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Conserved domains on  [gi|1820434419|ref|WP_165496750|]
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Rieske 2Fe-2S domain-containing protein [Burkholderia pseudomallei]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PobA super family cl47407
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
15-134 7.07e-41

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


The actual alignment was detected with superfamily member COG5749:

Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 145.91  E-value: 7.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  15 WMPVALSEQVSGRAALAVICMEQPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVtPDGRLQCAYHGWTYDGaTGACVAIP 94
Cdd:COG5749    20 WYPVAPSEDLKPNKPKPVTLLGEPLVIWRDSDGKVVALEDRCPHRGAPLSEGRV-EGGNLRCPYHGWQFDG-DGKCVHIP 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1820434419  95 NLSANERVPAHYAAHAYKTLERDGFIWACArDAPPPAEAI 134
Cdd:COG5749    98 QLPENQPIPKNAKVKSYPVQERYGLIWVWL-GDPPQADET 136
 
Name Accession Description Interval E-value
PobA COG5749
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
15-134 7.07e-41

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


Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 145.91  E-value: 7.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  15 WMPVALSEQVSGRAALAVICMEQPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVtPDGRLQCAYHGWTYDGaTGACVAIP 94
Cdd:COG5749    20 WYPVAPSEDLKPNKPKPVTLLGEPLVIWRDSDGKVVALEDRCPHRGAPLSEGRV-EGGNLRCPYHGWQFDG-DGKCVHIP 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1820434419  95 NLSANERVPAHYAAHAYKTLERDGFIWACArDAPPPAEAI 134
Cdd:COG5749    98 QLPENQPIPKNAKVKSYPVQERYGLIWVWL-GDPPQADET 136
Rieske_RO_Alpha_Tic55 cd04338
Tic55 is a 55kDa LLS1-related non-heme iron oxygenase associated with protein transport ...
 6-132 3.22e-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: 114.16  E-value: 3.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419   6 QIRFDSIARWMPVALSEQVSGRAALAVICMEQPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVTpDGRLQCAYHGWTYDG 85
Cdd:cd04338     9 VAEYDWREEWYPLYLLKDVPTDAPLGLSVYDEPFVLFRDQNGQLRCLEDRCPHRLAKLSEGQLI-DGKLECLYHGWQFGG 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1820434419  86 aTGACVAIPNLSANERVPAHYAAHAYKTLERDGFIWACARDAPPPAE 132
Cdd:cd04338    88 -EGKCVKIPQLPADAKIPKNACVKSYEVRDSQGVVWMWMSEATPPDE 133
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 15-98 5.02e-24

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: 93.95  E-value: 5.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  15 WMPVALSEQVSGRAALAVICMEQPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVTPDGRLQCAYHGWTYDGaTGACVAIP 94
Cdd:pfam00355   2 WYPVCHSSELPEGEPKVVEVGGEPLVVFRDEDGELYALEDRCPHRGAPLSEGKVNGGGRLECPYHGWRFDG-TGKVVKVP 80


                  ....
gi 1820434419  95 NLSA 98
Cdd:pfam00355  81 APRP 84
PLN00095 PLN00095
chlorophyllide a oxygenase; Provisional
 10-129 9.01e-18

chlorophyllide a oxygenase; Provisional


Pssm-ID: 165668 [Multi-domain]  Cd Length: 394  Bit Score: 83.19  E-value: 9.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  10 DSIARWMPVALSEQVSGRAAL-AVICMEQPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVTpDGRLQCAYHGWTYDgATG 88
Cdd:PLN00095   68 DARAHWFPVAFAAGLRDEDALiAFDLFNVPWVLFRDADGEAGCIKDECAHRACPLSLGKLV-DGKAQCPYHGWEYE-TGG 145

