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Conserved domains on  [gi|71983709|ref|NP_505629|]
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Cholesterol 7-desaturase [Caenorhabditis elegans]

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];
73-243 2.90e-34

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: 130.51  E-value: 2.90e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  73 MPPVFPNGWYCVCESEKLANNQIMEITVLGQFLSLIRSESGAVYITDSYCPHIGANFNiGGRVVrDNCIQCPFHGWIFSA 152
Cdd:COG5749  12 QPFIFRNHWYPVAPSEDLKPNKPKPVTLLGEPLVIWRDSDGKVVALEDRCPHRGAPLS-EGRVE-GGNLRCPYHGWQFDG 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709 153 EtGKCVEVPY--DEGRIPEQAKVTTWPCIERNNNIYLWYhcdGAEP---EWEIPEITEITDGFWHLGGrTEHEVMCHIQE 227
Cdd:COG5749  90 D-GKCVHIPQlpENQPIPKNAKVKSYPVQERYGLIWVWL---GDPPqadETPIPDIPELDDPEWVATS-SVRDLECHYSR 164

                       170
                ....*....|....*.
gi 71983709 228 IPENGADIAHLNYLHK 243
Cdd:COG5749 165 LIENLIDPSHVPFVHH 180
KshA_C super family cl41947
3-Ketosteroid 9alpha-hydroxylase C-terminal domain; KshAB is a complex of KshA and KshB that ...
 188-405 3.59e-33

3-Ketosteroid 9alpha-hydroxylase C-terminal domain; KshAB is a complex of KshA and KshB that catalyzes the 3-Ketosteroid 9alpha-hydroxylase reaction. This entry represents the C-terminal domain catalytic domain of KshA. This domain The catalytic domain shares the TBP-like fold found in other Rieske oxygenases.


The actual alignment was detected with superfamily member pfam19298:

Pssm-ID: 466031  Cd Length: 203  Bit Score: 123.51  E-value: 3.59e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709   188 WYHCDGAEPEWEIPEITEITDGF--WHLGgrtEHEVMCHIQEIPENGADIAHLNYLHKSAPPVTKgsdiiktdlsdpqpa 265
Cdd:pfam19298   2 WHDPEGNPPDVEIPRIEGDDPDWtdWRWD---TLVLEAHPREVVDNVVDMAHFFYVHGSFPTYFK--------------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709   266 vqHVWDGkwevkseedrHCGVmhlnQFMTFWGYKVPLTSS-----KLVAEQHGPG--IVHMLFDFGIW-GKGVVFQTVTP 337
Cdd:pfam19298  64 --NVFEG----------HVAT----QYMTGFGRGGSRTLDagsglRSVASYYGPAymISWLTYDYEGGdVESVLINCHTP 127

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71983709   338 EEALLQRVRFRIF--------SNIPWFFVKFFMTVEAMQFERDVFIWSNKKYIKSPLLVKNDGPIQKHRRWFSQFY 405
Cdd:pfam19298 128 VDDNSFVLQFGVIvkklpglsDEEAAALARGFADGVLRGFEQDVEIWKNKTRIDNPLLCEEDGPVYQLRRWYEQFY 203
 
Name Accession Description Interval E-value
PobA COG5749
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
73-243 2.90e-34

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


Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 130.51  E-value: 2.90e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  73 MPPVFPNGWYCVCESEKLANNQIMEITVLGQFLSLIRSESGAVYITDSYCPHIGANFNiGGRVVrDNCIQCPFHGWIFSA 152
Cdd:COG5749  12 QPFIFRNHWYPVAPSEDLKPNKPKPVTLLGEPLVIWRDSDGKVVALEDRCPHRGAPLS-EGRVE-GGNLRCPYHGWQFDG 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709 153 EtGKCVEVPY--DEGRIPEQAKVTTWPCIERNNNIYLWYhcdGAEP---EWEIPEITEITDGFWHLGGrTEHEVMCHIQE 227
Cdd:COG5749  90 D-GKCVHIPQlpENQPIPKNAKVKSYPVQERYGLIWVWL---GDPPqadETPIPDIPELDDPEWVATS-SVRDLECHYSR 164

                       170
                ....*....|....*.
gi 71983709 228 IPENGADIAHLNYLHK 243
Cdd:COG5749 165 LIENLIDPSHVPFVHH 180
KshA_C pfam19298
3-Ketosteroid 9alpha-hydroxylase C-terminal domain; KshAB is a complex of KshA and KshB that ...
 188-405 3.59e-33

3-Ketosteroid 9alpha-hydroxylase C-terminal domain; KshAB is a complex of KshA and KshB that catalyzes the 3-Ketosteroid 9alpha-hydroxylase reaction. This entry represents the C-terminal domain catalytic domain of KshA. This domain The catalytic domain shares the TBP-like fold found in other Rieske oxygenases.


