NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|297821841|ref|XP_002878803|]
View 

protein TIC 55, chloroplastic [Arabidopsis lyrata subsp. lyrata]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Rieske_RO_Alpha_Tic55 cd04338
Tic55 is a 55kDa LLS1-related non-heme iron oxygenase associated with protein transport ...
 72-204 9.29e-96

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: 287.11  E-value: 9.29e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  72 EEEKRVEVADYDWTEEWYPLYLTKNIPDDAPLGLTVYDRQIVLYKDGEGTLRCYEDRCPHRLAKLSEGQLIDGRLECLYH 151
Cdd:cd04338    2 EFETPENVAEYDWREEWYPLYLLKDVPTDAPLGLSVYDEPFVLFRDQNGQLRCLEDRCPHRLAKLSEGQLIDGKLECLYH 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 297821841 152 GWQFEGEGKCVKIPQLPASAKIPKAACVKTYEVKDSQGVVWVWMSTKTPPNPE 204
Cdd:cd04338   82 GWQFGGEGKCVKIPQLPADAKIPKNACVKSYEVRDSQGVVWMWMSEATPPDEE 134
PobA COG5749
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
83-412 3.53e-85

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


:

Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 267.64  E-value: 3.53e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  83 DWTEEWYPLYLTKNIPDDAPLGLTVYDRQIVLYKDGEGTLRCYEDRCPHRLAKLSEGQLIDGRLECLYHGWQFEGEGKCV 162
Cdd:COG5749   15 IFRNHWYPVAPSEDLKPNKPKPVTLLGEPLVIWRDSDGKVVALEDRCPHRGAPLSEGRVEGGNLRCPYHGWQFDGDGKCV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 163 KIPQLPASAKIPKAACVKTYEVKDSQGVVWVWMSTKTPPNPEKLPWFENFARPGFFDISTTHELPYDHSILLENLMDPAH 242
Cdd:COG5749   95 HIPQLPENQPIPKNAKVKSYPVQERYGLIWVWLGDPPQADETPIPDIPELDDPEWVATSSVRDLECHYSRLIENLIDPSH 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 243 VPISHDRTdfTAKREDAQPLVFEVtERSNRGFAGTW----GREKDGGKGSNL-----LRFDAPCVLQNNREFEGKDGVKN 313
Cdd:COG5749  175 VPFVHHGT--QGNRKQAQPLEMEI-ESTPNGITASYtaqsYYQLFFPFLGNLdetltITFIYPNTVSVDIGSGLGGRFGI 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 314 YfsglFLCRPTGQGKSMLIVRF--GVTKRsplvsvlPQW---FWHQNACKVFEQDMGFLSSQNEVLMKekvptKDLYLNL 388
Cdd:COG5749  252 V----LYATPIDEGKTRAYAIFfrNFAKK-------PRWlrhFLKLLRNGILEQDVIILESQQPALLQ-----LGSYELP 315

                        330       340
                 ....*....|....*....|....
gi 297821841 389 KSSDTWVAEYRKWMDKVGHGMPYH 412
Cdd:COG5749  316 TPADRAIIEFRRWLDKQAAGEGPW 339
 
Name Accession Description Interval E-value
Rieske_RO_Alpha_Tic55 cd04338
Tic55 is a 55kDa LLS1-related non-heme iron oxygenase associated with protein transport ...
 72-204 9.29e-96

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: 287.11  E-value: 9.29e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  72 EEEKRVEVADYDWTEEWYPLYLTKNIPDDAPLGLTVYDRQIVLYKDGEGTLRCYEDRCPHRLAKLSEGQLIDGRLECLYH 151
Cdd:cd04338    2 EFETPENVAEYDWREEWYPLYLLKDVPTDAPLGLSVYDEPFVLFRDQNGQLRCLEDRCPHRLAKLSEGQLIDGKLECLYH 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 297821841 152 GWQFEGEGKCVKIPQLPASAKIPKAACVKTYEVKDSQGVVWVWMSTKTPPNPE 204
Cdd:cd04338   82 GWQFGGEGKCVKIPQLPADAKIPKNACVKSYEVRDSQGVVWMWMSEATPPDEE 134
PobA COG5749
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
83-412 3.53e-85

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


Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 267.64  E-value: 3.53e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  83 DWTEEWYPLYLTKNIPDDAPLGLTVYDRQIVLYKDGEGTLRCYEDRCPHRLAKLSEGQLIDGRLECLYHGWQFEGEGKCV 162
Cdd:COG5749   15 IFRNHWYPVAPSEDLKPNKPKPVTLLGEPLVIWRDSDGKVVALEDRCPHRGAPLSEGRVEGGNLRCPYHGWQFDGDGKCV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 163 KIPQLPASAKIPKAACVKTYEVKDSQGVVWVWMSTKTPPNPEKLPWFENFARPGFFDISTTHELPYDHSILLENLMDPAH 242
Cdd:COG5749   95 HIPQLPENQPIPKNAKVKSYPVQERYGLIWVWLGDPPQADETPIPDIPELDDPEWVATSSVRDLECHYSRLIENLIDPSH 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 243 VPISHDRTdfTAKREDAQPLVFEVtERSNRGFAGTW----GREKDGGKGSNL-----LRFDAPCVLQNNREFEGKDGVKN 313
Cdd:COG5749  175 VPFVHHGT--QGNRKQAQPLEMEI-ESTPNGITASYtaqsYYQLFFPFLGNLdetltITFIYPNTVSVDIGSGLGGRFGI 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 314 YfsglFLCRPTGQGKSMLIVRF--GVTKRsplvsvlPQW---FWHQNACKVFEQDMGFLSSQNEVLMKekvptKDLYLNL 388
Cdd:COG5749  252 V----LYATPIDEGKTRAYAIFfrNFAKK-------PRWlrhFLKLLRNGILEQDVIILESQQPALLQ-----LGSYELP 315