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1820434419  89 ACVAIPnlSANERVPAHYaAHAYKTLERDGFIWACARDAPP 129
Cdd:PLN00095  146 ECAKMP--SCKKFLKGVF-ADAAPVIERDGFIFLWAGESDP 183
nirD_assim_sml TIGR02378
nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of ...
 15-121 2.92e-07

nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of nitrite reductase [NAD(P)H] (the assimilatory nitrite reductase), which associates with NirB, the large subunit (TIGR02374). In a few bacteria such as Klebsiella pneumoniae and in Fungi, the two regions are fused. [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 131431 [Multi-domain]  Cd Length: 105  Bit Score: 48.08  E-value: 2.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  15 WMPVALSEQVSGRAALAVICMEQPLVLFRDASGAVCAMEDRCAHRRA-PLSLGRV-TPDGRLQ--CAYHGWTYDGATGAC 90
Cdd:TIGR02378   2 WQDICAIDDIPEETGVCVLLGDTQIAIFRVPGDQVFAIQNMCPHKRAfVLSRGIVgDAQGELWvaCPLHKRNFRLEDGRC 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1820434419  91 VAipnlsanervPAHYAAHAYKTLERDGFIW 121
Cdd:TIGR02378  82 LE----------DDSGSVRTYEVRVEDGRVY 102
 
Name Accession Description Interval E-value
PobA COG5749
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
15-134 7.07e-41

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


Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 145.91  E-value: 7.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  15 WMPVALSEQVSGRAALAVICMEQPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVtPDGRLQCAYHGWTYDGaTGACVAIP 94
Cdd:COG5749    20 WYPVAPSEDLKPNKPKPVTLLGEPLVIWRDSDGKVVALEDRCPHRGAPLSEGRV-EGGNLRCPYHGWQFDG-DGKCVHIP 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1820434419  95 NLSANERVPAHYAAHAYKTLERDGFIWACArDAPPPAEAI 134
Cdd:COG5749    98 QLPENQPIPKNAKVKSYPVQERYGLIWVWL-GDPPQADET 136
Rieske_RO_Alpha_Tic55 cd04338
Tic55 is a 55kDa LLS1-related non-heme iron oxygenase associated with protein transport ...
 6-132 3.22e-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: 114.16  E-value: 3.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419   6 QIRFDSIARWMPVALSEQVSGRAALAVICMEQPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVTpDGRLQCAYHGWTYDG 85
Cdd:cd04338     9 VAEYDWREEWYPLYLLKDVPTDAPLGLSVYDEPFVLFRDQNGQLRCLEDRCPHRLAKLSEGQLI-DGKLECLYHGWQFGG 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1820434419  86 aTGACVAIPNLSANERVPAHYAAHAYKTLERDGFIWACARDAPPPAE 132
Cdd:cd04338    88 -EGKCVKIPQLPADAKIPKNACVKSYEVRDSQGVVWMWMSEATPPDE 133
Rieske_RO_Alpha_N cd03469
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ...
 15-130 2.11e-30

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: 111.53  E-value: 2.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  15 WMPVALSEQVSGR-AALAVICMEQPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVTPDGRLQCAYHGWTYDgATGACVAI 93
Cdd:cd03469     1 WYFVGHSSELPEPgDYVTLELGGEPLVLVRDRDGEVRAFHNVCPHRGARLCEGRGGNAGRLVCPYHGWTYD-LDGKLVGV 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1820434419  94 PNLSANERV-PAHYAAHAYKTLERDGFIWACARDAPPP 130
Cdd:cd03469    80 PREEGFPGFdKEKLGLRTVPVEEWGGLIFVNLDPDAPP 117
HcaE COG4638
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ...
 15-139 1.78e-29

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: 114.31  E-value: 1.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  15 WMPVALSEQVSGR-AALAVICMEQPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVTpDGRLQCAYHGWTYDGaTGACVAI 93
Cdd:COG4638    27 WYYVGHSSELPEPgDYLTRTILGEPVVLVRDKDGEVRAFHNVCPHRGAPLSEGRGN-GGRLVCPYHGWTYDL-DGRLVGI 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1820434419  94 PNLSANERV-PAHYAAHAYKTLERDGFIWACARDAPPPAEAIARDAR 139
Cdd:COG4638   105 PHMEGFPDFdPARAGLRSVPVEEWGGLIFVWLGPDAPPLAEYLGPLA 151
Rieske_RO_Alpha_PhDO_like cd03479
Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, ...
 15-130 1.42e-26

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: 102.32  E-value: 1.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  15 WMPVALSEQVS-GRAALAVICMEQPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVTPDGrLQCAYHGWTYDgATGACVAI 93
Cdd:cd03479    22 WQPVALSSELTeDGQPVRVRLLGEDLVAFRDTSGRVGLLDEHCPHRGASLVFGRVEECG-LRCCYHGWKFD-VDGQCLEM 99

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1820434419  94 PNLSANERVPAHYAAHAYKTLERDGFIWAC--ARDAPPP 130
Cdd:cd03479   100 PSEPPDSQLKQKVRQPAYPVRERGGLVWAYmgPAEEAPE 138
Rieske_RO_Alpha_PaO cd03480
Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, ...
 8-134 1.19e-25

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: 99.70  E-value: 1.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419   8 RFDSIARWMPVALSEQVSGRAALAVICMEQPLVLFRD-ASGAVCAMEDRCAHRRAPLSLGRVTPDGRLQCAYHGWTYDGa 86
Cdd:cd03480    11 KFDWREVWYPVAYVEDLDPSRPTPFTLLGRDLVIWWDrNSQQWRAFDDQCPHRLAPLSEGRIDEEGCLECPYHGWSFDG- 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1820434419  87 TGACVAIPNLSANERVPAHYAAHA--YKTLERDGFIWACArDAPPPAEAI 134
Cdd:cd03480    90 SGSCQRIPQAAEGGKAHTSPRACVasLPTAVRQGLLFVWP-GEPENAKAT 138
Rieske_RO_Alpha_Cao cd04337
Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the ...
 15-131 2.26e-25

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: 98.72  E-value: 2.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  15 WMPVALSEQVSGRAALAVICMEQPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVTpDGRLQCAYHGWTYDGaTGACVAIP 94
Cdd:cd04337    18 WYPVEFSKDLKMDTMVPFELFGQPWVLFRDEDGTPGCIRDECAHRACPLSLGKVI-EGRIQCPYHGWEYDG-DGECTKMP 95

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1820434419  95 NLSA-NERVpahyaaHAYKTLERDGFIWACARDAPPPA 131
Cdd:cd04337    96 STKClNVGI------AALPCMEQDGMIWVWPGDDPPAA 127
Rieske_RO_Alpha_VanA_DdmC cd03532
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and ...
 14-128 2.02e-24

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: 95.51  E-value: 2.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  14 RWMPVALSEQVSGRAALAVICmEQPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVTpDGRLQCAYHGWTYDGAtGACVAI 93
Cdd:cd03532     5 AWYVAAWADELGDKPLARTLL-GEPVVLYRTQDGRVAALEDRCPHRSAPLSKGSVE-GGGLVCGYHGLEFDSD-GRCVHM 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1820434419  94 PnlsANERVPAHYAAHAYKTLERDGFIWACARDAP 128
Cdd:cd03532    82 P---GQERVPAKACVRSYPVVERDALIWIWMGDAA 113
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 15-98 5.02e-24

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: 93.95  E-value: 5.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  15 WMPVALSEQVSGRAALAVICMEQPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVTPDGRLQCAYHGWTYDGaTGACVAIP 94
Cdd:pfam00355   2 WYPVCHSSELPEGEPKVVEVGGEPLVVFRDEDGELYALEDRCPHRGAPLSEGKVNGGGRLECPYHGWRFDG-TGKVVKVP 80