Pssm-ID: 466031  Cd Length: 203  Bit Score: 123.51  E-value: 3.59e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709   188 WYHCDGAEPEWEIPEITEITDGF--WHLGgrtEHEVMCHIQEIPENGADIAHLNYLHKSAPPVTKgsdiiktdlsdpqpa 265
Cdd:pfam19298   2 WHDPEGNPPDVEIPRIEGDDPDWtdWRWD---TLVLEAHPREVVDNVVDMAHFFYVHGSFPTYFK--------------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709   266 vqHVWDGkwevkseedrHCGVmhlnQFMTFWGYKVPLTSS-----KLVAEQHGPG--IVHMLFDFGIW-GKGVVFQTVTP 337
Cdd:pfam19298  64 --NVFEG----------HVAT----QYMTGFGRGGSRTLDagsglRSVASYYGPAymISWLTYDYEGGdVESVLINCHTP 127

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71983709   338 EEALLQRVRFRIF--------SNIPWFFVKFFMTVEAMQFERDVFIWSNKKYIKSPLLVKNDGPIQKHRRWFSQFY 405
Cdd:pfam19298 128 VDDNSFVLQFGVIvkklpglsDEEAAALARGFADGVLRGFEQDVEIWKNKTRIDNPLLCEEDGPVYQLRRWYEQFY 203
Rieske_RO_Alpha_N cd03469
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ...
 81-196 3.45e-27

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: 104.59  E-value: 3.45e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  81 WYCVCESEKLAN-NQIMEITVLGQFLSLIRSESGAVYITDSYCPHIGANFnIGGRVVRDNCIQCPFHGWIFSAEtGKCVE 159
Cdd:cd03469   1 WYFVGHSSELPEpGDYVTLELGGEPLVLVRDRDGEVRAFHNVCPHRGARL-CEGRGGNAGRLVCPYHGWTYDLD-GKLVG 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 71983709 160 VPY---DEGRIPEQAKVTTWPCIERNNNIYLWYHCDGAEP 196
Cdd:cd03469  79 VPReegFPGFDKEKLGLRTVPVEEWGGLIFVNLDPDAPPL 118
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 80-177 1.04e-17

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: 77.77  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709    80 GWYCVCESEKLANNQIMEITVLGQFLSLIRSESGAVYITDSYCPHIGANFnIGGRVVRDNCIQCPFHGWIFSaETGKCVE 159
Cdd:pfam00355   1 SWYPVCHSSELPEGEPKVVEVGGEPLVVFRDEDGELYALEDRCPHRGAPL-SEGKVNGGGRLECPYHGWRFD-GTGKVVK 78

                          90
                  ....*....|....*...
gi 71983709   160 VPYdegripeQAKVTTWP 177
Cdd:pfam00355  79 VPA-------PRPLKSYP 89
PLN02281 PLN02281
chlorophyllide a oxygenase
 57-271 1.87e-11

chlorophyllide a oxygenase


Pssm-ID: 177920 [Multi-domain]  Cd Length: 536  Bit Score: 65.91  E-value: 1.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709   57 RERQLERLKLLRRVGDMPPVFP---NGWYCVCESEKLANNQIMEITVLGQFLSLIRSESGAVYITDSYCPHIGANFNIGg 133
Cdd:PLN02281 194 REKTNTGAKSLNVSGPVPPYSPhlkNFWYPVAFTADLKHDTMVPIECFEQPWVIFRGEDGKPGCVRNTCAHRACPLDLG- 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  134 rVVRDNCIQCPFHGWIFSAEtGKCVEVPYDEgriPEQAKVTTWPCIERNNNIYLWyhcDGAEPEWEIPEITEITDGFW-H 212
Cdd:PLN02281 273 -TVNEGRIQCPYHGWEYSTD-GECKKMPSTK---LLKVKIKSLPCLEQEGMIWIW---PGDEPPAPILPSLQPPSGFLiH 344

