pyruvate:ferredoxin (flavodoxin) oxidoreductase [Enterobacter quasiroggenkampii]
Protein Classification
pyruvate:ferredoxin (flavodoxin) oxidoreductase( domain architecture ID 1000199)
pyruvate:ferredoxin (flavodoxin) oxidoreductase catalyzes the interconversion of pyruvate and acetyl-CoA, the electron acceptor being either ferredoxin or flavodoxin
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||||||||||
| pyruv_ox_red super family | cl31176 | pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single ... |
1-1166 | 0e+00 | ||||||||||||||||
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single chain form of pyruvate:ferredoxin (or flavodoxin) oxidoreductase. This enzyme may transfer electrons to nitrogenase in nitrogen-fixing species. Portions of this protein are homologous to gamma subunit of the four subunit pyruvate:ferredoxin (flavodoxin) oxidoreductase. The actual alignment was detected with superfamily member TIGR02176: Pssm-ID: 131231 [Multi-domain] Cd Length: 1165 Bit Score: 1608.67 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||||||||||||
| pyruv_ox_red | TIGR02176 | pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single ... |
1-1166 | 0e+00 | ||||||||||||||||
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single chain form of pyruvate:ferredoxin (or flavodoxin) oxidoreductase. This enzyme may transfer electrons to nitrogenase in nitrogen-fixing species. Portions of this protein are homologous to gamma subunit of the four subunit pyruvate:ferredoxin (flavodoxin) oxidoreductase. Pssm-ID: 131231 [Multi-domain] Cd Length: 1165 Bit Score: 1608.67 E-value: 0e+00
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| TPP_PFOR_PNO | cd03377 | Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ... |
811-1166 | 0e+00 | ||||||||||||||||
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of proteins similar to the single subunit pyruvate ferredoxin oxidoreductase (PFOR) of Desulfovibrio Africanus, present in bacteria and amitochondriate eukaryotes. This subfamily also includes proteins characterized as pyruvate NADP+ oxidoreductase (PNO). These enzymes are dependent on TPP and a divalent metal cation as cofactors. PFOR and PNO catalyze the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. The PFOR from cyanobacterium Anabaena (NifJ) is required for the transfer of electrons from pyruvate to flavodoxin, which reduces nitrogenase. The facultative anaerobic mitochondrion of the photosynthetic protist Euglena gracilis oxidizes pyruvate with PNO. Pssm-ID: 239472 Cd Length: 365 Bit Score: 626.17 E-value: 0e+00
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| PorA | COG0674 | Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha ... |
1-394 | 4.08e-126 | ||||||||||||||||
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha subunit is part of the Pathway/BioSystem: Pyruvate oxidation Pssm-ID: 440438 [Multi-domain] Cd Length: 372 Bit Score: 391.36 E-value: 4.08e-126
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| POR_N | pfam01855 | Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N ... |
13-243 | 2.12e-96 | ||||||||||||||||
Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N terminal structural domain of the pyruvate ferredoxin oxidoreductase. This domain binds thiamine diphosphate, and along with domains II and IV, is involved in inter subunit contacts. The family also includes pyruvate flavodoxin oxidoreductase as encoded by the nifJ gene in cyanobacterium which is required for growth on molecular nitrogen when iron is limited. Pssm-ID: 396432 Cd Length: 230 Bit Score: 306.49 E-value: 2.12e-96
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| porA | PRK09622 | 2-oxoacid:ferredoxin oxidoreductase subunit alpha; |
5-385 | 4.68e-53 | ||||||||||||||||
2-oxoacid:ferredoxin oxidoreductase subunit alpha; Pssm-ID: 181999 [Multi-domain] Cd Length: 407 Bit Score: 191.90 E-value: 4.68e-53
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| EKR | smart00890 | Domain of unknown function; EKR is a short, 33 residue, domain found in bacterial and some ... |
623-679 | 1.65e-25 | ||||||||||||||||
Domain of unknown function; EKR is a short, 33 residue, domain found in bacterial and some lower eukaryotic species which lies between a POR (pyruvate ferredoxin/flavodoxin oxidoreductase) and the 4Fe-4S binding domain Fer4. It contains a characteristic EKR sequence motif. The exact function of this domain is not known. Pssm-ID: 197958 [Multi-domain] Cd Length: 57 Bit Score: 100.00 E-value: 1.65e-25
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| Name | Accession | Description | Interval | E-value | ||||||||||||||||
| pyruv_ox_red | TIGR02176 | pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single ... |
1-1166 | 0e+00 | ||||||||||||||||
