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Conserved domains on  [gi|1167560559|gb|OQD29744|]
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Rieske (2Fe-2S) protein [Burkholderia cenocepacia]

Protein Classification

aromatic ring-hydroxylating dioxygenase subunit alpha( domain architecture ID 10131510)

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; similar to Comamonas sp. terephthalate 1,2-dioxygenase, terminal oxygenase component subunit alpha

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RHO_alpha_C_ahdA1c-like cd08880
C-terminal catalytic domain of the large/alpha subunit (ahdA1c) of a ring-hydroxylating ...
 200-422 2.07e-131

C-terminal catalytic domain of the large/alpha subunit (ahdA1c) of a ring-hydroxylating dioxygenase from Sphingomonas sp. strain P2 and related proteins; C-terminal catalytic domain of the large subunit (ahdA1c) of the AhdA3A4A2cA1c salicylate 1-hydroxylase complex from Sphingomonas sp. strain P2, and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). AhdA3A4A2cA1c is one of three known isofunctional salicylate 1-hydroxylase complexes in strain P2, involved in phenanthrene degradation, which catalyze the monooxygenation of salicylate, the metabolite of phenanthene degradation, to produce catechol. This complex prefers salicylate over other substituted salicylates; the other two salicylate 1-hydroxylases have different substrate preferences. 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 a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Other oxygenases belonging to this subgroup include the alpha subunits of anthranilate 1,2-dioxygenase from Burkholderia cepacia DBO1, a polycyclic aromatic hydrocarbon dioxygenase from Cycloclasticus sp. strain A5 (PhnA dioxygenase), salicylate-5-hydroxylase from Ralstonia sp. U2, ortho-halobenzoate 1,2-dioxygenase from Pseudomonas aeruginosa strain JB2, and the terephthalate 1,2-dioxygenase system from Delftia tsuruhatensis strain T7. 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: 176889  Cd Length: 222  Bit Score: 376.98  E-value: 2.07e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 200 LGCTRQYSKSNWKLYMENVKDPYHASMLHLFHTTFNIFRVGMKARSIPDaNHGLHSIITVTKTNDDTSAAYKQQNIRSFD 279
Cdd:cd08880     1 LGYYRQRIPGNWKLYAENVKDPYHASLLHLFFVTFGLWRADQKSSIIDD-EHGRHSVMTSTKSGDDEAAEKDSEEIRSFR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 280 EGFHLEDESILDLVSEYDEDCTNHIQPIFPQLVIQQIHNTLVARQILPKGPDNFELIFHFFGYADDTPELRALRIKQANL 359
Cdd:cd08880    80 DDFTLLDPSLLDGRAEFDDDITLVIQSIFPSLVVQQIQNTLAVRHIIPKGPDSFELVWTYFGYEDDDEEMTRLRLRQANL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167560559 360 VGPAGYISMEDTEATELVQRGTVRDADATSVIEMSRGNPDQQDTVITESLIRKFWVGYQKLMG 422
Cdd:cd08880   160 VGPAGFVSMEDGEAIEFVQRGVEGDGGDRSVIEMGGGDVESSDHMVTEAAIRGFWKYYRKVMG 222
Rieske_RO_Alpha_OHBDO_like cd03545
Rieske non-heme iron oxygenase (RO) family, Ortho-halobenzoate-1,2-dioxygenase (OHBDO)-like ...
 28-177 6.83e-107

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


:

Pssm-ID: 239616 [Multi-domain]  Cd Length: 150  Bit Score: 312.07  E-value: 6.83e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559  28 RVPYKVFSSRAVYDREQERIFRGPTWNFVALEAEIPNAGDFKSTFVGDTPVVVTRAEDGTLSAWVNRCAHRGAQVCRKSR 107
Cdd:cd03545     1 RVPYKVFTDRAYFDREQERIFRGKTWSYVGLEAEIPNAGDFKSTFVGDTPVVVTRAEDGSLHAWVNRCAHRGALVCRERR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 108 GNASSHTCVYHQWSFDNQGNLLGVPFRRGQKGMTGMPADFDPKQHGLRKLRVDSYRGLVFATFSDEVAPL 177
Cdd:cd03545    81 GNDGSLTCVYHQWAYDLKGNLKGVPFRRGLKGQGGMPKDFDMKQHGLEKLRVETVGGLVFASFSDEVEPL 150
 
Name Accession Description Interval E-value
RHO_alpha_C_ahdA1c-like cd08880
C-terminal catalytic domain of the large/alpha subunit (ahdA1c) of a ring-hydroxylating ...
 200-422 2.07e-131