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71983709  213 ----LGGRTEHEVMChiqeipENGADIAHLNYLHKSAppVTKGSDIIK-TDLSDPQPAVQHVWD 271
Cdd:PLN02281 345 aelvMDLPVEHGLLL------DNLLDLAHAPFTHTST--FAKGWSVPSlVKFLTPTSGLQGYWD 400
nirD_assim_sml TIGR02378
nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of ...
 81-187 4.23e-08

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: 50.78  E-value: 4.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709    81 WYCVCESEKLANNQIMEITVLGQFLSLIRSESGAVYITDSYCPHIGANFNIGGRVVRDN---CIQCPFHGWIFSAETGKC 157
Cdd:TIGR02378   2 WQDICAIDDIPEETGVCVLLGDTQIAIFRVPGDQVFAIQNMCPHKRAFVLSRGIVGDAQgelWVACPLHKRNFRLEDGRC 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 71983709   158 VEvpydegriPEQAKVTTWPCIERNNNIYL 187
Cdd:TIGR02378  82 LE--------DDSGSVRTYEVRVEDGRVYV 103
 
Name Accession Description Interval E-value
PobA COG5749
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
73-243 2.90e-34

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


Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 130.51  E-value: 2.90e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  73 MPPVFPNGWYCVCESEKLANNQIMEITVLGQFLSLIRSESGAVYITDSYCPHIGANFNiGGRVVrDNCIQCPFHGWIFSA 152
Cdd:COG5749  12 QPFIFRNHWYPVAPSEDLKPNKPKPVTLLGEPLVIWRDSDGKVVALEDRCPHRGAPLS-EGRVE-GGNLRCPYHGWQFDG 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709 153 EtGKCVEVPY--DEGRIPEQAKVTTWPCIERNNNIYLWYhcdGAEP---EWEIPEITEITDGFWHLGGrTEHEVMCHIQE 227
Cdd:COG5749  90 D-GKCVHIPQlpENQPIPKNAKVKSYPVQERYGLIWVWL---GDPPqadETPIPDIPELDDPEWVATS-SVRDLECHYSR 164

                       170
                ....*....|....*.
gi 71983709 228 IPENGADIAHLNYLHK 243
Cdd:COG5749 165 LIENLIDPSHVPFVHH 180
KshA_C pfam19298
3-Ketosteroid 9alpha-hydroxylase C-terminal domain; KshAB is a complex of KshA and KshB that ...
 188-405 3.59e-33

3-Ketosteroid 9alpha-hydroxylase C-terminal domain; KshAB is a complex of KshA and KshB that catalyzes the 3-Ketosteroid 9alpha-hydroxylase reaction. This entry represents the C-terminal domain catalytic domain of KshA. This domain The catalytic domain shares the TBP-like fold found in other Rieske oxygenases.


Pssm-ID: 466031  Cd Length: 203  Bit Score: 123.51  E-value: 3.59e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709   188 WYHCDGAEPEWEIPEITEITDGF--WHLGgrtEHEVMCHIQEIPENGADIAHLNYLHKSAPPVTKgsdiiktdlsdpqpa 265
Cdd:pfam19298   2 WHDPEGNPPDVEIPRIEGDDPDWtdWRWD---TLVLEAHPREVVDNVVDMAHFFYVHGSFPTYFK--------------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709   266 vqHVWDGkwevkseedrHCGVmhlnQFMTFWGYKVPLTSS-----KLVAEQHGPG--IVHMLFDFGIW-GKGVVFQTVTP 337
Cdd:pfam19298  64 --NVFEG----------HVAT----QYMTGFGRGGSRTLDagsglRSVASYYGPAymISWLTYDYEGGdVESVLINCHTP 127

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71983709   338 EEALLQRVRFRIF--------SNIPWFFVKFFMTVEAMQFERDVFIWSNKKYIKSPLLVKNDGPIQKHRRWFSQFY 405
Cdd:pfam19298 128 VDDNSFVLQFGVIvkklpglsDEEAAALARGFADGVLRGFEQDVEIWKNKTRIDNPLLCEEDGPVYQLRRWYEQFY 203
Rieske_RO_Alpha_N cd03469
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ...
 81-196 3.45e-27