                        330       340
                 ....*....|....*....|....
gi 297821841 389 KSSDTWVAEYRKWMDKVGHGMPYH 412
Cdd:COG5749  316 TPADRAIIEFRRWLDKQAAGEGPW 339
PLN02518 PLN02518
pheophorbide a oxygenase
 1-509 7.58e-58

pheophorbide a oxygenase


Pssm-ID: 215283 [Multi-domain]  Cd Length: 539  Bit Score: 201.63  E-value: 7.58e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841   1 MAVPFLSSSLQLTPTSPilFTKLTPPIIHNQ-RPTTCTVPTKpRLRLLRRSAVAG-----TAVADQIEGGGEVLLNLEEE 74
Cdd:PLN02518   1 MAVLLGIACNSLTLTSS--TPKSTPFFIPARtIPFVSSSRPR-RGKIFTPLRVAAppsvpSEAALQQDEGEEQRVEQELG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  75 KRVEVADYDWTEEWYPLYLTKNIPDDAPLGLTVYDRQIVLYKD-GEGTLRCYEDRCPHRLAKLSEGQLID-GRLECLYHG 152
Cdd:PLN02518  78 QESSDSKFSWRDHWYPVSLVEDLDPSVPTPFQLLGRDLVLWKDpNQGEWVAFDDKCPHRLAPLSEGRIDEnGHLQCSYHG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 153 WQFEGEGKCVKIPQLPASAKIPKA-----ACVKTYEVKDSQGVVWVWMSTK-----TPPNPEKLPwfENFARPGFFDIST 222
Cdd:PLN02518 158 WSFDGCGSCTRIPQAAPEGPEARAvksprACAIKFPTMVSQGLLFVWPDENgweraQATKPPMLP--DEFDDPEFSTVTI 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 223 THELPYDHSILLENLMDPAHVPISHDRTdfTAKREDAQPLVFEVTERSNRGFAGTwgrekDGGKGSNLLRFDAPCVLQNN 302
Cdd:PLN02518 236 QRDLFYGYDTLMENVSDPSHIDFAHHKV--TGRRDRAKPLPFKVESSGPWGFAGA-----NSDNPRITAKFVAPCYYINK 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 303 REFEGK---DGVKNYFsgLFLCR---PTGQGKSMLIV-----RFGVTKRSP-LVSVLPQWFWHQNACKVFEQDMGFLSSQ 370
Cdd:PLN02518 309 IEIDTKlpiVGDQKWV--IWICSfnvPMAPGKTRSIVcsarnFFQFSMPGPaWWQLVPRWYEHWTSNKVYDGDMIVLQGQ 386

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 371 NEV-LMKEKVPTKDL---YLNL----KSSDTWVAEYRKWMDKVGHGMPYHFGHRTISLPkVPPVVehapagliaaLSASy 442
Cdd:PLN02518 387 EKIfLSKSGEGSADVnaqYTKLtftpTQADRFVLAFRNWLRRHGNSQPEWFGETSSQQP-LPSTV----------LSKR- 454

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297821841 443 pakggigtmhapNLANRYFRHIIHCRSCSNVIKSFELWKNILSATAVALTTLAILVVSRQWKAVLLG 509
Cdd:PLN02518 455 ------------QMLDRFEQHTLNCSSCKGAYKAFQTLQKVLIGATVVFAATAGIPSDVQLRLILAG 509
PaO pfam08417
Pheophorbide a oxygenase; This domain is found in bacterial and plant proteins to the ...
 293-380 1.05e-30

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: 114.73  E-value: 1.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  293 FDAPCVLQNNREFEGKDGVKNYFSGLFLCRPTGQGKSMLIVRFGVTKRSPLVSVLPQWFWHQNACKVFEQDMGFLSSQNE 372
Cdd:pfam08417   1 FIPPCVVRNDITFADEGGGKKRLGLVFYCIPTGPGKSRLIARFPRNFASWLPKLTPRWLKHINQNKVLDQDLILLHGQER 80


                  ....*...
gi 297821841  373 VLMKEKVP 380
Cdd:pfam08417  81 RLARGGGS 88
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 87-174 8.63e-29

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: 109.36  E-value: 8.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841   87 EWYPLYLTKNIPDDAPLGLTVYDRQIVLYKDGEGTLRCYEDRCPHRLAKLSEGQLI-DGRLECLYHGWQFEGEGKCVKIP 165
Cdd:pfam00355   1 SWYPVCHSSELPEGEPKVVEVGGEPLVVFRDEDGELYALEDRCPHRGAPLSEGKVNgGGRLECPYHGWRFDGTGKVVKVP 80


                  ....*....
gi 297821841  166 QLPASAKIP 174
Cdd:pfam00355  81 APRPLKSYP 89
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 97-193 1.06e-18

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: 81.43  E-value: 1.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  97 IPDDAPLGLTVYDRQIVLYKDGeGTLRCYEDRCPHRLAKLSEGQLIDGRLECLYHGWQFEGE-GKCVkipqlpasaKIPK 175
Cdd:COG2146   12 LPEGGGVVVEVGGKQIAVFRTD-GEVYAYDNRCPHQGAPLSEGIVDGGVVTCPLHGARFDLRtGECL---------GGPA 81

                         90
                 ....*....|....*...
gi 297821841 176 AACVKTYEVKDSQGVVWV 193
Cdd:COG2146   82 TEPLKTYPVRVEDGDVYV 99
nirD_assim_sml TIGR02378
nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of ...
 97-193 7.06e-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: 7.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841   97 IPDDAplGLTVY--DRQIVLYKDGEGTLRCYEDRCPHRLAK-LSEGQLIDGRLE----CLYHGWQFEGE-GKCVKIPQLp 168
Cdd:TIGR02378  11 IPEET--GVCVLlgDTQIAIFRVPGDQVFAIQNMCPHKRAFvLSRGIVGDAQGElwvaCPLHKRNFRLEdGRCLEDDSG- 87

