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Conserved domains on  [gi|743678019|gb|AJC20153|]
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phthalate 4,5-dioxygenase [Pandoraea pulmonicola]

Protein Classification

aromatic ring-hydroxylating dioxygenase subunit alpha( domain architecture ID 10231820)

aromatic ring-hydroxylating dioxygenase subunit alpha is the catalytic component of a complex that catalyzes the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rieske super family cl00938
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 7-149 3.97e-63

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.


The actual alignment was detected with superfamily member cd03479:

Pssm-ID: 445190 [Multi-domain]  Cd Length: 144  Bit Score: 200.55  E-value: 3.97e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019   7 NQLLTQVGPGTPMGDLLRRYWHPIGAESEFDEI-SVRPARLFGEDLVLYKDLSGNYGLVDRQCPHRRADLAYGFVEKCGL 85
Cdd:cd03479    2 NELLTRVGPGTPMGELLRRYWQPVALSSELTEDgQPVRVRLLGEDLVAFRDTSGRVGLLDEHCPHRGASLVFGRVEECGL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743678019  86 RCNYHGWLYDEKGQCTEQPYEdiaNPQVRLKDRIKIKSYPVQVKAGMIWAYMGPL-PAPLVPTWE 149
Cdd:cd03479   82 RCCYHGWKFDVDGQCLEMPSE---PPDSQLKQKVRQPAYPVRERGGLVWAYMGPAeEAPEFPRYD 143
PobA super family cl47407
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
11-339 6.98e-55

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


The actual alignment was detected with superfamily member COG5749:

Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 185.97  E-value: 6.98e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  11 TQVGPGTPMGDLLRRYWHPIGAESEFDEISVRPARLFGEDLVLYKDLSGNYGLVDRQCPHRRADLAYGFVEKCGLRCNYH 90
Cdd:COG5749    4 TRQGPGFNQPFIFRNHWYPVAPSEDLKPNKPKPVTLLGEPLVIWRDSDGKVVALEDRCPHRGAPLSEGRVEGGNLRCPYH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  91 GWLYDEKGQCTEQPYEDianPQVRLKDRIKIKSYPVQVKAGMIWAYMGPLPA------PLVPTWEPFTWangFRQVVISE 164
Cdd:COG5749   84 GWQFDGDGKCVHIPQLP---ENQPIPKNAKVKSYPVQERYGLIWVWLGDPPQadetpiPDIPELDDPEW---VATSSVRD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019 165 VPCNWFQCQENSIDPVHFEWMHSNWSvrlrgdTGPYAPTHTKLGFEEFEYGLIYKRVREDTDEKHPLWAvGRLALW---- 240
Cdd:COG5749  158 LECHYSRLIENLIDPSHVPFVHHGTQ------GNRKQAQPLEMEIESTPNGITASYTAQSYYQLFFPFL-GNLDETltit 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019 241 ---PNV------FCLGDHFE---WRVPIDDENTLSITWAFNRVPrerepyvqeKIPAWYGPVKdeatgQWISSHVMNQD- 307
Cdd:COG5749  231 fiyPNTvsvdigSGLGGRFGivlYATPIDEGKTRAYAIFFRNFA---------KKPRWLRHFL-----KLLRNGILEQDv 296

                        330       340       350
                 ....*....|....*....|....*....|...
gi 743678019 308 -FVAWVGQGRIADRTRENLGASDRGIAMLRRHF 339
Cdd:COG5749  297 iILESQQPALLQLGSYELPTPADRAIIEFRRWL 329
 
Name Accession Description Interval E-value
Rieske_RO_Alpha_PhDO_like cd03479
Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, ...
 7-149 3.97e-63

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: 200.55  E-value: 3.97e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019   7 NQLLTQVGPGTPMGDLLRRYWHPIGAESEFDEI-SVRPARLFGEDLVLYKDLSGNYGLVDRQCPHRRADLAYGFVEKCGL 85
Cdd:cd03479    2 NELLTRVGPGTPMGELLRRYWQPVALSSELTEDgQPVRVRLLGEDLVAFRDTSGRVGLLDEHCPHRGASLVFGRVEECGL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743678019  86 RCNYHGWLYDEKGQCTEQPYEdiaNPQVRLKDRIKIKSYPVQVKAGMIWAYMGPL-PAPLVPTWE 149
Cdd:cd03479   82 RCCYHGWKFDVDGQCLEMPSE---PPDSQLKQKVRQPAYPVRERGGLVWAYMGPAeEAPEFPRYD 143
PobA COG5749
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
11-339 6.98e-55