C-terminal catalytic domain of the large/alpha subunit (ahdA1c) of a ring-hydroxylating dioxygenase from Sphingomonas sp. strain P2 and related proteins; C-terminal catalytic domain of the large subunit (ahdA1c) of the AhdA3A4A2cA1c salicylate 1-hydroxylase complex from Sphingomonas sp. strain P2, and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). AhdA3A4A2cA1c is one of three known isofunctional salicylate 1-hydroxylase complexes in strain P2, involved in phenanthrene degradation, which catalyze the monooxygenation of salicylate, the metabolite of phenanthene degradation, to produce catechol. This complex prefers salicylate over other substituted salicylates; the other two salicylate 1-hydroxylases have different substrate preferences. 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 a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Other oxygenases belonging to this subgroup include the alpha subunits of anthranilate 1,2-dioxygenase from Burkholderia cepacia DBO1, a polycyclic aromatic hydrocarbon dioxygenase from Cycloclasticus sp. strain A5 (PhnA dioxygenase), salicylate-5-hydroxylase from Ralstonia sp. U2, ortho-halobenzoate 1,2-dioxygenase from Pseudomonas aeruginosa strain JB2, and the terephthalate 1,2-dioxygenase system from Delftia tsuruhatensis strain T7. 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: 176889  Cd Length: 222  Bit Score: 376.98  E-value: 2.07e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 200 LGCTRQYSKSNWKLYMENVKDPYHASMLHLFHTTFNIFRVGMKARSIPDaNHGLHSIITVTKTNDDTSAAYKQQNIRSFD 279
Cdd:cd08880     1 LGYYRQRIPGNWKLYAENVKDPYHASLLHLFFVTFGLWRADQKSSIIDD-EHGRHSVMTSTKSGDDEAAEKDSEEIRSFR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 280 EGFHLEDESILDLVSEYDEDCTNHIQPIFPQLVIQQIHNTLVARQILPKGPDNFELIFHFFGYADDTPELRALRIKQANL 359
Cdd:cd08880    80 DDFTLLDPSLLDGRAEFDDDITLVIQSIFPSLVVQQIQNTLAVRHIIPKGPDSFELVWTYFGYEDDDEEMTRLRLRQANL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167560559 360 VGPAGYISMEDTEATELVQRGTVRDADATSVIEMSRGNPDQQDTVITESLIRKFWVGYQKLMG 422
Cdd:cd08880   160 VGPAGFVSMEDGEAIEFVQRGVEGDGGDRSVIEMGGGDVESSDHMVTEAAIRGFWKYYRKVMG 222
Rieske_RO_Alpha_OHBDO_like cd03545
Rieske non-heme iron oxygenase (RO) family, Ortho-halobenzoate-1,2-dioxygenase (OHBDO)-like ...
 28-177 6.83e-107

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


Pssm-ID: 239616 [Multi-domain]  Cd Length: 150  Bit Score: 312.07  E-value: 6.83e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559  28 RVPYKVFSSRAVYDREQERIFRGPTWNFVALEAEIPNAGDFKSTFVGDTPVVVTRAEDGTLSAWVNRCAHRGAQVCRKSR 107
Cdd:cd03545     1 RVPYKVFTDRAYFDREQERIFRGKTWSYVGLEAEIPNAGDFKSTFVGDTPVVVTRAEDGSLHAWVNRCAHRGALVCRERR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 108 GNASSHTCVYHQWSFDNQGNLLGVPFRRGQKGMTGMPADFDPKQHGLRKLRVDSYRGLVFATFSDEVAPL 177
Cdd:cd03545    81 GNDGSLTCVYHQWAYDLKGNLKGVPFRRGLKGQGGMPKDFDMKQHGLEKLRVETVGGLVFASFSDEVEPL 150
HcaE COG4638
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ...
 26-420 5.99e-84

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: 258.76  E-value: 5.99e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559  26 GSRVPYKVFSSRAVYDREQERIFRGpTWNFVALEAEIPNAGDFKSTFVGDTPVVVTRAEDGTLSAWVNRCAHRGAQVCRK 105
Cdd:COG4638     1 ASRLPAAFYTDPEIFELELERIFRR-GWYYVGHSSELPEPGDYLTRTILGEPVVLVRDKDGEVRAFHNVCPHRGAPLSEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 106 sRGNASSHTCVYHQWSFDNQGNLLGVPFRRGqkgmtgmPADFDPKQHGLRKLRVDSYRGLVFATFSDEVAPLPEYLGEqM 185
Cdd:COG4638    80 -RGNGGRLVCPYHGWTYDLDGRLVGIPHMEG-------FPDFDPARAGLRSVPVEEWGGLIFVWLGPDAPPLAEYLGP-L 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 186 RPWIDRIFHKPIEYLGCTRQYSKSNWKLYMENVKDPYHASMLHLFHTTFnifrvgmkarsipdanhglhsiitvtktndd 265
Cdd:COG4638   151 AEYLDPYDFGELKVAGRETYEVNANWKLVVENFLDGYHVPFVHPGIILF------------------------------- 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 266 tsaaykqqnirsfdegfhledesildlvseydedctnhiqpIFPQLVIQQIHNTLVARQILPKGPDNFELIFHFFGYADD 345
Cdd:COG4638   200 -----------------------------------------LFPNLMILDYPDHLVVRTVTPVSPDRTRVFVTFYVPKDA 238

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167560559 346 TPELRALRIKQANlvgpaGYISMEDTEATELVQRGTVRDADATSVIEMSRgnpdqqdtviTESLIRKFWVGYQKL 420
Cdd:COG4638   239 LDPEARADLEAFW-----GRVFEEDREIVERQQRGLRSLAYPGPYLSRSP----------AEGGVRHFRRWLRRL 298
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 52-138 6.07e-18

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: 78.16  E-value: 6.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559  52 TWNFVALEAEIPNaGDFKSTFVGDTPVVVTRAEDGTLSAWVNRCAHRGAQVCRkSRGNASSH-TCVYHQWSFDNQGNLLG 130
Cdd:pfam00355   1 SWYPVCHSSELPE-GEPKVVEVGGEPLVVFRDEDGELYALEDRCPHRGAPLSE-GKVNGGGRlECPYHGWRFDGTGKVVK 78


                  ....*...
gi 1167560559 131 VPFRRGQK 138
Cdd:pfam00355  79 VPAPRPLK 86
Ring_hydroxyl_A pfam00848
Ring hydroxylating alpha subunit (catalytic domain); This family is the catalytic domain of ...
 208-380 5.69e-06

Ring hydroxylating alpha subunit (catalytic domain); This family is the catalytic domain of aromatic-ring- hydroxylating dioxygenase systems. The active site contains a non-heme ferrous ion coordinated by three ligands.


