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Conserved domains on  [gi|109157069|pdb|1ZVF|A]
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Chain A, 3-hydroxyanthranilate 3,4-dioxygenase

Protein Classification

cupin domain-containing protein( domain architecture ID 1562428)

cupin domain-containing protein, part of a functionally diverse superfamily with the active site generally located at the center of a conserved domain forming a beta-barrel fold

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cupin_RmlC-like super family cl40423
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 2-156 4.72e-96

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 pfam06052:

Pssm-ID: 477354  Cd Length: 151  Bit Score: 274.73  E-value: 4.72e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVF_A          2 MFNTTPINIDKWLKENEGLLKPPVNNYCLHKGGFTVMIVGGPNERTDYHINPTPEWFYQKKGSMLLKVVDETDAEpkfiD 81
Cdd:pfam06052   1 MFNVTPINIDAWVKENRGLLKPPVCNKCLHQDGFKVMIVGGPNERTDYHIEEGPEWFYQLKGDMVLKVVDEGDAR----D 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1ZVF_A         82 IIINEGDSYLLPGNVPHSPVRFADTVGIVVEQDRPGGENDKIRWYCSHCRQVVHESELQMLDLGTQVKEAILDFE 156
Cdd:pfam06052  77 IVIRQGEIFLLPARVPHSPQRFANTVGLVVERERLGTENDGLRWYCGHCNQVLFESWFYLLDLGTQLPPAILEFY 151
 
Name Accession Description Interval E-value
3-HAO pfam06052
3-hydroxyanthranilic acid dioxygenase; In eukaryotes 3-hydroxyanthranilic acid dioxygenase (EC: ...
 2-156 4.72e-96

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: 274.73  E-value: 4.72e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVF_A          2 MFNTTPINIDKWLKENEGLLKPPVNNYCLHKGGFTVMIVGGPNERTDYHINPTPEWFYQKKGSMLLKVVDETDAEpkfiD 81
Cdd:pfam06052   1 MFNVTPINIDAWVKENRGLLKPPVCNKCLHQDGFKVMIVGGPNERTDYHIEEGPEWFYQLKGDMVLKVVDEGDAR----D 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1ZVF_A         82 IIINEGDSYLLPGNVPHSPVRFADTVGIVVEQDRPGGENDKIRWYCSHCRQVVHESELQMLDLGTQVKEAILDFE 156
Cdd:pfam06052  77 IVIRQGEIFLLPARVPHSPQRFANTVGLVVERERLGTENDGLRWYCGHCNQVLFESWFYLLDLGTQLPPAILEFY 151
cupin_HAO cd06123
3-Hydroxyanthranilate-3,4-dioxygenase, cupin domain; 3-Hydroxyanthranilate-3,4-dioxygenase ...
 12-167 2.78e-82

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: 239.70  E-value: 2.78e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVF_A       12 KWLKENEGLLKPPVNNYCLHKGG-FTVMIVGGPNERTDYHINPTPEWFYQKKGSMLLKVVDEtdaePKFIDIIINEGDSY 90
Cdd:cd06123   1 KWIEENRHLLKPPVGNKLLWQDSdFIVMVVGGPNSRKDFHINPGEEFFYQLKGDMVLKVIEP----GKFKDVVIKEGEIF 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1ZVF_A       91 LLPGNVPHSPVRFADTVGIVVEQDRPGGENDKIRWYCSHCRQVVHESELQMLDLGTQVKEAILDFENDVEKRTCFHC 167
Cdd:cd06123  77 LLPARVPHSPQRPADTVGLVIERKRPPGELDGLRWYCENCGELLHEVEFHCDDLGTQLKPAIEEFFASEELRTCKPC 153
PRK13264 PRK13264
3-hydroxyanthranilate 3,4-dioxygenase; Provisional
 2-170 6.28e-72

3-hydroxyanthranilate 3,4-dioxygenase; Provisional


Pssm-ID: 183930  Cd Length: 177  Bit Score: 214.39  E-value: 6.28e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVF_A         2 MFNTTPINIDKWLKENEGLLKPPVNNYCLHKGG-FTVMIVGGPNERTDYHINPTPEWFYQKKGSMLLKVVDETdaepKFI 80
Cdd:PRK13264   1 MKILKPFNLHKWIEEHRHLLKPPVGNKQIWQDSdFIVMVVGGPNARTDFHYDPGEEFFYQLEGDMYLKVQEDG----KRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVF_A        81 DIIINEGDSYLLPGNVPHSPVRFADTVGIVVEQDRPGGENDKIRWYCSHCRQVVHESELQMLDLGTQVKEAILDFENDVE 160
Cdd:PRK13264  77 DVPIREGEMFLLPPHVPHSPQREAGSIGLVIERKRPEGELDGFQWYCDECNHKVHEVEVQLTDIETDLPPVFAAFYASEE 156