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


Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 185.97  E-value: 6.98e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  11 TQVGPGTPMGDLLRRYWHPIGAESEFDEISVRPARLFGEDLVLYKDLSGNYGLVDRQCPHRRADLAYGFVEKCGLRCNYH 90
Cdd:COG5749    4 TRQGPGFNQPFIFRNHWYPVAPSEDLKPNKPKPVTLLGEPLVIWRDSDGKVVALEDRCPHRGAPLSEGRVEGGNLRCPYH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  91 GWLYDEKGQCTEQPYEDianPQVRLKDRIKIKSYPVQVKAGMIWAYMGPLPA------PLVPTWEPFTWangFRQVVISE 164
Cdd:COG5749   84 GWQFDGDGKCVHIPQLP---ENQPIPKNAKVKSYPVQERYGLIWVWLGDPPQadetpiPDIPELDDPEW---VATSSVRD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019 165 VPCNWFQCQENSIDPVHFEWMHSNWSvrlrgdTGPYAPTHTKLGFEEFEYGLIYKRVREDTDEKHPLWAvGRLALW---- 240
Cdd:COG5749  158 LECHYSRLIENLIDPSHVPFVHHGTQ------GNRKQAQPLEMEIESTPNGITASYTAQSYYQLFFPFL-GNLDETltit 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019 241 ---PNV------FCLGDHFE---WRVPIDDENTLSITWAFNRVPrerepyvqeKIPAWYGPVKdeatgQWISSHVMNQD- 307
Cdd:COG5749  231 fiyPNTvsvdigSGLGGRFGivlYATPIDEGKTRAYAIFFRNFA---------KKPRWLRHFL-----KLLRNGILEQDv 296

                        330       340       350
                 ....*....|....*....|....*....|...
gi 743678019 308 -FVAWVGQGRIADRTRENLGASDRGIAMLRRHF 339
Cdd:COG5749  297 iILESQQPALLQLGSYELPTPADRAIIEFRRWL 329
RHO_alpha_C_DMO-like cd08878
C-terminal catalytic domain of the oxygenase alpha subunit of dicamba O-demethylase and ...
 153-343 1.92e-41

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: 145.65  E-value: 1.92e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019 153 WANGFRqvvisEVPCNWFQCQENSIDPVHFEWMHSNWSVRLRGDTgpyaPTHTKLGFEEFEYGLIYKRVREDTD------ 226
Cdd:cd08878    1 WGGGYR-----HIDCNWLQVVENLMDPSHVSFVHRSSIGRDAADL----PSGPPKEVEEVPRGVTYRRWREDEDpppfgf 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019 227 EKHPLWAVGRLALWPNVFCLG---------------DHFEWRVPIdDENTLSITWAFNRVPREREPyvqekipaWYGPVK 291
Cdd:cd08878   72 EGPVDRWRVIEFLLPNVLLIDpgvapagtreqgvrmRVTHWITPI-DETTTHYFWFFVRNFAPDEE--------KKDDEE 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 743678019 292 DEATGQWISSHVMNQDFVAWVGQGRIADR--TRENLGASDRGIAMLRRHFFDEL 343
Cdd:cd08878  143 LTETLRSGLSGAFNEDKEAVEAQQRIIDRdpTREHLGLSDKGIVRFRRLLRRLL 196
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 27-125 2.01e-19

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: 82.40  E-value: 2.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019   27 WHPIGAESEFDEISVRPARLFGEDLVLYKDLSGNYGLVDRQCPHRRADLAYGFVEKCG-LRCNYHGWLYDEKGQCteqpy 105
Cdd:pfam00355   2 WYPVCHSSELPEGEPKVVEVGGEPLVVFRDEDGELYALEDRCPHRGAPLSEGKVNGGGrLECPYHGWRFDGTGKV----- 76

                          90       100
                  ....*....|....*....|
gi 743678019  106 edIANPQVRlkdriKIKSYP 125
Cdd:pfam00355  77 --VKVPAPR-----PLKSYP 89
PLN02281 PLN02281
chlorophyllide a oxygenase
 14-191 4.69e-18

chlorophyllide a oxygenase


Pssm-ID: 177920 [Multi-domain]  Cd Length: 536  Bit Score: 86.32  E-value: 4.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  14 GPGTPMGDLLRRYWHPIGAESEFDEISVRPARLFGEDLVLYKDLSGNYGLVDRQCPHRRADLAYGFVEKCGLRCNYHGWL 93
Cdd:PLN02281 208 GPVPPYSPHLKNFWYPVAFTADLKHDTMVPIECFEQPWVIFRGEDGKPGCVRNTCAHRACPLDLGTVNEGRIQCPYHGWE 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  94 YDEKGQCTEQPYEDIAnpqvrlkdRIKIKSYPVQVKAGMIWAYMG-PLPAPLVPTWEPftwANGF--RQVVISEVPCNWF 170
Cdd:PLN02281 288 YSTDGECKKMPSTKLL--------KVKIKSLPCLEQEGMIWIWPGdEPPAPILPSLQP---PSGFliHAELVMDLPVEHG 356

                        170       180
                 ....*....|....*....|....*.
gi 743678019 171 QCQENSIDPVHFEWMHSN-----WSV 191
Cdd:PLN02281 357 LLLDNLLDLAHAPFTHTStfakgWSV 382
LigXa_C pfam19301
LigXa C-terminal domain like; This entry represents the C-terminal domain of a Rieske ...
 135-356 1.48e-14

LigXa C-terminal domain like; This entry represents the C-terminal domain of a Rieske oxygenase enzyme. This entry includes the 5,5'-dehydrodivanillate O-demethylase three-component monooxygenase which is composed of an oxygenase (LigXa) in this entry, a ferredoxin (LigXc) and a ferredoxin reductase (LigXd).