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single chain form of pyruvate:ferredoxin (or flavodoxin) oxidoreductase. This enzyme may transfer electrons to nitrogenase in nitrogen-fixing species. Portions of this protein are homologous to gamma subunit of the four subunit pyruvate:ferredoxin (flavodoxin) oxidoreductase. Pssm-ID: 131231 [Multi-domain] Cd Length: 1165 Bit Score: 1608.67 E-value: 0e+00
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| TPP_PFOR_PNO | cd03377 | Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ... |
811-1166 | 0e+00 | ||||||||||||||||
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of proteins similar to the single subunit pyruvate ferredoxin oxidoreductase (PFOR) of Desulfovibrio Africanus, present in bacteria and amitochondriate eukaryotes. This subfamily also includes proteins characterized as pyruvate NADP+ oxidoreductase (PNO). These enzymes are dependent on TPP and a divalent metal cation as cofactors. PFOR and PNO catalyze the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. The PFOR from cyanobacterium Anabaena (NifJ) is required for the transfer of electrons from pyruvate to flavodoxin, which reduces nitrogenase. The facultative anaerobic mitochondrion of the photosynthetic protist Euglena gracilis oxidizes pyruvate with PNO. Pssm-ID: 239472 Cd Length: 365 Bit Score: 626.17 E-value: 0e+00
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| PorA | COG0674 | Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha ... |
1-394 | 4.08e-126 | ||||||||||||||||
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha subunit is part of the Pathway/BioSystem: Pyruvate oxidation Pssm-ID: 440438 [Multi-domain] Cd Length: 372 Bit Score: 391.36 E-value: 4.08e-126
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| POR_N | pfam01855 | Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N ... |
13-243 | 2.12e-96 | ||||||||||||||||
Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N terminal structural domain of the pyruvate ferredoxin oxidoreductase. This domain binds thiamine diphosphate, and along with domains II and IV, is involved in inter subunit contacts. The family also includes pyruvate flavodoxin oxidoreductase as encoded by the nifJ gene in cyanobacterium which is required for growth on molecular nitrogen when iron is limited. Pssm-ID: 396432 Cd Length: 230 Bit Score: 306.49 E-value: 2.12e-96
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| PorG | COG1014 | Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, gamma ... |
417-854 | 3.57e-71 | ||||||||||||||||
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, gamma subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, gamma subunit is part of the Pathway/BioSystem: Pyruvate oxidation Pssm-ID: 440638 [Multi-domain] Cd Length: 424 Bit Score: 244.21 E-value: 3.57e-71
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| TPP_PFOR | cd02018 | Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ... |
812-1103 | 1.27e-67 | ||||||||||||||||
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) subfamily, TPP-binding module; PFOR catalyzes the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. PFORs can be homodimeric, heterodimeric, or heterotetrameric, depending on the organism. These enzymes are dependent on TPP and a divalent metal cation as cofactors. Pssm-ID: 238976 [Multi-domain] Cd Length: 237 Bit Score: 227.37 E-value: 1.27e-67
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| porA | PRK09622 | 2-oxoacid:ferredoxin oxidoreductase subunit alpha; |
5-385 | 4.68e-53 | ||||||||||||||||
2-oxoacid:ferredoxin oxidoreductase subunit alpha; Pssm-ID: 181999 [Multi-domain] Cd Length: 407 Bit Score: 191.90 E-value: 4.68e-53
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| PorB | COG1013 | Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
816-1142 | 7.21e-52 | ||||||||||||||||
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation Pssm-ID: 440637 [Multi-domain] Cd Length: 262 Bit Score: 183.42 E-value: 7.21e-52
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| TPP_PYR_PFOR_IOR-alpha_like | cd07034 | Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ... |
6-169 | 7.17e-51 | ||||||||||||||||
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ferredoxin oxidoreductase alpha subunit (IOR-alpha), and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain, of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit (IOR-alpha), and related proteins, subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzyme Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit. This subfamily includes proteins characterized as pyruvate NADP+ oxidoreductase (PNO). PFOR and PNO catalyze the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. The facultative anaerobic mitochondrion of the photosynthetic protist Euglena gracilis oxidizes pyruvate with PNO. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate. Pssm-ID: 132917 [Multi-domain] Cd Length: 160 Bit Score: 176.54 E-value: 7.17e-51
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| POR | pfam01558 | Pyruvate ferredoxin/flavodoxin oxidoreductase; This family includes a region of the large ... |
426-610 | 1.15e-35 | ||||||||||||||||
Pyruvate ferredoxin/flavodoxin oxidoreductase; This family includes a region of the large protein pyruvate-flavodoxin oxidoreductase and the whole pyruvate ferredoxin oxidoreductase gamma subunit protein. It is not known whether the gamma subunit has a catalytic or regulatory role. Pyruvate oxidoreductase (POR) catalyzes the final step in the fermentation of carbohydrates in anaerobic microorganizms. This involves the oxidative decarboxylation of pyruvate with the participation of thiamine followed by the transfer of an acetyl moiety to coenzyme A for the synthesis of acetyl-CoA. The family also includes pyruvate flavodoxin oxidoreductase as encoded by the nifJ gene in cyanobacterium which is required for growth on molecular nitrogen when iron is limited. Pssm-ID: 426323 [Multi-domain] Cd Length: 172 Bit Score: 133.58 E-value: 1.15e-35
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| porA | PRK08367 | pyruvate ferredoxin oxidoreductase subunit alpha; Reviewed |
4-386 | 1.93e-35 | ||||||||||||||||
pyruvate ferredoxin oxidoreductase subunit alpha; Reviewed Pssm-ID: 181403 [Multi-domain] Cd Length: 394 Bit Score: 140.02 E-value: 1.93e-35
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| vorA | PRK08366 | 2-ketoisovalerate ferredoxin oxidoreductase subunit alpha; Reviewed |
2-363 | 8.53e-35 | ||||||||||||||||
2-ketoisovalerate ferredoxin oxidoreductase subunit alpha; Reviewed Pssm-ID: 169406 [Multi-domain] Cd Length: 390 Bit Score: 137.82 E-value: 8.53e-35
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| TPP_PFOR_porB_like | cd03376 | Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ... |
817-1100 | 9.72e-29 | ||||||||||||||||
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of proteins similar to the beta subunit (porB) of the Helicobacter pylori four-subunit pyruvate ferredoxin oxidoreductase (PFOR), which are also found in archaea and some hyperthermophilic bacteria. PFOR catalyzes the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. The 36-kDa porB subunit contains the binding sites for the cofactors, TPP and a divalent metal cation, which are required for activity. Pssm-ID: 239471 [Multi-domain] Cd Length: 235 Bit Score: 115.80 E-value: 9.72e-29
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| EKR | pfam10371 | Domain of unknown function; EKR is a short, 33 residue, domain found in bacterial and some ... |
626-678 | 1.62e-27 | ||||||||||||||||
Domain of unknown function; EKR is a short, 33 residue, domain found in bacterial and some lower eukaryotic species which lies between a POR (pyruvate ferredoxin/flavodoxin oxidoreductase) pfam01558 and the 4Fe-4S binding domain Fer4 pfam00037. It contains a characteriztic EKR sequence motif. The exact function of this domain is not known. Pssm-ID: 431238 [Multi-domain] Cd Length: 54 Bit Score: 105.63 E-value: 1.62e-27
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| NapF | COG1145 | Ferredoxin [Energy production and conversion]; |
509-776 | 1.11e-25 | ||||||||||||||||
Ferredoxin [Energy production and conversion]; Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 107.12 E-value: 1.11e-25
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| EKR | smart00890 | Domain of unknown function; EKR is a short, 33 residue, domain found in bacterial and some ... |
623-679 | 1.65e-25 | ||||||||||||||||
Domain of unknown function; EKR is a short, 33 residue, domain found in bacterial and some lower eukaryotic species which lies between a POR (pyruvate ferredoxin/flavodoxin oxidoreductase) and the 4Fe-4S binding domain Fer4. It contains a characteristic EKR sequence motif. The exact function of this domain is not known. Pssm-ID: 197958 [Multi-domain] Cd Length: 57 Bit Score: 100.00 E-value: 1.65e-25
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| PRK11865 | PRK11865 | pyruvate synthase subunit beta; |
818-1148 | 1.54e-23 | ||||||||||||||||
pyruvate synthase subunit beta; Pssm-ID: 183346 [Multi-domain] Cd Length: 299 Bit Score: 102.48 E-value: 1.54e-23
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| PorD | COG1144 | Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
664-781 | 1.01e-21 | ||||||||||||||||
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation Pssm-ID: 440759 [Multi-domain] Cd Length: 84 Bit Score: 90.50 E-value: 1.01e-21
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| TPP_enzyme_PYR | cd06586 | Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
9-169 | 2.95e-20 | ||||||||||||||||
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit. Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 88.56 E-value: 2.95e-20
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| PRK11864 | PRK11864 | 3-methyl-2-oxobutanoate dehydrogenase subunit beta; |
818-1145 | 1.74e-19 | ||||||||||||||||
3-methyl-2-oxobutanoate dehydrogenase subunit beta; Pssm-ID: 237005 [Multi-domain] Cd Length: 300 Bit Score: 90.54 E-value: 1.74e-19
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| PFOR_II | pfam17147 | Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic ... |
265-344 | 8.83e-18 | ||||||||||||||||
Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic enzyme pyruvate:ferredoxin oxidoreductase and is necessary for inter subunit contacts in conjunction with domains I and IV. Pssm-ID: 407280 [Multi-domain] Cd Length: 102 Bit Score: 79.61 E-value: 8.83e-18
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| PRK14028 | PRK14028 | pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional |
417-756 | 1.08e-14 | ||||||||||||||||
pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional Pssm-ID: 172522 [Multi-domain] Cd Length: 312 Bit Score: 76.57 E-value: 1.08e-14
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| TPP_OGFOR | cd03375 | Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
954-1071 | 2.22e-14 | ||||||||||||||||
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) subfamily, TPP-binding module; OGFOR catalyzes the oxidative decarboxylation of 2-oxo-acids, with ferredoxin acting as an electron acceptor. In the TCA cycle, OGFOR catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA. In the reductive tricarboxylic acid cycle found in the anaerobic autotroph Hydrogenobacter thermophilus, OGFOR catalyzes the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate. Thauera aromatica OGFOR has been shown to provide reduced ferredoxin to benzoyl-CoA reductase, a key enzyme in the anaerobic metabolism of aromatic compounds. OGFOR is dependent on TPP and a divalent metal cation for activity. Pssm-ID: 239470 [Multi-domain] Cd Length: 193 Bit Score: 72.94 E-value: 2.22e-14
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| PorC_KorC | TIGR02175 | 2-oxoacid:acceptor oxidoreductase, gamma subunit, pyruvate/2-ketoisovalerate family; A number ... |
418-611 | 1.38e-13 | ||||||||||||||||
2-oxoacid:acceptor oxidoreductase, gamma subunit, pyruvate/2-ketoisovalerate family; A number of anaerobic and microaerophilic species lack pyruvate dehydrogenase and have instead a four subunit, oxygen-sensitive pyruvate oxidoreductase, with either ferredoxins or flavodoxins (H. pylori) used as the acceptor. Several related four-subunit enzymes may exist in the same species. This model describes the gamma subunit. In Pyrococcus furious, enzymes active on pyruvate and 2-ketoisovalerate share a common gamma subunit. Pssm-ID: 274014 [Multi-domain] Cd Length: 177 Bit Score: 70.07 E-value: 1.38e-13
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| COG1149 | COG1149 | MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
677-773 | 5.47e-13 | ||||||||||||||||
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only]; Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 65.13 E-value: 5.47e-13
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| NuoI | COG1143 | Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
686-781 | 7.20e-13 | ||||||||||||||||
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 64.38 E-value: 7.20e-13
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| PRK11867 | PRK11867 | 2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
956-1148 | 1.05e-12 | ||||||||||||||||
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 69.87 E-value: 1.05e-12
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| Fer4_21 | pfam14697 | 4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
685-770 | 2.15e-10 | ||||||||||||||||
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters. Pssm-ID: 434137 [Multi-domain] Cd Length: 59 Bit Score: 57.29 E-value: 2.15e-10
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| PreA | COG1146 | NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
686-756 | 2.94e-10 | ||||||||||||||||
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism]; Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 57.03 E-value: 2.94e-10
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| COG2768 | COG2768 | Uncharacterized Fe-S cluster protein [Function unknown]; |
682-774 | 4.93e-10 | ||||||||||||||||
Uncharacterized Fe-S cluster protein [Function unknown]; Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 56.66 E-value: 4.93e-10
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| PRK05778 | PRK05778 | 2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
960-1071 | 5.86e-10 | ||||||||||||||||
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 61.82 E-value: 5.86e-10
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| Fer4_16 | pfam13484 | 4Fe-4S double cluster binding domain; |
689-758 | 8.90e-10 | ||||||||||||||||
4Fe-4S double cluster binding domain; Pssm-ID: 463893 [Multi-domain] Cd Length: 65 Bit Score: 55.57 E-value: 8.90e-10
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| Fer4_7 | pfam12838 | 4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
689-758 | 1.00e-09 | ||||||||||||||||
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters. Pssm-ID: 463724 [Multi-domain] Cd Length: 51 Bit Score: 55.23 E-value: 1.00e-09
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| DsrA | COG2221 | Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
677-758 | 9.62e-09 | ||||||||||||||||
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism]; Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 52.75 E-value: 9.62e-09
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| NapF_like | cd10564 | NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
689-757 | 1.62e-08 | ||||||||||||||||
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system. Pssm-ID: 319886 [Multi-domain] Cd Length: 139 Bit Score: 54.56 E-value: 1.62e-08
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| Fer4_9 | pfam13187 | 4Fe-4S dicluster domain; |
689-756 | 1.74e-08 | ||||||||||||||||
4Fe-4S dicluster domain; Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 51.79 E-value: 1.74e-08
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| PRK14029 | PRK14029 | pyruvate/ketoisovalerate ferredoxin oxidoreductase subunit gamma; Provisional |
418-612 | 1.96e-08 | ||||||||||||||||
pyruvate/ketoisovalerate ferredoxin oxidoreductase subunit gamma; Provisional Pssm-ID: 172523 [Multi-domain] Cd Length: 185 Bit Score: 55.41 E-value: 1.96e-08
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| porD | PRK09625 | pyruvate flavodoxin oxidoreductase subunit delta; Reviewed |
664-780 | 6.44e-08 | ||||||||||||||||
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed Pssm-ID: 236596 [Multi-domain] Cd Length: 133 Bit Score: 52.44 E-value: 6.44e-08
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| MtMvhB_like | cd10549 | Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
682-784 | 7.40e-08 | ||||||||||||||||
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction. Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 52.40 E-value: 7.40e-08
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| Fer4_10 | pfam13237 | 4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
686-756 | 8.83e-08 | ||||||||||||||||
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich. Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 49.94 E-value: 8.83e-08
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| PRK08534 | PRK08534 | pyruvate ferredoxin oxidoreductase subunit gamma; Reviewed |
419-615 | 1.95e-07 | ||||||||||||||||
pyruvate ferredoxin oxidoreductase subunit gamma; Reviewed Pssm-ID: 181460 [Multi-domain] Cd Length: 181 Bit Score: 52.35 E-value: 1.95e-07
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| PRK06853 | PRK06853 | indolepyruvate oxidoreductase subunit beta; Reviewed |
455-610 | 1.99e-07 | ||||||||||||||||
indolepyruvate oxidoreductase subunit beta; Reviewed Pssm-ID: 180732 [Multi-domain] Cd Length: 197 Bit Score: 52.56 E-value: 1.99e-07
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| IorA | COG4231 | TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
676-758 | 3.51e-07 | ||||||||||||||||
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion]; Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 48.89 E-value: 3.51e-07
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| MtMvhB_like | cd10549 | Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
686-797 | 4.38e-07 | ||||||||||||||||
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction. Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 50.09 E-value: 4.38e-07
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| TPP_enzyme_C | pfam02775 | Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
951-1067 | 1.25e-06 | ||||||||||||||||
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 49.51 E-value: 1.25e-06
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| PRK11866 | PRK11866 | 2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
961-1077 | 1.42e-06 | ||||||||||||||||
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 51.30 E-value: 1.42e-06
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| PRK13795 | PRK13795 | hypothetical protein; Provisional |
688-764 | 3.39e-06 | ||||||||||||||||
hypothetical protein; Provisional Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 51.15 E-value: 3.39e-06
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| Fer4_8 | pfam13183 | 4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
689-758 | 5.32e-06 | ||||||||||||||||
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters. Pssm-ID: 433017 [Multi-domain] Cd Length: 64 Bit Score: 44.99 E-value: 5.32e-06
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| HdrA | COG1148 | Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
673-768 | 1.04e-05 | ||||||||||||||||
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 49.47 E-value: 1.04e-05
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| DMSOR_beta_like | cd16373 | uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
651-768 | 1.48e-05 | ||||||||||||||||
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system. Pssm-ID: 319895 [Multi-domain] Cd Length: 154 Bit Score: 46.09 E-value: 1.48e-05
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| RnfB | COG2878 | Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
686-756 | 1.56e-05 | ||||||||||||||||
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase Pssm-ID: 442125 [Multi-domain] Cd Length: 254 Bit Score: 47.68 E-value: 1.56e-05
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| PRK08659 | PRK08659 | 2-oxoacid:acceptor oxidoreductase subunit alpha; |
4-322 | 2.00e-05 | ||||||||||||||||
2-oxoacid:acceptor oxidoreductase subunit alpha; Pssm-ID: 181526 [Multi-domain] Cd Length: 376 Bit Score: 48.32 E-value: 2.00e-05
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| SdhB/FrdB | COG0479 | Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
659-773 | 2.57e-05 | ||||||||||||||||
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit is part of the Pathway/BioSystem: TCA cycle Pssm-ID: 440247 [Multi-domain] Cd Length: 230 Bit Score: 47.05 E-value: 2.57e-05
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| PRK07118 | PRK07118 | Fe-S cluster domain-containing protein; |
677-797 | 3.93e-05 | ||||||||||||||||
Fe-S cluster domain-containing protein; Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 46.85 E-value: 3.93e-05
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| DMSOR_beta_like | cd10550 | uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
689-756 | 4.77e-05 | ||||||||||||||||
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system. Pssm-ID: 319872 [Multi-domain] Cd Length: 130 Bit Score: 44.10 E-value: 4.77e-05
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| PRK08318 | PRK08318 | NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
686-759 | 6.17e-05 | ||||||||||||||||
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 46.86 E-value: 6.17e-05
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| PRK12576 | PRK12576 | succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
683-756 | 1.52e-04 | ||||||||||||||||
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Pssm-ID: 237143 [Multi-domain] Cd Length: 279 Bit Score: 45.12 E-value: 1.52e-04
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| DMSOR_beta_like | cd16371 | uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
690-756 | 1.75e-04 | ||||||||||||||||
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system. Pssm-ID: 319893 [Multi-domain] Cd Length: 140 Bit Score: 42.93 E-value: 1.75e-04
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| COG1149 | COG1149 | MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
682-714 | 2.18e-04 | ||||||||||||||||
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only]; Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 40.48 E-value: 2.18e-04
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| ACS_1 | cd01916 | Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ... |
689-850 | 2.48e-04 | ||||||||||||||||
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA. Pssm-ID: 238897 [Multi-domain] Cd Length: 731 Bit Score: 45.48 E-value: 2.48e-04
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| PRK06991 | PRK06991 | electron transport complex subunit RsxB; |
686-756 | 2.53e-04 | ||||||||||||||||
electron transport complex subunit RsxB; Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 44.40 E-value: 2.53e-04
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| DMSOR_beta_like | cd16372 | uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
680-756 | 3.37e-04 | ||||||||||||||||
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system. Pssm-ID: 319894 [Multi-domain] Cd Length: 125 Bit Score: 41.55 E-value: 3.37e-04
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| Fer4_6 | pfam12837 | 4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ... |
681-704 | 3.67e-04 | ||||||||||||||||
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Pssm-ID: 432822 [Multi-domain] Cd Length: 24 Bit Score: 38.75 E-value: 3.67e-04