                        170
                 ....*....|
1ZVF_A       161 KRTCFHCKTL 170
Cdd:PRK13264 157 LRTCDNCGTV 166
anthran_nbaC TIGR03037
3-hydroxyanthranilate 3,4-dioxygenase; Members of this protein family, from both bacteria and ...
 8-167 2.06e-60

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: 184.98  E-value: 2.06e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVF_A          8 INIDKWLKENEGLLKPPVNNYCL-HKGGFTVMIVGGPNERTDYHINPTPEWFYQKKGSMLLKVVDETDAEpkfiDIIINE 86
Cdd:TIGR03037   1 FNFKKWIDEHKHLLKPPVGNQQIwQDSEFMVTVVGGPNARTDFHDDPGEEFFYQLKGEMYLKVTEEGKRE----DVPIRE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVF_A         87 GDSYLLPGNVPHSPVRFADTVGIVVEQDRPGGENDKIRWYCSHCRQVVHESELQMLDLGTQVKEAILDFENDVEKRTCFH 166
Cdd:TIGR03037  77 GDIFLLPPHVPHSPQRPAGSIGLVIERKRPQGELDGFQWFCPQCGHKLHRAEVQLENIVTDLPPVFEHFYSNEDARTCKN 156


                  .
1ZVF_A        167 C 167
Cdd:TIGR03037 157 C 157
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
32-118 6.76e-06

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 42.91  E-value: 6.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVF_A       32 KGGFTVMIVG-GPNERTDYHINPTPEWFYQKKGSMLLKVVDETdaepkfidIIINEGDSYLLPGNVPHSPVRFADTVGIV 110
Cdd:COG1917  20 EDELEVVRVTfEPGARTPWHSHPGEELIYVLEGEGEVEVGGEE--------YELKPGDVVFIPPGVPHAFRNLGDEPAVL 91


                ....*...
1ZVF_A      111 VEQDRPGG 118
Cdd:COG1917  92 LVVFSPGL 99
 
Name Accession Description Interval E-value
3-HAO pfam06052
3-hydroxyanthranilic acid dioxygenase; In eukaryotes 3-hydroxyanthranilic acid dioxygenase (EC: ...
 2-156 4.72e-96

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: 274.73  E-value: 4.72e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVF_A          2 MFNTTPINIDKWLKENEGLLKPPVNNYCLHKGGFTVMIVGGPNERTDYHINPTPEWFYQKKGSMLLKVVDETDAEpkfiD 81
Cdd:pfam06052   1 MFNVTPINIDAWVKENRGLLKPPVCNKCLHQDGFKVMIVGGPNERTDYHIEEGPEWFYQLKGDMVLKVVDEGDAR----D 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1ZVF_A         82 IIINEGDSYLLPGNVPHSPVRFADTVGIVVEQDRPGGENDKIRWYCSHCRQVVHESELQMLDLGTQVKEAILDFE 156
Cdd:pfam06052  77 IVIRQGEIFLLPARVPHSPQRFANTVGLVVERERLGTENDGLRWYCGHCNQVLFESWFYLLDLGTQLPPAILEFY 151
cupin_HAO cd06123
3-Hydroxyanthranilate-3,4-dioxygenase, cupin domain; 3-Hydroxyanthranilate-3,4-dioxygenase ...
 12-167 2.78e-82

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: 239.70  E-value: 2.78e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVF_A       12 KWLKENEGLLKPPVNNYCLHKGG-FTVMIVGGPNERTDYHINPTPEWFYQKKGSMLLKVVDEtdaePKFIDIIINEGDSY 90
Cdd:cd06123   1 KWIEENRHLLKPPVGNKLLWQDSdFIVMVVGGPNSRKDFHINPGEEFFYQLKGDMVLKVIEP----GKFKDVVIKEGEIF 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1ZVF_A       91 LLPGNVPHSPVRFADTVGIVVEQDRPGGENDKIRWYCSHCRQVVHESELQMLDLGTQVKEAILDFENDVEKRTCFHC 167
Cdd:cd06123  77 LLPARVPHSPQRPADTVGLVIERKRPPGELDGLRWYCENCGELLHEVEFHCDDLGTQLKPAIEEFFASEELRTCKPC 153
PRK13264 PRK13264
3-hydroxyanthranilate 3,4-dioxygenase; Provisional
 2-170 6.28e-72