Pssm-ID: 437133  Cd Length: 303  Bit Score: 74.00  E-value: 1.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  135 AYMGPlpAPLVPTWEPFTWA-NGFRQVVISEV--PCNWFQCQENSIDPVHFEWMHS----------------NWsVRLRG 195
Cdd:pfam19301   1 VYMGP--QDTVPEFEPPAWApTPDAKVSIAKIllPCNWAQILEGAIDSAHSSSLHSsdmvparvggaeatdkAW-LRPST 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  196 DTGPyapthtKLGFEEFEYGLIYKRVRE-----DTDE--KHPLWAVGRLALWP-----NVFCLgdhfewRVPIDDENTLS 263
Cdd:pfam19301  78 DKAP------RLQVQRTSYGFRYAAIRRpitnaATHDyvRSTVFVAPATVLIPpnnlyNVANV------NVPMDDTNTAF 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  264 --ITWAFNRVPREREPY-------VQEKIPAWYGPVKDEATGQWISSHVM------------NQDFVAWVGQGRIADRTR 322
Cdd:pfam19301 146 yfIAWGHPAKTPETETWrkflgaqVGVDLDPRYRPLRNRENNFWQDRQAMkagnftgipgfpNQDIAMWETMGPIADRSH 225

                         250       260       270
                  ....*....|....*....|....*....|....
gi 743678019  323 ENLGASDRGIAMLRRHFFDELDAVAQGRDPKGLV 356
Cdd:pfam19301 226 ERLGASDLAIVEFRRQMLEAAQAFAAGEPAIGTG 259
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 27-134 1.72e-12

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: 63.32  E-value: 1.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  27 WHPIGAESEFDEISVRPARLFGEDLVLYKdLSGNYGLVDRQCPHRRADLAYGFVEKCGLRCNYHGWLYD-EKGQCTEQPy 105
Cdd:COG2146    3 EVKVCALDDLPEGGGVVVEVGGKQIAVFR-TDGEVYAYDNRCPHQGAPLSEGIVDGGVVTCPLHGARFDlRTGECLGGP- 80

                         90       100
                 ....*....|....*....|....*....
gi 743678019 106 edianpqvrlkDRIKIKSYPVQVKAGMIW 134
Cdd:COG2146   81 -----------ATEPLKTYPVRVEDGDVY 98
nirD_assim_sml TIGR02378
nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of ...
 27-134 4.73e-05

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: 42.30  E-value: 4.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019   27 WHPIGAESEFDEISVRPARLFGEDLVLYKDLSGNYGLVDRQCPHRRAD-LAYGFVEKCGLR----CNYHGWLYD-EKGQC 100
Cdd:TIGR02378   2 WQDICAIDDIPEETGVCVLLGDTQIAIFRVPGDQVFAIQNMCPHKRAFvLSRGIVGDAQGElwvaCPLHKRNFRlEDGRC 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 743678019  101 TEQpyedianpqvrlkDRIKIKSYPVQVKAGMIW 134
Cdd:TIGR02378  82 LED-------------DSGSVRTYEVRVEDGRVY 102
 
Name Accession Description Interval E-value
Rieske_RO_Alpha_PhDO_like cd03479
Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, ...
 7-149 3.97e-63

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: 200.55  E-value: 3.97e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019   7 NQLLTQVGPGTPMGDLLRRYWHPIGAESEFDEI-SVRPARLFGEDLVLYKDLSGNYGLVDRQCPHRRADLAYGFVEKCGL 85
Cdd:cd03479    2 NELLTRVGPGTPMGELLRRYWQPVALSSELTEDgQPVRVRLLGEDLVAFRDTSGRVGLLDEHCPHRGASLVFGRVEECGL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743678019  86 RCNYHGWLYDEKGQCTEQPYEdiaNPQVRLKDRIKIKSYPVQVKAGMIWAYMGPL-PAPLVPTWE 149
Cdd:cd03479   82 RCCYHGWKFDVDGQCLEMPSE---PPDSQLKQKVRQPAYPVRERGGLVWAYMGPAeEAPEFPRYD 143
PobA COG5749
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
11-339 6.98e-55

