Family Search for PF01937 (ARMT1-like_dom)

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Running HMMer for PF01937

PF01937 hits 42 sequences in PaperBLAST's database above the trusted cutoff. Showing hits to curated sequences only. Or see all hits or try another family.

ARMT1_HUMAN / Q9H993 Damage-control phosphatase ARMT1; Acidic residue methyltransferase 1; Protein-glutamate O-methyltransferase; Sugar phosphate phosphatase ARMT1; EC 3.1.3.-; EC 2.1.1.- from Homo sapiens (Human) (see 2 papers)
Aligns to 20:419 / 441 (90.7%), covers 100.0% of PF01937, 318.9 bits

• function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate (By similarity). Its preference for fructose-1- phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism (By similarity). Has also been shown to have O-methyltransferase activity that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues (PubMed:25732820). Possibly methylates PCNA, suggesting it is involved in the DNA damage response (PubMed:25732820).
  catalytic activity: beta-D-fructose 1-phosphate + H2O = D-fructose + phosphate (RHEA:35603)
  catalytic activity: beta-D-fructose 6-phosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone (RHEA:28002)
  catalytic activity: L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L- glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine (RHEA:24452)
  cofactor: Mn(2+) Ni(2+)

ART1A_SCHPO / Q9UT55 Damage-control phosphatase SPAC806.04c; Sugar phosphate phosphatase SPAC806.04c; EC 3.1.3.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
Aligns to 23:416 / 438 (90.0%), covers 99.4% of PF01937, 302.1 bits

• function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate (By similarity). Its preference for fructose-1- phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism (By similarity).
  catalytic activity: beta-D-fructose 1-phosphate + H2O = D-fructose + phosphate (RHEA:35603)
  catalytic activity: beta-D-fructose 6-phosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone (RHEA:28002)
  cofactor: Mn(2+) Ni(2+)

ARMT1_YEAST / Q04371 Damage-control phosphatase YMR027W; Sugar phosphate phosphatase YMR027W; EC 3.1.3.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 4 papers)
Aligns to 19:438 / 470 (89.4%), covers 99.7% of PF01937, 298.6 bits

• function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate (PubMed:27322068). Its preference for fructose-1- phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism (PubMed:27322068).
  catalytic activity: beta-D-fructose 1-phosphate + H2O = D-fructose + phosphate (RHEA:35603)
  catalytic activity: beta-D-fructose 6-phosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone (RHEA:28002)
  cofactor: Mn(2+) Ni(2+) (Phosphatase activity is strongly promoted by several divalent cations but it is suggested that Mn(2+) and possibly Ni(2+) represent biologically relevant metal ion cofactors for damage-control phosphatases.)
  disruption phenotype: Leads to the accumulation of fructose-1-phosphate (PubMed:27322068). Leads to increased DNA damage or decreased repair (PubMed:18085829).

ARMT1_PIMHY / Q8MMH3 Damage-control phosphatase ARMT1; Acidic residue methyltransferase 1; Protein-glutamate O-methyltransferase; Sugar phosphate phosphatase ARMT1; Venom protein 2; EC 3.1.3.-; EC 2.1.1.- from Pimpla hypochondriaca (Parasitoid wasp) (see paper)
Aligns to 59:456 / 488 (81.6%), covers 97.1% of PF01937, 267.8 bits

• function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate (By similarity). Its preference for fructose-1- phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism (By similarity). Has also been shown to have O-methyltransferase activity that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues (By similarity). Possibly methylates PCNA, suggesting it is involved in the DNA damage response (By similarity).
  catalytic activity: beta-D-fructose 1-phosphate + H2O = D-fructose + phosphate (RHEA:35603)
  catalytic activity: beta-D-fructose 6-phosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone (RHEA:28002)
  catalytic activity: L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L- glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine (RHEA:24452)
  cofactor: Mn(2+) Ni(2+)

D89S1_PYRHO / O59272 Damage-control phosphatase PH1575; Nucleotides phosphatase PH1575; EC 3.1.3.- from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see paper)
Aligns to 3:279 / 287 (96.5%), covers 99.4% of PF01937, 249.5 bits

• function: Metal-dependent phosphatase with probable damage-control functions (PubMed:27322068). Shows phosphatase activity against p- nitrophenyl phosphate (pNPP), but natural substrates have not been identified yet (PubMed:27322068). Low phosphatase activity against 8- oxo nucleotides suggests that it could hydrolyze oxidatively damaged purine nucleotides or their biosynthetic intermediates (PubMed:27322068).
  cofactor: Mn(2+) Ni(2+) (Phosphatase activity is strongly promoted by several divalent cation ions but it is suggested that Mn(2+) and possibly Ni(2+) represent biologically relevant metal ion cofactors for damage-control phosphatase activity (PubMed:27322068).)
  cofactor: [2Fe-2S] cluster (The [2Fe-2S] cluster does not seem to be directly involved in catalysis (PubMed:27322068).)

D89S2_ARATH / Q949P3 Damage-control phosphatase At2g17340; Sugar phosphates phosphatase At2g17340; EC 3.1.3.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
Aligns to 48:359 / 367 (85.0%), covers 99.7% of PF01937, 221.2 bits

• function: Metal-dependent phosphatase with probable damage-control functions (PubMed:27322068). Shows phosphatase activity against several substrates, including sugar phosphates and p-nitrophenyl phosphate(pNPP) (PubMed:27322068). Prefers sugar phosphate substrates, including the extremely potent glycating agents ribose-5-phosphate and erythrose-4-phosphate (PubMed:27322068).
  cofactor: Mn(2+) Ni(2+) (Phosphatase activity is strongly promoted by several divalent cations but it is suggested that Mn(2+) and possibly Ni(2+) represent biologically relevant metal ion cofactors for damage-control phosphatases.)
  subunit: Multimer.

PANK4_RAT / Q923S8 4'-phosphopantetheine phosphatase; Inactive pantothenic acid kinase 4; rPanK4; EC 3.1.3.- from Rattus norvegicus (Rat) (see paper)
Q923S8 pantothenate kinase (EC 2.7.1.33) from Rattus norvegicus (see paper)
Aligns to 451:764 / 773 (40.6%), covers 98.1% of PF01937, 178.9 bits

• function: Phosphatase which shows a preference for 4'- phosphopantetheine and its oxidatively damaged forms (sulfonate or S- sulfonate), providing strong indirect evidence that the phosphatase activity pre-empts damage in the coenzyme A (CoA) pathway. Hydrolyzing excess 4'-phosphopantetheine could constitute a directed overflow mechanism to prevent its oxidation to the S-sulfonate, sulfonate, or other forms. Hydrolyzing 4'-phosphopantetheine sulfonate or S-sulfonate would forestall their conversion to inactive forms of CoA and acyl carrier protein. May play a role in the physiological regulation of CoA intracellular levels.
  catalytic activity: (R)-4'-phosphopantetheine + H2O = (R)-pantetheine + phosphate (RHEA:68328)
  catalytic activity: (R)-4'-phosphopantetheine sulfonate + H2O = (R)-pantetheine sulfonate + phosphate (RHEA:68336)
  catalytic activity: (R)-4'-phospho-S-sulfopantetheine + H2O = (R)-S- sulfopantetheine + phosphate (RHEA:68340)
  cofactor: Mn(2+) Ni(2+)
  subunit: Homodimer. Interacts with PKM.

PANK4 / Q9NVE7 Pantothenate kinase 4 (EC 2.7.1.33) from Homo sapiens (see 11 papers)
PANK4_HUMAN / Q9NVE7 4'-phosphopantetheine phosphatase; Inactive pantothenic acid kinase 4; hPanK4; EC 3.1.3.- from Homo sapiens (Human) (see 4 papers)
Aligns to 450:764 / 773 (40.8%), covers 97.4% of PF01937, 177.5 bits

• function: Phosphatase which shows a preference for 4'- phosphopantetheine and its oxidatively damaged forms (sulfonate or S- sulfonate), providing strong indirect evidence that the phosphatase activity pre-empts damage in the coenzyme A (CoA) pathway (PubMed:27322068). Hydrolyzing excess 4'-phosphopantetheine could constitute a directed overflow mechanism to prevent its oxidation to the S-sulfonate, sulfonate, or other forms (PubMed:27322068). Hydrolyzing 4'-phosphopantetheine sulfonate or S-sulfonate would forestall their conversion to inactive forms of CoA and acyl carrier protein (PubMed:27322068). May play a role in the physiological regulation of CoA intracellular levels (Probable).
  catalytic activity: (R)-4'-phosphopantetheine + H2O = (R)-pantetheine + phosphate (RHEA:68328)
  catalytic activity: (R)-4'-phosphopantetheine sulfonate + H2O = (R)-pantetheine sulfonate + phosphate (RHEA:68336)
  catalytic activity: (R)-4'-phospho-S-sulfopantetheine + H2O = (R)-S- sulfopantetheine + phosphate (RHEA:68340)
  cofactor: Mn(2+) Ni(2+) (Phosphatase activity is strongly promoted by several divalent cation ions but it is suggested s that Mn(2+) and possibly Ni(2+) represent biologically relevant metal ion cofactors for damage-control phosphatases.)
  subunit: Homodimer. Interacts with PKM.

