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Conserved domains on  [gi|499720141|ref|WP_011400875|]
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aromatic-ring-hydroxylating dioxygenase subunit beta [Burkholderia thailandensis]

Protein Classification

aromatic-ring-hydroxylating dioxygenase subunit beta( domain architecture ID 10791045)

aromatic-ring-hydroxylating dioxygenase subunit beta is part of the hydroxylase component of a dioxygenase multicomponent enzyme system that catalyzes the oxidation or hydroxylation of aromatic compounds; the beta subunit may be responsible for substrate specificity and/or may have a structural role

EC:  1.14.-.-
Gene Ontology:  GO:0006725|GO:0019439
SCOP:  3000472|4001024

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HcaF COG5517
3-phenylpropionate/cinnamic acid dioxygenase, small subunit [Secondary metabolites ...
 7-166 1.54e-40

3-phenylpropionate/cinnamic acid dioxygenase, small subunit [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 444268  Cd Length: 162  Bit Score: 133.81  E-value: 1.54e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499720141   7 APFTDRALARAVEFIWREAELLDRRDYRGWLALWNPAGHYVVPIDP-AATDFEATLNYVYDDHEMREKRVERMLSGHSAS 85
Cdd:COG5517    1 AAVDLELRAEVEQFLYREARLLDERRFDEWLALFTEDGHYWVPAREnRDTDPGLPLSLIYDDRAMLEDRVARLRTGNAWA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499720141  86 ASDAARTVRTVSRFTLERESADTIEVKSAQVVVAYKRGAAT-LFAADVAHRLELRGGDVRLAEKVIRLIDSTDALSAIGF 164
Cdd:COG5517   81 EDPPSRTRHLVSNVRVEETDGGEIEVRSNFLVYRTRRDGQTdLFVGRYEDRLRRTGGGLRIARRRVVLDNSVIPTKNLSY 160


                 ..
gi 499720141 165 LL 166
Cdd:COG5517  161 PL 162
 
Name Accession Description Interval E-value
HcaF COG5517
3-phenylpropionate/cinnamic acid dioxygenase, small subunit [Secondary metabolites ...
 7-166 1.54e-40

3-phenylpropionate/cinnamic acid dioxygenase, small subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 444268  Cd Length: 162  Bit Score: 133.81  E-value: 1.54e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499720141   7 APFTDRALARAVEFIWREAELLDRRDYRGWLALWNPAGHYVVPIDP-AATDFEATLNYVYDDHEMREKRVERMLSGHSAS 85
Cdd:COG5517    1 AAVDLELRAEVEQFLYREARLLDERRFDEWLALFTEDGHYWVPAREnRDTDPGLPLSLIYDDRAMLEDRVARLRTGNAWA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499720141  86 ASDAARTVRTVSRFTLERESADTIEVKSAQVVVAYKRGAAT-LFAADVAHRLELRGGDVRLAEKVIRLIDSTDALSAIGF 164
Cdd:COG5517   81 EDPPSRTRHLVSNVRVEETDGGEIEVRSNFLVYRTRRDGQTdLFVGRYEDRLRRTGGGLRIARRRVVLDNSVIPTKNLSY 160


                 ..
gi 499720141 165 LL 166
Cdd:COG5517  161 PL 162
ring_hydroxylating_dioxygenases_beta cd00667
Ring hydroxylating dioxygenase beta subunit. This subunit has a similar structure to NTF-2, ...
 12-165 1.43e-29

Ring hydroxylating dioxygenase beta subunit. This subunit has a similar structure to NTF-2, Ketosteroid isomerase and scytalone dehydratase.The degradation of aromatic compounds by aerobic bacteria frequently begins with the dihydroxylation of the substrate by nonheme iron-containing dioxygenases. These enzymes consist of two or three soluble proteins that interact to form an electron-transport chain that transfers electrons from reduced nucleotides (NADH) via flavin and [2Fe-2S] redox centers to a terminal dioxygenase. Aromatic-ring-hydroxylating dioxygenases oxidize aromatic hydrocarbons and related compounds to cis-arene diols. These enzymes utilize a mononuclear non-heme iron center to catalyze the addition of dioxygen to their respective substrates. The active site of these enzymes however is in the alpha sub-unit. No functional role has been attributed to the beta sub-unit except for a structural role.


