NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|504909752|ref|WP_015096854|]
View 

MULTISPECIES: Rieske (2Fe-2S) protein [Pseudomonas]

Protein Classification

Rieske (2Fe-2S) protein( domain architecture ID 10005408)

Rieske (2Fe-2S) protein 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

CATH:  2.102.10.10
Gene Ontology:  GO:0051537|GO:0046872

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 4-105 2.57e-22

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: 83.35  E-value: 2.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504909752   4 LCAGAELVNDSSRGFDIDGQKLFAVRRSGQVHVYINRCPHRGVALEwhpDQFLDpsNSLIQCATHGALFLIEDGECVAGP 83
Cdd:COG2146    6 VCALDDLPEGGGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLS---EGIVD--GGVVTCPLHGARFDLRTGECLGGP 80

                         90       100
                 ....*....|....*....|..
gi 504909752  84 CAGqALTRVACREDEQGIWISL 105
Cdd:COG2146   81 ATE-PLKTYPVRVEDGDVYVDL 101
 
Name Accession Description Interval E-value
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 4-105 2.57e-22

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: 83.35  E-value: 2.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504909752   4 LCAGAELVNDSSRGFDIDGQKLFAVRRSGQVHVYINRCPHRGVALEwhpDQFLDpsNSLIQCATHGALFLIEDGECVAGP 83
Cdd:COG2146    6 VCALDDLPEGGGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLS---EGIVD--GGVVTCPLHGARFDLRTGECLGGP 80

                         90       100
                 ....*....|....*....|..
gi 504909752  84 CAGqALTRVACREDEQGIWISL 105
Cdd:COG2146   81 ATE-PLKTYPVRVEDGDVYVDL 101
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 4-102 8.90e-15

Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron oxygenase (RO) systems such as naphthalene and biphenyl dioxygenases, as well as in plant/cyanobacterial chloroplast b6f and mitochondrial cytochrome bc(1) complexes. The Rieske domain can be divided into two subdomains, with an incomplete six-stranded, antiparallel beta-barrel at one end, and an iron-sulfur cluster binding subdomain at the other. The Rieske iron-sulfur center contains a [2Fe-2S] cluster, which is involved in electron transfer, and is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In RO systems, the N-terminal Rieske domain of the alpha subunit acts as an electron shuttle that accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron in the alpha subunit C-terminal domain to be used for catalysis.


Pssm-ID: 239550 [Multi-domain]  Cd Length: 98  Bit Score: 64.05  E-value: 8.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504909752   4 LCAGAELVNDSSRGFDIDGQKLFAVRRS-GQVHVYINRCPHRGVALEWHPDQfldpsNSLIQCATHGALFLIEDGECVAG 82
Cdd:cd03467    4 VGALSELPPGGGRVVVVGGGPVVVVRREgGEVYALSNRCTHQGCPLSEGEGE-----DGCIVCPCHGSRFDLRTGEVVSG 78

                         90       100
                 ....*....|....*....|
gi 504909752  83 PCAGQALTRVACREDEQGIW 102
Cdd:cd03467   79 PAPRPLPKYPVKVEGDGVVW 98
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 3-87 1.29e-08

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: 48.11  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504909752    3 LLCAGAELVNDSSRGFDIDGQKLFAVR-RSGQVHVYINRCPHRGVALewhpDQFLDPSNSLIQCATHGALFlIEDGECVA 81
Cdd:pfam00355   4 PVCHSSELPEGEPKVVEVGGEPLVVFRdEDGELYALEDRCPHRGAPL----SEGKVNGGGRLECPYHGWRF-DGTGKVVK 78


                  ....*.
gi 504909752   82 GPCAGQ 87
Cdd:pfam00355  79 VPAPRP 84
 
Name Accession Description Interval E-value
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 4-105 2.57e-22

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: 83.35  E-value: 2.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504909752   4 LCAGAELVNDSSRGFDIDGQKLFAVRRSGQVHVYINRCPHRGVALEwhpDQFLDpsNSLIQCATHGALFLIEDGECVAGP 83
Cdd:COG2146    6 VCALDDLPEGGGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLS---EGIVD--GGVVTCPLHGARFDLRTGECLGGP 80

                         90       100
                 ....*....|....*....|..
gi 504909752  84 CAGqALTRVACREDEQGIWISL 105
Cdd:COG2146   81 ATE-PLKTYPVRVEDGDVYVDL 101
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 4-102 8.90e-15

Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron oxygenase (RO) systems such as naphthalene and biphenyl dioxygenases, as well as in plant/cyanobacterial chloroplast b6f and mitochondrial cytochrome bc(1) complexes. The Rieske domain can be divided into two subdomains, with an incomplete six-stranded, antiparallel beta-barrel at one end, and an iron-sulfur cluster binding subdomain at the other. The Rieske iron-sulfur center contains a [2Fe-2S] cluster, which is involved in electron transfer, and is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In RO systems, the N-terminal Rieske domain of the alpha subunit acts as an electron shuttle that accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron in the alpha subunit C-terminal domain to be used for catalysis.


