NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2698881663|ref|WP_337016585|]
View 

aromatic-ring-hydroxylating dioxygenase subunit beta [Leclercia sp. AS011]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HcaF COG5517
3-phenylpropionate/cinnamic acid dioxygenase, small subunit [Secondary metabolites ...
 2-159 1.45e-39

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


:

Pssm-ID: 444268  Cd Length: 162  Bit Score: 131.12  E-value: 1.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2698881663   2 TPDSALFAAMSVINLEGDLLDQGEFNAWLDLWQRDGLYVVPIDPN-ENDFKNTLNYACDDHHMRERRVKRLYSGESISTT 80
Cdd:COG5517     3 VDLELRAEVEQFLYREARLLDERRFDEWLALFTEDGHYWVPARENrDTDPGLPLSLIYDDRAMLEDRVARLRTGNAWAED 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2698881663  81 PRARTLRTLSRFRLLESSEDLIVVRGAQSLWEHR-KGHSRHYAADITWHLKSQDGRLLITRKVIRLVNSDDVLHSIGYIL 159
Cdd:COG5517    83 PPSRTRHLVSNVRVEETDGGEIEVRSNFLVYRTRrDGQTDLFVGRYEDRLRRTGGGLRIARRRVVLDNSVIPTKNLSYPL 162
 
Name Accession Description Interval E-value
HcaF COG5517
3-phenylpropionate/cinnamic acid dioxygenase, small subunit [Secondary metabolites ...
 2-159 1.45e-39

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


Pssm-ID: 444268  Cd Length: 162  Bit Score: 131.12  E-value: 1.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2698881663   2 TPDSALFAAMSVINLEGDLLDQGEFNAWLDLWQRDGLYVVPIDPN-ENDFKNTLNYACDDHHMRERRVKRLYSGESISTT 80
Cdd:COG5517     3 VDLELRAEVEQFLYREARLLDERRFDEWLALFTEDGHYWVPARENrDTDPGLPLSLIYDDRAMLEDRVARLRTGNAWAED 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2698881663  81 PRARTLRTLSRFRLLESSEDLIVVRGAQSLWEHR-KGHSRHYAADITWHLKSQDGRLLITRKVIRLVNSDDVLHSIGYIL 159
Cdd:COG5517    83 PPSRTRHLVSNVRVEETDGGEIEVRSNFLVYRTRrDGQTDLFVGRYEDRLRRTGGGLRIARRRVVLDNSVIPTKNLSYPL 162
ring_hydroxylating_dioxygenases_beta cd00667
Ring hydroxylating dioxygenase beta subunit. This subunit has a similar structure to NTF-2, ...
 17-158 4.85e-23

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: 88.86  E-value: 4.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2698881663  17 EGDLLDQGEFNAWLDLWQRDGLYVVP-----IDPNENDFKNTLNYACDDHHMRERRVKRLYSGESISTTPRARTLRTLSR 91
Cdd:cd00667    13 EARLLDDRRWDEWLALFAEDCHYWVParenrERRDEDPGLELSAIYDDDRRMLEDRVVRLRTGRAWSEDPPSRTRHLVSN 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2698881663  92 FRLLESSEDLIVVRGAQSLWEHR-KGHSRHYAADITWHLKSQDGRLLITRKVIRLVNSDDVLHSIGYI 158
Cdd:cd00667    93 VRVLEGDGGEIEVRSNFVVVRTRlDGESDVFAGGRYDDLRRSEDGLRIASRRVVLDNDRIPTVNLSPF 160
Ring_hydroxyl_B pfam00866
Ring hydroxylating beta subunit; This subunit has a similar structure to NTF-2 and scytalone ...
 17-148 9.84e-11

