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Conserved domains on  [gi|2082249325|ref|XP_001691386|]
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uncharacterized protein CHLRE_06g305650v5 [Chlamydomonas reinhardtii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PobA COG5749
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
222-625 2.37e-80

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


:

Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 261.09  E-value: 2.37e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 222 FDWYRQWYPVAPLDTMDPARPHPFTLLGQELVLWRDGGGTWRAFRDACPHRLAPLSEGRIEaDGTLLCAYHGWRFNGSGG 301
Cdd:COG5749    14 FIFRNHWYPVAPSEDLKPNKPKPVTLLGEPLVIWRDSDGKVVALEDRCPHRGAPLSEGRVE-GGNLRCPYHGWQFDGDGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 302 CTTIPnftdeAAHAKATASRRACATAHPTRHLGGLLWVWgssgPGaEAESAAKQPvlPPEIqedgtgaPGVDAPGW---- 377
Cdd:COG5749    93 CVHIP-----QLPENQPIPKNAKVKSYPVQERYGLIWVW----LG-DPPQADETP--IPDI-------PELDDPEWvats 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 378 SFRDLPYGHVYFIENVVDPAHVPVSHHKVAGDRYRDLKKSFSMELSrpvtkDGGFEVS----------IPKSWRSDVQTS 447
Cdd:COG5749   154 SVRDLECHYSRLIENLIDPSHVPFVHHGTQGNRKQAQPLEMEIEST-----PNGITASytaqsyyqlfFPFLGNLDETLT 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 448 STgFYPPSHVRIQQNHHNGGTTILALYSTPTVPGWTRHVgmqllkkapdssakgsGIAFFG-LPLPRWLAH---LAGALF 523
Cdd:COG5749   229 IT-FIYPNTVSVDIGSGLGGRFGIVLYATPIDEGKTRAY----------------AIFFRNfAKKPRWLRHflkLLRNGI 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 524 LHQDMVFLHHQERTVARDQaerlqraaaaaaaagsssagqqqqggqqgataaaatagaggdgrmlpppKYYMPTSVDTGV 603
Cdd:COG5749   292 LEQDVIILESQQPALLQLG-------------------------------------------------SYELPTPADRAI 322

                         410       420
                  ....*....|....*....|..
gi 2082249325 604 TAWRHWLATFSDGDVPWAPGTP 625
Cdd:COG5749   323 IEFRRWLDKQAAGEGPWQEVSP 344
 
Name Accession Description Interval E-value
PobA COG5749
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
222-625 2.37e-80

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


Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 261.09  E-value: 2.37e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 222 FDWYRQWYPVAPLDTMDPARPHPFTLLGQELVLWRDGGGTWRAFRDACPHRLAPLSEGRIEaDGTLLCAYHGWRFNGSGG 301
Cdd:COG5749    14 FIFRNHWYPVAPSEDLKPNKPKPVTLLGEPLVIWRDSDGKVVALEDRCPHRGAPLSEGRVE-GGNLRCPYHGWQFDGDGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 302 CTTIPnftdeAAHAKATASRRACATAHPTRHLGGLLWVWgssgPGaEAESAAKQPvlPPEIqedgtgaPGVDAPGW---- 377
Cdd:COG5749    93 CVHIP-----QLPENQPIPKNAKVKSYPVQERYGLIWVW----LG-DPPQADETP--IPDI-------PELDDPEWvats 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 378 SFRDLPYGHVYFIENVVDPAHVPVSHHKVAGDRYRDLKKSFSMELSrpvtkDGGFEVS----------IPKSWRSDVQTS 447
Cdd:COG5749   154 SVRDLECHYSRLIENLIDPSHVPFVHHGTQGNRKQAQPLEMEIEST-----PNGITASytaqsyyqlfFPFLGNLDETLT 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 448 STgFYPPSHVRIQQNHHNGGTTILALYSTPTVPGWTRHVgmqllkkapdssakgsGIAFFG-LPLPRWLAH---LAGALF 523
Cdd:COG5749   229 IT-FIYPNTVSVDIGSGLGGRFGIVLYATPIDEGKTRAY----------------AIFFRNfAKKPRWLRHflkLLRNGI 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 524 LHQDMVFLHHQERTVARDQaerlqraaaaaaaagsssagqqqqggqqgataaaatagaggdgrmlpppKYYMPTSVDTGV 603
Cdd:COG5749   292 LEQDVIILESQQPALLQLG-------------------------------------------------SYELPTPADRAI 322