Pssm-ID: 238357  Cd Length: 160  Bit Score: 105.80  E-value: 1.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499720141  12 RALARAVEFIWREAELLDRRDYRGWLALWNPAGHYVVPI--DPAATDFEATLNYV---YDDHEMREKRVERMLSGHSASA 86
Cdd:cd00667    1 DLQAEVEQFLYREARLLDDRRWDEWLALFAEDCHYWVPAreNRERRDEDPGLELSaiyDDDRRMLEDRVVRLRTGRAWSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499720141  87 SDAARTVRTVSRFTLERESADTIEVKSAQVVVAYKRGAAT-LFAADVAHRLELRGGDVRLAEKVIRLIDSTDALSAIGFL 165
Cdd:cd00667   81 DPPSRTRHLVSNVRVLEGDGGEIEVRSNFVVVRTRLDGESdVFAGGRYDDLRRSEDGLRIASRRVVLDNDRIPTVNLSPF 160
Ring_hydroxyl_B pfam00866
Ring hydroxylating beta subunit; This subunit has a similar structure to NTF-2 and scytalone ...
 23-156 3.71e-20

Ring hydroxylating beta subunit; This subunit has a similar structure to NTF-2 and scytalone dehydratase.


Pssm-ID: 425916  Cd Length: 144  Bit Score: 81.19  E-value: 3.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499720141   23 REAELLDRRDYRGWLALWNPAGHYVVP-----IDPAATDFEATLNYVYDDHEMREKRVERMLSGHSASASDAARTVRTVS 97
Cdd:pfam00866   1 REARLLDDRDWDAWLALLAEDIHYWMPqredrQRRDRDPQREESAIFDDDRAGLEDRVFRIRTGRAWAEDPPSRTRHLVS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499720141   98 RFTL-ERESADTIEVKSAQVVVAYKRGA-ATLFAADVAHRLELRGGDVRLAEKVIRLIDST 156
Cdd:pfam00866  81 NVRVeETEADGELEVRSNFIVYRNRLERqVDSFAGRRTDVLRRSGDGFKIARRTILLDNSV 141
PRK10069 PRK10069
3-phenylpropionate/cinnamic acid dioxygenase subunit beta;
14-118 1.22e-06

3-phenylpropionate/cinnamic acid dioxygenase subunit beta;


Pssm-ID: 236647  Cd Length: 183  Bit Score: 46.17  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499720141  14 LARAVEFIWREAELLDRRDYRGWLALWNPAGHYVVPI----------DPAATDFEATLNYVYDDHEMREKRVERMLSGHS 83
Cdd:PRK10069  19 HHEISQFLYREARLLDEWRYDDWLALLAEDIHYTMPMrttvnaqrrdRREGVQTPPTMAWFDDNKDQLERRVARLETGMA 98

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 499720141  84 ASASDAARTVRTVSRFTLER-ESADTIEVKSAQVVV 118
Cdd:PRK10069  99 WAEEPPSRLRHLITNVRVEEtDIPDEFAVRSNFLLY 134
 
Name Accession Description Interval E-value
HcaF COG5517
3-phenylpropionate/cinnamic acid dioxygenase, small subunit [Secondary metabolites ...
 7-166 1.54e-40

3-phenylpropionate/cinnamic acid dioxygenase, small subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 444268  Cd Length: 162  Bit Score: 133.81  E-value: 1.54e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499720141   7 APFTDRALARAVEFIWREAELLDRRDYRGWLALWNPAGHYVVPIDP-AATDFEATLNYVYDDHEMREKRVERMLSGHSAS 85
Cdd:COG5517    1 AAVDLELRAEVEQFLYREARLLDERRFDEWLALFTEDGHYWVPAREnRDTDPGLPLSLIYDDRAMLEDRVARLRTGNAWA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499720141  86 ASDAARTVRTVSRFTLERESADTIEVKSAQVVVAYKRGAAT-LFAADVAHRLELRGGDVRLAEKVIRLIDSTDALSAIGF 164
Cdd:COG5517   81 EDPPSRTRHLVSNVRVEETDGGEIEVRSNFLVYRTRRDGQTdLFVGRYEDRLRRTGGGLRIARRRVVLDNSVIPTKNLSY 160


                 ..
gi 499720141 165 LL 166
Cdd:COG5517  161 PL 162
ring_hydroxylating_dioxygenases_beta cd00667
Ring hydroxylating dioxygenase beta subunit. This subunit has a similar structure to NTF-2, ...
 12-165 1.43e-29

Ring hydroxylating dioxygenase beta subunit. This subunit has a similar structure to NTF-2, Ketosteroid isomerase and scytalone dehydratase.The degradation of aromatic compounds by aerobic bacteria frequently begins with the dihydroxylation of the substrate by nonheme iron-containing dioxygenases. These enzymes consist of two or three soluble proteins that interact to form an electron-transport chain that transfers electrons from reduced nucleotides (NADH) via flavin and [2Fe-2S] redox centers to a terminal dioxygenase. Aromatic-ring-hydroxylating dioxygenases oxidize aromatic hydrocarbons and related compounds to cis-arene diols. These enzymes utilize a mononuclear non-heme iron center to catalyze the addition of dioxygen to their respective substrates. The active site of these enzymes however is in the alpha sub-unit. No functional role has been attributed to the beta sub-unit except for a structural role.