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


Pssm-ID: 425916  Cd Length: 144  Bit Score: 56.53  E-value: 9.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2698881663  17 EGDLLDQGEFNAWLDLWQRDGLYVVP-----IDPNENDFKNTLNYACDDHHMRERRVKRLYSGESISTTPRARTLRTLSR 91
Cdd:pfam00866   2 EARLLDDRDWDAWLALLAEDIHYWMPqredrQRRDRDPQREESAIFDDDRAGLEDRVFRIRTGRAWAEDPPSRTRHLVSN 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2698881663  92 FRLLESSED-LIVVRGAQSLWEHR-KGHSRHYAADITWHLKSQDGRLLITRKVIRLVNS 148
Cdd:pfam00866  82 VRVEETEADgELEVRSNFIVYRNRlERQVDSFAGRRTDVLRRSGDGFKIARRTILLDNS 140
 
Name Accession Description Interval E-value
HcaF COG5517
3-phenylpropionate/cinnamic acid dioxygenase, small subunit [Secondary metabolites ...
 2-159 1.45e-39

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


Pssm-ID: 444268  Cd Length: 162  Bit Score: 131.12  E-value: 1.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2698881663   2 TPDSALFAAMSVINLEGDLLDQGEFNAWLDLWQRDGLYVVPIDPN-ENDFKNTLNYACDDHHMRERRVKRLYSGESISTT 80
Cdd:COG5517     3 VDLELRAEVEQFLYREARLLDERRFDEWLALFTEDGHYWVPARENrDTDPGLPLSLIYDDRAMLEDRVARLRTGNAWAED 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2698881663  81 PRARTLRTLSRFRLLESSEDLIVVRGAQSLWEHR-KGHSRHYAADITWHLKSQDGRLLITRKVIRLVNSDDVLHSIGYIL 159
Cdd:COG5517    83 PPSRTRHLVSNVRVEETDGGEIEVRSNFLVYRTRrDGQTDLFVGRYEDRLRRTGGGLRIARRRVVLDNSVIPTKNLSYPL 162
ring_hydroxylating_dioxygenases_beta cd00667
Ring hydroxylating dioxygenase beta subunit. This subunit has a similar structure to NTF-2, ...
 17-158 4.85e-23

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: 88.86  E-value: 4.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2698881663  17 EGDLLDQGEFNAWLDLWQRDGLYVVP-----IDPNENDFKNTLNYACDDHHMRERRVKRLYSGESISTTPRARTLRTLSR 91
Cdd:cd00667    13 EARLLDDRRWDEWLALFAEDCHYWVParenrERRDEDPGLELSAIYDDDRRMLEDRVVRLRTGRAWSEDPPSRTRHLVSN 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2698881663  92 FRLLESSEDLIVVRGAQSLWEHR-KGHSRHYAADITWHLKSQDGRLLITRKVIRLVNSDDVLHSIGYI 158
Cdd:cd00667    93 VRVLEGDGGEIEVRSNFVVVRTRlDGESDVFAGGRYDDLRRSEDGLRIASRRVVLDNDRIPTVNLSPF 160
Ring_hydroxyl_B pfam00866
Ring hydroxylating beta subunit; This subunit has a similar structure to NTF-2 and scytalone ...
 17-148 9.84e-11

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


Pssm-ID: 425916  Cd Length: 144  Bit Score: 56.53  E-value: 9.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2698881663  17 EGDLLDQGEFNAWLDLWQRDGLYVVP-----IDPNENDFKNTLNYACDDHHMRERRVKRLYSGESISTTPRARTLRTLSR 91
Cdd:pfam00866   2 EARLLDDRDWDAWLALLAEDIHYWMPqredrQRRDRDPQREESAIFDDDRAGLEDRVFRIRTGRAWAEDPPSRTRHLVSN 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2698881663  92 FRLLESSED-LIVVRGAQSLWEHR-KGHSRHYAADITWHLKSQDGRLLITRKVIRLVNS 148
Cdd:pfam00866  82 VRVEETEADgELEVRSNFIVYRNRlERQVDSFAGRRTDVLRRSGDGFKIARRTILLDNS 140
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH