ThiF family adenylyltransferase [Vibrio sp. 10N.286.46.A8]
Protein Classification
HesA/MoeB/ThiF family protein( domain architecture ID 11422192)
HesA/MoeB/ThiF family protein is an E1-like enzyme containing an NAD/FAD-binding fold that is involved in molybdopterin and thiamine biosynthesis
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| ThiF | COG0476 | Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ... |
3-249 | 1.75e-107 | |||||
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis : Pssm-ID: 440244 [Multi-domain] Cd Length: 244 Bit Score: 310.52 E-value: 1.75e-107
|
|||||||||
| Name | Accession | Description | Interval | E-value | |||||
| ThiF | COG0476 | Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ... |
3-249 | 1.75e-107 | |||||
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis Pssm-ID: 440244 [Multi-domain] Cd Length: 244 Bit Score: 310.52 E-value: 1.75e-107
|
|||||||||
| ThiF_MoeB_HesA_family | cd00757 | ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ... |
9-238 | 2.41e-103 | |||||
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1). Pssm-ID: 238386 [Multi-domain] Cd Length: 228 Bit Score: 299.39 E-value: 2.41e-103
|
|||||||||
| adenyl_thiF | TIGR02356 | thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ... |
9-211 | 3.55e-97 | |||||
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with the Escherichia. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the more widely distributed clade of ThiF proteins such found in E. coli. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine] Pssm-ID: 274094 Cd Length: 202 Bit Score: 283.09 E-value: 3.55e-97
|
|||||||||
| PRK05690 | PRK05690 | molybdopterin biosynthesis protein MoeB; Provisional |
1-244 | 2.29e-92 | |||||
molybdopterin biosynthesis protein MoeB; Provisional Pssm-ID: 180204 [Multi-domain] Cd Length: 245 Bit Score: 272.49 E-value: 2.29e-92
|
|||||||||
| ThiF | pfam00899 | ThiF family; This domain is found in ubiquitin activating E1 family and members of the ... |
10-246 | 3.19e-83 | |||||
ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1. Pssm-ID: 459987 [Multi-domain] Cd Length: 238 Bit Score: 248.71 E-value: 3.19e-83
|
|||||||||
| Name | Accession | Description | Interval | E-value | |||||
| ThiF | COG0476 | Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ... |
3-249 | 1.75e-107 | |||||
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis Pssm-ID: 440244 [Multi-domain] Cd Length: 244 Bit Score: 310.52 E-value: 1.75e-107
|
|||||||||
| ThiF_MoeB_HesA_family | cd00757 | ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ... |
9-238 | 2.41e-103 | |||||
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1). Pssm-ID: 238386 [Multi-domain] Cd Length: 228 Bit Score: 299.39 E-value: 2.41e-103
|
|||||||||
| adenyl_thiF | TIGR02356 | thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ... |
9-211 | 3.55e-97 | |||||
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with the Escherichia. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the more widely distributed clade of ThiF proteins such found in E. coli. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine] Pssm-ID: 274094 Cd Length: 202 Bit Score: 283.09 E-value: 3.55e-97
|
|||||||||
| PRK05690 | PRK05690 | molybdopterin biosynthesis protein MoeB; Provisional |
1-244 | 2.29e-92 | |||||
molybdopterin biosynthesis protein MoeB; Provisional Pssm-ID: 180204 [Multi-domain] Cd Length: 245 Bit Score: 272.49 E-value: 2.29e-92
|
|||||||||
| ThiF | pfam00899 | ThiF family; This domain is found in ubiquitin activating E1 family and members of the ... |
10-246 | 3.19e-83 | |||||
ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1. Pssm-ID: 459987 [Multi-domain] Cd Length: 238 Bit Score: 248.71 E-value: 3.19e-83
|
|||||||||
| PRK08762 | PRK08762 | molybdopterin-synthase adenylyltransferase MoeB; |
9-252 | 3.06e-70 | |||||
molybdopterin-synthase adenylyltransferase MoeB; Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 220.27 E-value: 3.06e-70
|
|||||||||
| PRK05597 | PRK05597 | molybdopterin biosynthesis protein MoeB; Validated |
9-243 | 6.77e-56 | |||||
molybdopterin biosynthesis protein MoeB; Validated Pssm-ID: 235526 [Multi-domain] Cd Length: 355 Bit Score: 182.76 E-value: 6.77e-56
