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Conserved domains on  [gi|1720388795|ref|XP_030105302|]
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3-hydroxyanthranilate 3,4-dioxygenase isoform X3 [Mus musculus]

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 ...
 1-98 5.38e-59

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: 182.69  E-value: 5.38e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388795   1 MILRVLEQGQHRDVPIRQGEIFLLPARVPHSPQRFANTMGLVIERRRLESELDGLRYYVGDTEDVLFEKWFHCKDLGTQL 80
Cdd:cd06123    55 MVLKVIEPGKFKDVVIKEGEIFLLPARVPHSPQRPADTVGLVIERKRPPGELDGLRWYCENCGELLHEVEFHCDDLGTQL 134

                          90
                  ....*....|....*...
gi 1720388795  81 APIIQEFFHSEQYRTGKP 98
Cdd:cd06123   135 KPAIEEFFASEELRTCKP 152
cupin_RmlC-like super family cl40423
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 148-199 7.92e-04

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


The actual alignment was detected with superfamily member cd07006:

Pssm-ID: 477354 [Multi-domain]  Cd Length: 89  Bit Score: 37.34  E-value: 7.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720388795 148 TQVIAHGQ--GSSKGPRQDVDVWLWQQEGSSKVTMGGQCIALAPDDSLLVPAGT 199
Cdd:cd07006    14 TMVLAPGDteGGPDNRHRGSDQWLYVVSGSGEAIVEGERVALKPGSLLLIEAGE 67
 
Name Accession Description Interval E-value
cupin_HAO cd06123
3-Hydroxyanthranilate-3,4-dioxygenase, cupin domain; 3-Hydroxyanthranilate-3,4-dioxygenase ...
 1-98 5.38e-59

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: 182.69  E-value: 5.38e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388795   1 MILRVLEQGQHRDVPIRQGEIFLLPARVPHSPQRFANTMGLVIERRRLESELDGLRYYVGDTEDVLFEKWFHCKDLGTQL 80
Cdd:cd06123    55 MVLKVIEPGKFKDVVIKEGEIFLLPARVPHSPQRPADTVGLVIERKRPPGELDGLRWYCENCGELLHEVEFHCDDLGTQL 134

                          90
                  ....*....|....*...
gi 1720388795  81 APIIQEFFHSEQYRTGKP 98
Cdd:cd06123   135 KPAIEEFFASEELRTCKP 152
3-HAO pfam06052
3-hydroxyanthranilic acid dioxygenase; In eukaryotes 3-hydroxyanthranilic acid dioxygenase (EC: ...
 1-88 3.34e-51

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: 163.02  E-value: 3.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388795   1 MILRVLEQGQHRDVPIRQGEIFLLPARVPHSPQRFANTMGLVIERRRLESELDGLRYYVGDTEDVLFEKWFHCKDLGTQL 80
Cdd:pfam06052  64 MVLKVVDEGDARDIVIRQGEIFLLPARVPHSPQRFANTVGLVVERERLGTENDGLRWYCGHCNQVLFESWFYLLDLGTQL 143


                  ....*...
gi 1720388795  81 APIIQEFF 88
Cdd:pfam06052 144 PPAILEFY 151
PRK13264 PRK13264
3-hydroxyanthranilate 3,4-dioxygenase; Provisional
 1-95 1.25e-33

3-hydroxyanthranilate 3,4-dioxygenase; Provisional


Pssm-ID: 183930  Cd Length: 177  Bit Score: 118.86  E-value: 1.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388795   1 MILRVLEQGQHRDVPIRQGEIFLLPARVPHSPQRFANTMGLVIERRRLESELDGLRYYVGDTEDVLFEKWFHCKDLGTQL 80
Cdd:PRK13264   65 MYLKVQEDGKRRDVPIREGEMFLLPPHVPHSPQREAGSIGLVIERKRPEGELDGFQWYCDECNHKVHEVEVQLTDIETDL 144

                          90
                  ....*....|....*
gi 1720388795  81 APIIQEFFHSEQYRT 95
Cdd:PRK13264  145 PPVFAAFYASEELRT 159
cupin_XcTcmJ-like cd07006
Xanthomonas campestris XcTcmJ and related proteins, cupin domain; This family includes ...
 148-199 7.92e-04

Xanthomonas campestris XcTcmJ and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to plant pathogen Xanthomonas campestris tetracenomycin polyketide synthesis protein XcTcmJ, a protein encoded by the tcmJ gene. XcTcmJ is annotated as being involved in tetracenomycin polyketide biosynthesis. Also included is Xc5357 from a different strain of X. campestris. Structure studies show that binding of zinc induces conformational changes and serves a functional role in this cupin protein. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380409 [Multi-domain]  Cd Length: 89  Bit Score: 37.34  E-value: 7.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720388795 148 TQVIAHGQ--GSSKGPRQDVDVWLWQQEGSSKVTMGGQCIALAPDDSLLVPAGT 199
Cdd:cd07006    14 TMVLAPGDteGGPDNRHRGSDQWLYVVSGSGEAIVEGERVALKPGSLLLIEAGE 67
 