Pssm-ID: 238357  Cd Length: 160  Bit Score: 105.80  E-value: 1.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499720141  12 RALARAVEFIWREAELLDRRDYRGWLALWNPAGHYVVPI--DPAATDFEATLNYV---YDDHEMREKRVERMLSGHSASA 86
Cdd:cd00667    1 DLQAEVEQFLYREARLLDDRRWDEWLALFAEDCHYWVPAreNRERRDEDPGLELSaiyDDDRRMLEDRVVRLRTGRAWSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499720141  87 SDAARTVRTVSRFTLERESADTIEVKSAQVVVAYKRGAAT-LFAADVAHRLELRGGDVRLAEKVIRLIDSTDALSAIGFL 165
Cdd:cd00667   81 DPPSRTRHLVSNVRVLEGDGGEIEVRSNFVVVRTRLDGESdVFAGGRYDDLRRSEDGLRIASRRVVLDNDRIPTVNLSPF 160
Ring_hydroxyl_B pfam00866
Ring hydroxylating beta subunit; This subunit has a similar structure to NTF-2 and scytalone ...
 23-156 3.71e-20

Ring hydroxylating beta subunit; This subunit has a similar structure to NTF-2 and scytalone dehydratase.


Pssm-ID: 425916  Cd Length: 144  Bit Score: 81.19  E-value: 3.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499720141   23 REAELLDRRDYRGWLALWNPAGHYVVP-----IDPAATDFEATLNYVYDDHEMREKRVERMLSGHSASASDAARTVRTVS 97
Cdd:pfam00866   1 REARLLDDRDWDAWLALLAEDIHYWMPqredrQRRDRDPQREESAIFDDDRAGLEDRVFRIRTGRAWAEDPPSRTRHLVS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499720141   98 RFTL-ERESADTIEVKSAQVVVAYKRGA-ATLFAADVAHRLELRGGDVRLAEKVIRLIDST 156
Cdd:pfam00866  81 NVRVeETEADGELEVRSNFIVYRNRLERqVDSFAGRRTDVLRRSGDGFKIARRTILLDNSV 141
NTF2_like cd00531
Nuclear transport factor 2 (NTF2-like) superfamily. This family includes members of the NTF2 ...
 17-153 3.35e-08

Nuclear transport factor 2 (NTF2-like) superfamily. This family includes members of the NTF2 family, Delta-5-3-ketosteroid isomerases, Scytalone Dehydratases, and the beta subunit of Ring hydroxylating dioxygenases. This family is a classic example of divergent evolution wherein the proteins have many common structural details but diverge greatly in their function. For example, nuclear transport factor 2 (NTF2) mediates the nuclear import of RanGDP and binds to both RanGDP and FxFG repeat-containing nucleoporins while Ketosteroid isomerases catalyze the isomerization of delta-5-3-ketosteroid to delta-4-3-ketosteroid, by intramolecular transfer of the C4-beta proton to the C6-beta position. While the function of the beta sub-unit of the Ring hydroxylating dioxygenases is not known, Scytalone Dehydratases catalyzes two reactions in the biosynthetic pathway that produces fungal melanin. Members of the NTF2-like superfamily are widely distributed among bacteria, archaea and eukaryotes.


Pssm-ID: 238296 [Multi-domain]  Cd Length: 124  Bit Score: 49.44  E-value: 3.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499720141  17 AVEFIWREAELLDRRDyRGWLALWNPAGHYVVPIDPAATDfeatlnYVYDDHEMREKRVERMLSGHSasasdaaRTVRTV 96
Cdd:cd00531    1 AEQFLYRYARLLDAGD-REWLALLYADDAYFEPPGGDGLI------YPDDGREAIEDRVRRLPFGPS-------RTRHLV 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499720141  97 SRFTLERESADTIEVKSAQVVVAYKR-GAATLFAADVAHRLELRGGDVRLAEKVIRLI 153
Cdd:cd00531   67 SNVDVQPGDDGEGVVVSVFGVLRTRGdGEQDVFAGGQTFVLRPQGGGGKIANRRFRLD 124
PRK10069 PRK10069
3-phenylpropionate/cinnamic acid dioxygenase subunit beta;
14-118 1.22e-06

3-phenylpropionate/cinnamic acid dioxygenase subunit beta;


Pssm-ID: 236647  Cd Length: 183  Bit Score: 46.17  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499720141  14 LARAVEFIWREAELLDRRDYRGWLALWNPAGHYVVPI----------DPAATDFEATLNYVYDDHEMREKRVERMLSGHS 83
Cdd:PRK10069  19 HHEISQFLYREARLLDEWRYDDWLALLAEDIHYTMPMrttvnaqrrdRREGVQTPPTMAWFDDNKDQLERRVARLETGMA 98

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 499720141  84 ASASDAARTVRTVSRFTLER-ESADTIEVKSAQVVV 118
Cdd:PRK10069  99 WAEEPPSRLRHLITNVRVEEtDIPDEFAVRSNFLLY 134
 
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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