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Conserved domains on  [gi|1084852303|gb|OGQ83267|]
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hypothetical protein A3F90_10965 [Deltaproteobacteria bacterium RIFCSPLOWO2_12_FULL_60_19]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cupin_HAO cd06123
3-Hydroxyanthranilate-3,4-dioxygenase, cupin domain; 3-Hydroxyanthranilate-3,4-dioxygenase ...
 13-162 1.35e-61

3-Hydroxyanthranilate-3,4-dioxygenase, cupin domain; 3-Hydroxyanthranilate-3,4-dioxygenase (HAO or 3HAO) is a non-heme iron-dependent extradiol dioxygenase that catalyzes the oxidative ring opening of 3-hydroxyanthranilate (3-HAA) in the final enzymatic step of the kynurenine biosynthetic pathway in which tryptophan is converted to quinolinate, an endogenous neurotoxin, making HAO a target for pharmacological downregulation. Quinolate is also the universal de novo precursor to the pyridine ring of nicotinamide adenine dinucleotide. The enzyme forms homodimers, with two metal binding sites per molecule. One of the bound metal ions occupies the proposed ferrous-coordinated active site, which is located in a conserved double-strand beta-helix domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


:

Pssm-ID: 380378  Cd Length: 153  Bit Score: 187.31  E-value: 1.35e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084852303  13 IENVRSAGK---GRSILWQDSESIAFLSRGRKMRRDFHIDPSDEVTLQLAGEQRLHYKTPeGEEKIALIQPGQALLCPGG 89
Cdd:cd06123     3 IEENRHLLKppvGNKLLWQDSDFIVMVVGGPNSRKDFHINPGEEFFYQLKGDMVLKVIEP-GKFKDVVIKEGEIFLLPAR 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084852303  90 VPHSPRVTEDAWFVVFERKRRPGEEDRFLWFCETCGEKVYDVAAYVgDYSLDPVSKVHERFYGDESLRTCKKC 162
Cdd:cd06123    82 VPHSPQRPADTVGLVIERKRPPGELDGLRWYCENCGELLHEVEFHC-DDLGTQLKPAIEEFFASEELRTCKPC 153
 
Name Accession Description Interval E-value
cupin_HAO cd06123
3-Hydroxyanthranilate-3,4-dioxygenase, cupin domain; 3-Hydroxyanthranilate-3,4-dioxygenase ...
 13-162 1.35e-61

3-Hydroxyanthranilate-3,4-dioxygenase, cupin domain; 3-Hydroxyanthranilate-3,4-dioxygenase (HAO or 3HAO) is a non-heme iron-dependent extradiol dioxygenase that catalyzes the oxidative ring opening of 3-hydroxyanthranilate (3-HAA) in the final enzymatic step of the kynurenine biosynthetic pathway in which tryptophan is converted to quinolinate, an endogenous neurotoxin, making HAO a target for pharmacological downregulation. Quinolate is also the universal de novo precursor to the pyridine ring of nicotinamide adenine dinucleotide. The enzyme forms homodimers, with two metal binding sites per molecule. One of the bound metal ions occupies the proposed ferrous-coordinated active site, which is located in a conserved double-strand beta-helix domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380378  Cd Length: 153  Bit Score: 187.31  E-value: 1.35e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084852303  13 IENVRSAGK---GRSILWQDSESIAFLSRGRKMRRDFHIDPSDEVTLQLAGEQRLHYKTPeGEEKIALIQPGQALLCPGG 89
Cdd:cd06123     3 IEENRHLLKppvGNKLLWQDSDFIVMVVGGPNSRKDFHINPGEEFFYQLKGDMVLKVIEP-GKFKDVVIKEGEIFLLPAR 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084852303  90 VPHSPRVTEDAWFVVFERKRRPGEEDRFLWFCETCGEKVYDVAAYVgDYSLDPVSKVHERFYGDESLRTCKKC 162
Cdd:cd06123    82 VPHSPQRPADTVGLVIERKRPPGELDGLRWYCENCGELLHEVEFHC-DDLGTQLKPAIEEFFASEELRTCKPC 153
PRK13264 PRK13264
3-hydroxyanthranilate 3,4-dioxygenase; Provisional
 1-165 1.04e-39

3-hydroxyanthranilate 3,4-dioxygenase; Provisional


Pssm-ID: 183930  Cd Length: 177  Bit Score: 132.35  E-value: 1.04e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084852303   1 MKDLIAVDLNGAIENVRSAGK---GRSILWQDSESIAFLSRGRKMRRDFHIDPSDEVTLQLAGEQRLHYKTpEGEEKIAL 77
Cdd:PRK13264    1 MKILKPFNLHKWIEEHRHLLKppvGNKQIWQDSDFIVMVVGGPNARTDFHYDPGEEFFYQLEGDMYLKVQE-DGKRRDVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084852303  78 IQPGQALLCPGGVPHSPRVTEDAWFVVFERKRRPGEEDRFLWFCETCGEKVYDVAAYVGDYSLDpVSKVHERFYGDESLR 157
Cdd:PRK13264   80 IREGEMFLLPPHVPHSPQREAGSIGLVIERKRPEGELDGFQWYCDECNHKVHEVEVQLTDIETD-LPPVFAAFYASEELR 158


                  ....*...
gi 1084852303 158 TCKKCGTV 165
Cdd:PRK13264  159 TCDNCGTV 166
anthran_nbaC TIGR03037
3-hydroxyanthranilate 3,4-dioxygenase; Members of this protein family, from both bacteria and ...
 22-164 2.98e-36

3-hydroxyanthranilate 3,4-dioxygenase; Members of this protein family, from both bacteria and eukaryotes, are the enzyme 3-hydroxyanthranilate 3,4-dioxygenase. This enzyme acts on the tryptophan metabolite 3-hydroxyanthranilate and produces 2-amino-3-carboxymuconate semialdehyde, which can rearrange spontaneously to quinolinic acid and feed into nicotinamide biosynthesis, or undergo further enzymatic degradation.


Pssm-ID: 132082  Cd Length: 159  Bit Score: 123.34  E-value: 2.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084852303  22 GRSILWQDSESIAFLSRGRKMRRDFHIDPSDEVTLQLAGEQRLHYkTPEGEEKIALIQPGQALLCPGGVPHSPRVTEDAW 101
Cdd:TIGR03037  19 GNQQIWQDSEFMVTVVGGPNARTDFHDDPGEEFFYQLKGEMYLKV-TEEGKREDVPIREGDIFLLPPHVPHSPQRPAGSI 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084852303 102 FVVFERKRRPGEEDRFLWFCETCGEKVYDVAAYVGDYSLDpVSKVHERFYGDESLRTCKKCGT 164
Cdd:TIGR03037  98 GLVIERKRPQGELDGFQWFCPQCGHKLHRAEVQLENIVTD-LPPVFEHFYSNEDARTCKNCGH 159
3-HAO pfam06052
3-hydroxyanthranilic acid dioxygenase; In eukaryotes 3-hydroxyanthranilic acid dioxygenase (EC: ...
 39-151 4.39e-15

3-hydroxyanthranilic acid dioxygenase; In eukaryotes 3-hydroxyanthranilic acid dioxygenase (EC:1.13.11.6) is part of the kynurenine pathway for the degradation of tryptophan and the biosynthesis of nicotinic acid.The prokaryotic homolog is involved in the 2-nitrobenzoate degradation pathway.


Pssm-ID: 399210  Cd Length: 151  Bit Score: 68.26  E-value: 4.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084852303  39 GRKMRRDFHIDPSDEVTLQLAGEQRLHYkTPEGEEKIALIQPGQALLCPGGVPHSPRVTEDAWFVVFERKRRPGEEDRFL 118
Cdd:pfam06052  41 GPNERTDYHIEEGPEWFYQLKGDMVLKV-VDEGDARDIVIRQGEIFLLPARVPHSPQRFANTVGLVVERERLGTENDGLR 119

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1084852303 119 WFCETCGEKVYDVAAYVGDYSLDpVSKVHERFY 151
Cdd:pfam06052 120 WYCGHCNQVLFESWFYLLDLGTQ-LPPAILEFY 151
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
47-105 1.12e-04

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 39.45  E-value: 1.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1084852303  47 HIDPSDEVTLQLAGEQRLHYktpegEEKIALIQPGQALLCPGGVPHSPRVTEDAWFVVF 105
Cdd:COG1917    39 HSHPGEELIYVLEGEGEVEV-----GGEEYELKPGDVVFIPPGVPHAFRNLGDEPAVLL 92
 