Name Accession Description Interval E-value
cupin_HAO cd06123
3-Hydroxyanthranilate-3,4-dioxygenase, cupin domain; 3-Hydroxyanthranilate-3,4-dioxygenase ...
 1-98 5.38e-59

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: 182.69  E-value: 5.38e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388795   1 MILRVLEQGQHRDVPIRQGEIFLLPARVPHSPQRFANTMGLVIERRRLESELDGLRYYVGDTEDVLFEKWFHCKDLGTQL 80
Cdd:cd06123    55 MVLKVIEPGKFKDVVIKEGEIFLLPARVPHSPQRPADTVGLVIERKRPPGELDGLRWYCENCGELLHEVEFHCDDLGTQL 134

                          90
                  ....*....|....*...
gi 1720388795  81 APIIQEFFHSEQYRTGKP 98
Cdd:cd06123   135 KPAIEEFFASEELRTCKP 152
3-HAO pfam06052
3-hydroxyanthranilic acid dioxygenase; In eukaryotes 3-hydroxyanthranilic acid dioxygenase (EC: ...
 1-88 3.34e-51

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: 163.02  E-value: 3.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388795   1 MILRVLEQGQHRDVPIRQGEIFLLPARVPHSPQRFANTMGLVIERRRLESELDGLRYYVGDTEDVLFEKWFHCKDLGTQL 80
Cdd:pfam06052  64 MVLKVVDEGDARDIVIRQGEIFLLPARVPHSPQRFANTVGLVVERERLGTENDGLRWYCGHCNQVLFESWFYLLDLGTQL 143


                  ....*...
gi 1720388795  81 APIIQEFF 88
Cdd:pfam06052 144 PPAILEFY 151
PRK13264 PRK13264
3-hydroxyanthranilate 3,4-dioxygenase; Provisional
 1-95 1.25e-33

3-hydroxyanthranilate 3,4-dioxygenase; Provisional


Pssm-ID: 183930  Cd Length: 177  Bit Score: 118.86  E-value: 1.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388795   1 MILRVLEQGQHRDVPIRQGEIFLLPARVPHSPQRFANTMGLVIERRRLESELDGLRYYVGDTEDVLFEKWFHCKDLGTQL 80
Cdd:PRK13264   65 MYLKVQEDGKRRDVPIREGEMFLLPPHVPHSPQREAGSIGLVIERKRPEGELDGFQWYCDECNHKVHEVEVQLTDIETDL 144

                          90
                  ....*....|....*
gi 1720388795  81 APIIQEFFHSEQYRT 95
Cdd:PRK13264  145 PPVFAAFYASEELRT 159
cupin_XcTcmJ-like cd07006
Xanthomonas campestris XcTcmJ and related proteins, cupin domain; This family includes ...
 148-199 7.92e-04

Xanthomonas campestris XcTcmJ and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to plant pathogen Xanthomonas campestris tetracenomycin polyketide synthesis protein XcTcmJ, a protein encoded by the tcmJ gene. XcTcmJ is annotated as being involved in tetracenomycin polyketide biosynthesis. Also included is Xc5357 from a different strain of X. campestris. Structure studies show that binding of zinc induces conformational changes and serves a functional role in this cupin protein. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380409 [Multi-domain]  Cd Length: 89  Bit Score: 37.34  E-value: 7.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720388795 148 TQVIAHGQ--GSSKGPRQDVDVWLWQQEGSSKVTMGGQCIALAPDDSLLVPAGT 199
Cdd:cd07006    14 TMVLAPGDteGGPDNRHRGSDQWLYVVSGSGEAIVEGERVALKPGSLLLIEAGE 67
cupin_Bh2720-like cd02223
Bacillus halodurans Bh2720 and related proteins, cupin domain; This family includes bacterial, ...
 163-199 5.27e-03

Bacillus halodurans Bh2720 and related proteins, cupin domain; This family includes bacterial, archaeal, and eukaryotic proteins similar to Bh2720, a Bacillus halodurans protein of unknown function with a cupin beta-barrel fold.


Pssm-ID: 380352 [Multi-domain]  Cd Length: 98  Bit Score: 35.21  E-value: 5.27e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1720388795 163 QDVDVWLWQQEGSSKVTMGGQCIALAPDDSLLVPAGT 199
Cdd:cd02223    30 DDVDQFLRIEEGEGKAIMGGFESEVKDGDAIIVPAGT 66
 
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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