                  ....
gi 1820434419  95 NLSA 98
Cdd:pfam00355  81 APRP 84
PLN00095 PLN00095
chlorophyllide a oxygenase; Provisional
 10-129 9.01e-18

chlorophyllide a oxygenase; Provisional


Pssm-ID: 165668 [Multi-domain]  Cd Length: 394  Bit Score: 83.19  E-value: 9.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  10 DSIARWMPVALSEQVSGRAAL-AVICMEQPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVTpDGRLQCAYHGWTYDgATG 88
Cdd:PLN00095   68 DARAHWFPVAFAAGLRDEDALiAFDLFNVPWVLFRDADGEAGCIKDECAHRACPLSLGKLV-DGKAQCPYHGWEYE-TGG 145

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1820434419  89 ACVAIPnlSANERVPAHYaAHAYKTLERDGFIWACARDAPP 129
Cdd:PLN00095  146 ECAKMP--SCKKFLKGVF-ADAAPVIERDGFIFLWAGESDP 183
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 15-94 4.99e-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: 75.22  E-value: 4.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  15 WMPVALSEQVSGRAALAVICMEQPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVTpDGRLQCAYHGWTYDGATGACVAIP 94
Cdd:cd03467     1 WVVVGALSELPPGGGRVVVVGGGPVVVVRREGGEVYALSNRCTHQGCPLSEGEGE-DGCIVCPCHGSRFDLRTGEVVSGP 79
PLN02281 PLN02281
chlorophyllide a oxygenase
 15-129 8.97e-17

chlorophyllide a oxygenase


Pssm-ID: 177920 [Multi-domain]  Cd Length: 536  Bit Score: 80.93  E-value: 8.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  15 WMPVALSEQVSGRAALAVICMEQPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVTpDGRLQCAYHGWTYDgATGACVAIP 94
Cdd:PLN02281  221 WYPVAFTADLKHDTMVPIECFEQPWVIFRGEDGKPGCVRNTCAHRACPLDLGTVN-EGRIQCPYHGWEYS-TDGECKKMP 298

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1820434419  95 NLSAnervpAHYAAHAYKTLERDGFIWACARDAPP 129
Cdd:PLN02281  299 STKL-----LKVKIKSLPCLEQEGMIWIWPGDEPP 328
PLN02518 PLN02518
pheophorbide a oxygenase
 15-94 1.19e-15

pheophorbide a oxygenase


Pssm-ID: 215283 [Multi-domain]  Cd Length: 539  Bit Score: 77.60  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  15 WMPVALSEQVSGRAALAVICMEQPLVLFRD-ASGAVCAMEDRCAHRRAPLSLGRVTPDGRLQCAYHGWTYDGaTGACVAI 93
Cdd:PLN02518   91 WYPVSLVEDLDPSVPTPFQLLGRDLVLWKDpNQGEWVAFDDKCPHRLAPLSEGRIDENGHLQCSYHGWSFDG-CGSCTRI 169


                  .
gi 1820434419  94 P 94
Cdd:PLN02518  170 P 170
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 37-121 1.98e-13

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: 65.25  E-value: 1.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  37 QPLVLFRDAsGAVCAMEDRCAHRRAPLSLGRVTpDGRLQCAYHGWTYDGATGACVAipnlsanerVPAHYAAHAYKTLER 116
Cdd:COG2146    25 KQIAVFRTD-GEVYAYDNRCPHQGAPLSEGIVD-GGVVTCPLHGARFDLRTGECLG---------GPATEPLKTYPVRVE 93


                  ....*
gi 1820434419 117 DGFIW 121
Cdd:COG2146    94 DGDVY 98
Rieske_RO_Alpha_PrnD cd03537
This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit of ...
 37-121 4.20e-13

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: 65.34  E-value: 4.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  37 QPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVTpDGRLQCAYHGWTYDgATGACVAIPNLSAN----ERVPAHYAAHAYK 112
Cdd:cd03537    25 RPCVAWRGATGRAVVMDRHCSHLGANLADGRVK-DGCIQCPFHHWRYD-EQGQCVHIPGHSTAvrrlEPVPRGARQPTLV 102