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: 104.59  E-value: 3.45e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  81 WYCVCESEKLAN-NQIMEITVLGQFLSLIRSESGAVYITDSYCPHIGANFnIGGRVVRDNCIQCPFHGWIFSAEtGKCVE 159
Cdd:cd03469   1 WYFVGHSSELPEpGDYVTLELGGEPLVLVRDRDGEVRAFHNVCPHRGARL-CEGRGGNAGRLVCPYHGWTYDLD-GKLVG 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 71983709 160 VPY---DEGRIPEQAKVTTWPCIERNNNIYLWYHCDGAEP 196
Cdd:cd03469  79 VPReegFPGFDKEKLGLRTVPVEEWGGLIFVNLDPDAPPL 118
HcaE COG4638
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ...
 72-244 2.01e-25

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: 105.07  E-value: 2.01e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  72 DMPPVFPNGWYCVCESEKLAN-NQIMEITVLGQFLSLIRSESGAVYITDSYCPHIGAnfniggRVVR----DNCIQCPFH 146
Cdd:COG4638  18 ELERIFRRGWYYVGHSSELPEpGDYLTRTILGEPVVLVRDKDGEVRAFHNVCPHRGA------PLSEgrgnGGRLVCPYH 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709 147 GWIFSAEtGKCVEVPYDEGR---IPEQAKVTTWPCIERNNNIYLWYHCDGAEPEWEIPEITEITDGF----WHLGGRTEH 219
Cdd:COG4638  92 GWTYDLD-GRLVGIPHMEGFpdfDPARAGLRSVPVEEWGGLIFVWLGPDAPPLAEYLGPLAEYLDPYdfgeLKVAGRETY 170

                       170       180
                ....*....|....*....|....*
gi 71983709 220 EVMCHIQEIPENGADIAHLNYLHKS 244
Cdd:COG4638 171 EVNANWKLVVENFLDGYHVPFVHPG 195
Rieske_RO_Alpha_KSH cd03531
The alignment model represents the N-terminal rieske iron-sulfur domain of KshA, the oxygenase ...
 80-196 4.14e-22

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: 90.94  E-value: 4.14e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  80 GWYCVCESEKLANNQIMEITVLGQFLSLIRSESGAVYITDSYCPHIGANFNIGgrVVRDNCIQCPFHGWIFSAEtGKCVE 159
Cdd:cd03531   1 GWHCLGLARDFRDGKPHGVEAFGTKLVVFADSDGALNVLDAYCRHMGGDLSQG--TVKGDEIACPFHDWRWGGD-GRCKA 77

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 71983709 160 VPYDEgRIPEQAKVTTWPCIERNNNIYLWYHCDGAEP 196
Cdd:cd03531  78 IPYAR-RVPPLARTRAWPTLERNGQLFVWHDPEGNPP 113
Rieske_RO_Alpha_PrnD cd03537
This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit of ...
 81-189 8.72e-18

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: 79.21  E-value: 8.72e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  81 WYCVCESEKLANNQImEITVLGQFLSLIRSESGAVYITDSYCPHIGANFnIGGRVVrDNCIQCPFHGWIFSaETGKCVEV 160
Cdd:cd03537   4 WYVAMRSDDLKDKPT-ELTLFGRPCVAWRGATGRAVVMDRHCSHLGANL-ADGRVK-DGCIQCPFHHWRYD-EQGQCVHI 79

                        90       100       110
                ....*....|....*....|....*....|....*
gi 71983709 161 PYDEGR------IPEQAKVTTWPCIERNNNIYLWY 189
Cdd:cd03537  80 PGHSTAvrrlepVPRGARQPTLVTAERYGYVWVWY 114
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 80-177 1.04e-17

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: 77.77  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709    80 GWYCVCESEKLANNQIMEITVLGQFLSLIRSESGAVYITDSYCPHIGANFnIGGRVVRDNCIQCPFHGWIFSaETGKCVE 159
Cdd:pfam00355   1 SWYPVCHSSELPEGEPKVVEVGGEPLVVFRDEDGELYALEDRCPHRGAPL-SEGKVNGGGRLECPYHGWRFD-GTGKVVK 78

                          90
                  ....*....|....*...
gi 71983709   160 VPYdegripeQAKVTTWP 177
Cdd:pfam00355  79 VPA-------PRPLKSYP 89
Rieske_RO_Alpha_PhDO_like cd03479
Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, ...
 65-203 6.37e-17