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| DMSOR_beta_like | cd16374 | uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
687-756 | 3.72e-04 | ||||||||||||||||
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system. Pssm-ID: 319896 [Multi-domain] Cd Length: 139 Bit Score: 41.88 E-value: 3.72e-04
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| Fer4_7 | pfam12838 | 4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
666-703 | 4.39e-04 | ||||||||||||||||
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters. Pssm-ID: 463724 [Multi-domain] Cd Length: 51 Bit Score: 39.05 E-value: 4.39e-04
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| Fer4 | pfam00037 | 4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ... |
682-705 | 6.46e-04 | ||||||||||||||||
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Pssm-ID: 459642 [Multi-domain] Cd Length: 24 Bit Score: 38.00 E-value: 6.46e-04
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| PRK12385 | PRK12385 | succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
689-756 | 9.00e-04 | ||||||||||||||||
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Pssm-ID: 183490 [Multi-domain] Cd Length: 244 Bit Score: 42.38 E-value: 9.00e-04
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| dhsB | TIGR00384 | succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
689-776 | 1.11e-03 | ||||||||||||||||
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase and fumarate reductase are reverse directions of the same enzymatic interconversion, succinate + FAD+ = fumarate + FADH2 (EC 1.3.11.1). In E. coli, the forward and reverse reactions are catalyzed by distinct complexes: fumarate reductase operates under anaerobic conditions and succinate dehydrogenase operates under aerobic conditions. This model also describes a region of the B subunit of a cytosolic archaeal fumarate reductase. [Energy metabolism, Aerobic, Energy metabolism, Anaerobic, Energy metabolism, TCA cycle] Pssm-ID: 273049 [Multi-domain] Cd Length: 220 Bit Score: 41.65 E-value: 1.11e-03
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| Fer4 | pfam00037 | 4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ... |
742-756 | 1.15e-03 | ||||||||||||||||
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Pssm-ID: 459642 [Multi-domain] Cd Length: 24 Bit Score: 37.23 E-value: 1.15e-03
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| IorA | COG4231 | TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
726-758 | 1.21e-03 | ||||||||||||||||
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion]; Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 38.87 E-value: 1.21e-03
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| IorA | COG4231 | TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
686-712 | 1.44e-03 | ||||||||||||||||
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion]; Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 38.49 E-value: 1.44e-03
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| FDH_beta_like | cd16366 | beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ... |
660-756 | 1.57e-03 | ||||||||||||||||
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate. Pssm-ID: 319888 [Multi-domain] Cd Length: 156 Bit Score: 40.46 E-value: 1.57e-03
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| DsrA | COG2221 | Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
682-707 | 1.97e-03 | ||||||||||||||||
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism]; Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 38.11 E-value: 1.97e-03
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| TPP_IOR_alpha | cd02008 | Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
983-1071 | 1.97e-03 | ||||||||||||||||
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA. Pssm-ID: 238966 [Multi-domain] Cd Length: 178 Bit Score: 40.34 E-value: 1.97e-03
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| Fer4_18 | pfam13746 | 4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
693-756 | 2.04e-03 | ||||||||||||||||
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich. Pssm-ID: 404610 [Multi-domain] Cd Length: 114 Bit Score: 39.31 E-value: 2.04e-03
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| PreA | COG1146 | NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
740-758 | 2.14e-03 | ||||||||||||||||
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism]; Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 37.77 E-value: 2.14e-03
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| Fer4_9 | pfam13187 | 4Fe-4S dicluster domain; |
684-704 | 3.13e-03 | ||||||||||||||||
4Fe-4S dicluster domain; Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 36.76 E-value: 3.13e-03
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| PreA | COG1146 | NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
685-714 | 3.21e-03 | ||||||||||||||||
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism]; Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 37.38 E-value: 3.21e-03
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| Transketolase_C | pfam02780 | Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
268-374 | 3.67e-03 | ||||||||||||||||
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site. Pssm-ID: 460693 [Multi-domain] Cd Length: 124 Bit Score: 38.73 E-value: 3.67e-03
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| RnfB | COG2878 | Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
686-769 | 3.74e-03 | ||||||||||||||||
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase Pssm-ID: 442125 [Multi-domain] Cd Length: 254 Bit Score: 40.36 E-value: 3.74e-03
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| MtMvhB_like | cd10549 | Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
742-786 | 4.21e-03 | ||||||||||||||||
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction. Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 38.53 E-value: 4.21e-03
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| HycB_like | cd10554 | HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ... |
686-758 | 4.85e-03 | ||||||||||||||||
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation. Pssm-ID: 319876 [Multi-domain] Cd Length: 149 Bit Score: 38.78 E-value: 4.85e-03
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| oorD | PRK09626 | 2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed |
679-756 | 4.90e-03 | ||||||||||||||||
2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed Pssm-ID: 236597 [Multi-domain] Cd Length: 103 Bit Score: 37.78 E-value: 4.90e-03
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| TH_beta_N | cd10552 | N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ... |
674-720 | 5.14e-03 | ||||||||||||||||
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This family includes the beta subunit of pyrogallol-phloroglucinol transhydroxylase (TH), a cytoplasmic molybdenum (Mo) enzyme from anaerobic microorganisms like Pelobacter acidigallici and Desulfitobacterium hafniense which catalyzes the conversion of pyrogallol to phloroglucinol, an important building block of plant polymers. TH belongs to the DMSO reductase (DMSOR) family; it is a heterodimer consisting of a large alpha catalytic subunit and a small beta FeS subunit. The beta subunit has two domains with the N-terminal domain containing three [4Fe-4S] centers and a seven-stranded, mainly antiparallel beta-barrel domain. In the anaerobic bacterium Pelobacter acidigallici, gallic acid, pyrogallol, phloroglucinol, or phloroglucinol carboxylic acid are fermented to three molecules of acetate (plus CO2), and TH is the key enzyme in the fermentation pathway, which converts pyrogallol to phloroglucinol in the absence of O2. Pssm-ID: 319874 [Multi-domain] Cd Length: 186 Bit Score: 39.23 E-value: 5.14e-03
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| NapF_like | cd10564 | NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
651-705 | 5.46e-03 | ||||||||||||||||
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system. Pssm-ID: 319886 [Multi-domain] Cd Length: 139 Bit Score: 38.38 E-value: 5.46e-03
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| NuoI | COG1143 | Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
666-705 | 5.73e-03 | ||||||||||||||||
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 36.65 E-value: 5.73e-03
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| PRK09326 | PRK09326 | F420H2 dehydrogenase subunit F; Provisional |
677-759 | 6.07e-03 | ||||||||||||||||
F420H2 dehydrogenase subunit F; Provisional Pssm-ID: 181779 [Multi-domain] Cd Length: 341 Bit Score: 40.21 E-value: 6.07e-03
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| DMSOR_beta_like | cd16370 | uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
683-756 | 8.61e-03 | ||||||||||||||||
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system. Pssm-ID: 319892 [Multi-domain] Cd Length: 131 Bit Score: 37.64 E-value: 8.61e-03
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| PRK06273 | PRK06273 | ferredoxin; Provisional |
686-756 | 8.72e-03 | ||||||||||||||||
ferredoxin; Provisional Pssm-ID: 235764 [Multi-domain] Cd Length: 165 Bit Score: 38.54 E-value: 8.72e-03
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| PRK11869 | PRK11869 | 2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
961-1071 | 9.24e-03 | ||||||||||||||||
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional Pssm-ID: 183349 [Multi-domain] Cd Length: 280 Bit Score: 39.38 E-value: 9.24e-03
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