                  ....*....
gi 1820434419 113 TLERDGFIW 121
Cdd:cd03537   103 TAERYGYVW 111
Rieske_RO_Alpha_OMO_CARDO cd03548
Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole ...
 15-130 5.62e-11

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: 59.36  E-value: 5.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  15 WMPVALSEQVSGRAALAVICMEQPLVLFRDAsGAVCAMEDRCAHRRAPLSlGRVT--PDGRLQCAYHGWTYDGATGACVA 92
Cdd:cd03548    15 WYPALFSHELEEGEPKGIQLCGEPILLRRVD-GKVYALKDRCLHRGVPLS-KKPEcfTKGTITCWYHGWTYRLDDGKLVT 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1820434419  93 IPNLSANERVPAHyAAHAYKTLERDGFIWACARDA----PPP 130
Cdd:cd03548    93 ILANPDDPLIGRT-GLKTYPVEEAKGMIFVFVGDGdyadPPP 133
Rieske_RO_Alpha_OHBDO_like cd03545
Rieske non-heme iron oxygenase (RO) family, Ortho-halobenzoate-1,2-dioxygenase (OHBDO)-like ...
 36-94 8.14e-10

Rieske non-heme iron oxygenase (RO) family, Ortho-halobenzoate-1,2-dioxygenase (OHBDO)-like subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of OHBDO, salicylate 5-hydroxylase (S5H), terephthalate 1,2-dioxygenase system (TERDOS) and similar proteins. 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. OHBDO converts 2-chlorobenzoate (2-CBA) to catechol as well as 2,4-dCBA and 2,5-dCBA to 4-chlorocatechol, as part of the chlorobenzoate degradation pathway. Although ortho-substituted chlorobenzoates appear to be particularly recalcitrant to biodegradation, several strains utilize 2-CBA and the dCBA derivatives as a sole carbon and energy source. 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. TERDOS is present in gram-positive bacteria and proteobacteria where it converts terephthalate (1,4-dicarboxybenzene) to protocatechuate as part of the terephthalate degradation pathway. The oxygenase component of TERDOS, called TerZ, is a hetero-hexamer with 3 alpha (TerZalpha) and 3 beta (TerZbeta) subunits.


Pssm-ID: 239616 [Multi-domain]  Cd Length: 150  Bit Score: 56.68  E-value: 8.14e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1820434419  36 EQPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVTPDGRLQCAYHGWTYDgATGACVAIP 94
Cdd:cd03545    48 DTPVVVTRAEDGSLHAWVNRCAHRGALVCRERRGNDGSLTCVYHQWAYD-LKGNLKGVP 105
Rieske_RO_Alpha_KSH cd03531
The alignment model represents the N-terminal rieske iron-sulfur domain of KshA, the oxygenase ...
 39-131 2.42e-09

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: 54.34  E-value: 2.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  39 LVLFRDASGAVCAMEDRCAHRRAPLSLGRVTPDgRLQCAYHGWTYdGATGACVAIPnlsANERVPAHYAAHAYKTLERDG 118
Cdd:cd03531    26 LVVFADSDGALNVLDAYCRHMGGDLSQGTVKGD-EIACPFHDWRW-GGDGRCKAIP---YARRVPPLARTRAWPTLERNG 100