                         410       420
                  ....*....|....*....|..
gi 2082249325 604 TAWRHWLATFSDGDVPWAPGTP 625
Cdd:COG5749   323 IEFRRWLDKQAAGEGPWQEVSP 344
PLN02518 PLN02518
pheophorbide a oxygenase
 129-654 5.29e-67

pheophorbide a oxygenase


Pssm-ID: 215283 [Multi-domain]  Cd Length: 539  Bit Score: 231.30  E-value: 5.29e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 129 GVSATGPAAAAQPHAKSQSVIASGTSSCCGGGNGcgvaaagpvaPRRV----PFVVAAAsvvtetrPGAAGTEDGGAAAL 204
Cdd:PLN02518    5 LGIACNSLTLTSSTPKSTPFFIPARTIPFVSSSR----------PRRGkiftPLRVAAP-------PSVPSEAALQQDEG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 205 APWDEAAEQPQAVPGEKFDWYRQWYPVAPLDTMDPARPHPFTLLGQELVLWRDGG-GTWRAFRDACPHRLAPLSEGRIEA 283
Cdd:PLN02518   68 EEQRVEQELGQESSDSKFSWRDHWYPVSLVEDLDPSVPTPFQLLGRDLVLWKDPNqGEWVAFDDKCPHRLAPLSEGRIDE 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 284 DGTLLCAYHGWRFNGSGGCTTIPNFTDEAAHAKATASRRACATAHPTRHLGGLLWVWGSSGpGAEAESAAKQPVLPPEIq 363
Cdd:PLN02518  148 NGHLQCSYHGWSFDGCGSCTRIPQAAPEGPEARAVKSPRACAIKFPTMVSQGLLFVWPDEN-GWERAQATKPPMLPDEF- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 364 edgtgapgvDAPGWSF----RDLPYGHVYFIENVVDPAHVPVSHHKVAGDRYRDLKKSFSMELSRPvtkdGGFEVSipks 439
Cdd:PLN02518  226 ---------DDPEFSTvtiqRDLFYGYDTLMENVSDPSHIDFAHHKVTGRRDRAKPLPFKVESSGP----WGFAGA---- 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 440 wRSDVQTSSTGFYPPSH--------VRIQQNHHNGGTTILALYSTPTVPGWTRHVgmqllkkapDSSAKG------SGIA 505
Cdd:PLN02518  289 -NSDNPRITAKFVAPCYyinkieidTKLPIVGDQKWVIWICSFNVPMAPGKTRSI---------VCSARNffqfsmPGPA 358

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 506 FFGLpLPRWLAHLAGALFLHQDMVFLHHQERTVARDQAErlqraaaaaaaagsssagqqqqggqqgataaaatagAGGDG 585
Cdd:PLN02518  359 WWQL-VPRWYEHWTSNKVYDGDMIVLQGQEKIFLSKSGE------------------------------------GSADV 401

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2082249325 586 RMLPPPKYYMPTSVDTGVTAWRHWLATFSDGDVPWAPGTP---PLGPRERDPAKLFDTWHTHTSKCTVCLAA 654
Cdd:PLN02518  402 NAQYTKLTFTPTQADRFVLAFRNWLRRHGNSQPEWFGETSsqqPLPSTVLSKRQMLDRFEQHTLNCSSCKGA 473
Rieske_RO_Alpha_PaO cd03480
Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, ...
 218-350 1.46e-58

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: 194.85  E-value: 1.46e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 218 PGEKFDWYRQWYPVAPLDTMDPARPHPFTLLGQELVLWRDG-GGTWRAFRDACPHRLAPLSEGRIEADGTLLCAYHGWRF 296
Cdd:cd03480     8 DSDKFDWREVWYPVAYVEDLDPSRPTPFTLLGRDLVIWWDRnSQQWRAFDDQCPHRLAPLSEGRIDEEGCLECPYHGWSF 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2082249325 297 NGSGGCTTIPNftdEAAHAKATASRRACATAHPTRHLGGLLWVWGSSGPGAEAE 350
Cdd:cd03480    88 DGSGSCQRIPQ---AAEGGKAHTSPRACVASLPTAVRQGLLFVWPGEPENAKAT 138
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 227-306 8.03e-28

