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Conserved domains on  [gi|1525196418|gb|RQR95927|]
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hydroxyquinol 1,2-dioxygenase [Burkholderia sp. Bp8991]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PnpCD_PnpD_N super family cl39552
Hydroquinone 1,2-dioxygenase large subunit N-terminal; This is the N-terminal domain of the ...
 20-170 2.11e-87

Hydroquinone 1,2-dioxygenase large subunit N-terminal; This is the N-terminal domain of the alpha subunit, known as PnpD, of Hydroquinone 1,2-dioxygenase (PnpCD) present in Pseudomonas sp. strain WBC-3. PnpCD is the key enzyme in the degradation pathway of pollutant para-nitrophenol (PNP). The N-terminal domain residues Trp-76 and Phe-79 are indispensable in the formation of the active site pocket. The N-terminal domain also plays a vital role in formation of the heterotetrameric structure. Structural homologs of the N-terminal domain exhibit the nature to bind nucleic acids but due to the steric effect of the C-terminal domain, this N-terminal domain cannot bind nucleic acids.


The actual alignment was detected with superfamily member pfam18191:

Pssm-ID: 465673  Cd Length: 151  Bit Score: 259.63  E-value: 2.11e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525196418  20 ATQADAVTGYRRFHLGEFAFQRDEYFVKISWPAKGQTRTHAIPADAFLRAMMRDVAWGFFYGWVNFDHVFGTRNHYGKVD 99
Cdd:pfam18191   1 ASQPDAVTGYRSFRLGAFTLSRDEYFARIEWPAKGQLRSHLIPADAFLRAMMRDVAWGFFYGWVNFDAVIGTRNHYGKVD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525196418 100 VYAGTFNGILKEAGVDYTETFETPTIMATFKAMLHDWTNEGFDPFAAPEETGTAFGRKHGENGSAIERTRI 170
Cdd:pfam18191  81 LYAGTFNGVLKEAGVDYIEQFETPKIMATFKAILRDWTNAGFDPFAAPEETGSAFGRKHGDNIEAIERFRI 151
cupin_HQDO_large_C cd20492
hydroquinol 1,2-dioxygenase (HQDO) large subunit, C-terminal cupin domain; This model ...
 221-320 3.30e-77

hydroquinol 1,2-dioxygenase (HQDO) large subunit, C-terminal cupin domain; This model describes the C-terminal cupin domain of the large (or beta) subunit of hydroquinone 1,2-dioxygenase (HQDO), a heterotetramer of two alpha and two beta subunits of 19kDa and 38kDa, respectively. HQDO is a Fe(II) ring cleaving dioxygenase that is a key enzyme in the hydroquinone pathway of para-nitrophenol degradation, where it catalyzes the ring cleavage of hydroquinone to gamma-hydroxymuconic semialdehyde. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


:

Pssm-ID: 380449  Cd Length: 100  Bit Score: 231.73  E-value: 3.30e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525196418 221 KYLSRSDVTWNPSVTSVCGRSLFCPTTEEFILPVFHGNDRVEWFLQLSDEIVWDIGDKNTGAPRARVTMRAGDICAMPAD 300
Cdd:cd20492     1 KYLSRSDVTWNPSVTSVCKDSLFCPTTEEFILPVFHGNDRVEWFIQLSDEIVWDVKDKETGKPRARVTMRAGDVCAMPAD 80

                          90       100
                  ....*....|....*....|
gi 1525196418 301 IRHQGYSTKRSMLLVWENAT 320
Cdd:cd20492    81 IRHQGYSTKRSMLLVWENAS 100
 
Name Accession Description Interval E-value
PnpCD_PnpD_N pfam18191
Hydroquinone 1,2-dioxygenase large subunit N-terminal; This is the N-terminal domain of the ...
 20-170 2.11e-87

Hydroquinone 1,2-dioxygenase large subunit N-terminal; This is the N-terminal domain of the alpha subunit, known as PnpD, of Hydroquinone 1,2-dioxygenase (PnpCD) present in Pseudomonas sp. strain WBC-3. PnpCD is the key enzyme in the degradation pathway of pollutant para-nitrophenol (PNP). The N-terminal domain residues Trp-76 and Phe-79 are indispensable in the formation of the active site pocket. The N-terminal domain also plays a vital role in formation of the heterotetrameric structure. Structural homologs of the N-terminal domain exhibit the nature to bind nucleic acids but due to the steric effect of the C-terminal domain, this N-terminal domain cannot bind nucleic acids.


Pssm-ID: 465673  Cd Length: 151  Bit Score: 259.63  E-value: 2.11e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525196418  20 ATQADAVTGYRRFHLGEFAFQRDEYFVKISWPAKGQTRTHAIPADAFLRAMMRDVAWGFFYGWVNFDHVFGTRNHYGKVD 99
Cdd:pfam18191   1 ASQPDAVTGYRSFRLGAFTLSRDEYFARIEWPAKGQLRSHLIPADAFLRAMMRDVAWGFFYGWVNFDAVIGTRNHYGKVD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525196418 100 VYAGTFNGILKEAGVDYTETFETPTIMATFKAMLHDWTNEGFDPFAAPEETGTAFGRKHGENGSAIERTRI 170
Cdd:pfam18191  81 LYAGTFNGVLKEAGVDYIEQFETPKIMATFKAILRDWTNAGFDPFAAPEETGSAFGRKHGDNIEAIERFRI 151
cupin_HQDO_large_C cd20492
hydroquinol 1,2-dioxygenase (HQDO) large subunit, C-terminal cupin domain; This model ...
 221-320 3.30e-77