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: 77.29  E-value: 6.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  65 KLLRRVgdmppvfpngWYCVCESEKL-ANNQIMEITVLGQFLSLIRSESGAVYITDSYCPHIGANFNIGgrVVRDNCIQC 143
Cdd:cd03479  16 ELLRRY----------WQPVALSSELtEDGQPVRVRLLGEDLVAFRDTSGRVGLLDEHCPHRGASLVFG--RVEECGLRC 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71983709 144 PFHGWIFSAEtGKCVEVP--YDEGRIPEQAKVTTWPCIERNNNIYLWYHCDGAEPEWEIPEI 203
Cdd:cd03479  84 CYHGWKFDVD-GQCLEMPsePPDSQLKQKVRQPAYPVRERGGLVWAYMGPAEEAPEFPRYDW 144
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 81-187 8.05e-17

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: 75.65  E-value: 8.05e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  81 WYCVCESEKLANNQIMEITVLGQFLSLIRSEsGAVYITDSYCPHIGANFNIGgrVVRDNCIQCPFHGWIFSAETGKCVEV 160
Cdd:COG2146   3 EVKVCALDDLPEGGGVVVEVGGKQIAVFRTD-GEVYAYDNRCPHQGAPLSEG--IVDGGVVTCPLHGARFDLRTGECLGG 79

                        90       100
                ....*....|....*....|....*..
gi 71983709 161 pydegriPEQAKVTTWPCIERNNNIYL 187
Cdd:COG2146  80 -------PATEPLKTYPVRVEDGDVYV 99
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 81-188 2.65e-15

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: 71.37  E-value: 2.65e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  81 WYCVCESEKLANNQIMEITVLGQFLSLIRSESGAVYITDSYCPHIGANfnIGGRVVRDNCIQCPFHGWIFSAETGKCVEV 160
Cdd:cd03467   1 WVVVGALSELPPGGGRVVVVGGGPVVVVRREGGEVYALSNRCTHQGCP--LSEGEGEDGCIVCPCHGSRFDLRTGEVVSG 78

                        90       100
                ....*....|....*....|....*...
gi 71983709 161 PYdegripeQAKVTTWPCIERnNNIYLW 188
Cdd:cd03467  79 PA-------PRPLPKYPVKVE-GDGVVW 98
Rieske_RO_Alpha_VanA_DdmC cd03532
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and ...
 77-188 1.89e-13

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: 66.62  E-value: 1.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  77 FP-NGWYCVCESEKLANNQIMEiTVLGQFLSLIRSESGAVYITDSYCPHIGANFNIGgrVVRDNCIQCPFHGWIFSAEtG 155
Cdd:cd03532   1 FPrNAWYVAAWADELGDKPLAR-TLLGEPVVLYRTQDGRVAALEDRCPHRSAPLSKG--SVEGGGLVCGYHGLEFDSD-G 76

                        90       100       110
                ....*....|....*....|....*....|...
gi 71983709 156 KCVEVPYDEgRIPEQAKVTTWPCIERNNNIYLW 188
Cdd:cd03532  77 RCVHMPGQE-RVPAKACVRSYPVVERDALIWIW 108
Rieske_RO_Alpha_PaO cd03480
Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, ...
 81-199 1.36e-11

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: 61.95  E-value: 1.36e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  81 WYCVCESEKLANNQIMEITVLGQFLSLIRSESGAVY-ITDSYCPHIGANFNiGGRVVRDNCIQCPFHGWIFSAeTGKCVE 159
Cdd:cd03480  18 WYPVAYVEDLDPSRPTPFTLLGRDLVIWWDRNSQQWrAFDDQCPHRLAPLS-EGRIDEEGCLECPYHGWSFDG-SGSCQR 95