                          90       100
                  ....*....|....*....|....*
gi 297821841  169 asakipkaaCVKTYEVKDSQGVVWV 193
Cdd:TIGR02378  88 ---------SVRTYEVRVEDGRVYV 103
PRK09965 PRK09965
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional
 119-200 2.16e-03

3-phenylpropionate dioxygenase ferredoxin subunit; Provisional


Pssm-ID: 170182 [Multi-domain]  Cd Length: 106  Bit Score: 37.83  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 119 EGTLRCYEDRCPHRLAKLSEGQLIDG-RLECLYHGWQFE---GEGKCvkipqLPasAKIPkaacVKTYEVKDSQGVVWVW 194
Cdd:PRK09965  32 GGEFYAIDDRCSHGNASLSEGYLEDDaTVECPLHAASFClrtGKALC-----LP--ATDP----LRTYPVHVEGGDIFID 100


                 ....*.
gi 297821841 195 MSTKTP 200
Cdd:PRK09965 101 LPEAQP 106
RHO_alpha_C_DMO-like cd08878
C-terminal catalytic domain of the oxygenase alpha subunit of dicamba O-demethylase and ...
 225-283 4.86e-03

C-terminal catalytic domain of the oxygenase alpha subunit of dicamba O-demethylase and related aromatic ring hydroxylating dioxygenases; C-terminal catalytic domain of the oxygenase alpha subunit of Stenotrophomonas maltophilia dicamba O-demethylase (DMO) and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). RHOs utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and the C-terminal catalytic domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Oxygenases belonging to this subgroup include the alpha subunits of carbazole 1,9a-dioxygenase, phthalate dioxygenase, vanillate O-demethylase, Pseudomonas putida 2-oxoquinoline 8-monooxygenase, and Comamonas testosteroni T-2 p-toluenesulfonate dioxygenase. It also includes the C-terminal domain of the lignin biphenyl-specific O-demethylase (LigX) of the 5,5'-dehydrodivanillic acid O- demethylation system of Sphingomonas paucimobilis SYK-6. This subfamily belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket.


Pssm-ID: 176887  Cd Length: 196  Bit Score: 38.56  E-value: 4.86e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 297821841 225 ELPYDHSILLENLMDPAHVPISHDRTDFTAKREDAQPLVFEVTERSNRGFAGTWGREKD 283
Cdd:cd08878    7 HIDCNWLQVVENLMDPSHVSFVHRSSIGRDAADLPSGPPKEVEEVPRGVTYRRWREDED 65
 
Name Accession Description Interval E-value
Rieske_RO_Alpha_Tic55 cd04338
Tic55 is a 55kDa LLS1-related non-heme iron oxygenase associated with protein transport ...
 72-204 9.29e-96

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: 287.11  E-value: 9.29e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  72 EEEKRVEVADYDWTEEWYPLYLTKNIPDDAPLGLTVYDRQIVLYKDGEGTLRCYEDRCPHRLAKLSEGQLIDGRLECLYH 151
Cdd:cd04338    2 EFETPENVAEYDWREEWYPLYLLKDVPTDAPLGLSVYDEPFVLFRDQNGQLRCLEDRCPHRLAKLSEGQLIDGKLECLYH 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 297821841 152 GWQFEGEGKCVKIPQLPASAKIPKAACVKTYEVKDSQGVVWVWMSTKTPPNPE 204
Cdd:cd04338   82 GWQFGGEGKCVKIPQLPADAKIPKNACVKSYEVRDSQGVVWMWMSEATPPDEE 134
PobA COG5749
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
83-412 3.53e-85

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


Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 267.64  E-value: 3.53e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  83 DWTEEWYPLYLTKNIPDDAPLGLTVYDRQIVLYKDGEGTLRCYEDRCPHRLAKLSEGQLIDGRLECLYHGWQFEGEGKCV 162
Cdd:COG5749   15 IFRNHWYPVAPSEDLKPNKPKPVTLLGEPLVIWRDSDGKVVALEDRCPHRGAPLSEGRVEGGNLRCPYHGWQFDGDGKCV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 163 KIPQLPASAKIPKAACVKTYEVKDSQGVVWVWMSTKTPPNPEKLPWFENFARPGFFDISTTHELPYDHSILLENLMDPAH 242
Cdd:COG5749   95 HIPQLPENQPIPKNAKVKSYPVQERYGLIWVWLGDPPQADETPIPDIPELDDPEWVATSSVRDLECHYSRLIENLIDPSH 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 243 VPISHDRTdfTAKREDAQPLVFEVtERSNRGFAGTW----GREKDGGKGSNL-----LRFDAPCVLQNNREFEGKDGVKN 313
Cdd:COG5749  175 VPFVHHGT--QGNRKQAQPLEMEI-ESTPNGITASYtaqsYYQLFFPFLGNLdetltITFIYPNTVSVDIGSGLGGRFGI 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 314 YfsglFLCRPTGQGKSMLIVRF--GVTKRsplvsvlPQW---FWHQNACKVFEQDMGFLSSQNEVLMKekvptKDLYLNL 388
Cdd:COG5749  252 V----LYATPIDEGKTRAYAIFfrNFAKK-------PRWlrhFLKLLRNGILEQDVIILESQQPALLQ-----LGSYELP 315