PANK4_MOUSE / Q80YV4 4'-phosphopantetheine phosphatase; Inactive pantothenic acid kinase 4; mPanK4; EC 3.1.3.- from Mus musculus (Mouse) (see paper)
Aligns to 451:811 / 820 (44.0%), covers 98.1% of PF01937, 171.4 bits

• function: Phosphatase which shows a preference for 4'- phosphopantetheine and its oxidatively damaged forms (sulfonate or S- sulfonate), providing strong indirect evidence that the phosphatase activity pre-empts damage in the coenzyme A (CoA) pathway. Hydrolyzing excess 4'-phosphopantetheine could constitute a directed overflow mechanism to prevent its oxidation to the S-sulfonate, sulfonate, or other forms. Hydrolyzing 4'-phosphopantetheine sulfonate or S-sulfonate would forestall their conversion to inactive forms of CoA and acyl carrier protein. May play a role in the physiological regulation of CoA intracellular levels.
  catalytic activity: (R)-4'-phosphopantetheine + H2O = (R)-pantetheine + phosphate (RHEA:68328)
  catalytic activity: (R)-4'-phosphopantetheine sulfonate + H2O = (R)-pantetheine sulfonate + phosphate (RHEA:68336)
  catalytic activity: (R)-4'-phospho-S-sulfopantetheine + H2O = (R)-S- sulfopantetheine + phosphate (RHEA:68340)
  cofactor: Mn(2+) Ni(2+)
  subunit: Homodimer. Interacts with PKM.
  disruption phenotype: Knockout mice have a body weight and a lifespan similar to wild-type animals. About 10% of the animals start developing cataract at 2 months. At 15 months, 50% homozygous animals are affected. Heterozygous animals develop cataract later, with 10% animals affected at 9 months and 25% at 15.

AtPANK2 / Q8L5Y9 pantothenate kinase (EC 2.7.1.33) from Arabidopsis thaliana (see 9 papers)
PANK2_ARATH / Q8L5Y9 Pantothenate kinase 2; AtPANK2; Pantothenic acid kinase 2; EC 2.7.1.33; EC 3.1.3.- from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
Aligns to 553:892 / 901 (37.7%), covers 90.0% of PF01937, 154.1 bits

• function: Catalyzes the phosphorylation of pantothenate the first step in CoA biosynthesis. May play a role in the physiological regulation of the intracellular CoA concentration. Functionally redudant with PANK1 (PubMed:16897480). The phosphatase activity shows preference for normal or oxidatively damaged intermediates of 4'-phosphopantetheine, which provides strong indirect evidence that the phosphatase activity pre- empts damage in the CoA pathway (PubMed:27322068). Hydrolyzing excess 4'-phosphopantetheine could constitute a directed overflow mechanism to prevent its oxidation to the S-sulfonate, sulfonate, or other forms (PubMed:27322068). Hydrolyzing 4'-phosphopantetheine sulfonate or S- sulfonate would forestall their conversion to inactive forms of CoA and acyl carrier protein (PubMed:27322068).
  catalytic activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+) (RHEA:16373)
  catalytic activity: (R)-4'-phosphopantothenate + H2O = (R)-pantothenate + phosphate (RHEA:68332)
  catalytic activity: (R)-4'-phosphopantetheine + H2O = (R)-pantetheine + phosphate (RHEA:68328)
  catalytic activity: (R)-4'-phosphopantetheine sulfonate + H2O = (R)-pantetheine sulfonate + phosphate (RHEA:68336)
  cofactor: Mn(2+) Ni(2+) (Phosphatase activity is strongly promoted by several divalent cation ions but it is suggested s that Mn(2+) and possibly Ni(2+) represent biologically relevant metal ion cofactors for damage-control phosphatases.)
  disruption phenotype: No visible phenotype under normal growth conditions, but homozygous double mutants pank1-1 and pank2-1 are embryonic lethal.

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