Pssm-ID: 425905  Cd Length: 210  Bit Score: 47.06  E-value: 5.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 208 KSNWKLYMENVKDPYHASMLHLFHTTFNIFRVGMKARSIPDANHGLHSIITVTKTNDDTSAAYKQQ--NIRSFDEGFHLE 285
Cdd:pfam00848  15 AANWKLAAENFLECYHVPVLHPELLRASPPEDLPPSEAAHFDGFGPHGRLGQGGDLRLTPAAASMTldAEAGRPELPGLP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 286 DEsilDLVSEYdedctnHIQpIFPQLVIQQIHNTLVARQILPKGPDNFELIFHFFgYADDTPELRALRIKQANLVGPAGY 365
Cdd:pfam00848  95 EE---QDRGAL------FYT-LFPNLSILLAPDHVVVYQLIPTGPDTTRVEVYWY-VPPDALAEPEFAEELEAVWDRTFG 163

                         170
                  ....*....|....*
gi 1167560559 366 ISMEDTEATELVQRG 380
Cdd:pfam00848 164 VNQEDAELCERVQRG 178
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 52-123 2.93e-05

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: 42.91  E-value: 2.93e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167560559  52 TWNFVALEAEIPnAGDFKSTFVGDTPVVVTRAeDGTLSAWVNRCAHRGAQVcrkSRG--NASSHTCVYHQWSFD 123
Cdd:COG2146     2 SEVKVCALDDLP-EGGGVVVEVGGKQIAVFRT-DGEVYAYDNRCPHQGAPL---SEGivDGGVVTCPLHGARFD 70
 
Name Accession Description Interval E-value
RHO_alpha_C_ahdA1c-like cd08880
C-terminal catalytic domain of the large/alpha subunit (ahdA1c) of a ring-hydroxylating ...
 200-422 2.07e-131

C-terminal catalytic domain of the large/alpha subunit (ahdA1c) of a ring-hydroxylating dioxygenase from Sphingomonas sp. strain P2 and related proteins; C-terminal catalytic domain of the large subunit (ahdA1c) of the AhdA3A4A2cA1c salicylate 1-hydroxylase complex from Sphingomonas sp. strain P2, and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). AhdA3A4A2cA1c is one of three known isofunctional salicylate 1-hydroxylase complexes in strain P2, involved in phenanthrene degradation, which catalyze the monooxygenation of salicylate, the metabolite of phenanthene degradation, to produce catechol. This complex prefers salicylate over other substituted salicylates; the other two salicylate 1-hydroxylases have different substrate preferences. 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 a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Other oxygenases belonging to this subgroup include the alpha subunits of anthranilate 1,2-dioxygenase from Burkholderia cepacia DBO1, a polycyclic aromatic hydrocarbon dioxygenase from Cycloclasticus sp. strain A5 (PhnA dioxygenase), salicylate-5-hydroxylase from Ralstonia sp. U2, ortho-halobenzoate 1,2-dioxygenase from Pseudomonas aeruginosa strain JB2, and the terephthalate 1,2-dioxygenase system from Delftia tsuruhatensis strain T7. 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: 176889  Cd Length: 222  Bit Score: 376.98  E-value: 2.07e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 200 LGCTRQYSKSNWKLYMENVKDPYHASMLHLFHTTFNIFRVGMKARSIPDaNHGLHSIITVTKTNDDTSAAYKQQNIRSFD 279
Cdd:cd08880     1 LGYYRQRIPGNWKLYAENVKDPYHASLLHLFFVTFGLWRADQKSSIIDD-EHGRHSVMTSTKSGDDEAAEKDSEEIRSFR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 280 EGFHLEDESILDLVSEYDEDCTNHIQPIFPQLVIQQIHNTLVARQILPKGPDNFELIFHFFGYADDTPELRALRIKQANL 359
Cdd:cd08880    80 DDFTLLDPSLLDGRAEFDDDITLVIQSIFPSLVVQQIQNTLAVRHIIPKGPDSFELVWTYFGYEDDDEEMTRLRLRQANL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167560559 360 VGPAGYISMEDTEATELVQRGTVRDADATSVIEMSRGNPDQQDTVITESLIRKFWVGYQKLMG 422
Cdd:cd08880   160 VGPAGFVSMEDGEAIEFVQRGVEGDGGDRSVIEMGGGDVESSDHMVTEAAIRGFWKYYRKVMG 222
Rieske_RO_Alpha_OHBDO_like cd03545
Rieske non-heme iron oxygenase (RO) family, Ortho-halobenzoate-1,2-dioxygenase (OHBDO)-like ...
 28-177 6.83e-107

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


Pssm-ID: 239616 [Multi-domain]  Cd Length: 150  Bit Score: 312.07  E-value: 6.83e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559  28 RVPYKVFSSRAVYDREQERIFRGPTWNFVALEAEIPNAGDFKSTFVGDTPVVVTRAEDGTLSAWVNRCAHRGAQVCRKSR 107
Cdd:cd03545     1 RVPYKVFTDRAYFDREQERIFRGKTWSYVGLEAEIPNAGDFKSTFVGDTPVVVTRAEDGSLHAWVNRCAHRGALVCRERR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 108 GNASSHTCVYHQWSFDNQGNLLGVPFRRGQKGMTGMPADFDPKQHGLRKLRVDSYRGLVFATFSDEVAPL 177
Cdd:cd03545    81 GNDGSLTCVYHQWAYDLKGNLKGVPFRRGLKGQGGMPKDFDMKQHGLEKLRVETVGGLVFASFSDEVEPL 150
HcaE COG4638
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ...
 26-420 5.99e-84

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: 258.76  E-value: 5.99e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559  26 GSRVPYKVFSSRAVYDREQERIFRGpTWNFVALEAEIPNAGDFKSTFVGDTPVVVTRAEDGTLSAWVNRCAHRGAQVCRK 105
Cdd:COG4638     1 ASRLPAAFYTDPEIFELELERIFRR-GWYYVGHSSELPEPGDYLTRTILGEPVVLVRDKDGEVRAFHNVCPHRGAPLSEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 106 sRGNASSHTCVYHQWSFDNQGNLLGVPFRRGqkgmtgmPADFDPKQHGLRKLRVDSYRGLVFATFSDEVAPLPEYLGEqM 185
Cdd:COG4638    80 -RGNGGRLVCPYHGWTYDLDGRLVGIPHMEG-------FPDFDPARAGLRSVPVEEWGGLIFVWLGPDAPPLAEYLGP-L 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 186 RPWIDRIFHKPIEYLGCTRQYSKSNWKLYMENVKDPYHASMLHLFHTTFnifrvgmkarsipdanhglhsiitvtktndd 265
Cdd:COG4638   151 AEYLDPYDFGELKVAGRETYEVNANWKLVVENFLDGYHVPFVHPGIILF------------------------------- 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 266 tsaaykqqnirsfdegfhledesildlvseydedctnhiqpIFPQLVIQQIHNTLVARQILPKGPDNFELIFHFFGYADD 345
Cdd:COG4638   200 -----------------------------------------LFPNLMILDYPDHLVVRTVTPVSPDRTRVFVTFYVPKDA 238

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167560559 346 TPELRALRIKQANlvgpaGYISMEDTEATELVQRGTVRDADATSVIEMSRgnpdqqdtviTESLIRKFWVGYQKL 420
Cdd:COG4638   239 LDPEARADLEAFW-----GRVFEEDREIVERQQRGLRSLAYPGPYLSRSP----------AEGGVRHFRRWLRRL 298
Rieske_RO_Alpha_S5H cd03539
This alignment model represents the N-terminal rieske iron-sulfur domain of the oxygenase ...
 53-177 6.61e-48

This alignment model represents the N-terminal rieske iron-sulfur domain of the oxygenase alpha subunit (NagG) of salicylate 5-hydroxylase (S5H). S5H converts salicylate (2-hydroxybenzoate), a metabolic intermediate of phenanthrene, to gentisate (2,5-dihydroxybenzoate) as part of an alternate pathway for naphthalene catabolism. S5H is a multicomponent enzyme made up of NagGH (the oxygenase components), NagAa (the ferredoxin reductase component), and NagAb (the ferredoxin component). The oxygenase component is made up of alpha (NagG) and beta (NagH) subunits.


Pssm-ID: 239613 [Multi-domain]  Cd Length: 129  Bit Score: 160.09  E-value: 6.61e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559  53 WNFVALEAEIPNAGDFKSTFVGDTPVVVTRAEDGTLSAWVNRCAHRGAQVCRKSRGNASSHTCVYHQWSFDNQGNLLGVP 132
Cdd:cd03539     1 WCYVGLEAEIPNPGDFKRTLIGERSVIMTRDPDGGINVVENVCAHRGMRFCRERNGNAKDFVCPYHQWNYSLKGDLQGVP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1167560559 133 FRRGQKG----MTGMPADFDPKQHGLRKLRVDSYRGLVFATFSDEVAPL 177
Cdd:cd03539    81 FRRGVKKdgkvNGGMPKDFKTKDHGLTKLKVATRGGVVFASFDHDVESF 129
Rieske_RO_Alpha_N cd03469
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ...
 53-177 9.42e-47

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: 156.59  E-value: 9.42e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559  53 WNFVALEAEIPNAGDFKSTFVGDTPVVVTRAEDGTLSAWVNRCAHRGAQVCRKSRGNASSHTCVYHQWSFDNQGNLLGVP 132
Cdd:cd03469     1 WYFVGHSSELPEPGDYVTLELGGEPLVLVRDRDGEVRAFHNVCPHRGARLCEGRGGNAGRLVCPYHGWTYDLDGKLVGVP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1167560559 133 FRRGQKgmtgmpaDFDPKQHGLRKLRVDSYRGLVFATFSDEVAPL 177
Cdd:cd03469    81 REEGFP-------GFDKEKLGLRTVPVEEWGGLIFVNLDPDAPPL 118
Rieske_RO_Alpha_HBDO cd03542
Rieske non-heme iron oxygenase (RO) family, 2-Halobenzoate 1,2-dioxygenase (HBDO) subfamily, ...
 53-177 8.66e-38

Rieske non-heme iron oxygenase (RO) family, 2-Halobenzoate 1,2-dioxygenase (HBDO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. HBDO catalyzes the double hydroxylation of 2-halobenzoates with concomitant release of halogenide and carbon dioxide, yielding catechol.


Pssm-ID: 239615 [Multi-domain]  Cd Length: 123  Bit Score: 133.34  E-value: 8.66e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559  53 WNFVALEAEIPNAGDFKSTFVGDTPVVVTRAEDGTLSAWVNRCAHRGAQVCRKSRGNASSHTCVYHQWSFDNQGNLLGVP 132
Cdd:cd03542     1 WVYLAHESQIPNNNDYFTTTIGRQPVVITRDKDGELNAFINACSHRGAMLCRRKQGNKGTFTCPFHGWTFSNTGKLLKVK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1167560559 133 FRRGqkgmTGMPADFDPK-QHGLRKL-RVDSYRGLVFATFSDEVAPL 177
Cdd:cd03542    81 DPKT----AGYPEGFNCDgSHDLTKVaRFESYRGFLFGSLNADVAPL 123
Rieske_RO_Alpha_NDO cd03535
Rieske non-heme iron oxygenase (RO) family, Nathphalene 1,2-dioxygenase (NDO) subfamily, ...
 52-177 5.10e-37

Rieske non-heme iron oxygenase (RO) family, Nathphalene 1,2-dioxygenase (NDO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. NDO is a three-component RO system consisting of a reductase, a ferredoxin, and a hetero-hexameric alpha-beta subunit oxygenase component. NDO catalyzes the oxidation of naphthalene to cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene (naphthalene cis-dihydrodiol) with the consumption of O2 and NAD(P)H. NDO has a relaxed substrate specificity and can oxidize almost 100 substrates. Included in its varied activities are the enantiospecific cis-dihydroxylation of polycyclic aromatic hydrocarbons and benzocycloalkenes, benzylic hydroxylation, N- and O-dealkylation, sulfoxidation and desaturation reactions.


Pssm-ID: 239609 [Multi-domain]  Cd Length: 123  Bit Score: 131.01  E-value: 5.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559  52 TWNFVALEAEIPNAGDFKSTFVGDTPVVVTRAEDGTLSAWVNRCAHRGAQVCRKSRGNASSHTCVYHQWSFDNQGNLLGV 131
Cdd:cd03535     2 AWVFLGHESEIPNAGDYVVRYIGDDSFIVCRDEDGEIRAMFNSCRHRGMQVCRAEMGNTSHFRCPYHGWTYRNTGRLVGV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1167560559 132 PFRRGQKGmtgmpADFDPKQHGLRKL-RVDSYRGLVFATFSDEVAPL 177
Cdd:cd03535    82 PAQQEAYG-----GGFDKSQWGLRPApNLDSYNGLIFGSLDPKAPSL 123
Rieske_RO_Alpha_BPDO_like cd03472
Rieske non-heme iron oxygenase (RO) family, Biphenyl dioxygenase (BPDO)-like subfamily, ...
 45-176 9.92e-35

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: 125.34  E-value: 9.92e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559  45 ERIFrGPTWNFVALEAEIPNAGDFKSTFVGDTPVVVTRAEDGTLSAWVNRCAHRGAQVCRKSRGNASSHTCVYHQWSFDN 124
Cdd:cd03472     2 ERVF-ARSWLLLGHETHIPKAGDYLTTYMGEDPVIVVRQKDGSIRVFLNQCRHRGMRICRSDAGNAKAFTCTYHGWAYDT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1167560559 125 QGNLLGVPFRRgqkgmTGMPADFDPKQHGLRKLRVDSYRGLVFATFsDEVAP 176
Cdd:cd03472    81 AGNLVNVPFEK-----EAFCDGLDKADWGPLQARVETYKGLIFANW-DAEAP 126
Rieske_RO_Alpha_AntDO cd03538
Rieske non-heme iron oxygenase (RO) family, Anthranilate 1,2-dioxygenase (AntDO) subfamily, ...
 33-173 1.31e-30

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: 114.87  E-value: 1.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559  33 VFSSRAVYDREQERIFrGPTWNFVALEAEIPNAGDFKSTFVGDTPVVVTRAEDGTLSAWVNRCAHRGAQVCRKSRGNASS 112
Cdd:cd03538     4 VYTDPEIFALEMERLF-GNAWIYVGHESQVPNPGDYITTRIGDQPVVMVRHTDGSVHVLYNRCPHKGTKIVSDGCGNTGK 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167560559 113 -HTCVYHQWSFDNQGNLLGVPFRRGQKGmTGmpadFDPKQ--HGLRKL-RVDSYRGLVFATFSDE 173
Cdd:cd03538    83 fFRCPYHAWSFKTDGSLLAIPLKKGYEG-TG----FDPSHadKGMQRVgAVDIYRGFVFARLSPS 142
Rieske_RO_Alpha_DTDO cd03536
This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit ...
 53-171 1.48e-25