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 71983709 160 VP--YDEGRIPE--QAKVTTWPCIERNNNIYLWyhcdGAEPEWE 199
Cdd:cd03480  96 IPqaAEGGKAHTspRACVASLPTAVRQGLLFVW----PGEPENA 135
PLN02281 PLN02281
chlorophyllide a oxygenase
 57-271 1.87e-11

chlorophyllide a oxygenase


Pssm-ID: 177920 [Multi-domain]  Cd Length: 536  Bit Score: 65.91  E-value: 1.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709   57 RERQLERLKLLRRVGDMPPVFP---NGWYCVCESEKLANNQIMEITVLGQFLSLIRSESGAVYITDSYCPHIGANFNIGg 133
Cdd:PLN02281 194 REKTNTGAKSLNVSGPVPPYSPhlkNFWYPVAFTADLKHDTMVPIECFEQPWVIFRGEDGKPGCVRNTCAHRACPLDLG- 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  134 rVVRDNCIQCPFHGWIFSAEtGKCVEVPYDEgriPEQAKVTTWPCIERNNNIYLWyhcDGAEPEWEIPEITEITDGFW-H 212
Cdd:PLN02281 273 -TVNEGRIQCPYHGWEYSTD-GECKKMPSTK---LLKVKIKSLPCLEQEGMIWIW---PGDEPPAPILPSLQPPSGFLiH 344

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71983709  213 ----LGGRTEHEVMChiqeipENGADIAHLNYLHKSAppVTKGSDIIK-TDLSDPQPAVQHVWD 271
Cdd:PLN02281 345 aelvMDLPVEHGLLL------DNLLDLAHAPFTHTST--FAKGWSVPSlVKFLTPTSGLQGYWD 400
Rieske_RO_Alpha_Cao cd04337
Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the ...
 67-201 7.70e-11

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: 59.43  E-value: 7.70e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  67 LRRVGDMPPVFP---NGWYCVCESEKLANNQIMEITVLGQFLSLIRSESGAVYITDSYCPHIGANFNIGGrvVRDNCIQC 143
Cdd:cd04337   1 SRVLGSSLELEPglrNFWYPVEFSKDLKMDTMVPFELFGQPWVLFRDEDGTPGCIRDECAHRACPLSLGK--VIEGRIQC 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71983709 144 PFHGWIFSAEtGKCVEVPYDEGRipeQAKVTTWPCIERNNNIYLWyhcDGAEPEWEIP 201
Cdd:cd04337  79 PYHGWEYDGD-GECTKMPSTKCL---NVGIAALPCMEQDGMIWVW---PGDDPPAALP 129
Rieske_RO_Alpha_Tic55 cd04338
Tic55 is a 55kDa LLS1-related non-heme iron oxygenase associated with protein transport ...
 81-188 2.35e-10

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: 58.31  E-value: 2.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  81 WYCVCESEKLANNQIMEITVLGQFLSLIRSESGAVYITDSYCPHIGANFNIGGRVvrDNCIQCPFHGWIFSAEtGKCVEV 160
Cdd:cd04338  18 WYPLYLLKDVPTDAPLGLSVYDEPFVLFRDQNGQLRCLEDRCPHRLAKLSEGQLI--DGKLECLYHGWQFGGE-GKCVKI 94

                        90       100       110
                ....*....|....*....|....*....|
gi 71983709 161 PY--DEGRIPEQAKVTTWPCIERNNNIYLW 188
Cdd:cd04338  95 PQlpADAKIPKNACVKSYEVRDSQGVVWMW 124
Rieske_NirD cd03529
Assimilatory nitrite reductase (NirD) family, Rieske domain; Assimilatory nitrate and nitrite ...
 81-187 4.23e-10

Assimilatory nitrite reductase (NirD) family, Rieske domain; Assimilatory nitrate and nitrite reductases convert nitrate through nitrite to ammonium. Members include bacterial and fungal proteins. The bacterial NirD contains a single Rieske domain while fungal proteins have a C-terminal Rieske domain in addition to several other domains. The fungal NirD is involved in nutrient acquisition, functioning at the soil/fungus interface to control nutrient exchange between the fungus and the host plant. The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. The Rieske [2Fe-2S] cluster is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In this family, only a few members contain these residues. Other members may have lost the ability to bind the Rieske [2Fe-2S] cluster.


