Pheophorbide a oxygenase family protein with Rieske 2Fe-2S domain-containing protein [Arabidopsis thaliana]
Protein Classification
PLN02518 family protein( domain architecture ID 11476920)
PLN02518 family protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||
| PLN02518 | PLN02518 | pheophorbide a oxygenase |
1-537 | 0e+00 | ||||||||
pheophorbide a oxygenase : Pssm-ID: 215283 [Multi-domain] Cd Length: 539 Bit Score: 1066.41 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||||
| PLN02518 | PLN02518 | pheophorbide a oxygenase |
1-537 | 0e+00 | ||||||||
pheophorbide a oxygenase Pssm-ID: 215283 [Multi-domain] Cd Length: 539 Bit Score: 1066.41 E-value: 0e+00
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| PobA | COG5749 | Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism]; |
80-444 | 2.34e-95 | ||||||||
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism]; Pssm-ID: 444459 [Multi-domain] Cd Length: 349 Bit Score: 293.83 E-value: 2.34e-95
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| Rieske_RO_Alpha_PaO | cd03480 | Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, ... |
71-211 | 1.42e-89 | ||||||||
Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of a small subfamily of enzymes found in plants as well as oxygenic cyanobacterial photosynthesizers including LLS1 (lethal leaf spot 1, also known as PaO) and ACD1 (accelerated cell death 1). ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. PaO expression increases upon physical wounding of plant leaves and is thought to catalyze a key step in chlorophyll degradation. The Arabidopsis-accelerated cell death gene ACD1 is involved in oxygenation of PaO. Pssm-ID: 239562 [Multi-domain] Cd Length: 138 Bit Score: 271.12 E-value: 1.42e-89
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| Rieske | pfam00355 | Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ... |
87-170 | 1.22e-28 | ||||||||
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines coordinate one Fe ion, while the other Fe ion is coordinated by two conserved histidines. In hyperthermophilic archaea there is a SKTPCX(2-3)C motif at the C-terminus. The cysteines in this motif form a disulphide bridge, which stabilizes the protein. Pssm-ID: 425632 [Multi-domain] Cd Length: 89 Bit Score: 108.97 E-value: 1.22e-28
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| Name | Accession | Description | Interval | E-value | ||||||||
| PLN02518 | PLN02518 | pheophorbide a oxygenase |
1-537 | 0e+00 | ||||||||
pheophorbide a oxygenase Pssm-ID: 215283 [Multi-domain] Cd Length: 539 Bit Score: 1066.41 E-value: 0e+00
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| PobA | COG5749 | Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism]; |
80-444 | 2.34e-95 | ||||||||
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism]; Pssm-ID: 444459 [Multi-domain] Cd Length: 349 Bit Score: 293.83 E-value: 2.34e-95
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| Rieske_RO_Alpha_PaO | cd03480 | Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, ... |
71-211 | 1.42e-89 | ||||||||
Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of a small subfamily of enzymes found in plants as well as oxygenic cyanobacterial photosynthesizers including LLS1 (lethal leaf spot 1, also known as PaO) and ACD1 (accelerated cell death 1). ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. PaO expression increases upon physical wounding of plant leaves and is thought to catalyze a key step in chlorophyll degradation. The Arabidopsis-accelerated cell death gene ACD1 is involved in oxygenation of PaO. Pssm-ID: 239562 [Multi-domain] Cd Length: 138 Bit Score: 271.12 E-value: 1.42e-89
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| HcaE | COG4638 | Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ... |
84-427 | 9.57e-39 | ||||||||
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit [Inorganic ion transport and metabolism, General function prediction only]; Pssm-ID: 443676 [Multi-domain] Cd Length: 298 Bit Score: 143.59 E-value: 9.57e-39
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| Rieske_RO_Alpha_N | cd03469 | Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ... |
