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Conserved domains on  [gi|497366847|ref|WP_009681060|]
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benzoate 1,2-dioxygenase large subunit [Gordonia neofelifaecis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
benzo_1_2_benA super family cl31318
benzoate 1,2-dioxygenase, large subunit; Benzoate 1,2-dioxygenase (EC 1.14.12.10) belongs to ...
 29-460 0e+00

benzoate 1,2-dioxygenase, large subunit; Benzoate 1,2-dioxygenase (EC 1.14.12.10) belongs to the larger family of aromatic ring-hydroxylating dioxygenases. Members of this family all act on benzoate, but may have additional activities on various benozate analogs. This model describes the large subunit. Between the trusted and noise cutoffs are similar enzymes, likely to act on benzoate but perhaps best identified according to some other activity, such as 2-chlorobenzoate 1,2-dioxygenase (1.14.12.13). [Energy metabolism, Other]


The actual alignment was detected with superfamily member TIGR03229:

Pssm-ID: 132273 [Multi-domain]  Cd Length: 433  Bit Score: 805.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847   29 LDNAVIDDREAGVFRANRRIFTDEDVFELEMRHIFEGNWIYLAHESQVAKPGDYFTTYIGRQPIVITRGRDGELNCLINA 108
Cdd:TIGR03229   1 LDRLLEDDPEKGIFRCKREMFTDPELFDLEMKHIFEGNWIYLAHESQIPNNNDYYTTYMGRQPIFIARNKDGELNAFINA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  109 CAHRGAMICRRKTDNRMTLTCPFHGWTFRNDGTLLKVKDPEGAGYPATFDSEGSHNLTEVARFESYRGFLFGSLNPDVLP 188
Cdd:TIGR03229  81 CSHRGAMLCRHKRGNKTTYTCPFHGWTFNNSGKLLKVKDPEDAGYPECFNKDGSHDLKKVARFESYRGFLFGSLNPDVLP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  189 LDEHLGDTRQVIDMLVDQSPEGLEVLRGASTYTFDGNWKVQAENGADGYHVTATHWNYAATTSRRSTGESKNDAKVLDAG 268
Cdd:TIGR03229 161 LEEHLGETAKIIDMIVDQSPDGLEVLRGSSTYTYEGNWKLQAENGADGYHVSAVHWNYAATTNQRKQREAGDEIKAMSAG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  269 GWGKSGGGYWSYPNGHLCLWTWAANPQDRPLWDKMDELKAQFGDAKGEFMVKGSRNLCLYPNVYLMDQFSTQIRHFRPIA 348
Cdd:TIGR03229 241 TWGKQGGGSYSFEHGHMLLWTRWGNPEDRPLYERRDELAEKFGEAKADWMIENSRNLCLYPNVYLMDQFSSQIRVFRPIS 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  349 PDKTEVTIYCIAPKGESDAARAHRIRQYEDFFNASGMATPDDLEEFRSCQLTFRATAAPWNDMSRGSEHWLTGPDEVATA 428
Cdd:TIGR03229 321 VDKTEVTIYCIAPKGESAEARAKRIRQYEDFFNASGMATPDDLEEFRACQKGYNGTGLEWNDMSRGAKHWIEGPDEAAKE 400

                         410       420       430
                  ....*....|....*....|....*....|..
gi 497366847  429 LNMPNVISaGLKNEDEGLYPVQHGYWLETMRR 460
Cdd:TIGR03229 401 IGLNPVLS-GVRTEDEGLYVVQHHYWLDLMKR 431
 
Name Accession Description Interval E-value
benzo_1_2_benA TIGR03229
benzoate 1,2-dioxygenase, large subunit; Benzoate 1,2-dioxygenase (EC 1.14.12.10) belongs to ...
 29-460 0e+00

benzoate 1,2-dioxygenase, large subunit; Benzoate 1,2-dioxygenase (EC 1.14.12.10) belongs to the larger family of aromatic ring-hydroxylating dioxygenases. Members of this family all act on benzoate, but may have additional activities on various benozate analogs. This model describes the large subunit. Between the trusted and noise cutoffs are similar enzymes, likely to act on benzoate but perhaps best identified according to some other activity, such as 2-chlorobenzoate 1,2-dioxygenase (1.14.12.13). [Energy metabolism, Other]