Pssm-ID: 239605 [Multi-domain]  Cd Length: 103  Bit Score: 56.36  E-value: 4.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  81 WYCVCESEKLANNQIMEITVLGQFLSLIRSESGAVYITDSYCPHIGANF-------NIGGRVvrdnCIQCPFHGWIFSAE 153
Cdd:cd03529   1 WQTVCALDDLPPGSGVAALVGDTQIAIFRLPGREVYAVQNMDPHSRANVlsrgivgDIGGEP----VVASPLYKQHFSLK 76

                        90       100       110
                ....*....|....*....|....*....|....
gi 71983709 154 TGKCVEvpyDEGRipeqaKVTTWPCIERNNNIYL 187
Cdd:cd03529  77 TGRCLE---DEDV-----SVATFPVRVEDGEVYV 102
Rieske_AIFL_N cd03478
AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family ...
 84-161 8.16e-09

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: 52.62  E-value: 8.16e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71983709  84 VCESEKLANNQIMEITVLGQFLSLIRsESGAVYITDSYCPHIGANFNIGgrVVRDNCIQCPFHGWIFSAETGKCVEVP 161
Cdd:cd03478   3 VCRLSDLGDGEMKEVDVGDGKVLLVR-QGGEVHAIGAKCPHYGAPLAKG--VLTDGRIRCPWHGACFNLRTGDIEDAP 77
nirD_assim_sml TIGR02378
nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of ...
 81-187 4.23e-08

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: 50.78  E-value: 4.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709    81 WYCVCESEKLANNQIMEITVLGQFLSLIRSESGAVYITDSYCPHIGANFNIGGRVVRDN---CIQCPFHGWIFSAETGKC 157
Cdd:TIGR02378   2 WQDICAIDDIPEETGVCVLLGDTQIAIFRVPGDQVFAIQNMCPHKRAFVLSRGIVGDAQgelWVACPLHKRNFRLEDGRC 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 71983709   158 VEvpydegriPEQAKVTTWPCIERNNNIYL 187
Cdd:TIGR02378  82 LE--------DDSGSVRTYEVRVEDGRVYV 103
Rieske_RO_Alpha_OMO_CARDO cd03548
Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole ...
 77-197 8.56e-08

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: 50.88  E-value: 8.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  77 FPNGWYCVCESEKLANNQIMEITVLGQFLsLIRSESGAVYITDSYCPHIGANFNIGGRVVRDNCIQCPFHGWIFSAETGK 156
Cdd:cd03548  11 FRNHWYPALFSHELEEGEPKGIQLCGEPI-LLRRVDGKVYALKDRCLHRGVPLSKKPECFTKGTITCWYHGWTYRLDDGK 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 71983709 157 CVEV---PYDE--GRipeqAKVTTWPCIERNNNIYLwYHCDGAEPE 197
Cdd:cd03548  90 LVTIlanPDDPliGR----TGLKTYPVEEAKGMIFV-FVGDGDYAD 130
Rieske_2 pfam13806
Rieske-like [2Fe-2S] domain;
81-187 1.39e-06

Rieske-like [2Fe-2S] domain;


Pssm-ID: 433491 [Multi-domain]  Cd Length: 103  Bit Score: 46.39  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709    81 WYCVCESEKLANNQIMEITVLGQFLSLIRSESGAVYITDSYCPHIGAN---FNIGGRVVRDNCIQCPFHGWIFSAETGKC 157
Cdd:pfam13806   1 WTPVCALDDLPPGTGVCALVGGRQVAVFRLEDGQVYAIDNRDPFSGANvlsRGIVGDLGGELVVASPLYKQHFDLKTGEC 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 71983709   158 VEVPydegripeQAKVTTWPCIERNNNIYL 187
Cdd:pfam13806  81 LEDP--------EVSVPVYPVRVRDGNVEV 102
Rieske_RO_ferredoxin cd03528
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ...
 81-188 3.06e-06

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: 45.56  E-value: 3.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  81 WYCVCESEKLANNQIMEITVLGQFLSLIRSEsGAVYITDSYCPHIGANFNIGGrvVRDNCIQCPFHGWIFSAETGKCVev 160
Cdd:cd03528   1 WVRVCAVDELPEGEPKRVDVGGRPIAVYRVD-GEFYATDDLCTHGDASLSEGY--VEGGVIECPLHGGRFDLRTGKAL-- 75

                        90       100
                ....*....|....*....|....*...
gi 71983709 161 pydegRIPEQAKVTTWPCIERNNNIYLW 188
Cdd:cd03528  76 -----SLPATEPLKTYPVKVEDGDVYVD 98
Rieske_NirD_small_Bacillus cd03530
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar ...
 105-187 1.25e-05