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


Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 185.97  E-value: 6.98e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  11 TQVGPGTPMGDLLRRYWHPIGAESEFDEISVRPARLFGEDLVLYKDLSGNYGLVDRQCPHRRADLAYGFVEKCGLRCNYH 90
Cdd:COG5749    4 TRQGPGFNQPFIFRNHWYPVAPSEDLKPNKPKPVTLLGEPLVIWRDSDGKVVALEDRCPHRGAPLSEGRVEGGNLRCPYH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  91 GWLYDEKGQCTEQPYEDianPQVRLKDRIKIKSYPVQVKAGMIWAYMGPLPA------PLVPTWEPFTWangFRQVVISE 164
Cdd:COG5749   84 GWQFDGDGKCVHIPQLP---ENQPIPKNAKVKSYPVQERYGLIWVWLGDPPQadetpiPDIPELDDPEW---VATSSVRD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019 165 VPCNWFQCQENSIDPVHFEWMHSNWSvrlrgdTGPYAPTHTKLGFEEFEYGLIYKRVREDTDEKHPLWAvGRLALW---- 240
Cdd:COG5749  158 LECHYSRLIENLIDPSHVPFVHHGTQ------GNRKQAQPLEMEIESTPNGITASYTAQSYYQLFFPFL-GNLDETltit 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019 241 ---PNV------FCLGDHFE---WRVPIDDENTLSITWAFNRVPrerepyvqeKIPAWYGPVKdeatgQWISSHVMNQD- 307
Cdd:COG5749  231 fiyPNTvsvdigSGLGGRFGivlYATPIDEGKTRAYAIFFRNFA---------KKPRWLRHFL-----KLLRNGILEQDv 296

                        330       340       350
                 ....*....|....*....|....*....|...
gi 743678019 308 -FVAWVGQGRIADRTRENLGASDRGIAMLRRHF 339
Cdd:COG5749  297 iILESQQPALLQLGSYELPTPADRAIIEFRRWL 329
RHO_alpha_C_DMO-like cd08878
C-terminal catalytic domain of the oxygenase alpha subunit of dicamba O-demethylase and ...
 153-343 1.92e-41

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: 145.65  E-value: 1.92e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019 153 WANGFRqvvisEVPCNWFQCQENSIDPVHFEWMHSNWSVRLRGDTgpyaPTHTKLGFEEFEYGLIYKRVREDTD------ 226
Cdd:cd08878    1 WGGGYR-----HIDCNWLQVVENLMDPSHVSFVHRSSIGRDAADL----PSGPPKEVEEVPRGVTYRRWREDEDpppfgf 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019 227 EKHPLWAVGRLALWPNVFCLG---------------DHFEWRVPIdDENTLSITWAFNRVPREREPyvqekipaWYGPVK 291
Cdd:cd08878   72 EGPVDRWRVIEFLLPNVLLIDpgvapagtreqgvrmRVTHWITPI-DETTTHYFWFFVRNFAPDEE--------KKDDEE 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 743678019 292 DEATGQWISSHVMNQDFVAWVGQGRIADR--TRENLGASDRGIAMLRRHFFDEL 343
Cdd:cd08878  143 LTETLRSGLSGAFNEDKEAVEAQQRIIDRdpTREHLGLSDKGIVRFRRLLRRLL 196
HcaE COG4638
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ...
 22-338 4.41e-34

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: 128.95  E-value: 4.41e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  22 LLRRYWHPIGAESEFDEI-SVRPARLFGEDLVLYKDLSGNYGLVDRQCPHRRADLAYGFVEKCGLRCNYHGWLYDEKGQC 100
Cdd:COG4638   22 IFRRGWYYVGHSSELPEPgDYLTRTILGEPVVLVRDKDGEVRAFHNVCPHRGAPLSEGRGNGGRLVCPYHGWTYDLDGRL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019 101 TEQPYEDiANPQVRlKDRIKIKSYPVQVKAGMIWAYMGPLPAPLVPTWEPFTWANG--------FRQVVISEVPCNWFQC 172
Cdd:COG4638  102 VGIPHME-GFPDFD-PARAGLRSVPVEEWGGLIFVWLGPDAPPLAEYLGPLAEYLDpydfgelkVAGRETYEVNANWKLV 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019 173 QENSIDPVHFEWMHSNWSvrlrgdtgpyapthtklgfeefeygliykrvredtdekhplwavgrLALWPNVFCL--GDHF 250
Cdd:COG4638  180 VENFLDGYHVPFVHPGII----------------------------------------------LFLFPNLMILdyPDHL 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019 251 EWR--VPIDDENTLSITWAFNRvpreREPYVQEKIPAWygpvkdeatgQWISSHVMNQDFVAWVGQ-----GRIADRTRE 323
Cdd:COG4638  214 VVRtvTPVSPDRTRVFVTFYVP----KDALDPEARADL----------EAFWGRVFEEDREIVERQqrglrSLAYPGPYL 279