Name Accession Description Interval E-value
cupin_HAO cd06123
3-Hydroxyanthranilate-3,4-dioxygenase, cupin domain; 3-Hydroxyanthranilate-3,4-dioxygenase ...
 13-162 1.35e-61

3-Hydroxyanthranilate-3,4-dioxygenase, cupin domain; 3-Hydroxyanthranilate-3,4-dioxygenase (HAO or 3HAO) is a non-heme iron-dependent extradiol dioxygenase that catalyzes the oxidative ring opening of 3-hydroxyanthranilate (3-HAA) in the final enzymatic step of the kynurenine biosynthetic pathway in which tryptophan is converted to quinolinate, an endogenous neurotoxin, making HAO a target for pharmacological downregulation. Quinolate is also the universal de novo precursor to the pyridine ring of nicotinamide adenine dinucleotide. The enzyme forms homodimers, with two metal binding sites per molecule. One of the bound metal ions occupies the proposed ferrous-coordinated active site, which is located in a conserved double-strand beta-helix domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380378  Cd Length: 153  Bit Score: 187.31  E-value: 1.35e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084852303  13 IENVRSAGK---GRSILWQDSESIAFLSRGRKMRRDFHIDPSDEVTLQLAGEQRLHYKTPeGEEKIALIQPGQALLCPGG 89
Cdd:cd06123     3 IEENRHLLKppvGNKLLWQDSDFIVMVVGGPNSRKDFHINPGEEFFYQLKGDMVLKVIEP-GKFKDVVIKEGEIFLLPAR 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084852303  90 VPHSPRVTEDAWFVVFERKRRPGEEDRFLWFCETCGEKVYDVAAYVgDYSLDPVSKVHERFYGDESLRTCKKC 162
Cdd:cd06123    82 VPHSPQRPADTVGLVIERKRPPGELDGLRWYCENCGELLHEVEFHC-DDLGTQLKPAIEEFFASEELRTCKPC 153
PRK13264 PRK13264
3-hydroxyanthranilate 3,4-dioxygenase; Provisional
 1-165 1.04e-39

3-hydroxyanthranilate 3,4-dioxygenase; Provisional


Pssm-ID: 183930  Cd Length: 177  Bit Score: 132.35  E-value: 1.04e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084852303   1 MKDLIAVDLNGAIENVRSAGK---GRSILWQDSESIAFLSRGRKMRRDFHIDPSDEVTLQLAGEQRLHYKTpEGEEKIAL 77
Cdd:PRK13264    1 MKILKPFNLHKWIEEHRHLLKppvGNKQIWQDSDFIVMVVGGPNARTDFHYDPGEEFFYQLEGDMYLKVQE-DGKRRDVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084852303  78 IQPGQALLCPGGVPHSPRVTEDAWFVVFERKRRPGEEDRFLWFCETCGEKVYDVAAYVGDYSLDpVSKVHERFYGDESLR 157
Cdd:PRK13264   80 IREGEMFLLPPHVPHSPQREAGSIGLVIERKRPEGELDGFQWYCDECNHKVHEVEVQLTDIETD-LPPVFAAFYASEELR 158


                  ....*...
gi 1084852303 158 TCKKCGTV 165
Cdd:PRK13264  159 TCDNCGTV 166
anthran_nbaC TIGR03037
3-hydroxyanthranilate 3,4-dioxygenase; Members of this protein family, from both bacteria and ...
 22-164 2.98e-36

3-hydroxyanthranilate 3,4-dioxygenase; Members of this protein family, from both bacteria and eukaryotes, are the enzyme 3-hydroxyanthranilate 3,4-dioxygenase. This enzyme acts on the tryptophan metabolite 3-hydroxyanthranilate and produces 2-amino-3-carboxymuconate semialdehyde, which can rearrange spontaneously to quinolinic acid and feed into nicotinamide biosynthesis, or undergo further enzymatic degradation.


Pssm-ID: 132082  Cd Length: 159  Bit Score: 123.34  E-value: 2.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084852303  22 GRSILWQDSESIAFLSRGRKMRRDFHIDPSDEVTLQLAGEQRLHYkTPEGEEKIALIQPGQALLCPGGVPHSPRVTEDAW 101
Cdd:TIGR03037  19 GNQQIWQDSEFMVTVVGGPNARTDFHDDPGEEFFYQLKGEMYLKV-TEEGKREDVPIREGDIFLLPPHVPHSPQRPAGSI 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084852303 102 FVVFERKRRPGEEDRFLWFCETCGEKVYDVAAYVGDYSLDpVSKVHERFYGDESLRTCKKCGT 164
Cdd:TIGR03037  98 GLVIERKRPQGELDGFQWFCPQCGHKLHRAEVQLENIVTD-LPPVFEHFYSNEDARTCKNCGH 159
3-HAO pfam06052
3-hydroxyanthranilic acid dioxygenase; In eukaryotes 3-hydroxyanthranilic acid dioxygenase (EC: ...
 39-151 4.39e-15

3-hydroxyanthranilic acid dioxygenase; In eukaryotes 3-hydroxyanthranilic acid dioxygenase (EC:1.13.11.6) is part of the kynurenine pathway for the degradation of tryptophan and the biosynthesis of nicotinic acid.The prokaryotic homolog is involved in the 2-nitrobenzoate degradation pathway.


Pssm-ID: 399210  Cd Length: 151  Bit Score: 68.26  E-value: 4.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084852303  39 GRKMRRDFHIDPSDEVTLQLAGEQRLHYkTPEGEEKIALIQPGQALLCPGGVPHSPRVTEDAWFVVFERKRRPGEEDRFL 118
Cdd:pfam06052  41 GPNERTDYHIEEGPEWFYQLKGDMVLKV-VDEGDARDIVIRQGEIFLLPARVPHSPQRFANTVGLVVERERLGTENDGLR 119

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1084852303 119 WFCETCGEKVYDVAAYVGDYSLDpVSKVHERFY 151
Cdd:pfam06052 120 WYCGHCNQVLFESWFYLLDLGTQ-LPPAILEFY 151
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
47-105 1.12e-04

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 39.45  E-value: 1.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1084852303  47 HIDPSDEVTLQLAGEQRLHYktpegEEKIALIQPGQALLCPGGVPHSPRVTEDAWFVVF 105
Cdd:COG1917    39 HSHPGEELIYVLEGEGEVEV-----GGEEYELKPGDVVFIPPGVPHAFRNLGDEPAVLL 92
cupin_YdbB-like cd02226
Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial ...
 41-107 2.84e-03

Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial proteins homologous to YdbB, a Bacillus subtilis protein of unknown function. It also includes protein Nmb1881 From Neisseria meningitidis, also of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380355 [Multi-domain]  Cd Length: 94  Bit Score: 35.50  E-value: 2.84e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084852303  41 KMRRDFHI---DPSDEVTLQLAGEQRLHYktpegEEKIALIQPGQALLCPGGVPHSPRVTEDAWFVVFER 107
Cdd:cd02226    30 KLKGEFVWhkhDDEDELFLVLEGELTIDF-----RDRDVTLGPGEFFVVPKGVEHRPVAEEETVVLLIEP 94
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 50-100 8.78e-03

pectin degradation protein KdgF and related proteins, cupin domain; This family includes bacterial and archaeal pectin degradation protein KdgF that catalyzes the linearization of unsaturated uronates from both pectin and alginate, which are polysaccharides found in the cell walls of plants and brown algae, respectively, and represent an important source of carbon. These polysaccharides, mostly consisting of chains of uronates, can be metabolized by bacteria through a pathway of enzymatic steps to the key metabolite 2-keto-3-deoxygluconate (KDG). Pectin degradation is used by many plant-pathogenic bacteria during infection, and also, pectin and alginate can both represent abundant sources of carbohydrate for the production of biofuels. These proteins belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380366 [Multi-domain]  Cd Length: 104  Bit Score: 34.37  E-value: 8.78e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1084852303  50 PSDEVTLQLAGEQRLHYktpEGEEKIalIQPGQALLCPGGVPHSPRVTEDA 100
Cdd:cd02238    46 PHEQIGYVLSGRFEFTI---GGETRI--LKPGDSYYIPPNVPHGAEALEDS 91
 
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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