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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172798932   2 EQAIINDEREYLRHFWHPVCTVTELEKAhpsslGPLAVKLLNEQLVVAKLGD-EYVAMRDRCAHRSAKLSLGTVSGNRLQ 80
Cdd:COG5749     5 RQGPGFNQPFIFRNHWYPVAPSEDLKPN-----KPKPVTLLGEPLVIWRDSDgKVVALEDRCPHRGAPLSEGRVEGGNLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172798932  81 CPYHGWQYDTHGACQLVPACP-NSPIPNKAKVDRFDCEERYGLIWIRLD--SSFDCTEIPYFSAANDP---RLRIVIQEP 154
Cdd:COG5749    80 CPYHGWQFDGDGKCVHIPQLPeNQPIPKNAKVKSYPVQERYGLIWVWLGdpPQADETPIPDIPELDDPewvATSSVRDLE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172798932 155 YWWDATAerrwENFTDFSHFAFIHPGTLFDPNNAEPPIVPMDRFNGQFRFVYDTP--EDMAVPNQAPIGSFSYTC-SMPF 231
Cdd:COG5749   160 CHYSRLI----ENLIDPSHVPFVHHGTQGNRKQAQPLEMEIESTPNGITASYTAQsyYQLFFPFLGNLDETLTITfIYPN 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172798932 232 AINLEVSkYSSSSLHVLFNVSCPVDSHTTKNFLIFAREQSDDSDYL---HIAFNDLVFAEDKPVIESQWPKDAP--ADEV 306
Cdd:COG5749   236 TVSVDIG-SGLGGRFGIVLYATPIDEGKTRAYAIFFRNFAKKPRWLrhfLKLLRNGILEQDVIILESQQPALLQlgSYEL 314

                         330       340
                  ....*....|....*....|....*...
gi 1172798932 307 SVVADKVSIQYRKWLRELKEAHKEGSQA 334
Cdd:COG5749   315 PTPADRAIIEFRRWLDKQAAGEGPWQEV 342

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172798932   2 EQAIINDEREYLRHFWHPVCTVTELEKAhpsslGPLAVKLLNEQLVVAKLGD-EYVAMRDRCAHRSAKLSLGTVSGNRLQ 80
Cdd:COG5749     5 RQGPGFNQPFIFRNHWYPVAPSEDLKPN-----KPKPVTLLGEPLVIWRDSDgKVVALEDRCPHRGAPLSEGRVEGGNLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172798932  81 CPYHGWQYDTHGACQLVPACP-NSPIPNKAKVDRFDCEERYGLIWIRLD--SSFDCTEIPYFSAANDP---RLRIVIQEP 154
Cdd:COG5749    80 CPYHGWQFDGDGKCVHIPQLPeNQPIPKNAKVKSYPVQERYGLIWVWLGdpPQADETPIPDIPELDDPewvATSSVRDLE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172798932 155 YWWDATAerrwENFTDFSHFAFIHPGTLFDPNNAEPPIVPMDRFNGQFRFVYDTP--EDMAVPNQAPIGSFSYTC-SMPF 231
Cdd:COG5749   160 CHYSRLI----ENLIDPSHVPFVHHGTQGNRKQAQPLEMEIESTPNGITASYTAQsyYQLFFPFLGNLDETLTITfIYPN 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172798932 232 AINLEVSkYSSSSLHVLFNVSCPVDSHTTKNFLIFAREQSDDSDYL---HIAFNDLVFAEDKPVIESQWPKDAP--ADEV 306
Cdd:COG5749   236 TVSVDIG-SGLGGRFGIVLYATPIDEGKTRAYAIFFRNFAKKPRWLrhfLKLLRNGILEQDVIILESQQPALLQlgSYEL 314

                         330       340
                  ....*....|....*....|....*...
gi 1172798932 307 SVVADKVSIQYRKWLRELKEAHKEGSQA 334
Cdd:COG5749   315 PTPADRAIIEFRRWLDKQAAGEGPWQEV 342