|
|||||||||
| PRK07411 | PRK07411 | molybdopterin-synthase adenylyltransferase MoeB; |
2-246 | 6.04e-53 | |||||
molybdopterin-synthase adenylyltransferase MoeB; Pssm-ID: 180967 [Multi-domain] Cd Length: 390 Bit Score: 176.08 E-value: 6.04e-53
|
|||||||||
| PRK07878 | PRK07878 | molybdopterin biosynthesis-like protein MoeZ; Validated |
2-244 | 1.14e-49 | |||||
molybdopterin biosynthesis-like protein MoeZ; Validated Pssm-ID: 181156 [Multi-domain] Cd Length: 392 Bit Score: 167.58 E-value: 1.14e-49
|
|||||||||
| PRK07688 | PRK07688 | thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated |
9-235 | 6.79e-46 | |||||
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated Pssm-ID: 181084 [Multi-domain] Cd Length: 339 Bit Score: 156.69 E-value: 6.79e-46
|
|||||||||
| PRK05600 | PRK05600 | thiamine biosynthesis protein ThiF; Validated |
1-241 | 2.65e-42 | |||||
thiamine biosynthesis protein ThiF; Validated Pssm-ID: 235528 [Multi-domain] Cd Length: 370 Bit Score: 148.10 E-value: 2.65e-42
|
|||||||||
| E1_enzyme_family | cd01483 | Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ... |
31-163 | 1.03e-38 | |||||
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes classical ubiquitin-activating enzymes E1, ubiquitin-like (ubl) activating enzymes and other mechanistic homologes, like MoeB, Thif1 and others. The common reaction mechanism catalyzed by MoeB, ThiF and the E1 enzymes begins with a nucleophilic attack of the C-terminal carboxylate of MoaD, ThiS and ubiquitin, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. Pssm-ID: 238760 [Multi-domain] Cd Length: 143 Bit Score: 132.01 E-value: 1.03e-38
|
|||||||||
| PRK12475 | PRK12475 | thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional |
9-252 | 1.05e-38 | |||||
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional Pssm-ID: 183547 [Multi-domain] Cd Length: 338 Bit Score: 137.55 E-value: 1.05e-38
|
|||||||||
| PRK08328 | PRK08328 | hypothetical protein; Provisional |
1-212 | 7.93e-34 | |||||
hypothetical protein; Provisional Pssm-ID: 169382 [Multi-domain] Cd Length: 231 Bit Score: 122.21 E-value: 7.93e-34
|
|||||||||
| TcdA | COG1179 | tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ... |
19-149 | 3.65e-29 | |||||
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine dehydratase is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 440792 Cd Length: 247 Bit Score: 110.17 E-value: 3.65e-29
|
|||||||||
| YgdL_like | cd00755 | Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ... |
20-152 | 9.43e-29 | |||||
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli hypothetical protein ygdL. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown. Pssm-ID: 238384 [Multi-domain] Cd Length: 231 Bit Score: 108.85 E-value: 9.43e-29
|
|||||||||
| E1_ThiF_like | cd01487 | E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ... |
31-157 | 7.54e-27 | |||||
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown. Pssm-ID: 238764 [Multi-domain] Cd Length: 174 Bit Score: 102.46 E-value: 7.54e-27
|
|||||||||
| PRK08644 | PRK08644 | sulfur carrier protein ThiS adenylyltransferase ThiF; |
27-155 | 6.05e-26 | |||||
sulfur carrier protein ThiS adenylyltransferase ThiF; Pssm-ID: 236320 [Multi-domain] Cd Length: 212 Bit Score: 101.09 E-value: 6.05e-26
|
|||||||||
| thiF_fam2 | TIGR02354 | thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ... |
6-139 | 4.24e-23 | |||||
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with one the E. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the divergent clade of putative ThiF proteins such found in Campylobacter. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine] Pssm-ID: 162819 Cd Length: 200 Bit Score: 93.01 E-value: 4.24e-23
|
|||||||||
| Uba2_SUMO | cd01489 | Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ... |
32-173 | 2.37e-19 | |||||
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating enzyme (E1), specific for the SUMO family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by SUMO family of ubiquitin-like proteins (Ublps) is involved in cell division, nuclear transport, the stress response and signal transduction. UBA2 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2. Pssm-ID: 238766 [Multi-domain] Cd Length: 312 Bit Score: 85.51 E-value: 2.37e-19