hydroquinol 1,2-dioxygenase (HQDO) large subunit, C-terminal cupin domain; This model describes the C-terminal cupin domain of the large (or beta) subunit of hydroquinone 1,2-dioxygenase (HQDO), a heterotetramer of two alpha and two beta subunits of 19kDa and 38kDa, respectively. HQDO is a Fe(II) ring cleaving dioxygenase that is a key enzyme in the hydroquinone pathway of para-nitrophenol degradation, where it catalyzes the ring cleavage of hydroquinone to gamma-hydroxymuconic semialdehyde. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380449  Cd Length: 100  Bit Score: 231.73  E-value: 3.30e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525196418 221 KYLSRSDVTWNPSVTSVCGRSLFCPTTEEFILPVFHGNDRVEWFLQLSDEIVWDIGDKNTGAPRARVTMRAGDICAMPAD 300
Cdd:cd20492     1 KYLSRSDVTWNPSVTSVCKDSLFCPTTEEFILPVFHGNDRVEWFIQLSDEIVWDVKDKETGKPRARVTMRAGDVCAMPAD 80

                          90       100
                  ....*....|....*....|
gi 1525196418 301 IRHQGYSTKRSMLLVWENAT 320
Cdd:cd20492    81 IRHQGYSTKRSMLLVWENAS 100
PRK13264 PRK13264
3-hydroxyanthranilate 3,4-dioxygenase; Provisional
 255-303 4.60e-03

3-hydroxyanthranilate 3,4-dioxygenase; Provisional


Pssm-ID: 183930  Cd Length: 177  Bit Score: 37.59  E-value: 4.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1525196418 255 FHGNDRVEWFLQLSDEIVWDIGDknTGAPRaRVTMRAGDICAMPADIRH 303
Cdd:PRK13264   49 FHYDPGEEFFYQLEGDMYLKVQE--DGKRR-DVPIREGEMFLLPPHVPH 94
 
Name Accession Description Interval E-value
PnpCD_PnpD_N pfam18191
Hydroquinone 1,2-dioxygenase large subunit N-terminal; This is the N-terminal domain of the ...
 20-170 2.11e-87

Hydroquinone 1,2-dioxygenase large subunit N-terminal; This is the N-terminal domain of the alpha subunit, known as PnpD, of Hydroquinone 1,2-dioxygenase (PnpCD) present in Pseudomonas sp. strain WBC-3. PnpCD is the key enzyme in the degradation pathway of pollutant para-nitrophenol (PNP). The N-terminal domain residues Trp-76 and Phe-79 are indispensable in the formation of the active site pocket. The N-terminal domain also plays a vital role in formation of the heterotetrameric structure. Structural homologs of the N-terminal domain exhibit the nature to bind nucleic acids but due to the steric effect of the C-terminal domain, this N-terminal domain cannot bind nucleic acids.


Pssm-ID: 465673  Cd Length: 151  Bit Score: 259.63  E-value: 2.11e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525196418  20 ATQADAVTGYRRFHLGEFAFQRDEYFVKISWPAKGQTRTHAIPADAFLRAMMRDVAWGFFYGWVNFDHVFGTRNHYGKVD 99
Cdd:pfam18191   1 ASQPDAVTGYRSFRLGAFTLSRDEYFARIEWPAKGQLRSHLIPADAFLRAMMRDVAWGFFYGWVNFDAVIGTRNHYGKVD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525196418 100 VYAGTFNGILKEAGVDYTETFETPTIMATFKAMLHDWTNEGFDPFAAPEETGTAFGRKHGENGSAIERTRI 170
Cdd:pfam18191  81 LYAGTFNGVLKEAGVDYIEQFETPKIMATFKAILRDWTNAGFDPFAAPEETGSAFGRKHGDNIEAIERFRI 151
cupin_HQDO_large_C cd20492
hydroquinol 1,2-dioxygenase (HQDO) large subunit, C-terminal cupin domain; This model ...
 221-320 3.30e-77

hydroquinol 1,2-dioxygenase (HQDO) large subunit, C-terminal cupin domain; This model describes the C-terminal cupin domain of the large (or beta) subunit of hydroquinone 1,2-dioxygenase (HQDO), a heterotetramer of two alpha and two beta subunits of 19kDa and 38kDa, respectively. HQDO is a Fe(II) ring cleaving dioxygenase that is a key enzyme in the hydroquinone pathway of para-nitrophenol degradation, where it catalyzes the ring cleavage of hydroquinone to gamma-hydroxymuconic semialdehyde. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380449  Cd Length: 100  Bit Score: 231.73  E-value: 3.30e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525196418 221 KYLSRSDVTWNPSVTSVCGRSLFCPTTEEFILPVFHGNDRVEWFLQLSDEIVWDIGDKNTGAPRARVTMRAGDICAMPAD 300
Cdd:cd20492     1 KYLSRSDVTWNPSVTSVCKDSLFCPTTEEFILPVFHGNDRVEWFIQLSDEIVWDVKDKETGKPRARVTMRAGDVCAMPAD 80

                          90       100
                  ....*....|....*....|
gi 1525196418 301 IRHQGYSTKRSMLLVWENAT 320
Cdd:cd20492    81 IRHQGYSTKRSMLLVWENAS 100
PRK13264 PRK13264
3-hydroxyanthranilate 3,4-dioxygenase; Provisional
 255-303 4.60e-03

3-hydroxyanthranilate 3,4-dioxygenase; Provisional


Pssm-ID: 183930  Cd Length: 177  Bit Score: 37.59  E-value: 4.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1525196418 255 FHGNDRVEWFLQLSDEIVWDIGDknTGAPRaRVTMRAGDICAMPADIRH 303
Cdd:PRK13264   49 FHYDPGEEFFYQLEGDMYLKVQE--DGKRR-DVPIREGEMFLLPPHVPH 94
 
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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