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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820407785  26 SWQFLGFAGEVREPGDYVVRMLGRDEVVVIRGEDGEVRALHNSCTHRGTRLCRASLGNTAHLRCSYHGWTFANDGRLVGV 105
Cdd:cd03535     2 AWVFLGHESEIPNAGDYVVRYIGDDSFIVCRDEDGEIRAMFNSCRHRGMQVCRAEMGNTSHFRCPYHGWTYRNTGRLVGV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1820407785 106 PALRSGYPPDFDHAGHGLSAA-RVTSRRGFLFATWDPHAPDL 146
Cdd:cd03535    82 PAQQEAYGGGFDKSQWGLRPApNLDSYNGLIFGSLDPKAPSL 123

pheophorbide a oxygenase

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820407785  45 RMLGRDEVVVIRGEDGEVRALHNSCTHRGTRLCRASLGNTAHLRCSYHGWTFANDGRLVGVP-ALRSG 111
Cdd:PLN02518  109 QLLGRDLVLWKDPNQGEWVAFDDKCPHRLAPLSEGRIDENGHLQCSYHGWSFDGCGSCTRIPqAAPEG 176

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820407785  26 SWQFLGFAGEVREPGDYVVRMLGRDEVVVIRGEDGEVRALHNSCTHRGTRLCRASLGNTAHLRCSYHGWTFANDGRLVGV 105
Cdd:cd03535     2 AWVFLGHESEIPNAGDYVVRYIGDDSFIVCRDEDGEIRAMFNSCRHRGMQVCRAEMGNTSHFRCPYHGWTYRNTGRLVGV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1820407785 106 PALRSGYPPDFDHAGHGLSAA-RVTSRRGFLFATWDPHAPDL 146
Cdd:cd03535    82 PAQQEAYGGGFDKSQWGLRPApNLDSYNGLIFGSLDPKAPSL 123

C-terminal catalytic domain of the oxygenase alpha subunit of naphthalene 1,2-dioxygenase (NDO) and related aromatic ring hydroxylating dioxygenases; C-terminal catalytic domain of the oxygenase alpha subunit of naphthalene 1,2-dioxygenase (NDO) and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). This domain binds non-heme Fe(II). RHOs utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents form the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Proteins belonging to this subgroup include the terminal oxygenase alpha subunits of biphenyl dioxygenase, cumene dioxygenase from Pseudomonas fluorescens IP01, ethylbenzene dioxygenase, naphthalene 1,2-dioxygenase, nitrobenzene dioxygenase from Comamonas sp. strain JS765, toluene 2,3-dioxygenase from Pseudomonas putida F1, dioxin dioxygenase of Sphingomonas sp. Strain RW1, and the polycyclic aromatic hydrocarbons (PAHs)degrading ring-hydroxylating dioxygenase from Sphingomonas CHY-1. This subfamily belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820407785 169 EVCGPPQRVRAQGNWKIPTDNFAGDGYHMRTTHQIALDQGIYGDTlANGTRGRAGTDLTAVniatPAGHSVRAGYVidsg 248
Cdd:cd08881     3 EVVGGPQKWVIKANWKLAAENFAGDGYHTGTTHASALEAGLPPDA-ADLPPIDLGLQFTAP----WHGHGLGFFLD---- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820407785 249 ssledrdpaapqfpgypperwaelaaaqtpeqvrftSHcevAHGVVFPNTVFLSVAhdravgeesdpltrYLVVRSHVPV 328
Cdd:cd08881    74 ------------------------------------SP---QHGTIFPNLSFLPGY--------------FNTLRVWHPR 100

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820407785 329 SARETECLYWTLVPTAMDPQWRRRSYRFQARTQSAGGiLFEMDDFENFARIDDAlarSAPGRGGPVDLTLGAGLGTPARD 408
Cdd:cd08881   101 GPDETEVWTWTLVDKDAPEEVKDRVRRQYTRTFGPAG-TFEQDDGENWEEITRV---ARGYVARQVPLNYQMGLGVEPEP 176