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172798932  17 WHPVCTVTELEKAhpsslGPLAVKLLNEQLVVAKLGD-EYVAMRDRCAHRSAKLSLGTV-SGNRLQCPYHGWQYDTHGAC 94
Cdd:pfam00355   2 WYPVCHSSELPEG-----EPKVVEVGGEPLVVFRDEDgELYALEDRCPHRGAPLSEGKVnGGGRLECPYHGWRFDGTGKV 76

                  ....*...
gi 1172798932  95 QLVPACPN 102
Cdd:pfam00355  77 VKVPAPRP 84

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172798932   2 EQAIINDEREYLRHFWHPVCTVTELEKAhpsslGPLAVKLLNEQLVVAKLGD-EYVAMRDRCAHRSAKLSLGTVSGNRLQ 80
Cdd:COG5749     5 RQGPGFNQPFIFRNHWYPVAPSEDLKPN-----KPKPVTLLGEPLVIWRDSDgKVVALEDRCPHRGAPLSEGRVEGGNLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172798932  81 CPYHGWQYDTHGACQLVPACP-NSPIPNKAKVDRFDCEERYGLIWIRLD--SSFDCTEIPYFSAANDP---RLRIVIQEP 154
Cdd:COG5749    80 CPYHGWQFDGDGKCVHIPQLPeNQPIPKNAKVKSYPVQERYGLIWVWLGdpPQADETPIPDIPELDDPewvATSSVRDLE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172798932 155 YWWDATAerrwENFTDFSHFAFIHPGTLFDPNNAEPPIVPMDRFNGQFRFVYDTP--EDMAVPNQAPIGSFSYTC-SMPF 231
Cdd:COG5749   160 CHYSRLI----ENLIDPSHVPFVHHGTQGNRKQAQPLEMEIESTPNGITASYTAQsyYQLFFPFLGNLDETLTITfIYPN 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172798932 232 AINLEVSkYSSSSLHVLFNVSCPVDSHTTKNFLIFAREQSDDSDYL---HIAFNDLVFAEDKPVIESQWPKDAP--ADEV 306
Cdd:COG5749   236 TVSVDIG-SGLGGRFGIVLYATPIDEGKTRAYAIFFRNFAKKPRWLrhfLKLLRNGILEQDVIILESQQPALLQlgSYEL 314

                         330       340
                  ....*....|....*....|....*...
gi 1172798932 307 SVVADKVSIQYRKWLRELKEAHKEGSQA 334
Cdd:COG5749   315 PTPADRAIIEFRRWLDKQAAGEGPWQEV 342

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 1172798932  17 WHPVCTVTELEKAHpsslGPLAVKLLNEQLVVAKLGDEYV-AMRDRCAHRSAKLSLGTV-SGNRLQCPYHGWQYDTHGAC 94
Cdd:cd03469     1 WYFVGHSSELPEPG----DYVTLELGGEPLVLVRDRDGEVrAFHNVCPHRGARLCEGRGgNAGRLVCPYHGWTYDLDGKL 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1172798932  95 QLVPACPNSP--IPNKAKVDRFDCEERYGLIWIRLD 128
Cdd:cd03469    77 VGVPREEGFPgfDKEKLGLRTVPVEEWGGLIFVNLD 112

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172798932  12 YLRHFWHPVCTVTELEKahpsslGPLAVKLLNEQLVVAKLGD-EYVAMRDRCAHRSAKLSLGTVSGNRLQCPYHGWQYDT 90
Cdd:cd03532     1 FPRNAWYVAAWADELGD------KPLARTLLGEPVVLYRTQDgRVAALEDRCPHRSAPLSKGSVEGGGLVCGYHGLEFDS 74

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1172798932  91 HGACQLVPAcpNSPIPNKAKVDRFDCEERYGLIWI 125
Cdd:cd03532    75 DGRCVHMPG--QERVPAKACVRSYPVVERDALIWI 107

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 1172798932  11 EYLRHFWHPVCTVTELEKAHPsslgpLAVKLLNEQLVVAKLGDEYVA-MRDRCAHRSAKLSLGTVSGNRLQCPYHGWQYD 89
Cdd:cd04337    12 PGLRNFWYPVEFSKDLKMDTM-----VPFELFGQPWVLFRDEDGTPGcIRDECAHRACPLSLGKVIEGRIQCPYHGWEYD 86