                        330
                 ....*....|....*
gi 743678019 324 NLGASDRGIAMLRRH 338
Cdd:COG4638  280 SRSPAEGGVRHFRRW 294
Rieske_RO_Alpha_N cd03469
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ...
 27-144 7.26e-26

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: 101.13  E-value: 7.26e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  27 WHPIGAESEFDEI-SVRPARLFGEDLVLYKDLSGNYGLVDRQCPHRRADLAYGFVEKCG-LRCNYHGWLYDEKGQCTEQP 104
Cdd:cd03469    1 WYFVGHSSELPEPgDYVTLELGGEPLVLVRDRDGEVRAFHNVCPHRGARLCEGRGGNAGrLVCPYHGWTYDLDGKLVGVP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 743678019 105 YEDIANPQVrlKDRIKIKSYPVQVKAGMIWAYMGPLPAPL 144
Cdd:cd03469   81 REEGFPGFD--KEKLGLRTVPVEEWGGLIFVNLDPDAPPL 118
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 27-125 2.01e-19

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: 82.40  E-value: 2.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019   27 WHPIGAESEFDEISVRPARLFGEDLVLYKDLSGNYGLVDRQCPHRRADLAYGFVEKCG-LRCNYHGWLYDEKGQCteqpy 105
Cdd:pfam00355   2 WYPVCHSSELPEGEPKVVEVGGEPLVVFRDEDGELYALEDRCPHRGAPLSEGKVNGGGrLECPYHGWRFDGTGKV----- 76

                          90       100
                  ....*....|....*....|
gi 743678019  106 edIANPQVRlkdriKIKSYP 125
Cdd:pfam00355  77 --VKVPAPR-----PLKSYP 89
Rieske_RO_Alpha_VanA_DdmC cd03532
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and ...
 37-138 6.07e-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: 82.03  E-value: 6.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  37 DEISVRPA--RLFGEDLVLYKDLSGNYGLVDRQCPHRRADLAYGFVEKCGLRCNYHGWLYDEKGQCTEQPYEDIANPQVR 114
Cdd:cd03532   13 DELGDKPLarTLLGEPVVLYRTQDGRVAALEDRCPHRSAPLSKGSVEGGGLVCGYHGLEFDSDGRCVHMPGQERVPAKAC 92

                         90       100
                 ....*....|....*....|....
gi 743678019 115 lkdrikIKSYPVQVKAGMIWAYMG 138
Cdd:cd03532   93 ------VRSYPVVERDALIWIWMG 110
PLN02281 PLN02281
chlorophyllide a oxygenase
 14-191 4.69e-18

chlorophyllide a oxygenase


Pssm-ID: 177920 [Multi-domain]  Cd Length: 536  Bit Score: 86.32  E-value: 4.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  14 GPGTPMGDLLRRYWHPIGAESEFDEISVRPARLFGEDLVLYKDLSGNYGLVDRQCPHRRADLAYGFVEKCGLRCNYHGWL 93
Cdd:PLN02281 208 GPVPPYSPHLKNFWYPVAFTADLKHDTMVPIECFEQPWVIFRGEDGKPGCVRNTCAHRACPLDLGTVNEGRIQCPYHGWE 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  94 YDEKGQCTEQPYEDIAnpqvrlkdRIKIKSYPVQVKAGMIWAYMG-PLPAPLVPTWEPftwANGF--RQVVISEVPCNWF 170
Cdd:PLN02281 288 YSTDGECKKMPSTKLL--------KVKIKSLPCLEQEGMIWIWPGdEPPAPILPSLQP---PSGFliHAELVMDLPVEHG 356

                        170       180
                 ....*....|....*....|....*.
gi 743678019 171 QCQENSIDPVHFEWMHSN-----WSV 191
Cdd:PLN02281 357 LLLDNLLDLAHAPFTHTStfakgWSV 382
Rieske_RO_Alpha_Cao cd04337
Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the ...
 13-146 2.19e-17

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: 78.30  E-value: 2.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  13 VGPGTPMGDLLRRYWHPIGAESEFDEISVRPARLFGEDLVLYKDLSGNYGLVDRQCPHRRADLAYGFVEKCGLRCNYHGW 92
Cdd:cd04337    4 LGSSLELEPGLRNFWYPVEFSKDLKMDTMVPFELFGQPWVLFRDEDGTPGCIRDECAHRACPLSLGKVIEGRIQCPYHGW 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 743678019  93 LYDEKGQCTEQPYEDIANpqvrlkdrIKIKSYPVQVKAGMIWAYMGPLPAPLVP 146
Cdd:cd04337   84 EYDGDGECTKMPSTKCLN--------VGIAALPCMEQDGMIWVWPGDDPPAALP 129
Rieske_RO_Alpha_PaO cd03480
Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, ...
 24-138 7.26e-17