Pssm-ID: 132273 [Multi-domain]  Cd Length: 433  Bit Score: 805.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847   29 LDNAVIDDREAGVFRANRRIFTDEDVFELEMRHIFEGNWIYLAHESQVAKPGDYFTTYIGRQPIVITRGRDGELNCLINA 108
Cdd:TIGR03229   1 LDRLLEDDPEKGIFRCKREMFTDPELFDLEMKHIFEGNWIYLAHESQIPNNNDYYTTYMGRQPIFIARNKDGELNAFINA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  109 CAHRGAMICRRKTDNRMTLTCPFHGWTFRNDGTLLKVKDPEGAGYPATFDSEGSHNLTEVARFESYRGFLFGSLNPDVLP 188
Cdd:TIGR03229  81 CSHRGAMLCRHKRGNKTTYTCPFHGWTFNNSGKLLKVKDPEDAGYPECFNKDGSHDLKKVARFESYRGFLFGSLNPDVLP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  189 LDEHLGDTRQVIDMLVDQSPEGLEVLRGASTYTFDGNWKVQAENGADGYHVTATHWNYAATTSRRSTGESKNDAKVLDAG 268
Cdd:TIGR03229 161 LEEHLGETAKIIDMIVDQSPDGLEVLRGSSTYTYEGNWKLQAENGADGYHVSAVHWNYAATTNQRKQREAGDEIKAMSAG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  269 GWGKSGGGYWSYPNGHLCLWTWAANPQDRPLWDKMDELKAQFGDAKGEFMVKGSRNLCLYPNVYLMDQFSTQIRHFRPIA 348
Cdd:TIGR03229 241 TWGKQGGGSYSFEHGHMLLWTRWGNPEDRPLYERRDELAEKFGEAKADWMIENSRNLCLYPNVYLMDQFSSQIRVFRPIS 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  349 PDKTEVTIYCIAPKGESDAARAHRIRQYEDFFNASGMATPDDLEEFRSCQLTFRATAAPWNDMSRGSEHWLTGPDEVATA 428
Cdd:TIGR03229 321 VDKTEVTIYCIAPKGESAEARAKRIRQYEDFFNASGMATPDDLEEFRACQKGYNGTGLEWNDMSRGAKHWIEGPDEAAKE 400

                         410       420       430
                  ....*....|....*....|....*....|..
gi 497366847  429 LNMPNVISaGLKNEDEGLYPVQHGYWLETMRR 460
Cdd:TIGR03229 401 IGLNPVLS-GVRTEDEGLYVVQHHYWLDLMKR 431
Rieske_RO_Alpha_HBDO cd03542
Rieske non-heme iron oxygenase (RO) family, 2-Halobenzoate 1,2-dioxygenase (HBDO) subfamily, ...
 67-189 7.68e-84

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: 253.91  E-value: 7.68e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  67 WIYLAHESQVAKPGDYFTTYIGRQPIVITRGRDGELNCLINACAHRGAMICRRKTDNRMTLTCPFHGWTFRNDGTLLKVK 146
Cdd:cd03542    1 WVYLAHESQIPNNNDYFTTTIGRQPVVITRDKDGELNAFINACSHRGAMLCRRKQGNKGTFTCPFHGWTFSNTGKLLKVK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 497366847 147 DPEGAGYPATFDSEGSHNLTEVARFESYRGFLFGSLNPDVLPL 189
Cdd:cd03542   81 DPKTAGYPEGFNCDGSHDLTKVARFESYRGFLFGSLNADVAPL 123
HcaE COG4638
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ...
 42-413 1.38e-80

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: 252.21  E-value: 1.38e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  42 FRANRRIFTDEDVFELEMRHIFEGNWIYLAHESQVAKPGDYFTTYIGRQPIVITRGRDGELNCLINACAHRGAMICRRKT 121
Cdd:COG4638    2 SRLPAAFYTDPEIFELELERIFRRGWYYVGHSSELPEPGDYLTRTILGEPVVLVRDKDGEVRAFHNVCPHRGAPLSEGRG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847 122 DNRmTLTCPFHGWTFRNDGTLLKVkdPEGAGYPaTFDsEGSHNLTEVaRFESYRGFLFGSLNPDVLPLDEHLGDTRQVID 201
Cdd:COG4638   82 NGG-RLVCPYHGWTYDLDGRLVGI--PHMEGFP-DFD-PARAGLRSV-PVEEWGGLIFVWLGPDAPPLAEYLGPLAEYLD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847 202 MLvdqSPEGLEVlRGASTYTFDGNWKVQAENGADGYHVTATHWnyaattsrrstgeskndakvldaggwgksgggywsyp 281
Cdd:COG4638  156 PY---DFGELKV-AGRETYEVNANWKLVVENFLDGYHVPFVHP------------------------------------- 194

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847 282 nghlclwtwaanpqdrplwdkmdelkaqfgdakgefmvkgSRNLCLYPNVYLMDQF-STQIRHFRPIAPDKTEVTIYCIA 360
Cdd:COG4638  195 ----------------------------------------GIILFLFPNLMILDYPdHLVVRTVTPVSPDRTRVFVTFYV 234

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 497366847 361 PKGESDAARAHRIRQYEDFFNAsgmatpDDLEEFRSCQLTFRATAAPWNDMSR 413
Cdd:COG4638  235 PKDALDPEARADLEAFWGRVFE------EDREIVERQQRGLRSLAYPGPYLSR 281
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 66-154 3.33e-23

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: 93.18  E-value: 3.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847   66 NWIYLAHESQVaKPGDYFTTYIGRQPIVITRGRDGELNCLINACAHRGAMICRRKTDNRMTLTCPFHGWTFRNDGTLLKV 145
Cdd:pfam00355   1 SWYPVCHSSEL-PEGEPKVVEVGGEPLVVFRDEDGELYALEDRCPHRGAPLSEGKVNGGGRLECPYHGWRFDGTGKVVKV 79

                          90
                  ....*....|
gi 497366847  146 KDPEG-AGYP 154
Cdd:pfam00355  80 PAPRPlKSYP 89
PLN02281 PLN02281
chlorophyllide a oxygenase
 90-146 1.58e-07

chlorophyllide a oxygenase


Pssm-ID: 177920 [Multi-domain]  Cd Length: 536  Bit Score: 53.58  E-value: 1.58e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497366847  90 QPIVITRGRDGELNCLINACAHRGAMIcRRKTDNRMTLTCPFHGWTFRNDG--------TLLKVK 146
Cdd:PLN02281 243 QPWVIFRGEDGKPGCVRNTCAHRACPL-DLGTVNEGRIQCPYHGWEYSTDGeckkmpstKLLKVK 306
 