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1172798932  90 THGACQLVPACPNSPIPNKAkvdrFDCEERYGLIWI 125
Cdd:cd04337    87 GDGECTKMPSTKCLNVGIAA----LPCMEQDGMIWV 118

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172798932  14 RHFWHPVCTVTELekahPSSLgPLAVKLLNEQLVVAKLGD-EYVAMRDRCAHRSAKLSLGTVSGNRLQCPYHGWQYDTHG 92
Cdd:cd04338    15 REEWYPLYLLKDV----PTDA-PLGLSVYDEPFVLFRDQNgQLRCLEDRCPHRLAKLSEGQLIDGKLECLYHGWQFGGEG 89

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1172798932  93 ACQLVPACPNSP-IPNKAKVDRFDCEERYGLIWI 125
Cdd:cd04338    90 KCVKIPQLPADAkIPKNACVKSYEVRDSQGVVWM 123

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172798932  17 WHPVCTVTELEKAhpsslGPLAVKLLNEQLVVAKLGDEYVAMRDRCAHRSAKLSLGTVSGNRLQCPYHGWQYDTH-GACQ 95
Cdd:COG2146     3 EVKVCALDDLPEG-----GGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLSEGIVDGGVVTCPLHGARFDLRtGECL 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1172798932  96 LVPACpnspipnkAKVDRFDCEERYGLIWIRLD 128
Cdd:COG2146    78 GGPAT--------EPLKTYPVRVEDGDVYVDLP 102

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 1172798932  17 WHPVCTVTELEKAhpsslGPLAVKLLNEQLVVAKL-GDEYVAMRDRCAHRSAKLSLGTVSGNRLQCPYHGWQYDTH-GAC 94
Cdd:cd03467     1 WVVVGALSELPPG-----GGRVVVVGGGPVVVVRReGGEVYALSNRCTHQGCPLSEGEGEDGCIVCPCHGSRFDLRtGEV 75

                          90       100
                  ....*....|....*....|.
gi 1172798932  95 QLVPACPNSPIPnKAKVDRFD 115
Cdd:cd03467    76 VSGPAPRPLPKY-PVKVEGDG 95

pheophorbide a oxygenase

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172798932   8 DEREYLRHFWHPVCTVTELEKAHPSSLgplavKLLNEQLVVAKLGD--EYVAMRDRCAHRSAKLSLGTVSGN-RLQCPYH 84
Cdd:PLN02518   82 DSKFSWRDHWYPVSLVEDLDPSVPTPF-----QLLGRDLVLWKDPNqgEWVAFDDKCPHRLAPLSEGRIDENgHLQCSYH 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172798932  85 GWQYDTHGACQLVP-ACPNSPiPNKAKVDRFDCEERY------GLIWIRLD----SSFDCTEIPYFSAA-NDPRLRIV-I 151
Cdd:PLN02518  157 GWSFDGCGSCTRIPqAAPEGP-EARAVKSPRACAIKFptmvsqGLLFVWPDengwERAQATKPPMLPDEfDDPEFSTVtI 235

                         170       180
                  ....*....|....*....|....*....
gi 1172798932 152 QEP--YWWDATAerrwENFTDFSHFAFIH 178
Cdd:PLN02518  236 QRDlfYGYDTLM----ENVSDPSHIDFAH 260

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172798932  36 PLAVKLLNEQLVVAK-LGDEYVAMRDRCAHRSAKLSLGTVSGNRLQCPYHGWQYDTHGACQLVP----ACPN-SPIPNKA 109
Cdd:cd03537    17 PTELTLFGRPCVAWRgATGRAVVMDRHCSHLGANLADGRVKDGCIQCPFHHWRYDEQGQCVHIPghstAVRRlEPVPRGA 96

                          90
                  ....*....|....*.
gi 1172798932 110 KVDRFDCEERYGLIWI 125
Cdd:cd03537    97 RQPTLVTAERYGYVWV 112

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 1172798932  17 WHPVCTVTELEKAhpsslGPLAVKLLNEQLVVAKLGDEYVAMRDRCAHRSAKLSLGTVSGNRLQCPYHGWQYD-THGACQ 95
Cdd:cd03528     1 WVRVCAVDELPEG-----EPKRVDVGGRPIAVYRVDGEFYATDDLCTHGDASLSEGYVEGGVIECPLHGGRFDlRTGKAL 75