                          90
                  ....*....|....*
gi 1820434419 119 --FIWACARDAPPPA 131
Cdd:cd03531   101 qlFVWHDPEGNPPPP 115
nirD_assim_sml TIGR02378
nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of ...
 15-121 2.92e-07

nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of nitrite reductase [NAD(P)H] (the assimilatory nitrite reductase), which associates with NirB, the large subunit (TIGR02374). In a few bacteria such as Klebsiella pneumoniae and in Fungi, the two regions are fused. [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 131431 [Multi-domain]  Cd Length: 105  Bit Score: 48.08  E-value: 2.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  15 WMPVALSEQVSGRAALAVICMEQPLVLFRDASGAVCAMEDRCAHRRA-PLSLGRV-TPDGRLQ--CAYHGWTYDGATGAC 90
Cdd:TIGR02378   2 WQDICAIDDIPEETGVCVLLGDTQIAIFRVPGDQVFAIQNMCPHKRAfVLSRGIVgDAQGELWvaCPLHKRNFRLEDGRC 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1820434419  91 VAipnlsanervPAHYAAHAYKTLERDGFIW 121
Cdd:TIGR02378  82 LE----------DDSGSVRTYEVRVEDGRVY 102
Rieske_AIFL_N cd03478
AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family ...
 36-121 2.05e-06

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.


Pssm-ID: 239560 [Multi-domain]  Cd Length: 95  Bit Score: 45.31  E-value: 2.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  36 EQPLVLFRDAsGAVCAMEDRCAHRRAPLSLGRVTpDGRLQCAYHGWTYDGATGACvaipnlsanERVPAHYAAHAYKTLE 115
Cdd:cd03478    21 DGKVLLVRQG-GEVHAIGAKCPHYGAPLAKGVLT-DGRIRCPWHGACFNLRTGDI---------EDAPALDSLPCYEVEV 89


                  ....*.
gi 1820434419 116 RDGFIW 121
Cdd:cd03478    90 EDGRVY 95
Rieske_NirD_small_Bacillus cd03530
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar ...
 15-88 4.39e-06

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: 44.52  E-value: 4.39e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820434419  15 WMPVALSEQVSGRAALAVICMEQPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVTpDGRLQCAYHGWTYDGATG 88
Cdd:cd03530     1 WIDIGALEDIPPRGARKVQTGGGEIAVFRTADDEVFALENRCPHKGGPLSEGIVH-GEYVTCPLHNWVIDLETG 73
Rieske_RO_Alpha_HBDO cd03542
Rieske non-heme iron oxygenase (RO) family, 2-Halobenzoate 1,2-dioxygenase (HBDO) subfamily, ...
 37-83 5.95e-05

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.


Pssm-ID: 239615 [Multi-domain]  Cd Length: 123  Bit Score: 42.05  E-value: 5.95e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1820434419  37 QPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVTPDGRLQCAYHGWTY 83
Cdd:cd03542    24 QPVVITRDKDGELNAFINACSHRGAMLCRRKQGNKGTFTCPFHGWTF 70
Rieske_RO_Alpha_CMO cd03541
Rieske non-heme iron oxygenase (RO) family, Choline monooxygenase (CMO) subfamily, N-terminal ...
 15-100 7.79e-05

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: 41.77  E-value: 7.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  15 WMPVALSEQV-------SGRAALA--VICmeqplvlfRDASGAVCAMEDRCAHRRAPLSLGrvtpDGR---LQCAYHGWT 82
Cdd:cd03541     2 WQVAGYSDQVkeknqyfTGRLGNVeyVVC--------RDGNGKLHAFHNVCTHRASILACG----SGKkscFVCPYHGWV 69

                          90       100
                  ....*....|....*....|....
gi 1820434419  83 YdGATGACV------AIPNLSANE 100
Cdd:cd03541    70 Y-GLDGSLTkatqatGIQNFNPKE 92
Rieske_RO_Alpha_NDO cd03535
Rieske non-heme iron oxygenase (RO) family, Nathphalene 1,2-dioxygenase (NDO) subfamily, ...
 43-130 8.20e-05

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: 41.65  E-value: 8.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  43 RDASGAVCAMEDRCAHRRAPLSLGRVTPDGRLQCAYHGWTYDGaTGACVAIPnlSANERVPAHYAA------HAYKTLER 116
Cdd:cd03535    32 RDEDGEIRAMFNSCRHRGMQVCRAEMGNTSHFRCPYHGWTYRN-TGRLVGVP--AQQEAYGGGFDKsqwglrPAPNLDSY 108

                          90
                  ....*....|....
gi 1820434419 117 DGFIWACARDAPPP 130
Cdd:cd03535   109 NGLIFGSLDPKAPS 122
Rieske_RO_ferredoxin cd03528
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ...
 36-105 4.44e-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: 39.01  E-value: 4.44e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  36 EQPLVLFRDAsGAVCAMEDRCAHRRAPLSLGRVTpDGRLQCAYHGWTYDGATGACVAIPnlsANERVPAH 105
Cdd:cd03528    22 GRPIAVYRVD-GEFYATDDLCTHGDASLSEGYVE-GGVIECPLHGGRFDLRTGKALSLP---ATEPLKTY 86
Rieske_RO_Alpha_AntDO cd03538
Rieske non-heme iron oxygenase (RO) family, Anthranilate 1,2-dioxygenase (AntDO) subfamily, ...
 36-122 6.54e-04

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.


Pssm-ID: 239612 [Multi-domain]  Cd Length: 146  Bit Score: 39.37  E-value: 6.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820434419  36 EQPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVTPDGRL-QCAYHGWTYDgATGACVAIP-----------NLSANERVP 103
Cdd:cd03538    45 DQPVVMVRHTDGSVHVLYNRCPHKGTKIVSDGCGNTGKFfRCPYHAWSFK-TDGSLLAIPlkkgyegtgfdPSHADKGMQ 123

                          90
                  ....*....|....*....
gi 1820434419 104 AHYAAHAYKtlerdGFIWA 122
Cdd:cd03538   124 RVGAVDIYR-----GFVFA 137
Rieske_RO_Alpha_S5H cd03539
This alignment model represents the N-terminal rieske iron-sulfur domain of the oxygenase ...
 36-84 1.44e-03

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.


Pssm-ID: 239613 [Multi-domain]  Cd Length: 129  Bit Score: 38.37  E-value: 1.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1820434419  36 EQPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVTPDGRLQCAYHGWTYD 84
Cdd:cd03539    23 ERSVIMTRDPDGGINVVENVCAHRGMRFCRERNGNAKDFVCPYHQWNYS 71
Rieske_RO_Alpha_BPDO_like cd03472
Rieske non-heme iron oxygenase (RO) family, Biphenyl dioxygenase (BPDO)-like subfamily, ...
 36-94 9.80e-03

Rieske non-heme iron oxygenase (RO) family, Biphenyl dioxygenase (BPDO)-like subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of BPDO and similar proteins including cumene dioxygenase (CumDO), nitrobenzene dioxygenase (NBDO), alkylbenzene dioxygenase (AkbDO) and dibenzofuran 4,4a-dioxygenase (DFDO). 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. BPDO degrades biphenyls and polychlorinated biphenyls (PCB's) while CumDO degrades cumene (isopropylbenzene), an aromatic hydrocarbon that is intermediate in size between ethylbenzene and biphenyl. NBDO catalyzes the initial reaction in nitrobenzene degradation, oxidizing the aromatic rings of mono- and dinitrotoluenes to form catechol and nitrite. NBDO belongs to the naphthalene subfamily of ROs. AkbDO is involved in alkylbenzene catabolism, converting o-xylene to 2,3- and 3,4-dimethylphenol and ethylbenzene to cis-dihydrodiol. DFDO is involved in dibenzofuran degradation.


Pssm-ID: 239554 [Multi-domain]  Cd Length: 128  Bit Score: 35.59  E-value: 9.80e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1820434419  36 EQPLVLFRDASGAVCAMEDRCAHRRAPLSLGRVTPDGRLQCAYHGWTYDGAtGACVAIP 94
Cdd:cd03472    31 EDPVIVVRQKDGSIRVFLNQCRHRGMRICRSDAGNAKAFTCTYHGWAYDTA-GNLVNVP 88
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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