                         250       260
                  ....*....|....*....|....*...
gi 1820407785 409 FP-GPARAEVATLSEHNQRAFYRRWAAL 435
Cdd:cd08881   177 DPgGPGIVGPGFYSEANQRGFYRRWLEL 204

Rieske non-heme iron oxygenase (RO) family, Anthranilate 1,2-dioxygenase (AntDO) 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. AntDO converts anthranilate to catechol, a naturally occurring compound formed through tryptophan degradation and an important intermediate in the metabolism of many N-heterocyclic compounds such as indole, o-nitrobenzoate, carbazole, and quinaldine.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820407785   6 RRAFIDNSVLDIEFDRVFHPSWQFLGFAGEVREPGDYVVRMLGRDEVVVIRGEDGEVRALHNSCTHRGTRLCRASLGNT- 84
Cdd:cd03538     2 KDVYTDPEIFALEMERLFGNAWIYVGHESQVPNPGDYITTRIGDQPVVMVRHTDGSVHVLYNRCPHKGTKIVSDGCGNTg 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820407785  85 AHLRCSYHGWTFANDGRLVGVPaLRSGYPP---DFDHAGHGLSA-ARVTSRRGFLFATWDPHAPDL 146
Cdd:cd03538    82 KFFRCPYHAWSFKTDGSLLAIP-LKKGYEGtgfDPSHADKGMQRvGAVDIYRGFVFARLSPSGPDF 146

Rieske non-heme iron oxygenase (RO) family, 2-Halobenzoate 1,2-dioxygenase (HBDO) 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. HBDO catalyzes the double hydroxylation of 2-halobenzoates with concomitant release of halogenide and carbon dioxide, yielding catechol.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820407785  27 WQFLGFAGEVREPGDYVVRMLGRDEVVVIRGEDGEVRALHNSCTHRGTRLCRASLGNTAHLRCSYHGWTFANDGRLVGVP 106
Cdd:cd03542     1 WVYLAHESQIPNNNDYFTTTIGRQPVVITRDKDGELNAFINACSHRGAMLCRRKQGNKGTFTCPFHGWTFSNTGKLLKVK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1820407785 107 ALRS-GYPPDFDHAG-HGLS-AARVTSRRGFLFATWDPHAPDL 146
Cdd:cd03542    81 DPKTaGYPEGFNCDGsHDLTkVARFESYRGFLFGSLNADVAPL 123

This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit (DitA) of diterpenoid dioxygenase (DTDO). DTDO is a novel aromatic-ring-hydroxylating dioxygenase found in Pseudomonas and other proteobacteria that degrades dehydroabietic acid (DhA). Specifically, DitA hydroxylates 7-oxodehydroabietic acid to 7-oxo-11,12-dihydroxy-8, 13-abietadien acid. The ditA1 and ditA2 genes encode the alpha and beta subunits of the oxygenase component of DTDO while the ditA3 gene encodes the ferredoxin component of DTDO. The organization of the genes encoding the various diterpenoid dioxygenase components, the phylogenetic distinctiveness of both the alpha subunit and the ferredoxin component, and the unusual iron-sulfur cluster of the ferredoxin all suggest that this enzyme belongs to a new class of aromatic ring-hydroxylating dioxygenases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820407785  27 WQFLGFAGEVREPGDYVVRMLGRDEVVVIRGEDGEVRALHNSCTHRGTRLCRASLGNTAHLRCSYHGWTFANDGRLVGVP 106
Cdd:cd03536     1 WVLLGHESEIPNKGDFMVRDMGSDSVIVARDKDGEIHVSLNVCPHRGMRISTTDGGNTQIHVCIYHGWAFRPNGDFIGAP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1820407785 107 ALRSG-YPPDFDHAGHGLSAARVTSRRGFLFATWDPHAPDLEE 148
Cdd:cd03536    81 VEKECmHGKMRTKAELGLHKARVTLYGGLIFATWNIDGPSFED 123