|
|||||||||
| E1-2_like | cd01484 | Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ... |
32-173 | 6.03e-17 | |||||
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. A set of novel molecules with a structural similarity to Ub, called Ub-like proteins (Ubls), have similar conjugation cascades. In contrast to ubiquitin-E1, which is a single-chain protein with a weakly conserved two-fold repeat, many of the Ubls-E1are a heterodimer where each subunit corresponds to one half of a single-chain E1. This CD represents the family homologous to the second repeat of Ub-E1. Pssm-ID: 238761 [Multi-domain] Cd Length: 234 Bit Score: 77.62 E-value: 6.03e-17
|
|||||||||
| PRK08223 | PRK08223 | hypothetical protein; Validated |
19-163 | 2.55e-16 | |||||
hypothetical protein; Validated Pssm-ID: 181302 [Multi-domain] Cd Length: 287 Bit Score: 76.65 E-value: 2.55e-16
|
|||||||||
| Ube1 | TIGR01408 | ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ... |
9-157 | 4.42e-16 | |||||
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino acids, of a multicopy family of eukaryotic proteins, many of which are designated ubiquitin-activating enzyme E1. Members have two copies of the ThiF family domain (pfam00899), a repeat found in ubiquitin-activating proteins (pfam02134), and other regions. Pssm-ID: 273603 [Multi-domain] Cd Length: 1006 Bit Score: 77.62 E-value: 4.42e-16
|
|||||||||
| Ube1_repeat1 | cd01491 | Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ... |
10-163 | 1.28e-15 | |||||
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Ubiquitin-E1 is a single-chain protein with a weakly conserved two-fold repeat. This CD represents the first repeat of Ub-E1. Pssm-ID: 238768 [Multi-domain] Cd Length: 286 Bit Score: 74.61 E-value: 1.28e-15
|
|||||||||
| Aos1_SUMO | cd01492 | Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ... |
10-161 | 4.41e-15 | |||||
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating enzyme (E1), specific for the SUMO family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by SUMO family of ubiquitin-like proteins (Ublps) is involved in cell division, nuclear transport, the stress response and signal transduction. Aos1 contains part of the adenylation domain. Pssm-ID: 238769 [Multi-domain] Cd Length: 197 Bit Score: 71.55 E-value: 4.41e-15
|
|||||||||
| Uba3_RUB | cd01488 | Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ... |
31-184 | 7.20e-13 | |||||
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins. consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. UBA3 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2. Pssm-ID: 238765 [Multi-domain] Cd Length: 291 Bit Score: 67.00 E-value: 7.20e-13
|
|||||||||
| PRK15116 | PRK15116 | sulfur acceptor protein CsdL; Provisional |
20-158 | 7.30e-13 | |||||
sulfur acceptor protein CsdL; Provisional Pssm-ID: 185071 Cd Length: 268 Bit Score: 66.75 E-value: 7.30e-13
|
|||||||||
| Ube1_repeat2 | cd01490 | Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ... |
31-161 | 1.90e-12 | |||||
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Ubiquitin-E1 is a single-chain protein with a weakly conserved two-fold repeat. This CD represents the second repeat of Ub-E1. Pssm-ID: 238767 [Multi-domain] Cd Length: 435 Bit Score: 66.54 E-value: 1.90e-12
|
|||||||||
| E1-1_like | cd01485 | Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ... |
10-164 | 1.03e-11 | |||||
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. A set of novel molecules with a structural similarity to Ub, called Ub-like proteins (Ubls), have similar conjugation cascades. In contrast to ubiquitin-E1, which is a single-chain protein with a weakly conserved two-fold repeat, many of the Ubls-E1are a heterodimer where each subunit corresponds to one half of a single-chain E1. This CD represents the family homologous to the first repeat of Ub-E1. Pssm-ID: 238762 [Multi-domain] Cd Length: 198 Bit Score: 62.44 E-value: 1.03e-11
|
|||||||||
| PRK14852 | PRK14852 | hypothetical protein; Provisional |
8-162 | 1.29e-11 | |||||
hypothetical protein; Provisional Pssm-ID: 184854 [Multi-domain] Cd Length: 989 Bit Score: 64.33 E-value: 1.29e-11