                  ....*
gi 1172798932  96 LVPAC 100
Cdd:cd03528    76 SLPAT 80

C-terminal catalytic domain of the oxygenase alpha subunit of dicamba O-demethylase and related aromatic ring hydroxylating dioxygenases; C-terminal catalytic domain of the oxygenase alpha subunit of Stenotrophomonas maltophilia dicamba O-demethylase (DMO) and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). 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 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 the C-terminal catalytic domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Oxygenases belonging to this subgroup include the alpha subunits of carbazole 1,9a-dioxygenase, phthalate dioxygenase, vanillate O-demethylase, Pseudomonas putida 2-oxoquinoline 8-monooxygenase, and Comamonas testosteroni T-2 p-toluenesulfonate dioxygenase. It also includes the C-terminal domain of the lignin biphenyl-specific O-demethylase (LigX) of the 5,5'-dehydrodivanillic acid O- demethylation system of Sphingomonas paucimobilis SYK-6. 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 1172798932 166 ENFTDFSHFAFIHPGTLF-----DPNNAEPPIVPMDRFNGQFRFVYDTPEdMAVPNQAPIGSFSYT-CSMPFAINLEVSK 239
Cdd:cd08878    17 ENLMDPSHVSFVHRSSIGrdaadLPSGPPKEVEEVPRGVTYRRWREDEDP-PPFGFEGPVDRWRVIeFLLPNVLLIDPGV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172798932 240 YSSSSLHVLFNVS-----CPVDSHTTKNFLIFAREQSDDSDYL-HIAFNDL-------VFAEDKPVIESQWP--KDAPAD 304
Cdd:cd08878    96 APAGTREQGVRMRvthwiTPIDETTTHYFWFFVRNFAPDEEKKdDEELTETlrsglsgAFNEDKEAVEAQQRiiDRDPTR 175

                         170       180
                  ....*....|....*....|
gi 1172798932 305 EVSVVADKVSIQYRKWLREL 324
Cdd:cd08878   176 EHLGLSDKGIVRFRRLLRRL 195

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 1172798932  45 QLVVAKLGD-EYVAMRDR----------CAHRSAKLSLGTVSGNRLQCPYHGWQYDTHGAcqLVPACPNSPIPNkakvdr 113
Cdd:cd03541    16 QYFTGRLGNvEYVVCRDGngklhafhnvCTHRASILACGSGKKSCFVCPYHGWVYGLDGS--LTKATQATGIQN------ 87

                          90       100       110
                  ....*....|....*....|....*....|
gi 1172798932 114 FDCEErYGLI------W-----IRLDSSFD 132
Cdd:cd03541    88 FNPKE-LGLVplkvaeWgpfvlISVDRSLS 116

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.

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gi 1172798932  57 AMRDRCAHRSAKLSlGTVSGN--RLQCPYHGWQYDTHGACQLVPA 99
Cdd:cd03535    40 AMFNSCRHRGMQVC-RAEMGNtsHFRCPYHGWTYRNTGRLVGVPA 83

This alignment model represents the N-terminal rieske iron-sulfur domain of the oxygenase alpha subunit (NagG) of salicylate 5-hydroxylase (S5H). S5H converts salicylate (2-hydroxybenzoate), a metabolic intermediate of phenanthrene, to gentisate (2,5-dihydroxybenzoate) as part of an alternate pathway for naphthalene catabolism. S5H is a multicomponent enzyme made up of NagGH (the oxygenase components), NagAa (the ferredoxin reductase component), and NagAb (the ferredoxin component). The oxygenase component is made up of alpha (NagG) and beta (NagH) subunits.

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gi 1172798932  62 CAHRSAKLSLGTvSGNR--LQCPYHGWQYDTHGACQLVP 98
Cdd:cd03539    43 CAHRGMRFCRER-NGNAkdFVCPYHQWNYSLKGDLQGVP 80