Name Accession Description Interval E-value
benzo_1_2_benA TIGR03229
benzoate 1,2-dioxygenase, large subunit; Benzoate 1,2-dioxygenase (EC 1.14.12.10) belongs to ...
 29-460 0e+00

benzoate 1,2-dioxygenase, large subunit; Benzoate 1,2-dioxygenase (EC 1.14.12.10) belongs to the larger family of aromatic ring-hydroxylating dioxygenases. Members of this family all act on benzoate, but may have additional activities on various benozate analogs. This model describes the large subunit. Between the trusted and noise cutoffs are similar enzymes, likely to act on benzoate but perhaps best identified according to some other activity, such as 2-chlorobenzoate 1,2-dioxygenase (1.14.12.13). [Energy metabolism, Other]


Pssm-ID: 132273 [Multi-domain]  Cd Length: 433  Bit Score: 805.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847   29 LDNAVIDDREAGVFRANRRIFTDEDVFELEMRHIFEGNWIYLAHESQVAKPGDYFTTYIGRQPIVITRGRDGELNCLINA 108
Cdd:TIGR03229   1 LDRLLEDDPEKGIFRCKREMFTDPELFDLEMKHIFEGNWIYLAHESQIPNNNDYYTTYMGRQPIFIARNKDGELNAFINA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  109 CAHRGAMICRRKTDNRMTLTCPFHGWTFRNDGTLLKVKDPEGAGYPATFDSEGSHNLTEVARFESYRGFLFGSLNPDVLP 188
Cdd:TIGR03229  81 CSHRGAMLCRHKRGNKTTYTCPFHGWTFNNSGKLLKVKDPEDAGYPECFNKDGSHDLKKVARFESYRGFLFGSLNPDVLP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  189 LDEHLGDTRQVIDMLVDQSPEGLEVLRGASTYTFDGNWKVQAENGADGYHVTATHWNYAATTSRRSTGESKNDAKVLDAG 268
Cdd:TIGR03229 161 LEEHLGETAKIIDMIVDQSPDGLEVLRGSSTYTYEGNWKLQAENGADGYHVSAVHWNYAATTNQRKQREAGDEIKAMSAG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  269 GWGKSGGGYWSYPNGHLCLWTWAANPQDRPLWDKMDELKAQFGDAKGEFMVKGSRNLCLYPNVYLMDQFSTQIRHFRPIA 348
Cdd:TIGR03229 241 TWGKQGGGSYSFEHGHMLLWTRWGNPEDRPLYERRDELAEKFGEAKADWMIENSRNLCLYPNVYLMDQFSSQIRVFRPIS 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  349 PDKTEVTIYCIAPKGESDAARAHRIRQYEDFFNASGMATPDDLEEFRSCQLTFRATAAPWNDMSRGSEHWLTGPDEVATA 428
Cdd:TIGR03229 321 VDKTEVTIYCIAPKGESAEARAKRIRQYEDFFNASGMATPDDLEEFRACQKGYNGTGLEWNDMSRGAKHWIEGPDEAAKE 400

                         410       420       430
                  ....*....|....*....|....*....|..
gi 497366847  429 LNMPNVISaGLKNEDEGLYPVQHGYWLETMRR 460
Cdd:TIGR03229 401 IGLNPVLS-GVRTEDEGLYVVQHHYWLDLMKR 431
Rieske_RO_Alpha_HBDO cd03542
Rieske non-heme iron oxygenase (RO) family, 2-Halobenzoate 1,2-dioxygenase (HBDO) subfamily, ...
 67-189 7.68e-84

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: 253.91  E-value: 7.68e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  67 WIYLAHESQVAKPGDYFTTYIGRQPIVITRGRDGELNCLINACAHRGAMICRRKTDNRMTLTCPFHGWTFRNDGTLLKVK 146
Cdd:cd03542    1 WVYLAHESQIPNNNDYFTTTIGRQPVVITRDKDGELNAFINACSHRGAMLCRRKQGNKGTFTCPFHGWTFSNTGKLLKVK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 497366847 147 DPEGAGYPATFDSEGSHNLTEVARFESYRGFLFGSLNPDVLPL 189
Cdd:cd03542   81 DPKTAGYPEGFNCDGSHDLTKVARFESYRGFLFGSLNADVAPL 123
RHO_alpha_C_AntDO-like cd08879
C-terminal catalytic domain of the oxygenase alpha subunit of Pseudomonas resinovorans strain ...
 215-458 1.25e-82