|
|||||||||
| PRK14851 | PRK14851 | hypothetical protein; Provisional |
10-165 | 2.17e-11 | |||||
hypothetical protein; Provisional Pssm-ID: 184853 [Multi-domain] Cd Length: 679 Bit Score: 63.34 E-value: 2.17e-11
|
|||||||||
| APPBP1_RUB | cd01493 | Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ... |
9-96 | 4.08e-11 | |||||
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. ABPP1 contains part of the adenylation domain. Pssm-ID: 238770 [Multi-domain] Cd Length: 425 Bit Score: 62.32 E-value: 4.08e-11
|
|||||||||
| Ube1 | TIGR01408 | ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ... |
10-96 | 2.08e-09 | |||||
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino acids, of a multicopy family of eukaryotic proteins, many of which are designated ubiquitin-activating enzyme E1. Members have two copies of the ThiF family domain (pfam00899), a repeat found in ubiquitin-activating proteins (pfam02134), and other regions. Pssm-ID: 273603 [Multi-domain] Cd Length: 1006 Bit Score: 57.59 E-value: 2.08e-09
|
|||||||||
| NAD_bind_Shikimate_DH | cd01065 | NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ... |
21-60 | 1.55e-04 | |||||
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts. Pssm-ID: 133443 [Multi-domain] Cd Length: 155 Bit Score: 41.10 E-value: 1.55e-04
|
|||||||||
| Tdh | COG1063 | Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ... |
12-60 | 7.23e-04 | |||||
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway Pssm-ID: 440683 [Multi-domain] Cd Length: 341 Bit Score: 40.12 E-value: 7.23e-04
|
|||||||||
| MDR_TM0436_like | cd08231 | Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ... |
21-60 | 9.07e-04 | |||||
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This group contains the hypothetical TM0436 alcohol dehydrogenase from Thermotoga maritima, proteins annotated as 5-exo-alcohol dehydrogenase, and other members of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. MDR, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. Pssm-ID: 176193 [Multi-domain] Cd Length: 361 Bit Score: 39.94 E-value: 9.07e-04
|
|||||||||
| fabG | PRK08217 | 3-ketoacyl-(acyl-carrier-protein) reductase; Provisional |
28-88 | 1.13e-03 | |||||
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional Pssm-ID: 181297 [Multi-domain] Cd Length: 253 Bit Score: 39.56 E-value: 1.13e-03
|
|||||||||
| Zn_ADH8 | cd08262 | Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ... |
32-60 | 1.95e-03 | |||||
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Pssm-ID: 176223 [Multi-domain] Cd Length: 341 Bit Score: 38.83 E-value: 1.95e-03
|
|||||||||
| KR_FAS_SDR_x | cd05274 | ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ... |
27-59 | 2.76e-03 | |||||
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. Pssm-ID: 187582 [Multi-domain] Cd Length: 375 Bit Score: 38.52 E-value: 2.76e-03
|
|||||||||
| MDR | cd05188 | Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
29-127 | 3.49e-03 | |||||
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc. Pssm-ID: 176178 [Multi-domain] Cd Length: 271 Bit Score: 38.07 E-value: 3.49e-03
|
|||||||||
| Pyr_redox_2 | pfam07992 | Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
31-62 | 4.77e-03 | |||||
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain. Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 37.68 E-value: 4.77e-03
|
|||||||||
| AroE | COG0169 | Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ... |
29-60 | 5.48e-03 | |||||
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis Pssm-ID: 439939 [Multi-domain] Cd Length: 270 Bit Score: 37.43 E-value: 5.48e-03
|
|||||||||
| Apg7 | cd01486 | Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ... |
32-133 | 7.23e-03 | |||||
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and Apg8, and assigns them to specific E2 enzymes, Apg10 and Apg3, respectively. This leads to the covalent conjugation of Apg8 with phosphatidylethanolamine, an important step in autophagy. Autophagy is a dynamic membrane phenomenon for bulk protein degradation in the lysosome/vacuole. Pssm-ID: 238763 [Multi-domain] Cd Length: 307 Bit Score: 36.97 E-value: 7.23e-03
|
|||||||||
| Blast search parameters | ||||
|
