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Conserved domains on  [gi|1154708950|gb|KSR79914|]
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MFS transporter [Pseudomonas aeruginosa]

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

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List of domain hits

Name Accession Description Interval E-value
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
10-115 4.27e-25

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: 90.67  E-value: 4.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154708950  10 IHLCPSSHLAEGNSRGFLVDERRLFAVRRDGRAYIYLNRCPHRGIPLEwqpDAFLDDSAslIRCASHGALFLIESGECVA 89
Cdd:COG2146     4 VKVCALDDLPEGGGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLS---EGIVDGGV--VTCPLHGARFDLRTGECLG 78
                          90       100
                  ....*....|....*....|....*.
gi 1154708950  90 GPCAgERLRALPCREDAEGLWVELDD 115
Cdd:COG2146    79 GPAT-EPLKTYPVRVEDGDVYVDLPE 103
 
Name Accession Description Interval E-value
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
10-115 4.27e-25

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: 90.67  E-value: 4.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154708950  10 IHLCPSSHLAEGNSRGFLVDERRLFAVRRDGRAYIYLNRCPHRGIPLEwqpDAFLDDSAslIRCASHGALFLIESGECVA 89
Cdd:COG2146     4 VKVCALDDLPEGGGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLS---EGIVDGGV--VTCPLHGARFDLRTGECLG 78
                          90       100
                  ....*....|....*....|....*.
gi 1154708950  90 GPCAgERLRALPCREDAEGLWVELDD 115
Cdd:COG2146    79 GPAT-EPLKTYPVRVEDGDVYVDLPE 103
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
12-108 9.54e-18

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: 72.14  E-value: 9.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154708950  12 LCPSSHLAEGNSRGFLVDERRLFAVRR-DGRAYIYLNRCPHRGIPLEWQpdaflDDSASLIRCASHGALFLIESGECVAG 90
Cdd:cd03467     4 VGALSELPPGGGRVVVVGGGPVVVVRReGGEVYALSNRCTHQGCPLSEG-----EGEDGCIVCPCHGSRFDLRTGEVVSG 78
                          90
                  ....*....|....*...
gi 1154708950  91 PCAGeRLRALPCREDAEG 108
Cdd:cd03467    79 PAPR-PLPKYPVKVEGDG 95
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
12-95 1.70e-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: 1.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154708950  12 LCPSSHLAEGNSRGFLVDERRLFAVR-RDGRAYIYLNRCPHRGIPLEwqpDAFLDDSASlIRCASHGALFlIESGECVAG 90
Cdd:pfam00355   5 VCHSSELPEGEPKVVEVGGEPLVVFRdEDGELYALEDRCPHRGAPLS---EGKVNGGGR-LECPYHGWRF-DGTGKVVKV 79

                  ....*
gi 1154708950  91 PCAGE 95
Cdd:pfam00355  80 PAPRP 84
 
Name Accession Description Interval E-value
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
10-115 4.27e-25

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: 90.67  E-value: 4.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154708950  10 IHLCPSSHLAEGNSRGFLVDERRLFAVRRDGRAYIYLNRCPHRGIPLEwqpDAFLDDSAslIRCASHGALFLIESGECVA 89
Cdd:COG2146     4 VKVCALDDLPEGGGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLS---EGIVDGGV--VTCPLHGARFDLRTGECLG 78
                          90       100
                  ....*....|....*....|....*.
gi 1154708950  90 GPCAgERLRALPCREDAEGLWVELDD 115
Cdd:COG2146    79 GPAT-EPLKTYPVRVEDGDVYVDLPE 103
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
12-108 9.54e-18

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: 72.14  E-value: 9.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154708950  12 LCPSSHLAEGNSRGFLVDERRLFAVRR-DGRAYIYLNRCPHRGIPLEWQpdaflDDSASLIRCASHGALFLIESGECVAG 90
Cdd:cd03467     4 VGALSELPPGGGRVVVVGGGPVVVVRReGGEVYALSNRCTHQGCPLSEG-----EGEDGCIVCPCHGSRFDLRTGEVVSG 78
                          90
                  ....*....|....*...
gi 1154708950  91 PCAGeRLRALPCREDAEG 108
Cdd:cd03467    79 PAPR-PLPKYPVKVEGDG 95
Rieske_AIFL_N cd03478
AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family ...
12-102 2.58e-10

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


Pssm-ID: 239560 [Multi-domain]  Cd Length: 95  Bit Score: 52.62  E-value: 2.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154708950  12 LCPSSHLAEGNSRGFLVDERRLFAVRRDGRAYIYLNRCPHRGIPLEwqpDAFLDDsaSLIRCASHGALFLIESGECVAGP 91
Cdd:cd03478     3 VCRLSDLGDGEMKEVDVGDGKVLLVRQGGEVHAIGAKCPHYGAPLA---KGVLTD--GRIRCPWHGACFNLRTGDIEDAP 77
                          90
                  ....*....|.
gi 1154708950  92 CagerLRALPC 102
Cdd:cd03478    78 A----LDSLPC 84
Rieske_RO_Alpha_N cd03469
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ...
12-115 9.24e-09

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: 49.12  E-value: 9.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154708950  12 LCPSSHLAE-GNSRGFLVDERRLFAVR-RDGRAYIYLNRCPHRGIPLEWQPdaflDDSASLIRCASHGALFLIEsGECVA 89
Cdd:cd03469     4 VGHSSELPEpGDYVTLELGGEPLVLVRdRDGEVRAFHNVCPHRGARLCEGR----GGNAGRLVCPYHGWTYDLD-GKLVG 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1154708950  90 GPCAGE---------RLRALPCREDAEGLWVELDD 115
Cdd:cd03469    79 VPREEGfpgfdkeklGLRTVPVEEWGGLIFVNLDP 113
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
12-95 1.70e-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: 1.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154708950  12 LCPSSHLAEGNSRGFLVDERRLFAVR-RDGRAYIYLNRCPHRGIPLEwqpDAFLDDSASlIRCASHGALFlIESGECVAG 90
Cdd:pfam00355   5 VCHSSELPEGEPKVVEVGGEPLVVFRdEDGELYALEDRCPHRGAPLS---EGKVNGGGR-LECPYHGWRF-DGTGKVVKV 79

                  ....*
gi 1154708950  91 PCAGE 95
Cdd:pfam00355  80 PAPRP 84
Rieske_RO_ferredoxin cd03528
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ...
9-114 3.67e-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: 44.79  E-value: 3.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154708950   9 MIHLCPSSHLAEGNSRGFLVDERRLFAVRRDGRAYIYLNRCPHRGIPLEwqpDAFLDDSAslIRCASHGALFLIESGECV 88
Cdd:cd03528     1 WVRVCAVDELPEGEPKRVDVGGRPIAVYRVDGEFYATDDLCTHGDASLS---EGYVEGGV--IECPLHGGRFDLRTGKAL 75
                          90       100
                  ....*....|....*....|....*.
gi 1154708950  89 AGPCAgERLRALPCREdaEGLWVELD 114
Cdd:cd03528    76 SLPAT-EPLKTYPVKV--EDGDVYVD 98
HcaE COG4638
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ...
12-115 5.01e-06

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: 43.44  E-value: 5.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154708950  12 LCPSSHLAE-GNSRGFLVDERRLFAVR-RDGRAYIYLNRCPHRGIPLEWQPdafldDSASLIRCASHG---ALflieSGE 86
Cdd:COG4638    30 VGHSSELPEpGDYLTRTILGEPVVLVRdKDGEVRAFHNVCPHRGAPLSEGR-----GNGGRLVCPYHGwtyDL----DGR 100
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1154708950  87 CVAGPCAGE---------RLRALPCREdAEGL-WVELDD 115
Cdd:COG4638   101 LVGIPHMEGfpdfdparaGLRSVPVEE-WGGLiFVWLGP 138
PobA COG5749
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
39-115 5.11e-06

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


Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 43.45  E-value: 5.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154708950  39 DGRAYIYLNRCPHRGIPLewqpdaflddsaSL-------IRCASHGALFlIESGECVAGPCAGE--------RLRALPCR 103
Cdd:COG5749    51 DGKVVALEDRCPHRGAPL------------SEgrveggnLRCPYHGWQF-DGDGKCVHIPQLPEnqpipknaKVKSYPVQ 117
                          90
                  ....*....|..
gi 1154708950 104 EDAEGLWVELDD 115
Cdd:COG5749   118 ERYGLIWVWLGD 129
Rieske_RO_Alpha_VanA_DdmC cd03532
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and ...
27-102 5.79e-06

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: 41.97  E-value: 5.79e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154708950  27 LVDERRLFAVRRDGRAYIYLNRCPHRGIPLEwqpDAFLDDSAslIRCASHGALFLIEsGECVAGPcAGERLRALPC 102
Cdd:cd03532    24 LLGEPVVLYRTQDGRVAALEDRCPHRSAPLS---KGSVEGGG--LVCGYHGLEFDSD-GRCVHMP-GQERVPAKAC 92
Rieske_RO_Alpha_PhDO_like cd03479
Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, ...
5-111 1.30e-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: 41.46  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154708950   5 NGAPM--------IHLCPSSHLAEGNS--RGFLVDERrLFAVR-RDGRAYIYLNRCPHRGIPLEWqpdAFLDDSAslIRC 73
Cdd:cd03479    10 PGTPMgellrrywQPVALSSELTEDGQpvRVRLLGED-LVAFRdTSGRVGLLDEHCPHRGASLVF---GRVEECG--LRC 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1154708950  74 ASHGALFLIEsGECVAGPCAGE--------RLRALPCREDAEGLWV 111
Cdd:cd03479    84 CYHGWKFDVD-GQCLEMPSEPPdsqlkqkvRQPAYPVRERGGLVWA 128
Rieske_RO_Alpha_OMO_CARDO cd03548
Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole ...
15-88 3.60e-05

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: 40.10  E-value: 3.60e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154708950  15 SSHLAEGNSRGFLVDERRLFAVRRDGRAYIYLNRCPHRGIPLEWQPDAFLDDSaslIRCASHGALFLIESGECV 88
Cdd:cd03548    21 SHELEEGEPKGIQLCGEPILLRRVDGKVYALKDRCLHRGVPLSKKPECFTKGT---ITCWYHGWTYRLDDGKLV 91
Rieske_RO_Alpha_Cao cd04337
Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the ...
39-111 1.85e-03

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: 35.54  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154708950  39 DGRAYIYLNRCPHRGIPLewqpdaflddsaSL-------IRCASHGALFlIESGECVAGP---CAGERLRALPCREDAEG 108
Cdd:cd04337    49 DGTPGCIRDECAHRACPL------------SLgkviegrIQCPYHGWEY-DGDGECTKMPstkCLNVGIAALPCMEQDGM 115

                  ...
gi 1154708950 109 LWV 111
Cdd:cd04337   116 IWV 118
 
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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