HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ...
11-320
1.62e-139
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase biosynthesis. HypE dehydrates its own carbamoyl moiety in an ATP-dependent process to yield the enzyme thiocyanate. The N-terminal domain of HypE is related to the ATP-binding domains of the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP.
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Pssm-ID: 100033 [Multi-domain] Cd Length: 293 Bit Score: 397.59 E-value: 1.62e-139
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ...
11-320
1.62e-139
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase biosynthesis. HypE dehydrates its own carbamoyl moiety in an ATP-dependent process to yield the enzyme thiocyanate. The N-terminal domain of HypE is related to the ATP-binding domains of the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP.
Pssm-ID: 100033 [Multi-domain] Cd Length: 293 Bit Score: 397.59 E-value: 1.62e-139
hydrogenase expression/formation protein HypE; This family contains HypE (or HupE), a protein ...
16-351
1.87e-132
hydrogenase expression/formation protein HypE; This family contains HypE (or HupE), a protein required for expression of catalytically active hydrogenase in many systems. It appears to be an accessory protein involved in maturation rather than a regulatory protein involved in expression. HypE shows considerable homology to the thiamine-monophosphate kinase ThiL (TIGR01379) and other enzymes.
Pssm-ID: 273984 [Multi-domain] Cd Length: 320 Bit Score: 380.45 E-value: 1.87e-132
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ...
181-328
6.93e-23
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.
Pssm-ID: 460684 [Multi-domain] Cd Length: 152 Bit Score: 93.18 E-value: 6.93e-23
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ...
11-320
1.62e-139
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase biosynthesis. HypE dehydrates its own carbamoyl moiety in an ATP-dependent process to yield the enzyme thiocyanate. The N-terminal domain of HypE is related to the ATP-binding domains of the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP.
Pssm-ID: 100033 [Multi-domain] Cd Length: 293 Bit Score: 397.59 E-value: 1.62e-139
hydrogenase expression/formation protein HypE; This family contains HypE (or HupE), a protein ...
16-351
1.87e-132
hydrogenase expression/formation protein HypE; This family contains HypE (or HupE), a protein required for expression of catalytically active hydrogenase in many systems. It appears to be an accessory protein involved in maturation rather than a regulatory protein involved in expression. HypE shows considerable homology to the thiamine-monophosphate kinase ThiL (TIGR01379) and other enzymes.
Pssm-ID: 273984 [Multi-domain] Cd Length: 320 Bit Score: 380.45 E-value: 1.87e-132
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ...
51-319
5.26e-38
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM (formylglycinamidine ribonucleotide) synthase and Selenophosphate synthetase (SelD). The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.
Pssm-ID: 100027 [Multi-domain] Cd Length: 222 Bit Score: 135.22 E-value: 5.26e-38
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ...
13-319
7.77e-32
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM related proteins includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM synthase and Selenophosphate synthetase (SelD). They all contain two conserved domains and seem to dimerize. The N-terminal domain forms the dimer interface and is a putative ATP binding domain.
Pssm-ID: 100037 [Multi-domain] Cd Length: 298 Bit Score: 121.16 E-value: 7.77e-32
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ...
181-328
6.93e-23
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.
Pssm-ID: 460684 [Multi-domain] Cd Length: 152 Bit Score: 93.18 E-value: 6.93e-23
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ...
43-149
1.01e-20
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.
Pssm-ID: 459859 [Multi-domain] Cd Length: 104 Bit Score: 85.58 E-value: 1.01e-20
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ...
24-321
1.65e-15
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage of exogenous thiamine. Thiamine salvage occurs in two steps, with thiamine kinase catalyzing the formation of thiamine phosphate, and ThiL catalyzing the conversion of this intermediate to thiamine pyrophosphate. The N-terminal domain of ThiL binds ATP and is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, FGAM synthase and selenophosphate synthetase (SelD).
Pssm-ID: 100030 [Multi-domain] Cd Length: 291 Bit Score: 75.67 E-value: 1.65e-15
AIR synthase (PurM) related protein, archaeal subgroup 2 of unknown function. The family of ...
74-331
1.68e-09
AIR synthase (PurM) related protein, archaeal subgroup 2 of unknown function. The family of PurM related proteins includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM synthase and Selenophosphate synthetase (SelD). They all contain two conserved domains and seem to dimerize. The N-terminal domain forms the dimer interface and is a putative ATP binding domain.
Pssm-ID: 100036 Cd Length: 346 Bit Score: 58.55 E-value: 1.68e-09
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ...
72-308
4.59e-07
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM.
Pssm-ID: 100029 [Multi-domain] Cd Length: 272 Bit Score: 50.76 E-value: 4.59e-07
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ...
75-319
8.29e-06
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for purine biosynthesis, catalyzes the conversion of formylglycinamide ribonucleotide (FGAM) and ATP to AIR, ADP, and Pi, the fifth step in de novo purine biosynthesis. The N-terminal domain of PurM is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP.
Pssm-ID: 100032 [Multi-domain] Cd Length: 297 Bit Score: 46.70 E-value: 8.29e-06
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ...
179-323
1.15e-04
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM.
Pssm-ID: 100034 [Multi-domain] Cd Length: 313 Bit Score: 43.23 E-value: 1.15e-04
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and ...
43-323
1.47e-03
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and metabolism]; Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439816 [Multi-domain] Cd Length: 747 Bit Score: 40.42 E-value: 1.47e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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