                        330       340
                 ....*....|....*....|....
gi 297821841 389 KSSDTWVAEYRKWMDKVGHGMPYH 412
Cdd:COG5749  316 TPADRAIIEFRRWLDKQAAGEGPW 339
PLN02518 PLN02518
pheophorbide a oxygenase
 1-509 7.58e-58

pheophorbide a oxygenase


Pssm-ID: 215283 [Multi-domain]  Cd Length: 539  Bit Score: 201.63  E-value: 7.58e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841   1 MAVPFLSSSLQLTPTSPilFTKLTPPIIHNQ-RPTTCTVPTKpRLRLLRRSAVAG-----TAVADQIEGGGEVLLNLEEE 74
Cdd:PLN02518   1 MAVLLGIACNSLTLTSS--TPKSTPFFIPARtIPFVSSSRPR-RGKIFTPLRVAAppsvpSEAALQQDEGEEQRVEQELG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  75 KRVEVADYDWTEEWYPLYLTKNIPDDAPLGLTVYDRQIVLYKD-GEGTLRCYEDRCPHRLAKLSEGQLID-GRLECLYHG 152
Cdd:PLN02518  78 QESSDSKFSWRDHWYPVSLVEDLDPSVPTPFQLLGRDLVLWKDpNQGEWVAFDDKCPHRLAPLSEGRIDEnGHLQCSYHG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 153 WQFEGEGKCVKIPQLPASAKIPKA-----ACVKTYEVKDSQGVVWVWMSTK-----TPPNPEKLPwfENFARPGFFDIST 222
Cdd:PLN02518 158 WSFDGCGSCTRIPQAAPEGPEARAvksprACAIKFPTMVSQGLLFVWPDENgweraQATKPPMLP--DEFDDPEFSTVTI 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 223 THELPYDHSILLENLMDPAHVPISHDRTdfTAKREDAQPLVFEVTERSNRGFAGTwgrekDGGKGSNLLRFDAPCVLQNN 302
Cdd:PLN02518 236 QRDLFYGYDTLMENVSDPSHIDFAHHKV--TGRRDRAKPLPFKVESSGPWGFAGA-----NSDNPRITAKFVAPCYYINK 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 303 REFEGK---DGVKNYFsgLFLCR---PTGQGKSMLIV-----RFGVTKRSP-LVSVLPQWFWHQNACKVFEQDMGFLSSQ 370
Cdd:PLN02518 309 IEIDTKlpiVGDQKWV--IWICSfnvPMAPGKTRSIVcsarnFFQFSMPGPaWWQLVPRWYEHWTSNKVYDGDMIVLQGQ 386

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 371 NEV-LMKEKVPTKDL---YLNL----KSSDTWVAEYRKWMDKVGHGMPYHFGHRTISLPkVPPVVehapagliaaLSASy 442
Cdd:PLN02518 387 EKIfLSKSGEGSADVnaqYTKLtftpTQADRFVLAFRNWLRRHGNSQPEWFGETSSQQP-LPSTV----------LSKR- 454

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297821841 443 pakggigtmhapNLANRYFRHIIHCRSCSNVIKSFELWKNILSATAVALTTLAILVVSRQWKAVLLG 509
Cdd:PLN02518 455 ------------QMLDRFEQHTLNCSSCKGAYKAFQTLQKVLIGATVVFAATAGIPSDVQLRLILAG 509
HcaE COG4638
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ...
 84-404 8.55e-42

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: 151.68  E-value: 8.55e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  84 WTEEWYPLYLTKNIPDD-APLGLTVYDRQIVLYKDGEGTLRCYEDRCPHRLAKLSEGQLIDGRLECLYHGWQFEGEGKCV 162
Cdd:COG4638   23 FRRGWYYVGHSSELPEPgDYLTRTILGEPVVLVRDKDGEVRAFHNVCPHRGAPLSEGRGNGGRLVCPYHGWTYDLDGRLV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 163 KIPQLPASAKI-PKAACVKTYEVKDSQGVVWVWMSTKTPPNPEKL----PWFENFARPGF-FDISTTHELPYDHSILLEN 236
Cdd:COG4638  103 GIPHMEGFPDFdPARAGLRSVPVEEWGGLIFVWLGPDAPPLAEYLgplaEYLDPYDFGELkVAGRETYEVNANWKLVVEN 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 237 LMDPAHVPISHDRTDFTakredAQPlvfevtersnrgfagtwgrekdggkgsNLLRFDAPCVLQnnrefegkdgvknyfs 316
Cdd:COG4638  183 FLDGYHVPFVHPGIILF-----LFP---------------------------NLMILDYPDHLV---------------- 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 317 gLFLCRPTGQGKSMLIVRFGVTKR--SPLVSVLPQWFWHQnackVFEQDMGFLSSQNEVLMKEKVPtkDLYLNLKSSDTW 394
Cdd:COG4638  215 -VRTVTPVSPDRTRVFVTFYVPKDalDPEARADLEAFWGR----VFEEDREIVERQQRGLRSLAYP--GPYLSRSPAEGG 287

                        330
                 ....*....|
gi 297821841 395 VAEYRKWMDK 404
Cdd:COG4638  288 VRHFRRWLRR 297
Rieske_RO_Alpha_PaO cd03480
Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, ...
 82-195 1.73e-39

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: 140.15  E-value: 1.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  82 YDWTEEWYPLYLTKNIPDDAPLGLTVYDRQIVLYKDG-EGTLRCYEDRCPHRLAKLSEGQL-IDGRLECLYHGWQFEGEG 159
Cdd:cd03480   12 FDWREVWYPVAYVEDLDPSRPTPFTLLGRDLVIWWDRnSQQWRAFDDQCPHRLAPLSEGRIdEEGCLECPYHGWSFDGSG 91

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 297821841 160 KCVKIPQLPASAKIPKA--ACVKTYEVKDSQGVVWVWM 195
Cdd:cd03480   92 SCQRIPQAAEGGKAHTSprACVASLPTAVRQGLLFVWP 129
Rieske_RO_Alpha_N cd03469
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ...
 88-201 3.20e-31