Pssm-ID: 239550 [Multi-domain]  Cd Length: 98  Bit Score: 64.05  E-value: 8.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504909752   4 LCAGAELVNDSSRGFDIDGQKLFAVRRS-GQVHVYINRCPHRGVALEWHPDQfldpsNSLIQCATHGALFLIEDGECVAG 82
Cdd:cd03467    4 VGALSELPPGGGRVVVVGGGPVVVVRREgGEVYALSNRCTHQGCPLSEGEGE-----DGCIVCPCHGSRFDLRTGEVVSG 78

                         90       100
                 ....*....|....*....|
gi 504909752  83 PCAGQALTRVACREDEQGIW 102
Cdd:cd03467   79 PAPRPLPKYPVKVEGDGVVW 98
Rieske_RO_Alpha_N cd03469
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ...
 16-105 6.03e-10

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: 52.21  E-value: 6.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504909752  16 RGFDIDGQKLFAVR-RSGQVHVYINRCPHRGVALEWHPDQfldpSNSLIQCATHGALF-LieDGECVAGPCAGQA----- 88
Cdd:cd03469   17 VTLELGGEPLVLVRdRDGEVRAFHNVCPHRGARLCEGRGG----NAGRLVCPYHGWTYdL--DGKLVGVPREEGFpgfdk 90

                         90       100
                 ....*....|....*....|.
gi 504909752  89 ----LTRVACREDEQGIWISL 105
Cdd:cd03469   91 eklgLRTVPVEEWGGLIFVNL 111
Rieske_AIFL_N cd03478
AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family ...
 4-84 1.81e-09

AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family show similarity to human AIFL, containing an N-terminal Rieske domain and a C-terminal pyridine nucleotide-disulfide oxidoreductase domain (Pyr_redox). The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. AIFL shares 35% homology with human AIF (apoptosis-inducing factor), mainly in the Pyr_redox domain. AIFL is predominantly localized to the mitochondria. AIFL induces apoptosis in a caspase-dependent manner.


Pssm-ID: 239560 [Multi-domain]  Cd Length: 95  Bit Score: 50.31  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504909752   4 LCAGAELVNDSSRGFDIDGQKLFAVRRSGQVHVYINRCPHRGVALEwhpDQFLdpSNSLIQCATHGALFLIEDGECVAGP 83
Cdd:cd03478    3 VCRLSDLGDGEMKEVDVGDGKVLLVRQGGEVHAIGAKCPHYGAPLA---KGVL--TDGRIRCPWHGACFNLRTGDIEDAP 77


                 .
gi 504909752  84 C 84
Cdd:cd03478   78 A 78
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 3-87 1.29e-08

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: 48.11  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504909752    3 LLCAGAELVNDSSRGFDIDGQKLFAVR-RSGQVHVYINRCPHRGVALewhpDQFLDPSNSLIQCATHGALFlIEDGECVA 81
Cdd:pfam00355   4 PVCHSSELPEGEPKVVEVGGEPLVVFRdEDGELYALEDRCPHRGAPL----SEGKVNGGGRLECPYHGWRF-DGTGKVVK 78


                  ....*.
gi 504909752   82 GPCAGQ 87
Cdd:pfam00355  79 VPAPRP 84
HcaE COG4638
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ...
 16-105 2.75e-08

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: 49.60  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504909752  16 RGFDIDGQKLFAVR-RSGQVHVYINRCPHRGVALEWHPDqfldpSNSLIQCATHG---ALflieDGECVAGPCAGQA--- 88
Cdd:COG4638   43 LTRTILGEPVVLVRdKDGEVRAFHNVCPHRGAPLSEGRG-----NGGRLVCPYHGwtyDL----DGRLVGIPHMEGFpdf 113

                         90       100
                 ....*....|....*....|....
gi 504909752  89 ------LTRVACREdEQG-IWISL 105
Cdd:COG4638  114 dparagLRSVPVEE-WGGlIFVWL 136
Rieske_RO_Alpha_OMO_CARDO cd03548
Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole ...
 8-80 2.03e-07

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: 45.88  E-value: 2.03e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504909752   8 AELVNDSSRGFDIDGQKLFAVRRSGQVHVYINRCPHRGVALEWHPDQFldpSNSLIQCATHGALFLIEDGECV 80
Cdd:cd03548   22 HELEEGEPKGIQLCGEPILLRRVDGKVYALKDRCLHRGVPLSKKPECF---TKGTITCWYHGWTYRLDDGKLV 91
Rieske_RO_ferredoxin cd03528
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ...
 4-84 4.40e-07

Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the Rieske ferredoxin component of some three-component RO systems including biphenyl dioxygenase (BPDO) and carbazole 1,9a-dioxygenase (CARDO). The RO family comprise a large class of aromatic ring-hydroxylating dioxygenases found predominantly in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth. ROs consist of two or three components: reductase, oxygenase, and ferredoxin (in some cases) components. The ferredoxin component contains either a plant-type or Rieske-type [2Fe-2S] cluster. The Rieske ferredoxin component in this family carries an electron from the RO reductase component to the terminal RO oxygenase component. BPDO degrades biphenyls and polychlorinated biphenyls. BPDO ferredoxin (BphF) has structural features consistent with a minimal and perhaps archetypical Rieske protein in that the insertions that give other Rieske proteins unique structural features are missing. CARDO catalyzes dihydroxylation at the C1 and C9a positions of carbazole. Rieske ferredoxins are found as subunits of membrane oxidase complexes, cis-dihydrodiol-forming aromatic dioxygenases, bacterial assimilatory nitrite reductases, and arsenite oxidase. Rieske ferredoxins are also found as soluble electron carriers in bacterial dioxygenase and monooxygenase complexes.


Pssm-ID: 239604 [Multi-domain]  Cd Length: 98  Bit Score: 44.02  E-value: 4.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504909752   4 LCAGAELVNDSSRGFDIDGQKLFAVRRSGQVHVYINRCPHRGVALEwhpDQFLDpsNSLIQCATHGALFLIEDGECVAGP 83
Cdd:cd03528    4 VCAVDELPEGEPKRVDVGGRPIAVYRVDGEFYATDDLCTHGDASLS---EGYVE--GGVIECPLHGGRFDLRTGKALSLP 78


                 .
gi 504909752  84 C 84
Cdd:cd03528   79 A 79
Rieske_RO_Alpha_PhDO_like cd03479
Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, ...
 22-84 1.33e-05

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: 41.08  E-value: 1.33e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504909752  22 GQKLFAVR-RSGQVHVYINRCPHRGVALEwhpdqFLDPSNSLIQCATHGALFLIeDGECVAGPC 84
Cdd:cd03479   44 GEDLVAFRdTSGRVGLLDEHCPHRGASLV-----FGRVEECGLRCCYHGWKFDV-DGQCLEMPS 101
PobA COG5749
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
19-103 1.59e-05

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


Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 41.91  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504909752  19 DIDGQKLFAVRR-----------SGQVHVYINRCPHRGVALewhpdqfldpS-----NSLIQCATHGALFlIEDGECVAG 82
Cdd:COG5749   28 DLKPNKPKPVTLlgeplviwrdsDGKVVALEDRCPHRGAPL----------SegrveGGNLRCPYHGWQF-DGDGKCVHI 96

                         90       100       110
                 ....*....|....*....|....*....|
gi 504909752  83 PC--AGQALTRVAC------REdEQG-IWI 103
Cdd:COG5749   97 PQlpENQPIPKNAKvksypvQE-RYGlIWV 125
Rieske_RO_Alpha_AntDO cd03538
Rieske non-heme iron oxygenase (RO) family, Anthranilate 1,2-dioxygenase (AntDO) subfamily, ...
 20-53 2.69e-03

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: 35.13  E-value: 2.69e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 504909752  20 IDGQKLFAVRRS-GQVHVYINRCPHRGVALEWHPD 53
Cdd:cd03538   43 IGDQPVVMVRHTdGSVHVLYNRCPHKGTKIVSDGC 77
Rieske_RO_Alpha_VanA_DdmC cd03532
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and ...
 30-103 3.06e-03

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: 34.26  E-value: 3.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504909752  30 RSGQVHVYINRCPHRGVALEwhpDQFLdpSNSLIQCATHGALFlIEDGECVAGPcAGQALTRVAC------REDEQGIWI 103
Cdd:cd03532   35 QDGRVAALEDRCPHRSAPLS---KGSV--EGGGLVCGYHGLEF-DSDGRCVHMP-GQERVPAKACvrsypvVERDALIWI 107
Rieske_RO_Alpha_DTDO cd03536
This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit ...
 25-83 8.91e-03

This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit (DitA) of diterpenoid dioxygenase (DTDO). DTDO is a novel aromatic-ring-hydroxylating dioxygenase found in Pseudomonas and other proteobacteria that degrades dehydroabietic acid (DhA). Specifically, DitA hydroxylates 7-oxodehydroabietic acid to 7-oxo-11,12-dihydroxy-8, 13-abietadien acid. The ditA1 and ditA2 genes encode the alpha and beta subunits of the oxygenase component of DTDO while the ditA3 gene encodes the ferredoxin component of DTDO. The organization of the genes encoding the various diterpenoid dioxygenase components, the phylogenetic distinctiveness of both the alpha subunit and the ferredoxin component, and the unusual iron-sulfur cluster of the ferredoxin all suggest that this enzyme belongs to a new class of aromatic ring-hydroxylating dioxygenases.


Pssm-ID: 239610 [Multi-domain]  Cd Length: 123  Bit Score: 33.37  E-value: 8.91e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504909752  25 LFAVRRSGQVHVYINRCPHRGVALewhpdQFLDPSNSLIQ-CATHGALFLiEDGECVAGP 83
Cdd:cd03536   27 IVARDKDGEIHVSLNVCPHRGMRI-----STTDGGNTQIHvCIYHGWAFR-PNGDFIGAP 80
 
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