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: 254.96  E-value: 1.25e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847 215 RGASTYTFDGNWKVQAENGADGYHVTATHWNYAATTSRRStgeSKNDAKVLDAGGWGKSGGGYWSYPNGHLCLWTWAANP 294
Cdd:cd08879    1 GGTHRYRYRGNWKLQLENGTDGYHPPFVHASYVATTGAAA---ADATRGGLSSFMTGPQGGGVRDLGNGHSVLDSRPEIP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847 295 QD------RPLWDKMDELKAQFGDAKGEFMVKGS-RNLCLYPNVYLMDQFStQIRHFRPIAPDKTEVTIYCIAPKGESDA 367
Cdd:cd08879   78 RLdadrpkPPIAEYRAALVAAHGEERARRILRGRgRNLNIFPNLFIIDISQ-QIRVIRPIAVDETEVTSWALRPKGAPDE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847 368 ARAHRIRQYEDFFNASGMATPDDLEEFRSCQLTFRATAAPWNDMSRGSEHWLTGPDEVATALNMpnvisaglkneDEGLY 447
Cdd:cd08879  157 VNRRRLRYSEDFFGPSGFATPDDLEAFERCQRGLAARGEEWVDLSRGLGREKADEDGVVTGAVT-----------DELPM 225

                        250
                 ....*....|.
gi 497366847 448 PVQHGYWLETM 458
Cdd:cd08879  226 RNQWRAWKRLM 236
HcaE COG4638
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ...
 42-413 1.38e-80

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: 252.21  E-value: 1.38e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  42 FRANRRIFTDEDVFELEMRHIFEGNWIYLAHESQVAKPGDYFTTYIGRQPIVITRGRDGELNCLINACAHRGAMICRRKT 121
Cdd:COG4638    2 SRLPAAFYTDPEIFELELERIFRRGWYYVGHSSELPEPGDYLTRTILGEPVVLVRDKDGEVRAFHNVCPHRGAPLSEGRG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847 122 DNRmTLTCPFHGWTFRNDGTLLKVkdPEGAGYPaTFDsEGSHNLTEVaRFESYRGFLFGSLNPDVLPLDEHLGDTRQVID 201
Cdd:COG4638   82 NGG-RLVCPYHGWTYDLDGRLVGI--PHMEGFP-DFD-PARAGLRSV-PVEEWGGLIFVWLGPDAPPLAEYLGPLAEYLD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847 202 MLvdqSPEGLEVlRGASTYTFDGNWKVQAENGADGYHVTATHWnyaattsrrstgeskndakvldaggwgksgggywsyp 281
Cdd:COG4638  156 PY---DFGELKV-AGRETYEVNANWKLVVENFLDGYHVPFVHP------------------------------------- 194

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847 282 nghlclwtwaanpqdrplwdkmdelkaqfgdakgefmvkgSRNLCLYPNVYLMDQF-STQIRHFRPIAPDKTEVTIYCIA 360
Cdd:COG4638  195 ----------------------------------------GIILFLFPNLMILDYPdHLVVRTVTPVSPDRTRVFVTFYV 234

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 497366847 361 PKGESDAARAHRIRQYEDFFNAsgmatpDDLEEFRSCQLTFRATAAPWNDMSR 413
Cdd:COG4638  235 PKDALDPEARADLEAFWGRVFE------EDREIVERQQRGLRSLAYPGPYLSR 281
Rieske_RO_Alpha_N cd03469
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ...
 67-189 3.06e-43

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: 148.51  E-value: 3.06e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  67 WIYLAHESQVAKPGDYFTTYIGRQPIVITRGRDGELNCLINACAHRGAMICRRKTDNRMTLTCPFHGWTFRNDGTLLKVK 146
Cdd:cd03469    1 WYFVGHSSELPEPGDYVTLELGGEPLVLVRDRDGEVRAFHNVCPHRGARLCEGRGGNAGRLVCPYHGWTYDLDGKLVGVP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 497366847 147 DPEGAGypaTFDSEgSHNLTEVaRFESYRGFLFGSLNPDVLPL 189
Cdd:cd03469   81 REEGFP---GFDKE-KLGLRTV-PVEEWGGLIFVNLDPDAPPL 118
Rieske_RO_Alpha_AntDO cd03538
Rieske non-heme iron oxygenase (RO) family, Anthranilate 1,2-dioxygenase (AntDO) subfamily, ...
 46-185 1.33e-42

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: 147.99  E-value: 1.33e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  46 RRIFTDEDVFELEMRHIFEGNWIYLAHESQVAKPGDYFTTYIGRQPIVITRGRDGELNCLINACAHRGAMICRRKTDNRM 125
Cdd:cd03538    2 KDVYTDPEIFALEMERLFGNAWIYVGHESQVPNPGDYITTRIGDQPVVMVRHTDGSVHVLYNRCPHKGTKIVSDGCGNTG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497366847 126 T-LTCPFHGWTFRNDGTLLKVkdPEGAGYPAT-FD-SEGSHNLTEVARFESYRGFLFGSLNPD 185
Cdd:cd03538   82 KfFRCPYHAWSFKTDGSLLAI--PLKKGYEGTgFDpSHADKGMQRVGAVDIYRGFVFARLSPS 142
Rieske_RO_Alpha_OHBDO_like cd03545
Rieske non-heme iron oxygenase (RO) family, Ortho-halobenzoate-1,2-dioxygenase (OHBDO)-like ...
 43-189 2.51e-41