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: 116.92  E-value: 3.20e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  88 WYPLYLTKNIPD-DAPLGLTVYDRQIVLYKDGEGTLRCYEDRCPHRLAKLSEGQ-LIDGRLECLYHGWQFEGEGKCVKIP 165
Cdd:cd03469    1 WYFVGHSSELPEpGDYVTLELGGEPLVLVRDRDGEVRAFHNVCPHRGARLCEGRgGNAGRLVCPYHGWTYDLDGKLVGVP 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 297821841 166 QLPA-SAKIPKAACVKTYEVKDSQGVVWVWMSTKTPP 201
Cdd:cd03469   81 REEGfPGFDKEKLGLRTVPVEEWGGLIFVNLDPDAPP 117
PaO pfam08417
Pheophorbide a oxygenase; This domain is found in bacterial and plant proteins to the ...
 293-380 1.05e-30

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: 114.73  E-value: 1.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  293 FDAPCVLQNNREFEGKDGVKNYFSGLFLCRPTGQGKSMLIVRFGVTKRSPLVSVLPQWFWHQNACKVFEQDMGFLSSQNE 372
Cdd:pfam08417   1 FIPPCVVRNDITFADEGGGKKRLGLVFYCIPTGPGKSRLIARFPRNFASWLPKLTPRWLKHINQNKVLDQDLILLHGQER 80


                  ....*...
gi 297821841  373 VLMKEKVP 380
Cdd:pfam08417  81 RLARGGGS 88
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 87-174 8.63e-29

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: 109.36  E-value: 8.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841   87 EWYPLYLTKNIPDDAPLGLTVYDRQIVLYKDGEGTLRCYEDRCPHRLAKLSEGQLI-DGRLECLYHGWQFEGEGKCVKIP 165
Cdd:pfam00355   1 SWYPVCHSSELPEGEPKVVEVGGEPLVVFRDEDGELYALEDRCPHRGAPLSEGKVNgGGRLECPYHGWRFDGTGKVVKVP 80


                  ....*....
gi 297821841  166 QLPASAKIP 174
Cdd:pfam00355  81 APRPLKSYP 89
Rieske_RO_Alpha_VanA_DdmC cd03532
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and ...
 87-195 3.34e-28

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: 108.61  E-value: 3.34e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  87 EWYPLYLTKNIpDDAPLGLTVYDRQIVLYKDGEGTLRCYEDRCPHRLAKLSEGQLIDGRLECLYHGWQFEGEGKCVKIpq 166
Cdd:cd03532    5 AWYVAAWADEL-GDKPLARTLLGEPVVLYRTQDGRVAALEDRCPHRSAPLSKGSVEGGGLVCGYHGLEFDSDGRCVHM-- 81

                         90       100
                 ....*....|....*....|....*....
gi 297821841 167 lPASAKIPKAACVKTYEVKDSQGVVWVWM 195
Cdd:cd03532   82 -PGQERVPAKACVRSYPVVERDALIWIWM 109
PLN02281 PLN02281
chlorophyllide a oxygenase
 88-408 4.08e-28

chlorophyllide a oxygenase


Pssm-ID: 177920 [Multi-domain]  Cd Length: 536  Bit Score: 117.91  E-value: 4.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  88 WYPLYLTKNIPDDAPLGLTVYDRQIVLYKDGEGTLRCYEDRCPHRLAKLSEGQLIDGRLECLYHGWQFEGEGKCVKIPql 167
Cdd:PLN02281 221 WYPVAFTADLKHDTMVPIECFEQPWVIFRGEDGKPGCVRNTCAHRACPLDLGTVNEGRIQCPYHGWEYSTDGECKKMP-- 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 168 paSAKIPKAAcVKTYEVKDSQGVVWVWMSTKtPPNPeKLPWFENfarPGFFDIST--THELPYDHSILLENLMDPAHVPI 245
Cdd:PLN02281 299 --STKLLKVK-IKSLPCLEQEGMIWIWPGDE-PPAP-ILPSLQP---PSGFLIHAelVMDLPVEHGLLLDNLLDLAHAPF 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 246 SHDRTdfTAKREDAQPLVFEVTERSnrGFAGTWGREKDGgkgsnlLRFDAPCV------LQNNREFEGKDGVK--NYFSG 317
Cdd:PLN02281 371 THTST--FAKGWSVPSLVKFLTPTS--GLQGYWDPYPID------MEFKPPCIvlstigISKPGKLEGKSTQQcaTHLHQ 440

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 318 LFLCRPTGQGKSMLIVRFGVtKRSPLVSVLP--QWFWHQNACKVFEQDMGFLSSQNEvlmkEKVPTKDLYLNLKSSDTWV 395
Cdd:PLN02281 441 LHVCLPSSKNKTRLLYRMSL-DFAPILKNLPfmEHLWRHFAEQVLNEDLRLVLGQQE----RMLNGANIWNLPVAYDKLG 515

                        330
                 ....*....|...
gi 297821841 396 AEYRKWMDKVGHG 408
Cdd:PLN02281 516 VRYRLWRNAVDRG 528
Rieske_RO_Alpha_Cao cd04337
Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the ...
 88-201 1.12e-25

Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the plastid-envelope inner and thylakoid membranes, that catalyzes the conversion of chlorophyllide a to chlorophyllide b. CAO is found not only in plants but also in chlorophytes and prochlorophytes. This domain represents the N-terminal rieske domain of the oxygenase alpha subunit. ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. Cao is closely related to several other plant RO's including Tic 55, a 55 kDa protein associated with protein transport through the inner chloroplast membrane; Ptc 52, a novel 52 kDa protein isolated from chloroplasts; and LLS1/Pao (Lethal-leaf spot 1/pheophorbide a oxygenase).