88-206 | 4.43e-32 | ||||||||
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha subunit; The RO family comprise a large class of aromatic ring-hydroxylating dioxygenases found predominantly in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth. ROs consist of two or three components: reductase, oxygenase, and ferredoxin (in some cases) components. The oxygenase component may contain alpha and beta subunits, with the beta subunit having a purely structural function. Some oxygenase components contain only an alpha subunit. The oxygenase alpha subunit has two domains, an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from the reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. Reduced pyridine nucleotide is used as the initial source of two electrons for dioxygen activation. Pssm-ID: 239551 [Multi-domain] Cd Length: 118 Bit Score: 119.23 E-value: 4.43e-32
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| Rieske_RO_Alpha_Tic55 | cd04338 | Tic55 is a 55kDa LLS1-related non-heme iron oxygenase associated with protein transport ... |
74-204 | 1.77e-31 | ||||||||
Tic55 is a 55kDa LLS1-related non-heme iron oxygenase associated with protein transport through the plant inner chloroplast membrane. This domain represents the N-terminal Rieske domain of the Tic55 oxygenase alpha subunit. Tic55 is closely related to the oxygenase alpha subunits of a small subfamily of enzymes found in plants as well as oxygenic cyanobacterial photosynthesizers including LLS1 (lethal leaf spot 1, also known as PaO), Ptc52, and ACD1 (accelerated cell death 1). ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. Pssm-ID: 239830 [Multi-domain] Cd Length: 134 Bit Score: 118.40 E-value: 1.77e-31
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| Rieske | pfam00355 | Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ... |
87-170 | 1.22e-28 | ||||||||
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines coordinate one Fe ion, while the other Fe ion is coordinated by two conserved histidines. In hyperthermophilic archaea there is a SKTPCX(2-3)C motif at the C-terminus. The cysteines in this motif form a disulphide bridge, which stabilizes the protein. Pssm-ID: 425632 [Multi-domain] Cd Length: 89 Bit Score: 108.97 E-value: 1.22e-28
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| PaO | pfam08417 | Pheophorbide a oxygenase; This domain is found in bacterial and plant proteins to the ... |
296-390 | 2.09e-21 | ||||||||
Pheophorbide a oxygenase; This domain is found in bacterial and plant proteins to the C-terminus of a Rieske 2Fe-2S domain (pfam00355). One of the proteins the domain is found in is Pheophorbide a oxygenase (PaO) which seems to be a key regulator of chlorophyll catabolism. Arabidopsis PaO (AtPaO) is a Rieske-type 2Fe-2S enzyme that is identical to Arabidopsis accelerated cell death 1 and homologous to lethal leaf spot 1 (LLS1) of maize, in which the domain described here is also found. Pssm-ID: 429985 [Multi-domain] Cd Length: 89 Bit Score: 88.54 E-value: 2.09e-21
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| Rieske_RO_Alpha_PhDO_like | cd03479 | Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, ... |
85-220 | 2.66e-19 | ||||||||
Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of PhDO and similar proteins including 3-chlorobenzoate 3,4-dioxygenase (CBDO), phenoxybenzoate dioxygenase (POB-dioxygenase) and 3-nitrobenzoate oxygenase (MnbA). ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. PhDO and CBDO are two-component RO systems, containing oxygenase and reductase components. PhDO catalyzes the dihydroxylation of phthalate to form the 4,5-dihydro-cis-dihydrodiol of phthalate (DHD). CBDO, together with CbaC dehydrogenase, converts the environmental pollutant 3CBA to protocatechuate (PCA) and 5-Cl-PCA, which are then metabolized by the chromosomal PCA meta (extradiol) ring fission pathway. POB-dioxygenase catalyzes the initial catabolic step in the angular dioxygenation of phenoxybenzoate, converting mono- and dichlorinated phenoxybenzoates to protocatechuate and chlorophenols. These phenoxybenzoates are metabolic products formed during the degradation of pyrethroid insecticides. Pssm-ID: 239561 [Multi-domain] Cd Length: 144 Bit Score: 84.60 E-value: 2.66e-19
