ 54 ]. Gene products: PF0132, proposed -glucosidase; PF0196, phosphoglucose isomerase; PF0272, proposed 4--glucanotransferase; PF0287, pyrolysin; PF0464, glycerinaldehyde 3-phosphate:ferredoxin oxidoreductase; PF0477, proposed extracellular -amylase. PF0478, proposed extracellular cyclomaltodextrin glucano-transferase; PF0505, putative DNA binding protein; PF0588, phosphoglucose...”
- Functional-genomics-based identification and characterization of open reading frames encoding alpha-glucoside-processing enzymes in the hyperthermophilic archaeon Pyrococcus furiosus
Comfort, Applied and environmental microbiology 2008 - “...led to the identification of a novel isomaltase (PF0132) representing a new glycoside hydrolase (GH) family, a novel GH57 -amylase (PF0870), and an...”
- “...maltodextrin by PF0272 (8). The transcriptional response of PF0132 indicated that it is likely involved in processing -1,6-glucans. Since a recombinant version...”
- Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction
Anderson, Journal of bacteriology 2008 - “...be identified, and there is no homolog of PF0132, which encodes the invertase purified from P. furiosus (27). Genes encoding three glycosidases (Tpen_1511,...”
- Impact of substrate glycoside linkage and elemental sulfur on bioenergetics of and hydrogen production by the hyperthermophilic archaeon Pyrococcus furiosus
Chou, Applied and environmental microbiology 2007 - “...be hydrolyzed into glucose by a novel isomaltase (PF0132) (12) (Comfort and Kelly, unpublished data) and converted to glucose-6-phosphate by an ADP-dependent...”
- “...glucokinase (PF0312) (26). The transcription level of PF0132 was constitutively high under all conditions but was extraordinarily high in the culture...”
- Transcriptional and biochemical analysis of starch metabolism in the hyperthermophilic archaeon Pyrococcus furiosus
Lee, Journal of bacteriology 2006 - “...and maltose metabolism Cellular locationa Annotation PF0132 PF0272 PF0312 PF0477 PF0478* PF0588 PF1256 PF1535 PF1739 -Glucosidase 4--Glucanotransferase...”
- “...using N-terminal sequencing as the product of gene PF0132. This protein does not show sequence similarity to any known -glucosidase or any characterized protein...”
Desfe_0611 DUF2139 domain-containing protein from Desulfurococcus amylolyticus DSM 16532
Aligns to 28:369 / 489 (69.9%), covers 99.7% of PF09910, 519.2 bits
MA03_04210 DUF2139 domain-containing protein from Thermofilum uzonense
Aligns to 30:368 / 487 (69.6%), covers 99.7% of PF09910, 498.8 bits
SSO3037 Hypothetical protein from Sulfolobus solfataricus P2
Aligns to 37:144 / 159 (67.9%), covers 27.9% of PF09910, 53.0 bits
SSO3038 Hypothetical protein from Sulfolobus solfataricus P2
Aligns to 1:213 / 306 (69.6%), covers 62.6% of PF09910, 28.2 bits
Or search for genetic data about PF09910 in the Fitness Browser
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory