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Conserved domains on  [gi|568998597|ref|XP_006523526|]
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3-hydroxyanthranilate 3,4-dioxygenase isoform X1 [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 ...
 10-159 8.04e-100

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: 289.00  E-value: 8.04e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998597  10 WVEENRASFQPPVCNKLMHQE-QLKIMFVGGPNTRKDYHIEEGEEVFYQLEGDMILRVLEQGQHRDVPIRQGEIFLLPAR 88
Cdd:cd06123    2 WIEENRHLLKPPVGNKLLWQDsDFIVMVVGGPNSRKDFHINPGEEFFYQLKGDMVLKVIEPGKFKDVVIKEGEIFLLPAR 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568998597  89 VPHSPQRFANTMGLVIERRRLESELDGLRYYVGDTEDVLFEKWFHCKDLGTQLAPIIQEFFHSEQYRTGKP 159
Cdd:cd06123   82 VPHSPQRPADTVGLVIERKRPPGELDGLRWYCENCGELLHEVEFHCDDLGTQLKPAIEEFFASEELRTCKP 152
cupin_RmlC-like super family cl40423
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 209-260 9.54e-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: 37.73  E-value: 9.54e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568998597 209 TQVIAHGQ--GSSKGPRQDVDVWLWQQEGSSKVTMGGQCIALAPDDSLLVPAGT 260
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 ...
 10-159 8.04e-100

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: 289.00  E-value: 8.04e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998597  10 WVEENRASFQPPVCNKLMHQE-QLKIMFVGGPNTRKDYHIEEGEEVFYQLEGDMILRVLEQGQHRDVPIRQGEIFLLPAR 88
Cdd:cd06123    2 WIEENRHLLKPPVGNKLLWQDsDFIVMVVGGPNSRKDFHINPGEEFFYQLKGDMVLKVIEPGKFKDVVIKEGEIFLLPAR 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568998597  89 VPHSPQRFANTMGLVIERRRLESELDGLRYYVGDTEDVLFEKWFHCKDLGTQLAPIIQEFFHSEQYRTGKP 159
Cdd:cd06123   82 VPHSPQRPADTVGLVIERKRPPGELDGLRWYCENCGELLHEVEFHCDDLGTQLKPAIEEFFASEELRTCKP 152
3-HAO pfam06052
3-hydroxyanthranilic acid dioxygenase; In eukaryotes 3-hydroxyanthranilic acid dioxygenase (EC: ...
 2-149 1.24e-91

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: 268.18  E-value: 1.24e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998597    2 ERRVRVKSWVEENRASFQPPVCNKLMHQEQLKIMFVGGPNTRKDYHIEEGEEVFYQLEGDMILRVLEQGQHRDVPIRQGE 81
Cdd:pfam06052   4 VTPINIDAWVKENRGLLKPPVCNKCLHQDGFKVMIVGGPNERTDYHIEEGPEWFYQLKGDMVLKVVDEGDARDIVIRQGE 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568998597   82 IFLLPARVPHSPQRFANTMGLVIERRRLESELDGLRYYVGDTEDVLFEKWFHCKDLGTQLAPIIQEFF 149
Cdd:pfam06052  84 IFLLPARVPHSPQRFANTVGLVVERERLGTENDGLRWYCGHCNQVLFESWFYLLDLGTQLPPAILEFY 151
PRK13264 PRK13264
3-hydroxyanthranilate 3,4-dioxygenase; Provisional
 8-156 2.01e-64

3-hydroxyanthranilate 3,4-dioxygenase; Provisional


Pssm-ID: 183930  Cd Length: 177  Bit Score: 199.76  E-value: 2.01e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998597   8 KSWVEENRASFQPPVCNKLMHQE-QLKIMFVGGPNTRKDYHIEEGEEVFYQLEGDMILRVLEQGQHRDVPIRQGEIFLLP 86
Cdd:PRK13264  10 HKWIEEHRHLLKPPVGNKQIWQDsDFIVMVVGGPNARTDFHYDPGEEFFYQLEGDMYLKVQEDGKRRDVPIREGEMFLLP 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998597  87 ARVPHSPQRFANTMGLVIERRRLESELDGLRYYVGDTEDVLFEKWFHCKDLGTQLAPIIQEFFHSEQYRT 156
Cdd:PRK13264  90 PHVPHSPQREAGSIGLVIERKRPEGELDGFQWYCDECNHKVHEVEVQLTDIETDLPPVFAAFYASEELRT 159
anthran_nbaC TIGR03037
3-hydroxyanthranilate 3,4-dioxygenase; Members of this protein family, from both bacteria and ...
 8-158 2.49e-57

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: 181.12  E-value: 2.49e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998597    8 KSWVEENRASFQPPVCNKLMHQE-QLKIMFVGGPNTRKDYHIEEGEEVFYQLEGDMILRVLEQGQHRDVPIRQGEIFLLP 86
Cdd:TIGR03037   4 KKWIDEHKHLLKPPVGNQQIWQDsEFMVTVVGGPNARTDFHDDPGEEFFYQLKGEMYLKVTEEGKREDVPIREGDIFLLP 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568998597   87 ARVPHSPQRFANTMGLVIERRRLESELDGLRYYVGDTEDVLFEKWFHCKDLGTQLAPIIQEFFHSEQYRTGK 158
Cdd:TIGR03037  84 PHVPHSPQRPAGSIGLVIERKRPQGELDGFQWFCPQCGHKLHRAEVQLENIVTDLPPVFEHFYSNEDARTCK 155
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
40-92 4.64e-04

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 38.68  E-value: 4.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568998597  40 PNTRKDYHIEEGEEVFYQLEGDMILRVleqgQHRDVPIRQGEIFLLPARVPHS 92
Cdd:COG1917   32 PGARTPWHSHPGEELIYVLEGEGEVEV----GGEEYELKPGDVVFIPPGVPHA 80
cupin_XcTcmJ-like cd07006
Xanthomonas campestris XcTcmJ and related proteins, cupin domain; This family includes ...
 209-260 9.54e-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: 37.73  E-value: 9.54e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568998597 209 TQVIAHGQ--GSSKGPRQDVDVWLWQQEGSSKVTMGGQCIALAPDDSLLVPAGT 260
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 ...
 10-159 8.04e-100

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: 289.00  E-value: 8.04e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998597  10 WVEENRASFQPPVCNKLMHQE-QLKIMFVGGPNTRKDYHIEEGEEVFYQLEGDMILRVLEQGQHRDVPIRQGEIFLLPAR 88
Cdd:cd06123    2 WIEENRHLLKPPVGNKLLWQDsDFIVMVVGGPNSRKDFHINPGEEFFYQLKGDMVLKVIEPGKFKDVVIKEGEIFLLPAR 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568998597  89 VPHSPQRFANTMGLVIERRRLESELDGLRYYVGDTEDVLFEKWFHCKDLGTQLAPIIQEFFHSEQYRTGKP 159
Cdd:cd06123   82 VPHSPQRPADTVGLVIERKRPPGELDGLRWYCENCGELLHEVEFHCDDLGTQLKPAIEEFFASEELRTCKP 152
3-HAO pfam06052
3-hydroxyanthranilic acid dioxygenase; In eukaryotes 3-hydroxyanthranilic acid dioxygenase (EC: ...
 2-149 1.24e-91

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: 268.18  E-value: 1.24e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998597    2 ERRVRVKSWVEENRASFQPPVCNKLMHQEQLKIMFVGGPNTRKDYHIEEGEEVFYQLEGDMILRVLEQGQHRDVPIRQGE 81
Cdd:pfam06052   4 VTPINIDAWVKENRGLLKPPVCNKCLHQDGFKVMIVGGPNERTDYHIEEGPEWFYQLKGDMVLKVVDEGDARDIVIRQGE 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568998597   82 IFLLPARVPHSPQRFANTMGLVIERRRLESELDGLRYYVGDTEDVLFEKWFHCKDLGTQLAPIIQEFF 149
Cdd:pfam06052  84 IFLLPARVPHSPQRFANTVGLVVERERLGTENDGLRWYCGHCNQVLFESWFYLLDLGTQLPPAILEFY 151
PRK13264 PRK13264
3-hydroxyanthranilate 3,4-dioxygenase; Provisional
 8-156 2.01e-64

3-hydroxyanthranilate 3,4-dioxygenase; Provisional


Pssm-ID: 183930  Cd Length: 177  Bit Score: 199.76  E-value: 2.01e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998597   8 KSWVEENRASFQPPVCNKLMHQE-QLKIMFVGGPNTRKDYHIEEGEEVFYQLEGDMILRVLEQGQHRDVPIRQGEIFLLP 86
Cdd:PRK13264  10 HKWIEEHRHLLKPPVGNKQIWQDsDFIVMVVGGPNARTDFHYDPGEEFFYQLEGDMYLKVQEDGKRRDVPIREGEMFLLP 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998597  87 ARVPHSPQRFANTMGLVIERRRLESELDGLRYYVGDTEDVLFEKWFHCKDLGTQLAPIIQEFFHSEQYRT 156
Cdd:PRK13264  90 PHVPHSPQREAGSIGLVIERKRPEGELDGFQWYCDECNHKVHEVEVQLTDIETDLPPVFAAFYASEELRT 159
anthran_nbaC TIGR03037
3-hydroxyanthranilate 3,4-dioxygenase; Members of this protein family, from both bacteria and ...
 8-158 2.49e-57

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: 181.12  E-value: 2.49e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998597    8 KSWVEENRASFQPPVCNKLMHQE-QLKIMFVGGPNTRKDYHIEEGEEVFYQLEGDMILRVLEQGQHRDVPIRQGEIFLLP 86
Cdd:TIGR03037   4 KKWIDEHKHLLKPPVGNQQIWQDsEFMVTVVGGPNARTDFHDDPGEEFFYQLKGEMYLKVTEEGKREDVPIREGDIFLLP 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568998597   87 ARVPHSPQRFANTMGLVIERRRLESELDGLRYYVGDTEDVLFEKWFHCKDLGTQLAPIIQEFFHSEQYRTGK 158
Cdd:TIGR03037  84 PHVPHSPQRPAGSIGLVIERKRPQGELDGFQWFCPQCGHKLHRAEVQLENIVTDLPPVFEHFYSNEDARTCK 155
cupin_BLL4011-like cd02235
Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes ...
 40-92 8.62e-06

Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to BLL4011, a Bradyrhizobium diazoefficiens protein 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: 380363 [Multi-domain]  Cd Length: 100  Bit Score: 43.72  E-value: 8.62e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568998597  40 PNTRKDYHIEEGEEVFYQLEGDMILRVleQGQhRDVPIRQGEIFLLPARVPHS 92
Cdd:cd02235   28 PGAVAGRHTHPGEESGYVLEGSLELEV--DGQ-PPVTLKAGDSFFIPAGTVHN 77
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
40-92 4.64e-04

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 38.68  E-value: 4.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568998597  40 PNTRKDYHIEEGEEVFYQLEGDMILRVleqgQHRDVPIRQGEIFLLPARVPHS 92
Cdd:COG1917   32 PGARTPWHSHPGEELIYVLEGEGEVEV----GGEEYELKPGDVVFIPPGVPHA 80
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
46-99 5.46e-04

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 38.85  E-value: 5.46e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568998597  46 YHiEEGEEVFYQLEGDMILRVleqGQHRdVPIRQGEIFLLPARVPHspqRFANT 99
Cdd:COG3837   46 AH-SAEEEFVYVLEGELTLRI---GGEE-YVLEPGDSVGFPAGVPH---RLRNR 91
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 40-99 6.43e-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.


Pssm-ID: 380338 [Multi-domain]  Cd Length: 73  Bit Score: 37.46  E-value: 6.43e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568998597  40 PNTRKDYHI-EEGEEVFYQLEGDMILRVLEQGQhrdVPIRQGEIFLLPARVPHSpqrFANT 99
Cdd:cd02208    8 PGTSSPPHWhPEQDEIFYVLSGEGELTLDDGET---VELKAGDIVLIPPGVPHS---FVNT 62
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 46-94 7.78e-04

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: 38.41  E-value: 7.78e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568998597  46 YHIEEGEeVFYQLEGDMILRVLEQ-GQHRDVPIRQGEIFLLPARVPHSPQ 94
Cdd:COG2140   20 WHPNAAE-WYYVLSGEARMTVQDPpGRARTVDVGPGDVVYVPPGYGHYII 68
cupin_XcTcmJ-like cd07006
Xanthomonas campestris XcTcmJ and related proteins, cupin domain; This family includes ...
 209-260 9.54e-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: 37.73  E-value: 9.54e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568998597 209 TQVIAHGQ--GSSKGPRQDVDVWLWQQEGSSKVTMGGQCIALAPDDSLLVPAGT 260
Cdd:cd07006   14 TMVLAPGDteGGPDNRHRGSDQWLYVVSGSGEAIVEGERVALKPGSLLLIEAGE 67
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
31-99 9.88e-04

Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 38.20  E-value: 9.88e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998597  31 QLKIMFVGgPNTRKDYHI-EEGEEVFYQLEGDMILRVLEQgqhrDVPIRQGEIFLLPARVPHspqRFANT 99
Cdd:COG0662   28 SVKRITVP-PGAELSLHVhPHRDEFFYVLEGTGEVTIGDE----EVELKAGDSVYIPAGVPH---RLRNP 89
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 40-99 5.34e-03

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 34.93  E-value: 5.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568998597   40 PNTRKDYHIEEGE-EVFYQLEGDMILRVLEQgqhrDVPIRQGEIFLLPARVPHspqRFANT 99
Cdd:pfam07883   7 PGESSPPHRHPGEdEFFYVLEGEGELTVDGE----EVVLKAGDSVYFPAGVPH---RFRNT 60
cupin_Bh2720-like cd02223
Bacillus halodurans Bh2720 and related proteins, cupin domain; This family includes bacterial, ...
 224-260 7.13e-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: 7.13e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 568998597 224 QDVDVWLWQQEGSSKVTMGGQCIALAPDDSLLVPAGT 260
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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