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: 144.51  E-value: 2.51e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  43 RANRRIFTDEDVFELEMRHIFEGN-WIYLAHESQVAKPGDYFTTYIGRQPIVITRGRDGELNCLINACAHRGAMICRRKT 121
Cdd:cd03545    1 RVPYKVFTDRAYFDREQERIFRGKtWSYVGLEAEIPNAGDFKSTFVGDTPVVVTRAEDGSLHAWVNRCAHRGALVCRERR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497366847 122 DNRMTLTCPFHGWTFRNDGTLLKVKDPEG----AGYPATFDSEgSHNLTEVaRFESYRGFLFGSLNPDVLPL 189
Cdd:cd03545   81 GNDGSLTCVYHQWAYDLKGNLKGVPFRRGlkgqGGMPKDFDMK-QHGLEKL-RVETVGGLVFASFSDEVEPL 150
Rieske_RO_Alpha_NDO cd03535
Rieske non-heme iron oxygenase (RO) family, Nathphalene 1,2-dioxygenase (NDO) subfamily, ...
 67-189 6.48e-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: 131.78  E-value: 6.48e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  67 WIYLAHESQVAKPGDYFTTYIGRQPIVITRGRDGELNCLINACAHRGAMICRRKTDNRMTLTCPFHGWTFRNDGTLLKVK 146
Cdd:cd03535    3 WVFLGHESEIPNAGDYVVRYIGDDSFIVCRDEDGEIRAMFNSCRHRGMQVCRAEMGNTSHFRCPYHGWTYRNTGRLVGVP 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 497366847 147 DPEGAgYPATFDSEGsHNLTEVARFESYRGFLFGSLNPDVLPL 189
Cdd:cd03535   83 AQQEA-YGGGFDKSQ-WGLRPAPNLDSYNGLIFGSLDPKAPSL 123
Rieske_RO_Alpha_BPDO_like cd03472
Rieske non-heme iron oxygenase (RO) family, Biphenyl dioxygenase (BPDO)-like subfamily, ...
 59-185 1.65e-26

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: 103.77  E-value: 1.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  59 MRHIFEGNWIYLAHESQVAKPGDYFTTYIGRQPIVITRGRDGELNCLINACAHRGAMICRRKTDNRMTLTCPFHGWTFRN 138
Cdd:cd03472    1 LERVFARSWLLLGHETHIPKAGDYLTTYMGEDPVIVVRQKDGSIRVFLNQCRHRGMRICRSDAGNAKAFTCTYHGWAYDT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 497366847 139 DGTLLKVkdP-EGAGYPATFDSEGSHNLTevARFESYRGFLFGSLNPD 185
Cdd:cd03472   81 AGNLVNV--PfEKEAFCDGLDKADWGPLQ--ARVETYKGLIFANWDAE 124
Rieske_RO_Alpha_S5H cd03539
This alignment model represents the N-terminal rieske iron-sulfur domain of the oxygenase ...
 67-189 3.05e-23

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: 95.00  E-value: 3.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  67 WIYLAHESQVAKPGDYFTTYIGRQPIVITRGRDGELNCLINACAHRGAMICRRKTDNRMTLTCPFHGWTFRNDGTLLKVK 146
Cdd:cd03539    1 WCYVGLEAEIPNPGDFKRTLIGERSVIMTRDPDGGINVVENVCAHRGMRFCRERNGNAKDFVCPYHQWNYSLKGDLQGVP 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 497366847 147 DPEG--------AGYPATFDSEgSHNLTEVaRFESYRGFLFGSLNPDVLPL 189
Cdd:cd03539   81 FRRGvkkdgkvnGGMPKDFKTK-DHGLTKL-KVATRGGVVFASFDHDVESF 129
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 66-154 3.33e-23

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: 93.18  E-value: 3.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847   66 NWIYLAHESQVaKPGDYFTTYIGRQPIVITRGRDGELNCLINACAHRGAMICRRKTDNRMTLTCPFHGWTFRNDGTLLKV 145
Cdd:pfam00355   1 SWYPVCHSSEL-PEGEPKVVEVGGEPLVVFRDEDGELYALEDRCPHRGAPLSEGKVNGGGRLECPYHGWRFDGTGKVVKV 79

                          90
                  ....*....|
gi 497366847  146 KDPEG-AGYP 154
Cdd:pfam00355  80 PAPRPlKSYP 89
RHO_alpha_C_NDO-like cd08881
C-terminal catalytic domain of the oxygenase alpha subunit of naphthalene 1,2-dioxygenase (NDO) ...
 210-458 1.21e-19

C-terminal catalytic domain of the oxygenase alpha subunit of naphthalene 1,2-dioxygenase (NDO) and related aromatic ring hydroxylating dioxygenases; C-terminal catalytic domain of the oxygenase alpha subunit of naphthalene 1,2-dioxygenase (NDO) and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). This domain binds non-heme Fe(II). 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 form 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. Proteins belonging to this subgroup include the terminal oxygenase alpha subunits of biphenyl dioxygenase, cumene dioxygenase from Pseudomonas fluorescens IP01, ethylbenzene dioxygenase, naphthalene 1,2-dioxygenase, nitrobenzene dioxygenase from Comamonas sp. strain JS765, toluene 2,3-dioxygenase from Pseudomonas putida F1, dioxin dioxygenase of Sphingomonas sp. Strain RW1, and the polycyclic aromatic hydrocarbons (PAHs)degrading ring-hydroxylating dioxygenase from Sphingomonas CHY-1. 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: 176890 [Multi-domain]  Cd Length: 206  Bit Score: 86.92  E-value: 1.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847 210 GLEVLRGASTYTFDGNWKVQAEN-GADGYHVTATHwnyaATTSRRSTGESKNDAKVLDAGGWgksgggYWSYPNGHlclw 288
Cdd:cd08881    1 GLEVVGGPQKWVIKANWKLAAENfAGDGYHTGTTH----ASALEAGLPPDAADLPPIDLGLQ------FTAPWHGH---- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847 289 twaanpqdrplwdkmdelkaqfgdaKGEFMVKGSRNLCLYPNVYLMDQFSTQIRHFRPIAPDKTEVTIYCIAPKGESDAA 368
Cdd:cd08881   67 -------------------------GLGFFLDSPQHGTIFPNLSFLPGYFNTLRVWHPRGPDETEVWTWTLVDKDAPEEV 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847 369 RAHRIRQYEDFFNASGMATPDDLEEFRSCQLTFRATAA---PWN-DMSRGSEhwlTGPDEVatalnMPNVISAGLKNED- 443
Cdd:cd08881  122 KDRVRRQYTRTFGPAGTFEQDDGENWEEITRVARGYVArqvPLNyQMGLGVE---PEPDPG-----GPGIVGPGFYSEAn 193

                        250
                 ....*....|....*.
gi 497366847 444 -EGLYpvqhGYWLETM 458
Cdd:cd08881  194 qRGFY----RRWLELM 205
Rieske_RO_Alpha_DTDO cd03536
This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit ...
 67-185 1.06e-15

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: 73.43  E-value: 1.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  67 WIYLAHESQVAKPGDYFTTYIGRQPIVITRGRDGELNCLINACAHRGAMICRRKTDNRMTLTCPFHGWTFRNDGTLL--K 144
Cdd:cd03536    1 WVLLGHESEIPNKGDFMVRDMGSDSVIVARDKDGEIHVSLNVCPHRGMRISTTDGGNTQIHVCIYHGWAFRPNGDFIgaP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 497366847 145 VKDPEGAGYPATFDSEGSHNltevARFESYRGFLFGSLNPD 185
Cdd:cd03536   81 VEKECMHGKMRTKAELGLHK----ARVTLYGGLIFATWNID 117
RHO_alpha_C cd00680
C-terminal catalytic domain of the oxygenase alpha subunit of Rieske-type non-heme iron ...
 218-416 2.85e-15

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: 74.14  E-value: 2.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847 218 STYTFDGNWKVQAENGADGYHVTATHWNYAATTSRRSTGESKndakvldaggwgksgggywSYpnGHLCLWTWAANPQDR 297
Cdd:cd00680    3 YEYEVDCNWKLAVENFLECYHVPTVHPDTLATGLPLPLLFGD-------------------HY--RVDDTGEGPGEGLSR 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847 298 PLWDKMDELKAQFGDAKGEFmvkgsRNLCLYPNVYLMDQFST-QIRHFRPIAPDKTEVTIYCIAPKGESdaARAHRIRQY 376
Cdd:cd00680   62 HWGDGKGPQSALPGLKPGGY-----LYLYLFPNLMIGLYPDSlQVQQFVPIGPNKTRLEVRLYRPKDED--AREEFDAEL 134

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 497366847 377 EDFFNASGMATPDDLEEFRSCQLTFRATAAPWNDMSRGSE 416
Cdd:cd00680  135 ESLAGILRQVLDEDIELCERIQRGLRSGAFRGGPLSPLEE 174
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 67-161 4.07e-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: 70.98  E-value: 4.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  67 WIYLAHESQVaKPGDYFTTYIGRQPIVITRGRDGELNCLINACAHRGAMICRRKTDNRmTLTCPFHGWTFR-NDGTLlkV 145
Cdd:cd03467    1 WVVVGALSEL-PPGGGRVVVVGGGPVVVVRREGGEVYALSNRCTHQGCPLSEGEGEDG-CIVCPCHGSRFDlRTGEV--V 76

                         90
                 ....*....|....*....
gi 497366847 146 KDPEGAG---YPATFDSEG 161
Cdd:cd03467   77 SGPAPRPlpkYPVKVEGDG 95
Rieske_RO_Alpha_CMO cd03541
Rieske non-heme iron oxygenase (RO) family, Choline monooxygenase (CMO) subfamily, N-terminal ...
 67-144 8.59e-12

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: 62.18  E-value: 8.59e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497366847  67 WIYLAHESQVAKPGDYFTTYIGRQPIVITRGRDGELNCLINACAHRgAMICRRKTDNRMTLTCPFHGWTFRNDGTLLK 144
Cdd:cd03541    2 WQVAGYSDQVKEKNQYFTGRLGNVEYVVCRDGNGKLHAFHNVCTHR-ASILACGSGKKSCFVCPYHGWVYGLDGSLTK 78
PobA COG5749
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
90-243 4.92e-09

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


Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 57.70  E-value: 4.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  90 QPIVITRGRDGELNCLINACAHRGAMIC--RRKTDNrmtLTCPFHGWTFRNDGTLLKV-KDPEGAGYPATfdsegshnlt 166
Cdd:COG5749   42 EPLVIWRDSDGKVVALEDRCPHRGAPLSegRVEGGN---LRCPYHGWQFDGDGKCVHIpQLPENQPIPKN---------- 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847 167 evARFESY-----RGFLFgslnpdVLPldehlGDTRQVIDMLVDQSPE----GLEVLRgaSTYTFDGNWKVQAENGADGY 237
Cdd:COG5749  109 --AKVKSYpvqerYGLIW------VWL-----GDPPQADETPIPDIPElddpEWVATS--SVRDLECHYSRLIENLIDPS 173


                 ....*.
gi 497366847 238 HVTATH 243
Cdd:COG5749  174 HVPFVH 179
Ring_hydroxyl_A pfam00848
Ring hydroxylating alpha subunit (catalytic domain); This family is the catalytic domain of ...
 215-382 2.77e-08

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: 54.00  E-value: 2.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  215 RGASTYTFDGNWKVQAENGADGYHVTATHWNYAATTSRRSTGESKNdakvldagGWGKSGGGYWSYPNGHLCLWTWAANP 294
Cdd:pfam00848   7 VARITLDVAANWKLAAENFLECYHVPVLHPELLRASPPEDLPPSEA--------AHFDGFGPHGRLGQGGDLRLTPAAAS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  295 QDRPLWDKMDELKAQFGDAKGefmvkGSRNLCLYPNVY-LMDQFSTQIRHFRPIAPDKTEVTIYCIAPKGESdaARAHRI 373
Cdd:pfam00848  79 MTLDAEAGRPELPGLPEEQDR-----GALFYTLFPNLSiLLAPDHVVVYQLIPTGPDTTRVEVYWYVPPDAL--AEPEFA 151


                  ....*....
gi 497366847  374 RQYEDFFNA 382
Cdd:pfam00848 152 EELEAVWDR 160
PLN02281 PLN02281
chlorophyllide a oxygenase
 90-146 1.58e-07

chlorophyllide a oxygenase


Pssm-ID: 177920 [Multi-domain]  Cd Length: 536  Bit Score: 53.58  E-value: 1.58e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497366847  90 QPIVITRGRDGELNCLINACAHRGAMIcRRKTDNRMTLTCPFHGWTFRNDG--------TLLKVK 146
Cdd:PLN02281 243 QPWVIFRGEDGKPGCVRNTCAHRACPL-DLGTVNEGRIQCPYHGWEYSTDGeckkmpstKLLKVK 306
Rieske_RO_Alpha_Cao cd04337
Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the ...
 90-145 1.70e-07

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: 50.18  E-value: 1.70e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 497366847  90 QPIVITRGRDGELNCLINACAHRGAMICRRKTdNRMTLTCPFHGWTFRNDGTLLKV 145
Cdd:cd04337   40 QPWVLFRDEDGTPGCIRDECAHRACPLSLGKV-IEGRIQCPYHGWEYDGDGECTKM 94
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 66-137 2.38e-07

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: 48.68  E-value: 2.38e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497366847  66 NWIYLAHESQVAkPGDYFTTYIGRQPIVITRgRDGELNCLINACAHRGAMICRRKTDNRmTLTCPFHGWTFR 137
Cdd:COG2146    2 SEVKVCALDDLP-EGGGVVVEVGGKQIAVFR-TDGEVYAYDNRCPHQGAPLSEGIVDGG-VVTCPLHGARFD 70
Rieske_RO_Alpha_Tic55 cd04338
Tic55 is a 55kDa LLS1-related non-heme iron oxygenase associated with protein transport ...
 50-154 3.72e-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: 49.06  E-value: 3.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  50 TDEDVFELEMRHifegNW--IYLAHEsqVAKPGDY-FTTYigRQPIVITRGRDGELNCLINACAHRGAMICRRK-TDNRm 125
Cdd:cd04338    5 TPENVAEYDWRE----EWypLYLLKD--VPTDAPLgLSVY--DEPFVLFRDQNGQLRCLEDRCPHRLAKLSEGQlIDGK- 75

                         90       100       110
                 ....*....|....*....|....*....|
gi 497366847 126 tLTCPFHGWTFRNDGTLLKVKD-PEGAGYP 154
Cdd:cd04338   76 -LECLYHGWQFGGEGKCVKIPQlPADAKIP 104
Rieske_RO_Alpha_OMO_CARDO cd03548
Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole ...
 63-142 4.71e-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: 45.88  E-value: 4.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847  63 FEGNWiYLAHESQVAKPGDYFTTYIGRQPIVITRgRDGELNCLINACAHRGAMICRR---KTDNrmTLTCPFHGWTFR-N 138
Cdd:cd03548   11 FRNHW-YPALFSHELEEGEPKGIQLCGEPILLRR-VDGKVYALKDRCLHRGVPLSKKpecFTKG--TITCWYHGWTYRlD 86


                 ....
gi 497366847 139 DGTL 142
Cdd:cd03548   87 DGKL 90
PLN00095 PLN00095
chlorophyllide a oxygenase; Provisional
 91-145 1.29e-05