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820407785  27 WQFLGFAGEVREPGDYVVRMLGRDEVVVIRGEDGEVRALHNSCTHRGTRLCRASlGNTAHLRCSYHGWTFANDGRLvgVP 106
Cdd:cd03541     2 WQVAGYSDQVKEKNQYFTGRLGNVEYVVCRDGNGKLHAFHNVCTHRASILACGS-GKKSCFVCPYHGWVYGLDGSL--TK 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1820407785 107 ALRSGYPPDFDHAGHGLSAARVtsrrgflfATWDP 141
Cdd:cd03541    79 ATQATGIQNFNPKELGLVPLKV--------AEWGP 105

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 1820407785  27 WQFLGFAGEVrEPGDYVVRMLGRDEVVVIRGEDGEVRALHNSCTHRGTRLCRASlGNTAHLRCSYHGWTF-ANDGRLVGV 105
Cdd:cd03467     1 WVVVGALSEL-PPGGGRVVVVGGGPVVVVRREGGEVYALSNRCTHQGCPLSEGE-GEDGCIVCPCHGSRFdLRTGEVVSG 78

                  ....
gi 1820407785 106 PALR 109
Cdd:cd03467    79 PAPR 82

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 1820407785  27 WQFLGFAGEVREPGDYV-VRMLGRDeVVVIRGEDGEVRALHNSCTHRGTRLCrasLGNTAH--LRCSYHGWTFANDGRLV 103
Cdd:cd03479    22 WQPVALSSELTEDGQPVrVRLLGED-LVAFRDTSGRVGLLDEHCPHRGASLV---FGRVEEcgLRCCYHGWKFDVDGQCL 97

                  ....
gi 1820407785 104 GVPA 107
Cdd:cd03479    98 EMPS 101

Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820407785  38 EPGDYVVRMLGRDEVVVIRgEDGEVRALHNSCTHRGTRLCRASLGNTaHLRCSYHGWTF-ANDGRLVGVPALRS 110
Cdd:COG2146    13 PEGGGVVVEVGGKQIAVFR-TDGEVYAYDNRCPHQGAPLSEGIVDGG-VVTCPLHGARFdLRTGECLGGPATEP 84

chlorophyllide a oxygenase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820407785  27 WQFLGFAGEVREPGDYVVRMLGRDEVVVIRGEDGEVRALHNSCTHRGtrlCRASLGNTAHLR--CSYHGWTFANDGRLVG 104
Cdd:PLN00095   73 WFPVAFAAGLRDEDALIAFDLFNVPWVLFRDADGEAGCIKDECAHRA---CPLSLGKLVDGKaqCPYHGWEYETGGECAK 149

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1820407785 105 VPALRSGYPPDFdhaghgLSAARVTSRRGFLF---ATWDP 141
Cdd:PLN00095  150 MPSCKKFLKGVF------ADAAPVIERDGFIFlwaGESDP 183

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
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1820407785  53 VVIRGEDGEVRALHNSCTHRGtrlCRASLG--NTAHLRCSYHGWTFANDGRLVGVPALR 109
Cdd:cd04337    43 VLFRDEDGTPGCIRDECAHRA---CPLSLGkvIEGRIQCPYHGWEYDGDGECTKMPSTK 98

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820407785  32 FAGEVREPGDYVVRMLGrdEVVVIRGEDGEVRALHNSCTHRGTRLCRASLGNT-AHLRCSYHGWTFA-NDGRLVGVPAlr 109
Cdd:cd03548    20 FSHELEEGEPKGIQLCG--EPILLRRVDGKVYALKDRCLHRGVPLSKKPECFTkGTITCWYHGWTYRlDDGKLVTILA-- 95

                          90       100
                  ....*....|....*....|....*..
gi 1820407785 110 sgYPPDFDHAGHGLSAARVTSRRGFLF 136
Cdd:cd03548    96 --NPDDPLIGRTGLKTYPVEEAKGMIF 120