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: 76.98  E-value: 7.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  24 RRYWHPIGAESEFDEISVRPARLFGEDLVLYKDLSGN-YGLVDRQCPHRRADLAYGFVEKCG-LRCNYHGWLYDEKGQCT 101
Cdd:cd03480   15 REVWYPVAYVEDLDPSRPTPFTLLGRDLVIWWDRNSQqWRAFDDQCPHRLAPLSEGRIDEEGcLECPYHGWSFDGSGSCQ 94

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 743678019 102 EQPyEDIANPQVRLKDRIKIKSYPVQVKAGMIWAYMG 138
Cdd:cd03480   95 RIP-QAAEGGKAHTSPRACVASLPTAVRQGLLFVWPG 130
Rieske_RO_Alpha_Tic55 cd04338
Tic55 is a 55kDa LLS1-related non-heme iron oxygenase associated with protein transport ...
 24-143 7.37e-15

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: 71.02  E-value: 7.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  24 RRYWHPIGAESEFDEISVRPARLFGEDLVLYKDLSGNYGLVDRQCPHRRADLAYGFVEKCGLRCNYHGWLYDEKGQCTEQ 103
Cdd:cd04338   15 REEWYPLYLLKDVPTDAPLGLSVYDEPFVLFRDQNGQLRCLEDRCPHRLAKLSEGQLIDGKLECLYHGWQFGGEGKCVKI 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 743678019 104 PyedianpqvRLKDRIKI------KSYPVQVKAGMIWAYMGPLPAP 143
Cdd:cd04338   95 P---------QLPADAKIpknacvKSYEVRDSQGVVWMWMSEATPP 131
LigXa_C pfam19301
LigXa C-terminal domain like; This entry represents the C-terminal domain of a Rieske ...
 135-356 1.48e-14

LigXa C-terminal domain like; This entry represents the C-terminal domain of a Rieske oxygenase enzyme. This entry includes the 5,5'-dehydrodivanillate O-demethylase three-component monooxygenase which is composed of an oxygenase (LigXa) in this entry, a ferredoxin (LigXc) and a ferredoxin reductase (LigXd).


Pssm-ID: 437133  Cd Length: 303  Bit Score: 74.00  E-value: 1.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  135 AYMGPlpAPLVPTWEPFTWA-NGFRQVVISEV--PCNWFQCQENSIDPVHFEWMHS----------------NWsVRLRG 195
Cdd:pfam19301   1 VYMGP--QDTVPEFEPPAWApTPDAKVSIAKIllPCNWAQILEGAIDSAHSSSLHSsdmvparvggaeatdkAW-LRPST 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  196 DTGPyapthtKLGFEEFEYGLIYKRVRE-----DTDE--KHPLWAVGRLALWP-----NVFCLgdhfewRVPIDDENTLS 263
Cdd:pfam19301  78 DKAP------RLQVQRTSYGFRYAAIRRpitnaATHDyvRSTVFVAPATVLIPpnnlyNVANV------NVPMDDTNTAF 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  264 --ITWAFNRVPREREPY-------VQEKIPAWYGPVKDEATGQWISSHVM------------NQDFVAWVGQGRIADRTR 322
Cdd:pfam19301 146 yfIAWGHPAKTPETETWrkflgaqVGVDLDPRYRPLRNRENNFWQDRQAMkagnftgipgfpNQDIAMWETMGPIADRSH 225

                         250       260       270
                  ....*....|....*....|....*....|....
gi 743678019  323 ENLGASDRGIAMLRRHFFDELDAVAQGRDPKGLV 356
Cdd:pfam19301 226 ERLGASDLAIVEFRRQMLEAAQAFAAGEPAIGTG 259
PLN02518 PLN02518
pheophorbide a oxygenase
 24-136 2.42e-14

pheophorbide a oxygenase


Pssm-ID: 215283 [Multi-domain]  Cd Length: 539  Bit Score: 74.90  E-value: 2.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  24 RRYWHPIGAESEFDEISVRPARLFGEDLVLYKDL-SGNYGLVDRQCPHRRADLAYGFVEKCG-LRCNYHGWLYDEKGQCT 101
Cdd:PLN02518  88 RDHWYPVSLVEDLDPSVPTPFQLLGRDLVLWKDPnQGEWVAFDDKCPHRLAPLSEGRIDENGhLQCSYHGWSFDGCGSCT 167

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 743678019 102 EQPYEDIANPQVRLK--DRIKIKSYPVQVKAGMIWAY 136
Cdd:PLN02518 168 RIPQAAPEGPEARAVksPRACAIKFPTMVSQGLLFVW 204
Rieske_RO_Alpha_PrnD cd03537
This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit of ...
 37-146 2.83e-13

This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit of aminopyrrolnitrin oxygenase (PrnD). PrnD is a novel Rieske N-oxygenase that catalyzes the final step in the pyrrolnitrin biosynthetic pathway, the oxidation of the amino group in aminopyrrolnitrin to a nitro group, forming the antibiotic pyrrolnitrin. The biosynthesis of pyrrolnitrin is one of the best examples of enzyme-catalyzed arylamine oxidation. Although arylamine oxygenases are widely distributed within the microbial world and used in a variety of metabolic reactions, PrnD represents one of only two known examples of arylamine oxygenases or N-oxygenases involved in arylnitro group formation, the other being AurF involved in aureothin biosynthesis.


Pssm-ID: 239611 [Multi-domain]  Cd Length: 123  Bit Score: 66.11  E-value: 2.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  37 DEISVRPA--RLFGEDLVLYKDLSGNYGLVDRQCPHRRADLAYGFVEKCGLRCNYHGWLYDEKGQCTEQPYEDIANPQVR 114
Cdd:cd03537   11 DDLKDKPTelTLFGRPCVAWRGATGRAVVMDRHCSHLGANLADGRVKDGCIQCPFHHWRYDEQGQCVHIPGHSTAVRRLE 90

                         90       100       110
                 ....*....|....*....|....*....|...
gi 743678019 115 LKDR-IKIKSYPVQVKAGMIWAYMGPlPAPLVP 146
Cdd:cd03537   91 PVPRgARQPTLVTAERYGYVWVWYGS-PQPLHP 122
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 27-134 1.72e-12

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: 63.32  E-value: 1.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  27 WHPIGAESEFDEISVRPARLFGEDLVLYKdLSGNYGLVDRQCPHRRADLAYGFVEKCGLRCNYHGWLYD-EKGQCTEQPy 105
Cdd:COG2146    3 EVKVCALDDLPEGGGVVVEVGGKQIAVFR-TDGEVYAYDNRCPHQGAPLSEGIVDGGVVTCPLHGARFDlRTGECLGGP- 80

                         90       100
                 ....*....|....*....|....*....
gi 743678019 106 edianpqvrlkDRIKIKSYPVQVKAGMIW 134
Cdd:COG2146   81 -----------ATEPLKTYPVRVEDGDVY 98
Rieske_RO_Alpha_OMO_CARDO cd03548
Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole ...
 23-138 1.90e-11

Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole 1,9a-dioxygenase (CARDO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. OMO catalyzes the NADH-dependent oxidation of the N-heterocyclic aromatic compound 2-oxoquinoline to 8-hydroxy-2-oxoquinoline, the second step in the bacterial degradation of quinoline. OMO consists of a reductase component (OMR) and an oxygenase component (OMO) that together function to shuttle electrons from the reduced pyridine nucleotide to the active site of OMO, where O2 activation and 2-oxoquinoline hydroxylation occurs. CARDO, which contains oxygenase (CARDO-O), ferredoxin (CARDO-F) and ferredoxin reductase (CARDO-R) components, catalyzes the dihydroxylation at the C1 and C9a positions of carbazole. The oxygenase component of OMO and CARDO contain only alpha subunits arranged in a trimeric structure.


Pssm-ID: 239617 [Multi-domain]  Cd Length: 136  Bit Score: 61.28  E-value: 1.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  23 LRRYWHPIGAESEFDEISVRPARLFGEDLVLYKDLSGNYGLVDRqCPHRRADLA---YGFVEKCgLRCNYHGWLYD-EKG 98
Cdd:cd03548   11 FRNHWYPALFSHELEEGEPKGIQLCGEPILLRRVDGKVYALKDR-CLHRGVPLSkkpECFTKGT-ITCWYHGWTYRlDDG 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 743678019  99 QCTEQpyedIANPQVRLKDRIKIKSYPVQVKAGMIWAYMG 138
Cdd:cd03548   89 KLVTI----LANPDDPLIGRTGLKTYPVEEAKGMIFVFVG 124
Rieske_RO_Alpha_KSH cd03531
The alignment model represents the N-terminal rieske iron-sulfur domain of KshA, the oxygenase ...
 27-139 4.52e-11

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: 59.73  E-value: 4.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  27 WHPIGAESEFDEISVRPARLFGEDLVLYKDLSGNYGLVDRQCPHRRADLAYGFVEKCGLRCNYHGWLYDEKGQCTEQPYE 106
Cdd:cd03531    2 WHCLGLARDFRDGKPHGVEAFGTKLVVFADSDGALNVLDAYCRHMGGDLSQGTVKGDEIACPFHDWRWGGDGRCKAIPYA 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 743678019 107 DianpqvRLKDRIKIKSYPVQVKAGMIWAYMGP 139
Cdd:cd03531   82 R------RVPPLARTRAWPTLERNGQLFVWHDP 108
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 27-104 1.77e-10