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| Rieske_RO_Alpha_VanA_DdmC | cd03532 | Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and ... |
85-202 | 3.97e-19 | ||||||||
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and dicamba O-demethylase oxygenase (DdmC) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. Vanillate-O-demethylase is a heterodimeric enzyme consisting of a terminal oxygenase (VanA) and reductase (VanB) components. This enzyme reductively catalyzes the conversion of vanillate into protocatechuate and formaldehyde. Protocatechuate and vanillate are important intermediate metabolites in the degradation pathway of lignin-derived compounds such as ferulic acid and vanillin by soil microbes. DDmC is the oxygenase component of a three-component dicamba O-demethylase found in Pseudomonas maltophila, that catalyzes the conversion of a widely used herbicide called herbicide dicamba (2-methoxy-3,6-dichlorobenzoic acid) to DCSA (3,6-dichlorosalicylic acid). Pssm-ID: 239608 [Multi-domain] Cd Length: 116 Bit Score: 83.18 E-value: 3.97e-19
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| Rieske_RO_Alpha_Cao | cd04337 | Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the ... |
85-202 | 1.93e-18 | ||||||||
Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the plastid-envelope inner and thylakoid membranes, that catalyzes the conversion of chlorophyllide a to chlorophyllide b. CAO is found not only in plants but also in chlorophytes and prochlorophytes. This domain represents the N-terminal rieske domain of the oxygenase alpha subunit. ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. Cao is closely related to several other plant RO's including Tic 55, a 55 kDa protein associated with protein transport through the inner chloroplast membrane; Ptc 52, a novel 52 kDa protein isolated from chloroplasts; and LLS1/Pao (Lethal-leaf spot 1/pheophorbide a oxygenase). Pssm-ID: 239829 [Multi-domain] Cd Length: 129 Bit Score: 81.38 E-value: 1.93e-18
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| Rieske | cd03467 | Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ... |
88-201 | 7.69e-17 | ||||||||
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron oxygenase (RO) systems such as naphthalene and biphenyl dioxygenases, as well as in plant/cyanobacterial chloroplast b6f and mitochondrial cytochrome bc(1) complexes. The Rieske domain can be divided into two subdomains, with an incomplete six-stranded, antiparallel beta-barrel at one end, and an iron-sulfur cluster binding subdomain at the other. The Rieske iron-sulfur center contains a [2Fe-2S] cluster, which is involved in electron transfer, and is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In RO systems, the N-terminal Rieske domain of the alpha subunit acts as an electron shuttle that accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron in the alpha subunit C-terminal domain to be used for catalysis. Pssm-ID: 239550 [Multi-domain] Cd Length: 98 Bit Score: 75.99 E-value: 7.69e-17
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| PLN00095 | PLN00095 | chlorophyllide a oxygenase; Provisional |
85-337 | 1.66e-15 | ||||||||
chlorophyllide a oxygenase; Provisional Pssm-ID: 165668 [Multi-domain] Cd Length: 394 Bit Score: 78.57 E-value: 1.66e-15
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| NirD | COG2146 | Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ... |
88-204 | 3.40e-15 | ||||||||
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 441749 [Multi-domain] Cd Length: 103 Bit Score: 71.41 E-value: 3.40e-15
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| PLN02281 | PLN02281 | chlorophyllide a oxygenase |
85-306 | 8.70e-14 | ||||||||
chlorophyllide a oxygenase Pssm-ID: 177920 [Multi-domain] Cd Length: 536 Bit Score: 73.99 E-value: 8.70e-14
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| Rieske_RO_Alpha_KSH | cd03531 | The alignment model represents the N-terminal rieske iron-sulfur domain of KshA, the oxygenase ... |