chlorophyllide a oxygenase; Provisional


Pssm-ID: 165668 [Multi-domain]  Cd Length: 394  Bit Score: 47.37  E-value: 1.29e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 497366847  91 PIVITRGRDGELNCLINACAHRGAMICRRKTDNRmTLTCPFHGWTFRNDGTLLKV 145
Cdd:PLN00095  97 PWVLFRDADGEAGCIKDECAHRACPLSLGKLVDG-KAQCPYHGWEYETGGECAKM 150
RHO_alpha_C_3 cd08887
C-terminal catalytic domain of the oxygenase alpha subunit of an uncharacterized subgroup of ...
 218-407 2.33e-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 a putative Parvibaculum lavamentivorans (T) DS-1 oxygenase; 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: 176896  Cd Length: 185  Bit Score: 44.99  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847 218 STYTFDGNWKVQAENGADGYHVTATHWN--YAATTSRRSTGESKndakvldaggwgksgggywsYPNGHLCL-WTWAANP 294
Cdd:cd08887    4 RRFDVAANWKLALDGFLEGYHFKVLHKNtiAPYFYDNLSVYDAF--------------------GPHSRIVFpRKSIESL 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497366847 295 QDRPL--WDKMDELKAQFgdakgefmvkgsrnlCLYPNVYL-MDQFSTQIRHFRPIAPDKTEVTIYCIAPKGESDAARAH 371
Cdd:cd08887   64 RDLPEdeWDLRRHLTVIY---------------TLFPNVSLlVQPDHLEIIQIEPGSPDRTRVTVYLLIPPPPDTEEARA 128

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 497366847 372 RIRQYEDFFNASGMAtpDDLEEFRSCQLTFRATAAP 407
Cdd:cd08887  129 YWDKNWDFLMAVVLD--EDFEVAEEIQRGLASGAND 162
Rieske_RO_Alpha_PhDO_like cd03479
Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, ...
 93-143 3.00e-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: 43.77  E-value: 3.00e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 497366847  93 VITRGRDGELNCLINACAHRGA-MICRRKTDNrmTLTCPFHGWTFRNDGTLL 143
Cdd:cd03479   48 VAFRDTSGRVGLLDEHCPHRGAsLVFGRVEEC--GLRCCYHGWKFDVDGQCL 97
Rieske_RO_Alpha_VanA_DdmC cd03532
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and ...
 90-150 5.22e-05

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: 42.74  E-value: 5.22e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497366847  90 QPIVITRGRDGELNCLINACAHRGAMICRRKTDNRmTLTCPFHGWTFRNDGTLLKVKDPEG 150
Cdd:cd03532   27 EPVVLYRTQDGRVAALEDRCPHRSAPLSKGSVEGG-GLVCGYHGLEFDSDGRCVHMPGQER 86
Rieske_RO_Alpha_PaO cd03480
Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, ...
 92-140 1.50e-03

Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of a small subfamily of enzymes found in plants as well as oxygenic cyanobacterial photosynthesizers including LLS1 (lethal leaf spot 1, also known as PaO) and ACD1 (accelerated cell death 1). ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. PaO expression increases upon physical wounding of plant leaves and is thought to catalyze a key step in chlorophyll degradation. The Arabidopsis-accelerated cell death gene ACD1 is involved in oxygenation of PaO.


Pssm-ID: 239562 [Multi-domain]  Cd Length: 138  Bit Score: 38.84  E-value: 1.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 497366847  92 IVITRGR-DGELNCLINACAHRGAMICRRKTDNRMTLTCPFHGWTFRNDG 140
Cdd:cd03480   42 LVIWWDRnSQQWRAFDDQCPHRLAPLSEGRIDEEGCLECPYHGWSFDGSG 91
PLN02518 PLN02518
pheophorbide a oxygenase
 87-150 3.67e-03

pheophorbide a oxygenase


Pssm-ID: 215283 [Multi-domain]  Cd Length: 539  Bit Score: 39.85  E-value: 3.67e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497366847  87 IGRQPIVITRGRDGELNCLINACAHRGAMICRRKTDNRMTLTCPFHGWTFRNDGTLLKVKD--PEG 150
Cdd:PLN02518 111 LGRDLVLWKDPNQGEWVAFDDKCPHRLAPLSEGRIDENGHLQCSYHGWSFDGCGSCTRIPQaaPEG 176
RHO_alpha_C_1 cd08885
C-terminal catalytic domain of the oxygenase alpha subunit of an uncharacterized subgroup of ...
 223-243 4.58e-03

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: 38.13  E-value: 4.58e-03
                         10        20
                 ....*....|....*....|.
gi 497366847 223 DGNWKVQAENGADGYHVTATH 243
Cdd:cd08885    9 DTNWKVLAENFMEGYHLPGLH 29
Rieske_RO_Alpha_KSH cd03531
The alignment model represents the N-terminal rieske iron-sulfur domain of KshA, the oxygenase ...
 92-140 4.91e-03

The alignment model represents the N-terminal rieske iron-sulfur domain of KshA, the oxygenase component of 3-ketosteroid 9-alpha-hydroxylase (KSH). The terminal oxygenase component of KSH is a key enzyme in the microbial steroid degradation pathway, catalyzing the 9 alpha-hydroxylation of 4-androstene-3,17-dione (AD) and 1,4-androstadiene-3,17-dione (ADD). KSH is a two-component class IA monooxygenase, with terminal oxygenase (KshA) and oxygenase reductase (KshB) components. KSH activity has been found in many actino- and proteo- bacterial genera including Rhodococcus, Nocardia, Arthrobacter, Mycobacterium, and Burkholderia.


Pssm-ID: 239607 [Multi-domain]  Cd Length: 115  Bit Score: 37.01  E-value: 4.91e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 497366847  92 IVITRGRDGELNCLINACAHRGAMICRR--KTDNrmtLTCPFHGWTFRNDG 140
Cdd:cd03531   26 LVVFADSDGALNVLDAYCRHMGGDLSQGtvKGDE---IACPFHDWRWGGDG 73
 
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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