Pssm-ID: 239829 [Multi-domain]  Cd Length: 129  Bit Score: 102.18  E-value: 1.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  88 WYPLYLTKNIPDDAPLGLTVYDRQIVLYKDGEGTLRCYEDRCPHRLAKLSEGQLIDGRLECLYHGWQFEGEGKCVKIPQL 167
Cdd:cd04337   18 WYPVEFSKDLKMDTMVPFELFGQPWVLFRDEDGTPGCIRDECAHRACPLSLGKVIEGRIQCPYHGWEYDGDGECTKMPST 97

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 297821841 168 PA-SAKIPKAACVktyevkDSQGVVWVWMSTKTPP 201
Cdd:cd04337   98 KClNVGIAALPCM------EQDGMIWVWPGDDPPA 126
Rieske_RO_Alpha_PhDO_like cd03479
Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, ...
 88-213 9.08e-22

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: 91.54  E-value: 9.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  88 WYPLYLTKNIP-DDAPLGLTVYDRQIVLYKDGEGTLRCYEDRCPHRLAKLSEGQLIDGRLECLYHGWQFEGEGKCVKIPQ 166
Cdd:cd03479   22 WQPVALSSELTeDGQPVRVRLLGEDLVAFRDTSGRVGLLDEHCPHRGASLVFGRVEECGLRCCYHGWKFDVDGQCLEMPS 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 297821841 167 LPASAKIPKAACVKTYEVKDSQGVVWVWMSTktppnPEKLPWFENFA 213
Cdd:cd03479  102 EPPDSQLKQKVRQPAYPVRERGGLVWAYMGP-----AEEAPEFPRYD 143
PLN00095 PLN00095
chlorophyllide a oxygenase; Provisional
 88-337 2.03e-20

chlorophyllide a oxygenase; Provisional


Pssm-ID: 165668 [Multi-domain]  Cd Length: 394  Bit Score: 93.21  E-value: 2.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  88 WYPLYLTKNIPD-DAPLGLTVYDRQIVLYKDGEGTLRCYEDRCPHRLAKLSEGQLIDGRLECLYHGWQFEGEGKCVKipq 166
Cdd:PLN00095  73 WFPVAFAAGLRDeDALIAFDLFNVPWVLFRDADGEAGCIKDECAHRACPLSLGKLVDGKAQCPYHGWEYETGGECAK--- 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 167 LPASAKIPKAACVKTYEVKDSQGVVWVWMSTKTP-----PNPEKLPWFEN---------FARP-GFFDIS-TTHELPYDH 230
Cdd:PLN00095 150 MPSCKKFLKGVFADAAPVIERDGFIFLWAGESDPadfvgPEAACESIDDDvlaanepgmFAPGeGFTPMAeVIADIKLDA 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 231 SILLENLMDPahvpishdrtdftAKREDAQPLVFEVTERSNRGFAGTWgrEKDGGK-GSNLLR-----------FDAPCV 298
Cdd:PLN00095 230 DEVLERLLAI-------------GERARREATVSFDVSDAKRGRDALF--PVDGTKiIAKVLRggrdavpqsatFKPACV 294

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 297821841 299 LQNNREFE----GKDGVKNYFSGLFLCRPTGQGKSMLIVRFGV 337
Cdd:PLN00095 295 IASTIALEdgpgGGDGTDMNVEQLHVCLPAKPGLCRLLFRLAF 337
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 88-192 5.68e-19

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: 82.15  E-value: 5.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  88 WYPLYLTKNIPDDAPLGLTVYDRQIVLYKDGEGTLRCYEDRCPHRLAKLSEGQLIDGRLECLYHGWQFEGE-GKCVKIPQ 166
Cdd:cd03467    1 WVVVGALSELPPGGGRVVVVGGGPVVVVRREGGEVYALSNRCTHQGCPLSEGEGEDGCIVCPCHGSRFDLRtGEVVSGPA 80

                         90       100
                 ....*....|....*....|....*..
gi 297821841 167 lpasakipkAACVKTYEVK-DSQGVVW 192
Cdd:cd03467   81 ---------PRPLPKYPVKvEGDGVVW 98
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 97-193 1.06e-18

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: 81.43  E-value: 1.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  97 IPDDAPLGLTVYDRQIVLYKDGeGTLRCYEDRCPHRLAKLSEGQLIDGRLECLYHGWQFEGE-GKCVkipqlpasaKIPK 175
Cdd:COG2146   12 LPEGGGVVVEVGGKQIAVFRTD-GEVYAYDNRCPHQGAPLSEGIVDGGVVTCPLHGARFDLRtGECL---------GGPA 81

                         90
                 ....*....|....*...
gi 297821841 176 AACVKTYEVKDSQGVVWV 193
Cdd:COG2146   82 TEPLKTYPVRVEDGDVYV 99
Rieske_RO_Alpha_PrnD cd03537
This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit of ...
 88-203 2.37e-17

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: 78.05  E-value: 2.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  88 WYpLYLTKNIPDDAPLGLTVYDRQIVLYKDGEGTLRCYEDRCPHRLAKLSEGQLIDGRLECLYHGWQFEGEGKCVKIP-- 165
Cdd:cd03537    4 WY-VAMRSDDLKDKPTELTLFGRPCVAWRGATGRAVVMDRHCSHLGANLADGRVKDGCIQCPFHHWRYDEQGQCVHIPgh 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 297821841 166 --QLPASAKIPKAACVKTYEVKDSQGVVWVWMSTKTPPNP 203
Cdd:cd03537   83 stAVRRLEPVPRGARQPTLVTAERYGYVWVWYGSPQPLHP 122
Rieske_RO_Alpha_OMO_CARDO cd03548
Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole ...
 88-195 2.39e-15

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: 72.84  E-value: 2.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  88 WYPLYLTKNIPDDAPLGLTVYDRQIVLYKDGeGTLRCYEDRCPHRLAKLSEGQ--LIDGRLECLYHGWQFE-GEGKCVKI 164
Cdd:cd03548   15 WYPALFSHELEEGEPKGIQLCGEPILLRRVD-GKVYALKDRCLHRGVPLSKKPecFTKGTITCWYHGWTYRlDDGKLVTI 93