88-206 | 2.69e-13 | ||||||||
The alignment model represents the N-terminal rieske iron-sulfur domain of KshA, the oxygenase component of 3-ketosteroid 9-alpha-hydroxylase (KSH). The terminal oxygenase component of KSH is a key enzyme in the microbial steroid degradation pathway, catalyzing the 9 alpha-hydroxylation of 4-androstene-3,17-dione (AD) and 1,4-androstadiene-3,17-dione (ADD). KSH is a two-component class IA monooxygenase, with terminal oxygenase (KshA) and oxygenase reductase (KshB) components. KSH activity has been found in many actino- and proteo- bacterial genera including Rhodococcus, Nocardia, Arthrobacter, Mycobacterium, and Burkholderia. Pssm-ID: 239607 [Multi-domain] Cd Length: 115 Bit Score: 66.28 E-value: 2.69e-13
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| Rieske_RO_Alpha_OMO_CARDO | cd03548 | Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole ... |
83-218 | 6.30e-10 | ||||||||
Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole 1,9a-dioxygenase (CARDO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. OMO catalyzes the NADH-dependent oxidation of the N-heterocyclic aromatic compound 2-oxoquinoline to 8-hydroxy-2-oxoquinoline, the second step in the bacterial degradation of quinoline. OMO consists of a reductase component (OMR) and an oxygenase component (OMO) that together function to shuttle electrons from the reduced pyridine nucleotide to the active site of OMO, where O2 activation and 2-oxoquinoline hydroxylation occurs. CARDO, which contains oxygenase (CARDO-O), ferredoxin (CARDO-F) and ferredoxin reductase (CARDO-R) components, catalyzes the dihydroxylation at the C1 and C9a positions of carbazole. The oxygenase component of OMO and CARDO contain only alpha subunits arranged in a trimeric structure. Pssm-ID: 239617 [Multi-domain] Cd Length: 136 Bit Score: 57.43 E-value: 6.30e-10
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| Rieske_RO_Alpha_PrnD | cd03537 | This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit of ... |
88-201 | 2.23e-09 | ||||||||
This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit of aminopyrrolnitrin oxygenase (PrnD). PrnD is a novel Rieske N-oxygenase that catalyzes the final step in the pyrrolnitrin biosynthetic pathway, the oxidation of the amino group in aminopyrrolnitrin to a nitro group, forming the antibiotic pyrrolnitrin. The biosynthesis of pyrrolnitrin is one of the best examples of enzyme-catalyzed arylamine oxidation. Although arylamine oxygenases are widely distributed within the microbial world and used in a variety of metabolic reactions, PrnD represents one of only two known examples of arylamine oxygenases or N-oxygenases involved in arylnitro group formation, the other being AurF involved in aureothin biosynthesis. Pssm-ID: 239611 [Multi-domain] Cd Length: 123 Bit Score: 55.32 E-value: 2.23e-09
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| VanA_C | pfam19112 | Vanillate O-demethylase oxygenase C-terminal domain; This domain is found in a wide variety of ... |
240-346 | 3.68e-05 | ||||||||
Vanillate O-demethylase oxygenase C-terminal domain; This domain is found in a wide variety of oxygenases such as Vanillate O-demethylase oxygenase and Toluene-4-sulfonate monooxygenase. Pssm-ID: 436978 Cd Length: 195 Bit Score: 44.71 E-value: 3.68e-05
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| Rieske_T4moC | cd03474 | Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske ... |
125-161 | 4.13e-05 | ||||||||
Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. T4mo is a four-protein complex that catalyzes the NADH- and O2-dependent hydroxylation of toluene to form p-cresol. T4mo consists of an NADH oxidoreductase (T4moF), a diiron hydroxylase (T4moH), a catalytic effector protein (T4moD), and a Rieske ferredoxin (T4moC). T4moC contains a Rieske domain and functions as an obligate electron carrier between T4moF and T4moH. Rieske ferredoxins are found as subunits of membrane oxidase complexes, cis-dihydrodiol-forming aromatic dioxygenases, bacterial assimilatory nitrite reductases, and arsenite oxidase. Rieske ferredoxins are also found as soluble electron carriers in bacterial dioxygenase and monooxygenase complexes. Pssm-ID: 239556 [Multi-domain] Cd Length: 108 Bit Score: 42.71 E-value: 4.13e-05