C-terminal catalytic domain of the oxygenase alpha subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases; C-terminal catalytic domain of the oxygenase alpha subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenase (RHO) family. RHOs, also known as aromatic ring hydroxylating dioxygenases, utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC), and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Oxygenases belonging to this family include the alpha subunits of Pseudomonas resinovorans strain CA10 anthranilate 1,2-dioxygenase, Stenotrophomonas maltophilia dicamba O-demethylase, Ralstonia sp. U2 salicylate-5-hydroxylase, Cycloclasticus sp. strain A5 polycyclic aromatic hydrocarbon dioxygenase, toluene 2,3-dioxygenase from Pseudomonas putida F1, dioxin dioxygenase of Sphingomonas sp. Strain RW1, plant choline monooxygenase, and the polycyclic aromatic hydrocarbon (PAH)-degrading ring-hydroxylating dioxygenase from Sphingomonas CHY-1. This group also includes the C-terminal catalytic domains of MupW, part of the mupirocin biosynthetic gene cluster in Pseudomonas fluorescens, and Pseudomonas aeruginosa GbcA (glycine betaine catabolism A). This family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820407785 175 QRVRAQGNWKIPTDNFAgDGYHMRTTHQialdqgiygDTLANGtrgragtdltavniaTPAGHSVRAGYVIDSGSSlEDR 254
Cdd:cd00680     3 YEYEVDCNWKLAVENFL-ECYHVPTVHP---------DTLATG---------------LPLPLLFGDHYRVDDTGE-GPG 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820407785 255 DPAAPQFPGYPPERWAELAAAQTpeqvrftshcEVAHGVVFPNTVFLSVAHdravgeesdpltrYLVVRSHVPVSARETE 334
Cdd:cd00680    57 EGLSRHWGDGKGPQSALPGLKPG----------GYLYLYLFPNLMIGLYPD-------------SLQVQQFVPIGPNKTR 113

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1820407785 335 CLYWTLVPTAMDPQWRRRSYRfqaRTQSAGGILFEMDDFENFARIDDALARSAPGRG 391
Cdd:cd00680   114 LEVRLYRPKDEDAREEFDAEL---ESLAGILRQVLDEDIELCERIQRGLRSGAFRGG 167

AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family show similarity to human AIFL, containing an N-terminal Rieske domain and a C-terminal pyridine nucleotide-disulfide oxidoreductase domain (Pyr_redox). The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. AIFL shares 35% homology with human AIF (apoptosis-inducing factor), mainly in the Pyr_redox domain. AIFL is predominantly localized to the mitochondria. AIFL induces apoptosis in a caspase-dependent manner.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820407785  46 MLGRDEVVVIRgEDGEVRALHNSCTHRGTRLCRASLGNtAHLRCSYHGWTF-ANDGRLVGVPALRS 110
Cdd:cd03478    18 DVGDGKVLLVR-QGGEVHAIGAKCPHYGAPLAKGVLTD-GRIRCPWHGACFnLRTGDIEDAPALDS 81

Ring hydroxylating alpha subunit (catalytic domain); This family is the catalytic domain of aromatic-ring- hydroxylating dioxygenase systems. The active site contains a non-heme ferrous ion coordinated by three ligands.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820407785 180 QGNWKIPTDNFAgDGYHMRTTHqialdqgiygdtlANGTRGRAGTDLTAVNIATPAGHSvRAGYVIDSGSSLEDRDPAap 259
Cdd:pfam00848  15 AANWKLAAENFL-ECYHVPVLH-------------PELLRASPPEDLPPSEAAHFDGFG-PHGRLGQGGDLRLTPAAA-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820407785 260 qfpgyPPERWAElAAAQTPEQVRFTSHCEVAHGVVFPNTVFLsvahdravgeesdPLTRYLVVRSHVPVSARETECLYWT 339
Cdd:pfam00848  78 -----SMTLDAE-AGRPELPGLPEEQDRGALFYTLFPNLSIL-------------LAPDHVVVYQLIPTGPDTTRVEVYW 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820407785 340 LVPTAMDPQWRRRSYRFQARTQSAGgilFEMDDFENFARIddalarsapgrggpvdltlGAGLGTPARDfPGParaeVAT 419
Cdd:pfam00848 139 YVPPDALAEPEFAEELEAVWDRTFG---VNQEDAELCERV-------------------QRGLRSRGYE-PGP----VFG 191

                         250
                  ....*....|....*....
gi 1820407785 420 LSEHNQRAFYRRWAALVGE 438
Cdd:pfam00848 192 RQEGGVRHFHEWVRDRLAE 210