3-hydroxyanthranilate 3,4-dioxygenase; Provisional


Pssm-ID: 183930  Cd Length: 177  Bit Score: 214.39  E-value: 6.28e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVF_A         2 MFNTTPINIDKWLKENEGLLKPPVNNYCLHKGG-FTVMIVGGPNERTDYHINPTPEWFYQKKGSMLLKVVDETdaepKFI 80
Cdd:PRK13264   1 MKILKPFNLHKWIEEHRHLLKPPVGNKQIWQDSdFIVMVVGGPNARTDFHYDPGEEFFYQLEGDMYLKVQEDG----KRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVF_A        81 DIIINEGDSYLLPGNVPHSPVRFADTVGIVVEQDRPGGENDKIRWYCSHCRQVVHESELQMLDLGTQVKEAILDFENDVE 160
Cdd:PRK13264  77 DVPIREGEMFLLPPHVPHSPQREAGSIGLVIERKRPEGELDGFQWYCDECNHKVHEVEVQLTDIETDLPPVFAAFYASEE 156

                        170
                 ....*....|
1ZVF_A       161 KRTCFHCKTL 170
Cdd:PRK13264 157 LRTCDNCGTV 166
anthran_nbaC TIGR03037
3-hydroxyanthranilate 3,4-dioxygenase; Members of this protein family, from both bacteria and ...
 8-167 2.06e-60

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: 184.98  E-value: 2.06e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVF_A          8 INIDKWLKENEGLLKPPVNNYCL-HKGGFTVMIVGGPNERTDYHINPTPEWFYQKKGSMLLKVVDETDAEpkfiDIIINE 86
Cdd:TIGR03037   1 FNFKKWIDEHKHLLKPPVGNQQIwQDSEFMVTVVGGPNARTDFHDDPGEEFFYQLKGEMYLKVTEEGKRE----DVPIRE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVF_A         87 GDSYLLPGNVPHSPVRFADTVGIVVEQDRPGGENDKIRWYCSHCRQVVHESELQMLDLGTQVKEAILDFENDVEKRTCFH 166
Cdd:TIGR03037  77 GDIFLLPPHVPHSPQRPAGSIGLVIERKRPQGELDGFQWFCPQCGHKLHRAEVQLENIVTDLPPVFEHFYSNEDARTCKN 156


                  .
1ZVF_A        167 C 167
Cdd:TIGR03037 157 C 157
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
32-118 6.76e-06

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 42.91  E-value: 6.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVF_A       32 KGGFTVMIVG-GPNERTDYHINPTPEWFYQKKGSMLLKVVDETdaepkfidIIINEGDSYLLPGNVPHSPVRFADTVGIV 110
Cdd:COG1917  20 EDELEVVRVTfEPGARTPWHSHPGEELIYVLEGEGEVEVGGEE--------YELKPGDVVFIPPGVPHAFRNLGDEPAVL 91


                ....*...
1ZVF_A      111 VEQDRPGG 118
Cdd:COG1917  92 LVVFSPGL 99
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 62-109 1.55e-04

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: 38.99  E-value: 1.55e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
1ZVF_A       62 KGSMLLKVVDETdaepkfidIIINEGDSYLLPGNVPHSPVRFADTVGI 109
Cdd:cd02238  55 SGRFEFTIGGET--------RILKPGDSYYIPPNVPHGAEALEDSVLL 94
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 33-101 3.07e-03

Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 441743 [Multi-domain]  Cd Length: 115  Bit Score: 35.71  E-value: 3.07e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1ZVF_A       33 GGFTVMIVGGPNERtDYHiNPTPEWFYQKKGSMLLKVVDEtdaEPKFIDIIINEGDSYLLPGNVPHSPV 101
Cdd:COG2140   5 GGLTVLEPGGVREE-HWH-PNAAEWYYVLSGEARMTVQDP---PGRARTVDVGPGDVVYVPPGYGHYII 68
bicupin_oxalic TIGR03404
bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins ...
 50-99 6.46e-03

bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins as they have two copies of the cupin domain (pfam00190). Two different known activities for members of this family are oxalate decarboxylase (EC 4.1.1.2) and oxalate oxidase (EC 1.2.3.4), although the latter activity has more often been found in distantly related monocupin (germin) proteins.


Pssm-ID: 274565 [Multi-domain]  Cd Length: 367  Bit Score: 36.14  E-value: 6.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
1ZVF_A         50 HINPTPEWFYQKKGSMLLKVVDEtDAEPkFIDiIINEGDSYLLPGNVPHS 99
Cdd:TIGR03404  83 HWHKEAEWAYVLYGSCRITAVDE-NGRN-YID-DVGAGDLWYFPPGIPHS 129
 
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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