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: 107.43  E-value: 8.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 227 QWYPVAPLDTMDPARPHPFTLLGQELVLWRDGGGTWRAFRDACPHRLAPLSEGRIEADGTLLCAYHGWRFNGSGGCTTIP 306
Cdd:pfam00355   1 SWYPVCHSSELPEGEPKVVEVGGEPLVVFRDEDGELYALEDRCPHRGAPLSEGKVNGGGRLECPYHGWRFDGTGKVVKVP 80
 
Name Accession Description Interval E-value
PobA COG5749
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
222-625 2.37e-80

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


Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 261.09  E-value: 2.37e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 222 FDWYRQWYPVAPLDTMDPARPHPFTLLGQELVLWRDGGGTWRAFRDACPHRLAPLSEGRIEaDGTLLCAYHGWRFNGSGG 301
Cdd:COG5749    14 FIFRNHWYPVAPSEDLKPNKPKPVTLLGEPLVIWRDSDGKVVALEDRCPHRGAPLSEGRVE-GGNLRCPYHGWQFDGDGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 302 CTTIPnftdeAAHAKATASRRACATAHPTRHLGGLLWVWgssgPGaEAESAAKQPvlPPEIqedgtgaPGVDAPGW---- 377
Cdd:COG5749    93 CVHIP-----QLPENQPIPKNAKVKSYPVQERYGLIWVW----LG-DPPQADETP--IPDI-------PELDDPEWvats 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 378 SFRDLPYGHVYFIENVVDPAHVPVSHHKVAGDRYRDLKKSFSMELSrpvtkDGGFEVS----------IPKSWRSDVQTS 447
Cdd:COG5749   154 SVRDLECHYSRLIENLIDPSHVPFVHHGTQGNRKQAQPLEMEIEST-----PNGITASytaqsyyqlfFPFLGNLDETLT 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 448 STgFYPPSHVRIQQNHHNGGTTILALYSTPTVPGWTRHVgmqllkkapdssakgsGIAFFG-LPLPRWLAH---LAGALF 523
Cdd:COG5749   229 IT-FIYPNTVSVDIGSGLGGRFGIVLYATPIDEGKTRAY----------------AIFFRNfAKKPRWLRHflkLLRNGI 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 524 LHQDMVFLHHQERTVARDQaerlqraaaaaaaagsssagqqqqggqqgataaaatagaggdgrmlpppKYYMPTSVDTGV 603
Cdd:COG5749   292 LEQDVIILESQQPALLQLG-------------------------------------------------SYELPTPADRAI 322

                         410       420
                  ....*....|....*....|..
gi 2082249325 604 TAWRHWLATFSDGDVPWAPGTP 625
Cdd:COG5749   323 IEFRRWLDKQAAGEGPWQEVSP 344
PLN02518 PLN02518
pheophorbide a oxygenase
 129-654 5.29e-67

pheophorbide a oxygenase


Pssm-ID: 215283 [Multi-domain]  Cd Length: 539  Bit Score: 231.30  E-value: 5.29e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 129 GVSATGPAAAAQPHAKSQSVIASGTSSCCGGGNGcgvaaagpvaPRRV----PFVVAAAsvvtetrPGAAGTEDGGAAAL 204
Cdd:PLN02518    5 LGIACNSLTLTSSTPKSTPFFIPARTIPFVSSSR----------PRRGkiftPLRVAAP-------PSVPSEAALQQDEG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 205 APWDEAAEQPQAVPGEKFDWYRQWYPVAPLDTMDPARPHPFTLLGQELVLWRDGG-GTWRAFRDACPHRLAPLSEGRIEA 283
Cdd:PLN02518   68 EEQRVEQELGQESSDSKFSWRDHWYPVSLVEDLDPSVPTPFQLLGRDLVLWKDPNqGEWVAFDDKCPHRLAPLSEGRIDE 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 284 DGTLLCAYHGWRFNGSGGCTTIPNFTDEAAHAKATASRRACATAHPTRHLGGLLWVWGSSGpGAEAESAAKQPVLPPEIq 363
Cdd:PLN02518  148 NGHLQCSYHGWSFDGCGSCTRIPQAAPEGPEARAVKSPRACAIKFPTMVSQGLLFVWPDEN-GWERAQATKPPMLPDEF- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 364 edgtgapgvDAPGWSF----RDLPYGHVYFIENVVDPAHVPVSHHKVAGDRYRDLKKSFSMELSRPvtkdGGFEVSipks 439
Cdd:PLN02518  226 ---------DDPEFSTvtiqRDLFYGYDTLMENVSDPSHIDFAHHKVTGRRDRAKPLPFKVESSGP----WGFAGA---- 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 440 wRSDVQTSSTGFYPPSH--------VRIQQNHHNGGTTILALYSTPTVPGWTRHVgmqllkkapDSSAKG------SGIA 505
Cdd:PLN02518  289 -NSDNPRITAKFVAPCYyinkieidTKLPIVGDQKWVIWICSFNVPMAPGKTRSI---------VCSARNffqfsmPGPA 358

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 506 FFGLpLPRWLAHLAGALFLHQDMVFLHHQERTVARDQAErlqraaaaaaaagsssagqqqqggqqgataaaatagAGGDG 585
Cdd:PLN02518  359 WWQL-VPRWYEHWTSNKVYDGDMIVLQGQEKIFLSKSGE------------------------------------GSADV 401

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2082249325 586 RMLPPPKYYMPTSVDTGVTAWRHWLATFSDGDVPWAPGTP---PLGPRERDPAKLFDTWHTHTSKCTVCLAA 654
Cdd:PLN02518  402 NAQYTKLTFTPTQADRFVLAFRNWLRRHGNSQPEWFGETSsqqPLPSTVLSKRQMLDRFEQHTLNCSSCKGA 473
Rieske_RO_Alpha_PaO cd03480
Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, ...
 218-350 1.46e-58

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: 194.85  E-value: 1.46e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 218 PGEKFDWYRQWYPVAPLDTMDPARPHPFTLLGQELVLWRDG-GGTWRAFRDACPHRLAPLSEGRIEADGTLLCAYHGWRF 296
Cdd:cd03480     8 DSDKFDWREVWYPVAYVEDLDPSRPTPFTLLGRDLVIWWDRnSQQWRAFDDQCPHRLAPLSEGRIDEEGCLECPYHGWSF 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2082249325 297 NGSGGCTTIPNftdEAAHAKATASRRACATAHPTRHLGGLLWVWGSSGPGAEAE 350
Cdd:cd03480    88 DGSGSCQRIPQ---AAEGGKAHTSPRACVASLPTAVRQGLLFVWPGEPENAKAT 138
HcaE COG4638
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ...
 224-404 3.11e-35

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: 135.88  E-value: 3.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 224 WYRQWYPVAPLDTM-DPARPHPFTLLGQELVLWRDGGGTWRAFRDACPHRLAPLSEGRIEAdGTLLCAYHGWRFNGSGGC 302
Cdd:COG4638    23 FRRGWYYVGHSSELpEPGDYLTRTILGEPVVLVRDKDGEVRAFHNVCPHRGAPLSEGRGNG-GRLVCPYHGWTYDLDGRL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 303 TTIPNFTDEAAHAKAtasrRACATAHPTRHLGGLLWVWgssgPGAEAESAAkqPVLPPEIQE-DGTGAPGVDAPGWSFRD 381
Cdd:COG4638   102 VGIPHMEGFPDFDPA----RAGLRSVPVEEWGGLIFVW----LGPDAPPLA--EYLGPLAEYlDPYDFGELKVAGRETYE 171

                         170       180
                  ....*....|....*....|...
gi 2082249325 382 LPYGHVYFIENVVDPAHVPVSHH 404
Cdd:COG4638   172 VNANWKLVVENFLDGYHVPFVHP 194
Rieske_RO_Alpha_Tic55 cd04338
Tic55 is a 55kDa LLS1-related non-heme iron oxygenase associated with protein transport ...
 212-342 1.20e-30

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: 117.24  E-value: 1.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 212 EQPQAVPGEKFDWYRQWYPVAPLDTMDPARPHPFTLLGQELVLWRDGGGTWRAFRDACPHRLAPLSEGRIeADGTLLCAY 291
Cdd:cd04338     2 EFETPENVAEYDWREEWYPLYLLKDVPTDAPLGLSVYDEPFVLFRDQNGQLRCLEDRCPHRLAKLSEGQL-IDGKLECLY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2082249325 292 HGWRFNGSGGCTTIPNFTDEaahakATASRRACATAHPTRHLGGLLWVWGS 342
Cdd:cd04338    81 HGWQFGGEGKCVKIPQLPAD-----AKIPKNACVKSYEVRDSQGVVWMWMS 126
Rieske_RO_Alpha_N cd03469
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ...
 228-351 6.27e-28

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: 108.83  E-value: 6.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 228 WYPVAPLDTM-DPARPHPFTLLGQELVLWRDGGGTWRAFRDACPHRLAPLSEGRIEADGTLLCAYHGWRFNGSGGCTTIP 306
Cdd:cd03469     1 WYFVGHSSELpEPGDYVTLELGGEPLVLVRDRDGEVRAFHNVCPHRGARLCEGRGGNAGRLVCPYHGWTYDLDGKLVGVP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2082249325 307 NFTDEAAHAKAtasrRACATAHPTRHLGGLLWVWgssgPGAEAES 351
Cdd:cd03469    81 REEGFPGFDKE----KLGLRTVPVEEWGGLIFVN----LDPDAPP 117
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 227-306 8.03e-28

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: 107.43  E-value: 8.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 227 QWYPVAPLDTMDPARPHPFTLLGQELVLWRDGGGTWRAFRDACPHRLAPLSEGRIEADGTLLCAYHGWRFNGSGGCTTIP 306
Cdd:pfam00355   1 SWYPVCHSSELPEGEPKVVEVGGEPLVVFRDEDGELYALEDRCPHRGAPLSEGKVNGGGRLECPYHGWRFDGTGKVVKVP 80
Rieske_RO_Alpha_VanA_DdmC cd03532
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and ...
 227-340 2.07e-19

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: 84.34  E-value: 2.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 227 QWYpVAPLDTMDPARPHPFTLLGQELVLWRDGGGTWRAFRDACPHRLAPLSEGRIEADGtLLCAYHGWRFNGSGGCTTIP 306
Cdd:cd03532     5 AWY-VAAWADELGDKPLARTLLGEPVVLYRTQDGRVAALEDRCPHRSAPLSKGSVEGGG-LVCGYHGLEFDSDGRCVHMP 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2082249325 307 nftdeaahAKATASRRACATAHPTRHLGGLLWVW 340
Cdd:cd03532    83 --------GQERVPAKACVRSYPVVERDALIWIW 108
Rieske_RO_Alpha_PhDO_like cd03479
Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, ...
 226-360 2.39e-19

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: 84.99  E-value: 2.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 226 RQWYPVAPLDTM-DPARPHPFTLLGQELVLWRDGGGTWRAFRDACPHRLAPLSEGRIEADGtLLCAYHGWRFNGSGGCTT 304
Cdd:cd03479    20 RYWQPVALSSELtEDGQPVRVRLLGEDLVAFRDTSGRVGLLDEHCPHRGASLVFGRVEECG-LRCCYHGWKFDVDGQCLE 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2082249325 305 IPNftdeaAHAKATASRRACATAHPTRHLGGLLWVWgsSGPgaeaesAAKQPVLPP 360
Cdd:cd03479    99 MPS-----EPPDSQLKQKVRQPAYPVRERGGLVWAY--MGP------AEEAPEFPR 141
Rieske_RO_Alpha_Cao cd04337
Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the ...
 228-348 1.11e-18

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: 82.54  E-value: 1.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 228 WYPVAPLDTMDPARPHPFTLLGQELVLWRDGGGTWRAFRDACPHRLAPLSEGRIeADGTLLCAYHGWRFNGSGGCTTIPn 307
Cdd:cd04337    18 WYPVEFSKDLKMDTMVPFELFGQPWVLFRDEDGTPGCIRDECAHRACPLSLGKV-IEGRIQCPYHGWEYDGDGECTKMP- 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2082249325 308 ftdeaahakATASRRACATAHPTRHLGGLLWVWGSSGPGAE 348
Cdd:cd04337    96 ---------STKCLNVGIAALPCMEQDGMIWVWPGDDPPAA 127
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 228-306 2.00e-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: 77.91  E-value: 2.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 228 WYPVAPLDTMDPARPHPFTLLGQELVLWRDGGGTWRAFRDACPHRLAPLSEGRIEaDGTLLCAYHGWRFNGSGG-CTTIP 306
Cdd:cd03467     1 WVVVGALSELPPGGGRVVVVGGGPVVVVRREGGEVYALSNRCTHQGCPLSEGEGE-DGCIVCPCHGSRFDLRTGeVVSGP 79
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 228-306 4.29e-14

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: 68.71  E-value: 4.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 228 WYPVAPLDTMDPARPHPFTLLGQELVLWRDGGgTWRAFRDACPHRLAPLSEGRIEaDGTLLCAYHGWRFN-GSGGCTTIP 306
Cdd:COG2146     3 EVKVCALDDLPEGGGVVVEVGGKQIAVFRTDG-EVYAYDNRCPHQGAPLSEGIVD-GGVVTCPLHGARFDlRTGECLGGP 80
Rieske_RO_Alpha_KSH cd03531
The alignment model represents the N-terminal rieske iron-sulfur domain of KshA, the oxygenase ...
 228-340 4.39e-14

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: 68.98  E-value: 4.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 228 WYPVAPLDTMDPARPHPFTLLGQELVLWRDGGGTWRAFRDACPHRLAPLSEGRIEADgTLLCAYHGWRFNGSGGCTTIPn 307
Cdd:cd03531     2 WHCLGLARDFRDGKPHGVEAFGTKLVVFADSDGALNVLDAYCRHMGGDLSQGTVKGD-EIACPFHDWRWGGDGRCKAIP- 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2082249325 308 ftdeaaHAKATaSRRACATAHPTRHLGGLLWVW 340
Cdd:cd03531    80 ------YARRV-PPLARTRAWPTLERNGQLFVW 105
PaO pfam08417
Pheophorbide a oxygenase; This domain is found in bacterial and plant proteins to the ...
 451-540 6.53e-14

Pheophorbide a oxygenase; This domain is found in bacterial and plant proteins to the C-terminus of a Rieske 2Fe-2S domain (pfam00355). One of the proteins the domain is found in is Pheophorbide a oxygenase (PaO) which seems to be a key regulator of chlorophyll catabolism. Arabidopsis PaO (AtPaO) is a Rieske-type 2Fe-2S enzyme that is identical to Arabidopsis accelerated cell death 1 and homologous to lethal leaf spot 1 (LLS1) of maize, in which the domain described here is also found.


Pssm-ID: 429985 [Multi-domain]  Cd Length: 89  Bit Score: 67.73  E-value: 6.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 451 FYPPSHVR----IQQNHHNGGTTILALYSTPTVPGWTRHVGMQLLKKAPdssakgsgiaFFGLPLPRWLAHLAGALFLHQ 526
Cdd:pfam08417   1 FIPPCVVRnditFADEGGGKKRLGLVFYCIPTGPGKSRLIARFPRNFAS----------WLPKLTPRWLKHINQNKVLDQ 70

                          90
                  ....*....|....
gi 2082249325 527 DMVFLHHQERTVAR 540
Cdd:pfam08417  71 DLILLHGQERRLAR 84
Rieske_RO_Alpha_PrnD cd03537
This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit of ...
 241-345 9.42e-12

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: 62.64  E-value: 9.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 241 RPHPFTLLGQELVLWRDGGGTWRAFRDACPHRLAPLSEGRIEaDGTLLCAYHGWRFNGSGGCTTIPNFTDEAAHAKATaS 320
Cdd:cd03537    16 KPTELTLFGRPCVAWRGATGRAVVMDRHCSHLGANLADGRVK-DGCIQCPFHHWRYDEQGQCVHIPGHSTAVRRLEPV-P 93

                          90       100
                  ....*....|....*....|....*.
gi 2082249325 321 RRACATAHPTRHLGGLLWVW-GSSGP 345
Cdd:cd03537    94 RGARQPTLVTAERYGYVWVWyGSPQP 119
PLN02281 PLN02281
chlorophyllide a oxygenase
 228-403 1.02e-11

chlorophyllide a oxygenase


Pssm-ID: 177920 [Multi-domain]  Cd Length: 536  Bit Score: 68.22  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 228 WYPVAPLDTMDPARPHPFTLLGQELVLWRDGGGTWRAFRDACPHRLAPLSEGRIEaDGTLLCAYHGWRFNGSGGCTTIPn 307
Cdd:PLN02281  221 WYPVAFTADLKHDTMVPIECFEQPWVIFRGEDGKPGCVRNTCAHRACPLDLGTVN-EGRIQCPYHGWEYSTDGECKKMP- 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 308 ftdeaahakATASRRACATAHPTRHLGGLLWVWgssgPGAEAESAAKQPVLPPEiqedgtgapGVDAPGWSFRDLPYGHV 387
Cdd:PLN02281  299 ---------STKLLKVKIKSLPCLEQEGMIWIW----PGDEPPAPILPSLQPPS---------GFLIHAELVMDLPVEHG 356

                         170
                  ....*....|....*.
gi 2082249325 388 YFIENVVDPAHVPVSH 403
Cdd:PLN02281  357 LLLDNLLDLAHAPFTH 372
PLN00095 PLN00095
chlorophyllide a oxygenase; Provisional
 228-379 2.41e-09

chlorophyllide a oxygenase; Provisional


Pssm-ID: 165668 [Multi-domain]  Cd Length: 394  Bit Score: 60.08  E-value: 2.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 228 WYPVA-PLDTMDPARPHPFTLLGQELVLWRDGGGTWRAFRDACPHRLAPLSEGRIeADGTLLCAYHGWRFNGSGGCTTIP 306
Cdd:PLN00095   73 WFPVAfAAGLRDEDALIAFDLFNVPWVLFRDADGEAGCIKDECAHRACPLSLGKL-VDGKAQCPYHGWEYETGGECAKMP 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2082249325 307 NFTDEAAHAKATASrracatahPTRHLGGLLWVW-GSSGPGAEAESAAKQPVLPPEIQEdgTGAPGVDAPGWSF 379
Cdd:PLN00095  152 SCKKFLKGVFADAA--------PVIERDGFIFLWaGESDPADFVGPEAACESIDDDVLA--ANEPGMFAPGEGF 215
Rieske_T4moC cd03474
Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske ...
 228-340 5.71e-09

Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. T4mo is a four-protein complex that catalyzes the NADH- and O2-dependent hydroxylation of toluene to form p-cresol. T4mo consists of an NADH oxidoreductase (T4moF), a diiron hydroxylase (T4moH), a catalytic effector protein (T4moD), and a Rieske ferredoxin (T4moC). T4moC contains a Rieske domain and functions as an obligate electron carrier between T4moF and T4moH. 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: 239556 [Multi-domain]  Cd Length: 108  Bit Score: 54.27  E-value: 5.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 228 WYPVAPLDTMDPARPHPFTLLGQELVLWRDGGGTWRAFRDACPHRLAPLSEGRIEAdGTLLCAYHGWRFNGSGGCTTIPn 307
Cdd:cd03474     1 FTKVCSLDDVWEGEMELVDVDGEEVLLVAPEGGEFRAFQGICPHQEIPLAEGGFDG-GVLTCRAHLWQFDADTGEGLNP- 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2082249325 308 ftdeaahakatasRRACATAHPTRHLGGLLWVW 340
Cdd:cd03474    79 -------------RDCRLARYPVKVEGGDILVD 98
Rieske_RO_Alpha_OMO_CARDO cd03548
Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole ...
 228-340 2.90e-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: 53.19  E-value: 2.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 228 WYPVAPLDTMDPARPHPFTLLGQELVLWRDGGGTWrAFRDACPHRLAPLSEgRIE--ADGTLLCAYHGWRFNGSGG--CT 303
Cdd:cd03548    15 WYPALFSHELEEGEPKGIQLCGEPILLRRVDGKVY-ALKDRCLHRGVPLSK-KPEcfTKGTITCWYHGWTYRLDDGklVT 92

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2082249325 304 TIPNFTDEAAHakatasrRACATAHPTRHLGGLLWVW 340
Cdd:cd03548    93 ILANPDDPLIG-------RTGLKTYPVEEAKGMIFVF 122
Rieske_RO_ferredoxin cd03528
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ...
 228-297 6.24e-07

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: 48.25  E-value: 6.24e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 228 WYPVAPLDTMDPARPHPFTLLGQELVLWRDGGGTWrAFRDACPHRLAPLSEGRIEaDGTLLCAYHGWRFN 297
Cdd:cd03528     1 WVRVCAVDELPEGEPKRVDVGGRPIAVYRVDGEFY-ATDDLCTHGDASLSEGYVE-GGVIECPLHGGRFD 68
Rieske_RO_Alpha_HBDO cd03542
Rieske non-heme iron oxygenase (RO) family, 2-Halobenzoate 1,2-dioxygenase (HBDO) subfamily, ...
 250-300 2.04e-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: 44.74  E-value: 2.04e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2082249325 250 QELVLWRDGGGTWRAFRDACPHRLAPLSEGRIEADGTLLCAYHGWRFNGSG 300
Cdd:cd03542    24 QPVVITRDKDGELNAFINACSHRGAMLCRRKQGNKGTFTCPFHGWTFSNTG 74
Rieske_RO_Alpha_CMO cd03541
Rieske non-heme iron oxygenase (RO) family, Choline monooxygenase (CMO) subfamily, N-terminal ...
 251-311 8.75e-04

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: 39.84  E-value: 8.75e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2082249325 251 ELVLWRDGGGTWRAFRDACPHRLAPLSEGRIEADgTLLCAYHGWRFNGSGGCTTIPNFTDE 311
Cdd:cd03541    26 EYVVCRDGNGKLHAFHNVCTHRASILACGSGKKS-CFVCPYHGWVYGLDGSLTKATQATGI 85
Rieske_AIFL_N cd03478
AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family ...
 231-297 1.31e-03

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: 38.76  E-value: 1.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2082249325 231 VAPLDTMDPARPHPFTLLGQELVLWRDGGGTwRAFRDACPHRLAPLSEGrIEADGTLLCAYHGWRFN 297
Cdd:cd03478     3 VCRLSDLGDGEMKEVDVGDGKVLLVRQGGEV-HAIGAKCPHYGAPLAKG-VLTDGRIRCPWHGACFN 67
Rieske_NirD_small_Bacillus cd03530
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar ...
 228-339 1.31e-03

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: 38.74  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082249325 228 WYPVAPLDTMDPARPHPFTLLGQELVLWRDGGGTWRAFRDACPHRLAPLSEGrIEADGTLLCAYHGWRFNGSGGcttipn 307
Cdd:cd03530     1 WIDIGALEDIPPRGARKVQTGGGEIAVFRTADDEVFALENRCPHKGGPLSEG-IVHGEYVTCPLHNWVIDLETG------ 73

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2082249325 308 ftdeaahaKATASRRACATAHPTRHLGGLLWV 339
Cdd:cd03530    74 --------EAQGPDEGCVRTFPVKVEDGRVYL 97
Rieske_RO_Alpha_NDO cd03535
Rieske non-heme iron oxygenase (RO) family, Nathphalene 1,2-dioxygenase (NDO) subfamily, ...
 247-306 4.32e-03

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: 37.79  E-value: 4.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2082249325 247 LLGQELVLWRDGGGTWRAFRDACPHRLAPLSegRIEADGT--LLCAYHGWRFNGSGGCTTIP 306
Cdd:cd03535    23 IGDDSFIVCRDEDGEIRAMFNSCRHRGMQVC--RAEMGNTshFRCPYHGWTYRNTGRLVGVP 82
 
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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