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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154708950  12 LCPSSHLAEGNSRGFLVDERRLFAVRR-DGRAYIYLNRCPHRGIPLEWQpdaflDDSASLIRCASHGALFLIESGECVAG 90
Cdd:cd03467     4 VGALSELPPGGGRVVVVGGGPVVVVRReGGEVYALSNRCTHQGCPLSEG-----EGEDGCIVCPCHGSRFDLRTGEVVSG 78

                          90
                  ....*....|....*...
gi 1154708950  91 PCAGeRLRALPCREDAEG 108
Cdd:cd03467    79 PAPR-PLPKYPVKVEGDG 95

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154708950  12 LCPSSHLAEGNSRGFLVDERRLFAVRR-DGRAYIYLNRCPHRGIPLEWQpdaflDDSASLIRCASHGALFLIESGECVAG 90
Cdd:cd03467     4 VGALSELPPGGGRVVVVGGGPVVVVRReGGEVYALSNRCTHQGCPLSEG-----EGEDGCIVCPCHGSRFDLRTGEVVSG 78

                          90
                  ....*....|....*...
gi 1154708950  91 PCAGeRLRALPCREDAEG 108
Cdd:cd03467    79 PAPR-PLPKYPVKVEGDG 95

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154708950  12 LCPSSHLAE-GNSRGFLVDERRLFAVR-RDGRAYIYLNRCPHRGIPLEWQPdaflDDSASLIRCASHGALFLIEsGECVA 89
Cdd:cd03469     4 VGHSSELPEpGDYVTLELGGEPLVLVRdRDGEVRAFHNVCPHRGARLCEGR----GGNAGRLVCPYHGWTYDLD-GKLVG 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1154708950  90 GPCAGE---------RLRALPCREDAEGLWVELDD 115
Cdd:cd03469    79 VPREEGfpgfdkeklGLRTVPVEEWGGLIFVNLDP 113

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154708950   9 MIHLCPSSHLAEGNSRGFLVDERRLFAVRRDGRAYIYLNRCPHRGIPLEwqpDAFLDDSAslIRCASHGALFLIESGECV 88
Cdd:cd03528     1 WVRVCAVDELPEGEPKRVDVGGRPIAVYRVDGEFYATDDLCTHGDASLS---EGYVEGGV--IECPLHGGRFDLRTGKAL 75

                          90       100
                  ....*....|....*....|....*.
gi 1154708950  89 AGPCAgERLRALPCREdaEGLWVELD 114
Cdd:cd03528    76 SLPAT-EPLKTYPVKV--EDGDVYVD 98

Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154708950  39 DGRAYIYLNRCPHRGIPLewqpdaflddsaSL-------IRCASHGALFlIESGECVAGPCAGE--------RLRALPCR 103
Cdd:COG5749    51 DGKVVALEDRCPHRGAPL------------SEgrveggnLRCPYHGWQF-DGDGKCVHIPQLPEnqpipknaKVKSYPVQ 117

                          90
                  ....*....|..
gi 1154708950 104 EDAEGLWVELDD 115
Cdd:COG5749   118 ERYGLIWVWLGD 129

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154708950   5 NGAPM--------IHLCPSSHLAEGNS--RGFLVDERrLFAVR-RDGRAYIYLNRCPHRGIPLEWqpdAFLDDSAslIRC 73
Cdd:cd03479    10 PGTPMgellrrywQPVALSSELTEDGQpvRVRLLGED-LVAFRdTSGRVGLLDEHCPHRGASLVF---GRVEECG--LRC 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1154708950  74 ASHGALFLIEsGECVAGPCAGE--------RLRALPCREDAEGLWV 111
Cdd:cd03479    84 CYHGWKFDVD-GQCLEMPSEPPdsqlkqkvRQPAYPVRERGGLVWA 128

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154708950  39 DGRAYIYLNRCPHRGIPLewqpdaflddsaSL-------IRCASHGALFlIESGECVAGP---CAGERLRALPCREDAEG 108
Cdd:cd04337    49 DGTPGCIRDECAHRACPL------------SLgkviegrIQCPYHGWEY-DGDGECTKMPstkCLNVGIAALPCMEQDGM 115

                  ...
gi 1154708950 109 LWV 111
Cdd:cd04337   116 IWV 118