                         90       100       110
                 ....*....|....*....|....*....|.
gi 297821841 165 PQLPASAKIPKAAcVKTYEVKDSQGVVWVWM 195
Cdd:cd03548   94 LANPDDPLIGRTG-LKTYPVEEAKGMIFVFV 123
Rieske_RO_Alpha_KSH cd03531
The alignment model represents the N-terminal rieske iron-sulfur domain of KshA, the oxygenase ...
 88-194 2.62e-13

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: 66.28  E-value: 2.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  88 WYPLYLTKNIPDDAPLGLTVYDRQIVLYKDGEGTLRCYEDRCPHRLAKLSEGQLIDGRLECLYHGWQFEGEGKCVKIPQl 167
Cdd:cd03531    2 WHCLGLARDFRDGKPHGVEAFGTKLVVFADSDGALNVLDAYCRHMGGDLSQGTVKGDEIACPFHDWRWGGDGRCKAIPY- 80

                         90       100
                 ....*....|....*....|....*..
gi 297821841 168 paSAKIPKAACVKTYEVKDSQGVVWVW 194
Cdd:cd03531   81 --ARRVPPLARTRAWPTLERNGQLFVW 105
Rieske_RO_ferredoxin cd03528
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ...
 97-194 7.62e-11

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: 58.65  E-value: 7.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  97 IPDDAPLGLTVYDRQIVLYKDGeGTLRCYEDRCPHRLAKLSEGQLIDGRLECLYHGWQFE---GEGKCvkipqLPasAKI 173
Cdd:cd03528   10 LPEGEPKRVDVGGRPIAVYRVD-GEFYATDDLCTHGDASLSEGYVEGGVIECPLHGGRFDlrtGKALS-----LP--ATE 81

                         90       100
                 ....*....|....*....|.
gi 297821841 174 PkaacVKTYEVKDSQGVVWVW 194
Cdd:cd03528   82 P----LKTYPVKVEDGDVYVD 98
Rieske_NirD_small_Bacillus cd03530
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar ...
 109-193 2.16e-08

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: 51.84  E-value: 2.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 109 DRQIVLYKDGEGTLRCYEDRCPHRLAKLSEGQLIDGRLECLYHGWQFE---GEgkcvkipqlpasAKIPKAACVKTYEVK 185
Cdd:cd03530   22 GGEIAVFRTADDEVFALENRCPHKGGPLSEGIVHGEYVTCPLHNWVIDletGE------------AQGPDEGCVRTFPVK 89


                 ....*...
gi 297821841 186 DSQGVVWV 193
Cdd:cd03530   90 VEDGRVYL 97
nirD_assim_sml TIGR02378
nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of ...
 97-193 7.06e-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: 7.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841   97 IPDDAplGLTVY--DRQIVLYKDGEGTLRCYEDRCPHRLAK-LSEGQLIDGRLE----CLYHGWQFEGE-GKCVKIPQLp 168
Cdd:TIGR02378  11 IPEET--GVCVLlgDTQIAIFRVPGDQVFAIQNMCPHKRAFvLSRGIVGDAQGElwvaCPLHKRNFRLEdGRCLEDDSG- 87

                          90       100
                  ....*....|....*....|....*
gi 297821841  169 asakipkaaCVKTYEVKDSQGVVWV 193
Cdd:TIGR02378  88 ---------SVRTYEVRVEDGRVYV 103
Rieske_AIFL_N cd03478
AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family ...
 97-192 8.63e-07

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: 47.23  E-value: 8.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  97 IPDDAPLGLTVYDRQIVLYKDGeGTLRCYEDRCPHRLAKLSEGQLIDGRLECLYHGWQFEGE-GKCVKIPQLpasakipk 175
Cdd:cd03478    9 LGDGEMKEVDVGDGKVLLVRQG-GEVHAIGAKCPHYGAPLAKGVLTDGRIRCPWHGACFNLRtGDIEDAPAL-------- 79

                         90
                 ....*....|....*..
gi 297821841 176 aACVKTYEVKDSQGVVW 192
Cdd:cd03478   80 -DSLPCYEVEVEDGRVY 95
Rieske_T4moC cd03474
Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske ...
 112-194 4.06e-06

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: 45.79  E-value: 4.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 112 IVLYKDGeGTLRCYEDRCPHRLAKLSEGQLiDGR-LECLYHGWQFEGEGKCvkipqlpasAKIPKAACVKTYEVKDSQGV 190
Cdd:cd03474   26 LLVAPEG-GEFRAFQGICPHQEIPLAEGGF-DGGvLTCRAHLWQFDADTGE---------GLNPRDCRLARYPVKVEGGD 94


                 ....
gi 297821841 191 VWVW 194
Cdd:cd03474   95 ILVD 98
Rieske_RO_Alpha_OHBDO_like cd03545
Rieske non-heme iron oxygenase (RO) family, Ortho-halobenzoate-1,2-dioxygenase (OHBDO)-like ...
 88-165 2.38e-05

Rieske non-heme iron oxygenase (RO) family, Ortho-halobenzoate-1,2-dioxygenase (OHBDO)-like subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of OHBDO, salicylate 5-hydroxylase (S5H), terephthalate 1,2-dioxygenase system (TERDOS) and similar proteins. ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. OHBDO converts 2-chlorobenzoate (2-CBA) to catechol as well as 2,4-dCBA and 2,5-dCBA to 4-chlorocatechol, as part of the chlorobenzoate degradation pathway. Although ortho-substituted chlorobenzoates appear to be particularly recalcitrant to biodegradation, several strains utilize 2-CBA and the dCBA derivatives as a sole carbon and energy source. S5H converts salicylate (2-hydroxybenzoate), a metabolic intermediate of phenanthrene, to gentisate (2,5-dihydroxybenzoate) as part of an alternate pathway for naphthalene catabolism. S5H is a multicomponent enzyme made up of NagGH (the oxygenase components), NagAa (the ferredoxin reductase component), and NagAb (the ferredoxin component). The oxygenase component is made up of alpha (NagG) and beta (NagH) subunits. TERDOS is present in gram-positive bacteria and proteobacteria where it converts terephthalate (1,4-dicarboxybenzene) to protocatechuate as part of the terephthalate degradation pathway. The oxygenase component of TERDOS, called TerZ, is a hetero-hexamer with 3 alpha (TerZalpha) and 3 beta (TerZbeta) subunits.