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: 100.39  E-value: 1.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559  53 WNFVALEAEIPNAGDFKSTFVGDTPVVVTRAEDGTLSAWVNRCAHRGAQVCRKSRGNASSHTCVYHQWSFDNQGNLLGVP 132
Cdd:cd03536     1 WVLLGHESEIPNKGDFMVRDMGSDSVIVARDKDGEIHVSLNVCPHRGMRISTTDGGNTQIHVCIYHGWAFRPNGDFIGAP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1167560559 133 FRRgqkgmTGMPADFDPK-QHGLRKLRVDSYRGLVFATFS 171
Cdd:cd03536    81 VEK-----ECMHGKMRTKaELGLHKARVTLYGGLIFATWN 115
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 52-138 6.07e-18

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: 78.16  E-value: 6.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559  52 TWNFVALEAEIPNaGDFKSTFVGDTPVVVTRAEDGTLSAWVNRCAHRGAQVCRkSRGNASSH-TCVYHQWSFDNQGNLLG 130
Cdd:pfam00355   1 SWYPVCHSSELPE-GEPKVVEVGGEPLVVFRDEDGELYALEDRCPHRGAPLSE-GKVNGGGRlECPYHGWRFDGTGKVVK 78


                  ....*...
gi 1167560559 131 VPFRRGQK 138
Cdd:pfam00355  79 VPAPRPLK 86
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 53-138 1.62e-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: 71.75  E-value: 1.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559  53 WNFVALEAEIPnAGDFKSTFVGDTPVVVTRAEDGTLSAWVNRCAHRGAQVCrKSRGNASSHTCVYHQWSFDNQ-GNLLGV 131
Cdd:cd03467     1 WVVVGALSELP-PGGGRVVVVGGGPVVVVRREGGEVYALSNRCTHQGCPLS-EGEGEDGCIVCPCHGSRFDLRtGEVVSG 78


                  ....*..
gi 1167560559 132 PFRRGQK 138
Cdd:cd03467    79 PAPRPLP 85
RHO_alpha_C_AntDO-like cd08879
C-terminal catalytic domain of the oxygenase alpha subunit of Pseudomonas resinovorans strain ...
 201-422 4.81e-14

C-terminal catalytic domain of the oxygenase alpha subunit of Pseudomonas resinovorans strain CA10 anthranilate 1,2-dioxygenase and related aromatic ring hydroxylating dioxygenases; C-terminal catalytic domain of the oxygenase alpha subunit of anthranilate 1,2-dioxygenase (AntDO) 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 AntDO, aniline dioxygenase, Acinetobacter calcoaceticus benzoate 1,2-dioxygenase, 2-halobenzoate 1,2-dioxygenase from Pseudomonas cepacia 2CBS, 2,4,5-trichlorophenoxyacetic acid oxygenase from Pseudomonas cepacia AC1100, 2,4-dichlorophenoxyacetic acid oxygenase from Bradyrhizobium sp. strain HW13, p-cumate 2,3-dioxygenase, 2-halobenzoate 1,2-dioxygenase form Pseudomonas cepacia 2CBS, and Pseudomonas putida IacC, which may be involved in the catabolism of the plant hormone indole 3-acetic acid. 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: 176888 [Multi-domain]  Cd Length: 237  Bit Score: 71.22  E-value: 4.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 201 GCTRQYSKSNWKLYMENVKDPYHASMLhlfHTTFnifrVGMKARSIPDAnhglhsiitVTKTNDDTSAAYKQQNIRSFDE 280
Cdd:cd08879     2 GTHRYRYRGNWKLQLENGTDGYHPPFV---HASY----VATTGAAAADA---------TRGGLSSFMTGPQGGGVRDLGN 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 281 GfHLEDESILDLVSEYDEDCTNHIQP--------------------------IFPQLVIQQIHNTLvaRQILPKGPDNFE 334
Cdd:cd08879    66 G-HSVLDSRPEIPRLDADRPKPPIAEyraalvaahgeerarrilrgrgrnlnIFPNLFIIDISQQI--RVIRPIAVDETE 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 335 LIFHFFGYADDTPELRALRIKQANLV-GPAGYISMEDTEATELVQRGTVRDADATsvIEMSRGNPDQQ--------DTVI 405
Cdd:cd08879   143 VTSWALRPKGAPDEVNRRRLRYSEDFfGPSGFATPDDLEAFERCQRGLAARGEEW--VDLSRGLGREKadedgvvtGAVT 220

                         250
                  ....*....|....*..
gi 1167560559 406 TESLIRKFWVGYQKLMG 422
Cdd:cd08879   221 DELPMRNQWRAWKRLMT 237
RHO_alpha_C cd00680
C-terminal catalytic domain of the oxygenase alpha subunit of Rieske-type non-heme iron ...
 201-380 9.73e-14

C-terminal catalytic domain of the oxygenase alpha subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases; C-terminal catalytic domain of the oxygenase alpha subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenase (RHO) family. RHOs, also known as aromatic ring hydroxylating dioxygenases, 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 a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Oxygenases belonging to this family include the alpha subunits of Pseudomonas resinovorans strain CA10 anthranilate 1,2-dioxygenase, Stenotrophomonas maltophilia dicamba O-demethylase, Ralstonia sp. U2 salicylate-5-hydroxylase, Cycloclasticus sp. strain A5 polycyclic aromatic hydrocarbon dioxygenase, toluene 2,3-dioxygenase from Pseudomonas putida F1, dioxin dioxygenase of Sphingomonas sp. Strain RW1, plant choline monooxygenase, and the polycyclic aromatic hydrocarbon (PAH)-degrading ring-hydroxylating dioxygenase from Sphingomonas CHY-1. This group also includes the C-terminal catalytic domains of MupW, part of the mupirocin biosynthetic gene cluster in Pseudomonas fluorescens, and Pseudomonas aeruginosa GbcA (glycine betaine catabolism A). This family 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: 176852 [Multi-domain]  Cd Length: 188  Bit Score: 69.52  E-value: 9.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 201 GCTRQYSKSNWKLYMENVKDPYHASMLHLFHTtfnifrvgmkaRSIPDANHGLHSIITVTKTNDDTSAAYKQQNIRSFDE 280
Cdd:cd00680     1 GRYEYEVDCNWKLAVENFLECYHVPTVHPDTL-----------ATGLPLPLLFGDHYRVDDTGEGPGEGLSRHWGDGKGP 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 281 GFHLEDESILDLVSEYdedctnhiqpIFPQLVIQQIHNTLVARQILPKGPDNFELIFHFFGYADDtPELRALRIKQANLV 360
Cdd:cd00680    70 QSALPGLKPGGYLYLY----------LFPNLMIGLYPDSLQVQQFVPIGPNKTRLEVRLYRPKDE-DAREEFDAELESLA 138

                         170       180
                  ....*....|....*....|
gi 1167560559 361 GPAGYISMEDTEATELVQRG 380
Cdd:cd00680   139 GILRQVLDEDIELCERIQRG 158
Rieske_RO_Alpha_CMO cd03541
Rieske non-heme iron oxygenase (RO) family, Choline monooxygenase (CMO) subfamily, N-terminal ...
 53-170 1.75e-09

Rieske non-heme iron oxygenase (RO) family, Choline monooxygenase (CMO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. CMO is a novel RO found in certain plants which catalyzes the first step in betaine synthesis. CMO is not found in animals or bacteria. In these organisms, the first step in betaine synthesis is catalyzed by either the membrane-bound choline dehydrogenase (CDH) or the soluble choline oxidase (COX).


Pssm-ID: 239614 [Multi-domain]  Cd Length: 118  Bit Score: 55.25  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559  53 WNFVALEAEIPNAGDFKSTFVGDTPVVVTRAEDGTLSAWVNRCAHRgAQVCRKSRGNASSHTCVYHQWSFDNQGNLLGVp 132
Cdd:cd03541     2 WQVAGYSDQVKEKNQYFTGRLGNVEYVVCRDGNGKLHAFHNVCTHR-ASILACGSGKKSCFVCPYHGWVYGLDGSLTKA- 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1167560559 133 frrgqKGMTGMpADFDPKQHGLRKLRVDSYRGLVFATF 170
Cdd:cd03541    80 -----TQATGI-QNFNPKELGLVPLKVAEWGPFVLISV 111
Rieske_RO_Alpha_Tic55 cd04338
Tic55 is a 55kDa LLS1-related non-heme iron oxygenase associated with protein transport ...
 73-179 9.52e-07

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: 47.91  E-value: 9.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559  73 VGDTPVVVTRAEDGTLSAWVNRCAHRGAQVcrkSRGNA--SSHTCVYHQWSFDNQGNLLGVPfrrgqkgmtGMPADFD-P 149
Cdd:cd04338    37 VYDEPFVLFRDQNGQLRCLEDRCPHRLAKL---SEGQLidGKLECLYHGWQFGGEGKCVKIP---------QLPADAKiP 104

                          90       100       110
                  ....*....|....*....|....*....|
gi 1167560559 150 KQHGLRKLRVDSYRGLVFATFSDEVAPLPE 179
Cdd:cd04338   105 KNACVKSYEVRDSQGVVWMWMSEATPPDEE 134
Rieske_RO_Alpha_VanA_DdmC cd03532
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and ...
 75-145 2.80e-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: 46.21  E-value: 2.80e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167560559  75 DTPVVVTRAEDGTLSAWVNRCAHRGAQVCRKSRGNASShTCVYHQWSFDNQGNLLGVPfrrGQKGMTGMPA 145
Cdd:cd03532    26 GEPVVLYRTQDGRVAALEDRCPHRSAPLSKGSVEGGGL-VCGYHGLEFDSDGRCVHMP---GQERVPAKAC 92
Ring_hydroxyl_A pfam00848
Ring hydroxylating alpha subunit (catalytic domain); This family is the catalytic domain of ...
 208-380 5.69e-06

Ring hydroxylating alpha subunit (catalytic domain); This family is the catalytic domain of aromatic-ring- hydroxylating dioxygenase systems. The active site contains a non-heme ferrous ion coordinated by three ligands.


Pssm-ID: 425905  Cd Length: 210  Bit Score: 47.06  E-value: 5.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 208 KSNWKLYMENVKDPYHASMLHLFHTTFNIFRVGMKARSIPDANHGLHSIITVTKTNDDTSAAYKQQ--NIRSFDEGFHLE 285
Cdd:pfam00848  15 AANWKLAAENFLECYHVPVLHPELLRASPPEDLPPSEAAHFDGFGPHGRLGQGGDLRLTPAAASMTldAEAGRPELPGLP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 286 DEsilDLVSEYdedctnHIQpIFPQLVIQQIHNTLVARQILPKGPDNFELIFHFFgYADDTPELRALRIKQANLVGPAGY 365
Cdd:pfam00848  95 EE---QDRGAL------FYT-LFPNLSILLAPDHVVVYQLIPTGPDTTRVEVYWY-VPPDALAEPEFAEELEAVWDRTFG 163

                         170
                  ....*....|....*
gi 1167560559 366 ISMEDTEATELVQRG 380
Cdd:pfam00848 164 VNQEDAELCERVQRG 178
Rieske_RO_Alpha_OMO_CARDO cd03548
Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole ...
 53-179 6.43e-06

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: 45.49  E-value: 6.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559  53 WNFVALEAEIPNaGDFKSTFVGDTPVVVTRaEDGTLSAWVNRCAHRGAQVCRKSRG-NASSHTCVYHQWSFD-NQGNLlg 130
Cdd:cd03548    15 WYPALFSHELEE-GEPKGIQLCGEPILLRR-VDGKVYALKDRCLHRGVPLSKKPECfTKGTITCWYHGWTYRlDDGKL-- 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1167560559 131 vpfrrgqKGMTGMPADFDPKQHGLRKLRVDSYRGLVFATFSD----EVAPLPE 179
Cdd:cd03548    91 -------VTILANPDDPLIGRTGLKTYPVEEAKGMIFVFVGDgdyaDPPPLAH 136
Rieske_RO_Alpha_PhDO_like cd03479
Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, ...
 53-180 1.06e-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: 44.93  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559  53 WNFVALEAEIPNAGDFKSTFVGDTPVVVTRAEDGTLSAWVNRCAHRGAQVCRksrGNASSHT--CVYHQWSFDNQGNLLG 130
Cdd:cd03479    22 WQPVALSSELTEDGQPVRVRLLGEDLVAFRDTSGRVGLLDEHCPHRGASLVF---GRVEECGlrCCYHGWKFDVDGQCLE 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1167560559 131 VPFRrgqkgmtgmPADFDPKQhglrKLRVDSY-----RGLVFATFSD-EVAP-LPEY 180
Cdd:cd03479    99 MPSE---------PPDSQLKQ----KVRQPAYpvrerGGLVWAYMGPaEEAPeFPRY 142
RHO_alpha_C_1 cd08885
C-terminal catalytic domain of the oxygenase alpha subunit of an uncharacterized subgroup of ...
 210-381 1.70e-05

C-terminal catalytic domain of the oxygenase alpha subunit of an uncharacterized subgroup of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases; C-terminal catalytic domain of the oxygenase alpha subunit of a functionally uncharacterized subgroup of the Rieske-type non-heme iron aromatic ring-hydroxylating oxygenase (RHO) family. RHOs, also known as aromatic ring hydroxylating dioxygenases, 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 a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. This group contains two putative Parvibaculum lavamentivorans (T) DS-1 oxygenases; this organism catabolizes commercial linear alkylbenzenesulfonate surfactant (LAS) and other surfactants, by a pathway involving an undefined 'omega-oxygenation' and beta-oxidation of the LAS side chain. The nature of the LAS-oxygenase is unknown but is likely a multicomponent system. 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: 176894  Cd Length: 190  Bit Score: 45.44  E-value: 1.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 210 NWKLYMENVKDPYHASMLHlfHTTF-NIFRVGMKARSIPDANHglHSIITVTKTNDDTSAAYKQQNIRsfdegfhLEDEs 288
Cdd:cd08885    11 NWKVLAENFMEGYHLPGLH--PGTLhPFMPAELSYFRPEDGRG--FTRHKGTKHFNETIEPAHPPNPG-------LTEE- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559 289 ildlvseydEDCTNHIQPIFPQLVIQQIHNTLVARQILPKGPDNFELIFHFFGYADDTPELRALRIKqANLVGPAGYISM 368
Cdd:cd08885    79 ---------WRRRLVLFAIFPTHLLALTPDYVWWLSLLPEGAGRVRVRWGVLVAPEAADDPEAAEYI-AELKALLDAIND 148

                         170
                  ....*....|...
gi 1167560559 369 EDTEATELVQRGT 381
Cdd:cd08885   149 EDRLVVEGVQRGL 161
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 52-123 2.93e-05

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: 42.91  E-value: 2.93e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167560559  52 TWNFVALEAEIPnAGDFKSTFVGDTPVVVTRAeDGTLSAWVNRCAHRGAQVcrkSRG--NASSHTCVYHQWSFD 123
Cdd:COG2146     2 SEVKVCALDDLP-EGGGVVVEVGGKQIAVFRT-DGEVYAYDNRCPHQGAPL---SEGivDGGVVTCPLHGARFD 70
Rieske_RO_Alpha_Cao cd04337
Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the ...
 75-132 1.71e-04

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: 41.32  E-value: 1.71e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167560559  75 DTPVVVTRAEDGTLSAWVNRCAHRGaqvCRKSRG--NASSHTCVYHQWSFDNQGNLLGVP 132
Cdd:cd04337    39 GQPWVLFRDEDGTPGCIRDECAHRA---CPLSLGkvIEGRIQCPYHGWEYDGDGECTKMP 95
 
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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