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| Rieske_RO_ferredoxin | cd03528 | Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ... |
88-157 | 1.13e-04 | ||||||||
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the Rieske ferredoxin component of some three-component RO systems including biphenyl dioxygenase (BPDO) and carbazole 1,9a-dioxygenase (CARDO). The RO family comprise a large class of aromatic ring-hydroxylating dioxygenases found predominantly in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth. ROs consist of two or three components: reductase, oxygenase, and ferredoxin (in some cases) components. The ferredoxin component contains either a plant-type or Rieske-type [2Fe-2S] cluster. The Rieske ferredoxin component in this family carries an electron from the RO reductase component to the terminal RO oxygenase component. BPDO degrades biphenyls and polychlorinated biphenyls. BPDO ferredoxin (BphF) has structural features consistent with a minimal and perhaps archetypical Rieske protein in that the insertions that give other Rieske proteins unique structural features are missing. CARDO catalyzes dihydroxylation at the C1 and C9a positions of carbazole. Rieske ferredoxins are found as subunits of membrane oxidase complexes, cis-dihydrodiol-forming aromatic dioxygenases, bacterial assimilatory nitrite reductases, and arsenite oxidase. Rieske ferredoxins are also found as soluble electron carriers in bacterial dioxygenase and monooxygenase complexes. Pssm-ID: 239604 [Multi-domain] Cd Length: 98 Bit Score: 41.32 E-value: 1.13e-04
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| Rieske_RO_Alpha_NDO | cd03535 | Rieske non-heme iron oxygenase (RO) family, Nathphalene 1,2-dioxygenase (NDO) subfamily, ... |
125-167 | 2.72e-03 | ||||||||
Rieske non-heme iron oxygenase (RO) family, Nathphalene 1,2-dioxygenase (NDO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. NDO is a three-component RO system consisting of a reductase, a ferredoxin, and a hetero-hexameric alpha-beta subunit oxygenase component. NDO catalyzes the oxidation of naphthalene to cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene (naphthalene cis-dihydrodiol) with the consumption of O2 and NAD(P)H. NDO has a relaxed substrate specificity and can oxidize almost 100 substrates. Included in its varied activities are the enantiospecific cis-dihydroxylation of polycyclic aromatic hydrocarbons and benzocycloalkenes, benzylic hydroxylation, N- and O-dealkylation, sulfoxidation and desaturation reactions. Pssm-ID: 239609 [Multi-domain] Cd Length: 123 Bit Score: 37.79 E-value: 2.72e-03
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| Rieske_RO_Alpha_CMO | cd03541 | Rieske non-heme iron oxygenase (RO) family, Choline monooxygenase (CMO) subfamily, N-terminal ... |
125-170 | 3.64e-03 | ||||||||
Rieske non-heme iron oxygenase (RO) family, Choline monooxygenase (CMO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. CMO is a novel RO found in certain plants which catalyzes the first step in betaine synthesis. CMO is not found in animals or bacteria. In these organisms, the first step in betaine synthesis is catalyzed by either the membrane-bound choline dehydrogenase (CDH) or the soluble choline oxidase (COX). Pssm-ID: 239614 [Multi-domain] Cd Length: 118 Bit Score: 37.53 E-value: 3.64e-03
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| Rieske_NirD_small_Bacillus | cd03530 | Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar ... |
88-200 | 3.67e-03 | ||||||||
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar to the Bacillus subtilis small subunit of assimilatory nitrite reductase containing a Rieske domain. The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. Assimilatory nitrate and nitrite reductases convert nitrate through nitrite to ammonium. Pssm-ID: 239606 [Multi-domain] Cd Length: 98 Bit Score: 36.81 E-value: 3.67e-03
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