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: 43.75  E-value: 1.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709 105 LSLIRSESGAVYITDSYCPHIGANFNIGgrVVRDNCIQCPFHGWIFSAETGKcVEVPyDEGRipeqakVTTWPCIERNNN 184
Cdd:cd03530  25 IAVFRTADDEVFALENRCPHKGGPLSEG--IVHGEYVTCPLHNWVIDLETGE-AQGP-DEGC------VRTFPVKVEDGR 94


                ...
gi 71983709 185 IYL 187
Cdd:cd03530  95 VYL 97
PLN00095 PLN00095
chlorophyllide a oxygenase; Provisional
 81-188 1.56e-05

chlorophyllide a oxygenase; Provisional


Pssm-ID: 165668 [Multi-domain]  Cd Length: 394  Bit Score: 46.98  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709   81 WYCVCESEKLANNQIM-EITVLGQFLSLIRSESGAVYITDSYCPHIGANFNIGGRVvrDNCIQCPFHGWIFSAeTGKCVE 159
Cdd:PLN00095  73 WFPVAFAAGLRDEDALiAFDLFNVPWVLFRDADGEAGCIKDECAHRACPLSLGKLV--DGKAQCPYHGWEYET-GGECAK 149

                         90       100
                 ....*....|....*....|....*....
gi 71983709  160 VPYDEGRIPeQAKVTTWPCIERNNNIYLW 188
Cdd:PLN00095 150 MPSCKKFLK-GVFADAAPVIERDGFIFLW 177
Rieske_RO_Alpha_AntDO cd03538
Rieske non-heme iron oxygenase (RO) family, Anthranilate 1,2-dioxygenase (AntDO) subfamily, ...
 72-150 4.11e-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: 40.52  E-value: 4.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  72 DMPPVFPNGWYCVCESEKLANNQIMEITVLG-QFLSLIRSESGAVYITDSYCPHIGAnfniggRVVRDNC------IQCP 144
Cdd:cd03538  14 EMERLFGNAWIYVGHESQVPNPGDYITTRIGdQPVVMVRHTDGSVHVLYNRCPHKGT------KIVSDGCgntgkfFRCP 87


                ....*.
gi 71983709 145 FHGWIF 150
Cdd:cd03538  88 YHAWSF 93
PLN02518 PLN02518
pheophorbide a oxygenase
 57-242 1.32e-03

pheophorbide a oxygenase


Pssm-ID: 215283 [Multi-domain]  Cd Length: 539  Bit Score: 41.01  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709   57 RERQLERLKLLRRVGDMPPVFPNGWYCVCESEKLANNQIMEITVLGQFLSLIRSESGAVYIT-DSYCPHIGANFNiGGRV 135
Cdd:PLN02518  67 GEEQRVEQELGQESSDSKFSWRDHWYPVSLVEDLDPSVPTPFQLLGRDLVLWKDPNQGEWVAfDDKCPHRLAPLS-EGRI 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  136 VRDNCIQCPFHGWIFSAEtGKCVEVPYDEGRIPE-------QAKVTTWPCIERNNNIYLWYHCDGAE-----------PE 197
Cdd:PLN02518 146 DENGHLQCSYHGWSFDGC-GSCTRIPQAAPEGPEaravkspRACAIKFPTMVSQGLLFVWPDENGWEraqatkppmlpDE 224

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 71983709  198 WEIPEITEIT---DGFWhlGGRTehevmchiqeIPENGADIAHLNYLH 242
Cdd:PLN02518 225 FDDPEFSTVTiqrDLFY--GYDT----------LMENVSDPSHIDFAH 260
Rieske_RO_Alpha_HBDO cd03542
Rieske non-heme iron oxygenase (RO) family, 2-Halobenzoate 1,2-dioxygenase (HBDO) subfamily, ...
 81-160 6.22e-03

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: 36.65  E-value: 6.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983709  81 W-YCVCESEKLANNQIMEITVLGQFLSLIRSESGAVYITDSYCPHIGANFnigGRVVRDN--CIQCPFHGWIFSaETGKC 157
Cdd:cd03542   1 WvYLAHESQIPNNNDYFTTTIGRQPVVITRDKDGELNAFINACSHRGAML---CRRKQGNkgTFTCPFHGWTFS-NTGKL 76


                ...
gi 71983709 158 VEV 160
Cdd:cd03542  77 LKV 79
 
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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