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: 57.50  E-value: 1.77e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743678019  27 WHPIGAESEFDEISVRPARLFGEDLVLYKDLSGNYGLVDRQCPHRRADLAYGFVEKCGLRCNYHGWLYDEK-GQCTEQP 104
Cdd:cd03467    1 WVVVGALSELPPGGGRVVVVGGGPVVVVRREGGEVYALSNRCTHQGCPLSEGEGEDGCIVCPCHGSRFDLRtGEVVSGP 79
PLN00095 PLN00095
chlorophyllide a oxygenase; Provisional
 24-150 3.27e-10

chlorophyllide a oxygenase; Provisional


Pssm-ID: 165668 [Multi-domain]  Cd Length: 394  Bit Score: 61.62  E-value: 3.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  24 RRYWHPIG-AESEFDEISVRPARLFGEDLVLYKDLSGNYGLVDRQCPHRRADLAYGFVEKCGLRCNYHGWLYDEKGQCTE 102
Cdd:PLN00095  70 RAHWFPVAfAAGLRDEDALIAFDLFNVPWVLFRDADGEAGCIKDECAHRACPLSLGKLVDGKAQCPYHGWEYETGGECAK 149

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 743678019 103 QPYEDIANPQVRlkdrikIKSYPVQVKAGMIWAYMGplpaplvpTWEP 150
Cdd:PLN00095 150 MPSCKKFLKGVF------ADAAPVIERDGFIFLWAG--------ESDP 183
Rieske_RO_ferredoxin cd03528
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ...
 27-134 4.15e-05

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: 42.09  E-value: 4.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  27 WHPIGAESEFDEISVRPARLFGEDLVLYKDlSGNYGLVDRQCPHRRADLAYGFVEKCGLRCNYHGWLYDEK-GQCTEQP- 104
Cdd:cd03528    1 WVRVCAVDELPEGEPKRVDVGGRPIAVYRV-DGEFYATDDLCTHGDASLSEGYVEGGVIECPLHGGRFDLRtGKALSLPa 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 743678019 105 YEDianpqvrlkdrikIKSYPVQVKAGMIW 134
Cdd:cd03528   80 TEP-------------LKTYPVKVEDGDVY 96
nirD_assim_sml TIGR02378
nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of ...
 27-134 4.73e-05

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: 42.30  E-value: 4.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019   27 WHPIGAESEFDEISVRPARLFGEDLVLYKDLSGNYGLVDRQCPHRRAD-LAYGFVEKCGLR----CNYHGWLYD-EKGQC 100
Cdd:TIGR02378   2 WQDICAIDDIPEETGVCVLLGDTQIAIFRVPGDQVFAIQNMCPHKRAFvLSRGIVGDAQGElwvaCPLHKRNFRlEDGRC 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 743678019  101 TEQpyedianpqvrlkDRIKIKSYPVQVKAGMIW 134
Cdd:TIGR02378  82 LED-------------DSGSVRTYEVRVEDGRVY 102
Rieske_RO_Alpha_BPDO_like cd03472
Rieske non-heme iron oxygenase (RO) family, Biphenyl dioxygenase (BPDO)-like subfamily, ...
 25-135 2.24e-03

Rieske non-heme iron oxygenase (RO) family, Biphenyl dioxygenase (BPDO)-like subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of BPDO and similar proteins including cumene dioxygenase (CumDO), nitrobenzene dioxygenase (NBDO), alkylbenzene dioxygenase (AkbDO) and dibenzofuran 4,4a-dioxygenase (DFDO). ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. BPDO degrades biphenyls and polychlorinated biphenyls (PCB's) while CumDO degrades cumene (isopropylbenzene), an aromatic hydrocarbon that is intermediate in size between ethylbenzene and biphenyl. NBDO catalyzes the initial reaction in nitrobenzene degradation, oxidizing the aromatic rings of mono- and dinitrotoluenes to form catechol and nitrite. NBDO belongs to the naphthalene subfamily of ROs. AkbDO is involved in alkylbenzene catabolism, converting o-xylene to 2,3- and 3,4-dimethylphenol and ethylbenzene to cis-dihydrodiol. DFDO is involved in dibenzofuran degradation.


Pssm-ID: 239554 [Multi-domain]  Cd Length: 128  Bit Score: 37.90  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743678019  25 RYWHPIGAESEFDEISVRPARLFGED-LVLYKDLSGNYGLVDRQCPHR-----RADL--AYGFVekcglrCNYHGWLYDE 96
Cdd:cd03472    7 RSWLLLGHETHIPKAGDYLTTYMGEDpVIVVRQKDGSIRVFLNQCRHRgmricRSDAgnAKAFT------CTYHGWAYDT 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 743678019  97 KGQCTEQPYEDIANPQVRLKDRIKIKSYPVQVKAGMIWA 135
Cdd:cd03472   81 AGNLVNVPFEKEAFCDGLDKADWGPLQARVETYKGLIFA 119
 
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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