Pssm-ID: 239616 [Multi-domain]  Cd Length: 150  Bit Score: 44.36  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841  88 WYPLYLTKNIPDDAPLGLT-VYDRQIVLYKDGEGTLRCYEDRCPHRLAKLSE---GQliDGRLECLYHGWQFEGEGKCVK 163
Cdd:cd03545   26 WSYVGLEAEIPNAGDFKSTfVGDTPVVVTRAEDGSLHAWVNRCAHRGALVCRerrGN--DGSLTCVYHQWAYDLKGNLKG 103


                 ..
gi 297821841 164 IP 165
Cdd:cd03545  104 VP 105
Rieske_RO_Alpha_AntDO cd03538
Rieske non-heme iron oxygenase (RO) family, Anthranilate 1,2-dioxygenase (AntDO) subfamily, ...
 106-165 2.94e-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: 41.29  E-value: 2.94e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297821841 106 TVYDRQIVLYKDGEGTLRCYEDRCPHRLAKL-SEGQLIDGR-LECLYHGWQFEGEGKCVKIP 165
Cdd:cd03538   42 RIGDQPVVMVRHTDGSVHVLYNRCPHKGTKIvSDGCGNTGKfFRCPYHAWSFKTDGSLLAIP 103
Rieske_RO_Alpha_CMO cd03541
Rieske non-heme iron oxygenase (RO) family, Choline monooxygenase (CMO) subfamily, N-terminal ...
 113-166 7.71e-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: 39.46  E-value: 7.71e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 297821841 113 VLYKDGEGTLRCYEDRCPHRLAKLSEGQLIDGRLECLYHGWQFEGEGKCVKIPQ 166
Cdd:cd03541   28 VVCRDGNGKLHAFHNVCTHRASILACGSGKKSCFVCPYHGWVYGLDGSLTKATQ 81
Rieske_RO_Alpha_NDO cd03535
Rieske non-heme iron oxygenase (RO) family, Nathphalene 1,2-dioxygenase (NDO) subfamily, ...
 107-165 1.04e-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: 39.34  E-value: 1.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 107 VYDRQIVLYKDGEGTLRCYEDRCPHRLAKLSEGQLID-GRLECLYHGWQFEGEGKCVKIP 165
Cdd:cd03535   23 IGDDSFIVCRDEDGEIRAMFNSCRHRGMQVCRAEMGNtSHFRCPYHGWTYRNTGRLVGVP 82
PRK09965 PRK09965
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional
 119-200 2.16e-03

3-phenylpropionate dioxygenase ferredoxin subunit; Provisional


Pssm-ID: 170182 [Multi-domain]  Cd Length: 106  Bit Score: 37.83  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297821841 119 EGTLRCYEDRCPHRLAKLSEGQLIDG-RLECLYHGWQFE---GEGKCvkipqLPasAKIPkaacVKTYEVKDSQGVVWVW 194
Cdd:PRK09965  32 GGEFYAIDDRCSHGNASLSEGYLEDDaTVECPLHAASFClrtGKALC-----LP--ATDP----LRTYPVHVEGGDIFID 100


                 ....*.
gi 297821841 195 MSTKTP 200
Cdd:PRK09965 101 LPEAQP 106
Rieske_RO_Alpha_HBDO cd03542
Rieske non-heme iron oxygenase (RO) family, 2-Halobenzoate 1,2-dioxygenase (HBDO) subfamily, ...
 110-164 3.41e-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: 37.81  E-value: 3.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 297821841 110 RQ-IVLYKDGEGTLRCYEDRCPHRLAKLSE-GQLIDGRLECLYHGWQFEGEGKCVKI 164
Cdd:cd03542   23 RQpVVITRDKDGELNAFINACSHRGAMLCRrKQGNKGTFTCPFHGWTFSNTGKLLKV 79
RHO_alpha_C_DMO-like cd08878
C-terminal catalytic domain of the oxygenase alpha subunit of dicamba O-demethylase and ...
 225-283 4.86e-03

C-terminal catalytic domain of the oxygenase alpha subunit of dicamba O-demethylase and related aromatic ring hydroxylating dioxygenases; C-terminal catalytic domain of the oxygenase alpha subunit of Stenotrophomonas maltophilia dicamba O-demethylase (DMO) and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). RHOs utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and the C-terminal catalytic domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Oxygenases belonging to this subgroup include the alpha subunits of carbazole 1,9a-dioxygenase, phthalate dioxygenase, vanillate O-demethylase, Pseudomonas putida 2-oxoquinoline 8-monooxygenase, and Comamonas testosteroni T-2 p-toluenesulfonate dioxygenase. It also includes the C-terminal domain of the lignin biphenyl-specific O-demethylase (LigX) of the 5,5'-dehydrodivanillic acid O- demethylation system of Sphingomonas paucimobilis SYK-6. This subfamily belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket.


Pssm-ID: 176887  Cd Length: 196  Bit Score: 38.56  E-value: 4.86e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 297821841 225 ELPYDHSILLENLMDPAHVPISHDRTDFTAKREDAQPLVFEVTERSNRGFAGTWGREKD 283
Cdd:cd08878    7 HIDCNWLQVVENLMDPSHVSFVHRSSIGRDAADLPSGPPKEVEEVPRGVTYRRWREDED 65
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH