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Conserved domains on  [gi|1806016548|gb|KAF1869875|]
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hypothetical protein Lal_00017452 [Lupinus albus]

Protein Classification

Glyoxal_oxid_N and E_set_GO_C domain-containing protein( domain architecture ID 12073929)

Glyoxal_oxid_N and E_set_GO_C domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyoxal_oxid_N pfam07250
Glyoxal oxidase N-terminus; This family represents the N-terminus (approximately 300 residues) ...
 49-291 0e+00

Glyoxal oxidase N-terminus; This family represents the N-terminus (approximately 300 residues) of a number of plant and fungal glyoxal oxidase enzymes. Glyoxal oxidase catalyzes the oxidation of aldehydes to carboxylic acids, coupled with reduction of dioxygen to hydrogen peroxide. It is an essential component of the extracellular lignin degradation pathways of the wood-rot fungus Phanerochaete chrysosporium.


:

Pssm-ID: 399910 [Multi-domain]  Cd Length: 243  Bit Score: 514.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806016548  49 MHMQLLHNDKVIMFDRTDFGPSNLPLPYGHCRVDPYDKALTTDCTAHSLIYDITTNSFRPLMVQTDTWCSSASVLPNGTL 128
Cdd:pfam07250   1 MHMQLLHNNKVIMFDRTDFGPSNLSLPNGRCRNDPRDKALKTDCTAHSVEYDVATNTVRPLTILTDTWCSSGAFLPDGTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806016548 129 VQTGGFNDGERNIRMFTPCWDETCDWNEFPGYLSQRRWYATNQILPDGRVIVVGGRRQFNYEFYPKN-QNNNSPIHLSFL 207
Cdd:pfam07250  81 VQTGGFNDGERKVRYFSPCDSGTCDWVELPNGLAAGRWYATNQILPDGRVIVVGGRRAFSYEFVPKEgQSNEGVFELPFL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806016548 208 QETSDPNdENNLYPFLHLLPDGNLFIFANTRSVLFDYNQNRVIKEFPPIPGNdPRNYPSSGSSILLPLDENKD-YIEAEI 286
Cdd:pfam07250 161 RETNDPQ-ENNLYPFVHLLPDGNLFIFANNRSILLDYKTNKVVREFPTLPGG-PRNYPSSGSSVLLPLDLNNDgFIEAEV 238


                  ....*
gi 1806016548 287 MVCGG 291
Cdd:pfam07250 239 LVCGG 243
GO-like_E_set pfam09118
Galactose oxidase-like, Early set domain; E or 'early' set domains are associated with the ...
 468-552 2.79e-29

Galactose oxidase-like, Early set domain; E or 'early' set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates, and possesses a unique mononuclear copper site essential for catalysing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active centre necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end, and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family adopt a secondary structure consisting of a bundle of seven, mostly antiparallel, beta-strands surrounding a hydrophobic core. The 7 strands are arranged in 2 sheets, in a Greek-key topology. This domain is found in sugar-utilizing enzymes, such as galactose oxidase or chitinase.


:

Pssm-ID: 462683  Cd Length: 91  Bit Score: 110.73  E-value: 2.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806016548 468 TFTVTrYTSASEVSVRIIAPSFTTHSFGMNQRMVVLKlvgVTQMNGDTYYATIVGPSTAQIAPSGYYMLFVVHAGIPSSG 547
Cdd:pfam09118  11 TFTVT-FGVAGNVKVSLIRPGFVTHSVNMGQRLVFLD---VTSTGGTGYTVTVTAPPNPNIAPPGYYMLFVVDNGVPSVG 86


                  ....*
gi 1806016548 548 LWVQV 552
Cdd:pfam09118  87 KWVRV 91
 
Name Accession Description Interval E-value
Glyoxal_oxid_N pfam07250
Glyoxal oxidase N-terminus; This family represents the N-terminus (approximately 300 residues) ...
 49-291 0e+00

Glyoxal oxidase N-terminus; This family represents the N-terminus (approximately 300 residues) of a number of plant and fungal glyoxal oxidase enzymes. Glyoxal oxidase catalyzes the oxidation of aldehydes to carboxylic acids, coupled with reduction of dioxygen to hydrogen peroxide. It is an essential component of the extracellular lignin degradation pathways of the wood-rot fungus Phanerochaete chrysosporium.


Pssm-ID: 399910 [Multi-domain]  Cd Length: 243  Bit Score: 514.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806016548  49 MHMQLLHNDKVIMFDRTDFGPSNLPLPYGHCRVDPYDKALTTDCTAHSLIYDITTNSFRPLMVQTDTWCSSASVLPNGTL 128
Cdd:pfam07250   1 MHMQLLHNNKVIMFDRTDFGPSNLSLPNGRCRNDPRDKALKTDCTAHSVEYDVATNTVRPLTILTDTWCSSGAFLPDGTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806016548 129 VQTGGFNDGERNIRMFTPCWDETCDWNEFPGYLSQRRWYATNQILPDGRVIVVGGRRQFNYEFYPKN-QNNNSPIHLSFL 207
Cdd:pfam07250  81 VQTGGFNDGERKVRYFSPCDSGTCDWVELPNGLAAGRWYATNQILPDGRVIVVGGRRAFSYEFVPKEgQSNEGVFELPFL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806016548 208 QETSDPNdENNLYPFLHLLPDGNLFIFANTRSVLFDYNQNRVIKEFPPIPGNdPRNYPSSGSSILLPLDENKD-YIEAEI 286
Cdd:pfam07250 161 RETNDPQ-ENNLYPFVHLLPDGNLFIFANNRSILLDYKTNKVVREFPTLPGG-PRNYPSSGSSVLLPLDLNNDgFIEAEV 238


                  ....*
gi 1806016548 287 MVCGG 291
Cdd:pfam07250 239 LVCGG 243
GO-like_E_set pfam09118
Galactose oxidase-like, Early set domain; E or 'early' set domains are associated with the ...
 468-552 2.79e-29

Galactose oxidase-like, Early set domain; E or 'early' set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates, and possesses a unique mononuclear copper site essential for catalysing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active centre necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end, and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family adopt a secondary structure consisting of a bundle of seven, mostly antiparallel, beta-strands surrounding a hydrophobic core. The 7 strands are arranged in 2 sheets, in a Greek-key topology. This domain is found in sugar-utilizing enzymes, such as galactose oxidase or chitinase.


Pssm-ID: 462683  Cd Length: 91  Bit Score: 110.73  E-value: 2.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806016548 468 TFTVTrYTSASEVSVRIIAPSFTTHSFGMNQRMVVLKlvgVTQMNGDTYYATIVGPSTAQIAPSGYYMLFVVHAGIPSSG 547
Cdd:pfam09118  11 TFTVT-FGVAGNVKVSLIRPGFVTHSVNMGQRLVFLD---VTSTGGTGYTVTVTAPPNPNIAPPGYYMLFVVDNGVPSVG 86


                  ....*
gi 1806016548 548 LWVQV 552
Cdd:pfam09118  87 KWVRV 91
E_set_GO_C cd02851
C-terminal Early set domain associated with the catalytic domain of galactose oxidase; E or ...
 445-552 4.80e-25

C-terminal Early set domain associated with the catalytic domain of galactose oxidase; E or "early" set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalyzing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active center necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.


Pssm-ID: 199882  Cd Length: 103  Bit Score: 99.24  E-value: 4.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806016548 445 DQVRPNIQYMSSDILGYRVFSyITFTVTRytsASEVSVRIIAPSFTTHSFGMNQRMVVLKLVGvtqmNGDTYYATIVGPS 524
Cdd:cd02851     3 GAPRPTITSAPKTVGYGQTFT-VTVSGPG---GGIVRVTLVRPGFVTHSFNMGQRLVKLPVTG----SGGDYTVTVTAPP 74

                          90       100
                  ....*....|....*....|....*....
gi 1806016548 525 TAQIAPSGYYMLFVVHA-GIPSSGLWVQV 552
Cdd:cd02851    75 NANVAPPGYYMLFVVNAdGVPSVAKWVRV 103
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
93-185 5.61e-05

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 45.15  E-value: 5.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806016548  93 TAHSLIYDITTNSFRPLMVQTDTWCSSASVLPNGTLVQTGGFNDGERN--IRMFTPCWDEtcdWNEFPgYLSQRRWYATN 170
Cdd:COG3055    89 LNDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGGWDDGGNVawVEVYDPATGT---WTQLA-PLPTPRDHLAA 164

                          90
                  ....*....|....*
gi 1806016548 171 QILPDGRVIVVGGRR 185
Cdd:COG3055   165 AVLPDGKILVIGGRN 179
 
Name Accession Description Interval E-value
Glyoxal_oxid_N pfam07250
Glyoxal oxidase N-terminus; This family represents the N-terminus (approximately 300 residues) ...
 49-291 0e+00

Glyoxal oxidase N-terminus; This family represents the N-terminus (approximately 300 residues) of a number of plant and fungal glyoxal oxidase enzymes. Glyoxal oxidase catalyzes the oxidation of aldehydes to carboxylic acids, coupled with reduction of dioxygen to hydrogen peroxide. It is an essential component of the extracellular lignin degradation pathways of the wood-rot fungus Phanerochaete chrysosporium.


Pssm-ID: 399910 [Multi-domain]  Cd Length: 243  Bit Score: 514.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806016548  49 MHMQLLHNDKVIMFDRTDFGPSNLPLPYGHCRVDPYDKALTTDCTAHSLIYDITTNSFRPLMVQTDTWCSSASVLPNGTL 128
Cdd:pfam07250   1 MHMQLLHNNKVIMFDRTDFGPSNLSLPNGRCRNDPRDKALKTDCTAHSVEYDVATNTVRPLTILTDTWCSSGAFLPDGTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806016548 129 VQTGGFNDGERNIRMFTPCWDETCDWNEFPGYLSQRRWYATNQILPDGRVIVVGGRRQFNYEFYPKN-QNNNSPIHLSFL 207
Cdd:pfam07250  81 VQTGGFNDGERKVRYFSPCDSGTCDWVELPNGLAAGRWYATNQILPDGRVIVVGGRRAFSYEFVPKEgQSNEGVFELPFL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806016548 208 QETSDPNdENNLYPFLHLLPDGNLFIFANTRSVLFDYNQNRVIKEFPPIPGNdPRNYPSSGSSILLPLDENKD-YIEAEI 286
Cdd:pfam07250 161 RETNDPQ-ENNLYPFVHLLPDGNLFIFANNRSILLDYKTNKVVREFPTLPGG-PRNYPSSGSSVLLPLDLNNDgFIEAEV 238


                  ....*
gi 1806016548 287 MVCGG 291
Cdd:pfam07250 239 LVCGG 243
GO-like_E_set pfam09118
Galactose oxidase-like, Early set domain; E or 'early' set domains are associated with the ...
 468-552 2.79e-29

Galactose oxidase-like, Early set domain; E or 'early' set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates, and possesses a unique mononuclear copper site essential for catalysing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active centre necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end, and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family adopt a secondary structure consisting of a bundle of seven, mostly antiparallel, beta-strands surrounding a hydrophobic core. The 7 strands are arranged in 2 sheets, in a Greek-key topology. This domain is found in sugar-utilizing enzymes, such as galactose oxidase or chitinase.


Pssm-ID: 462683  Cd Length: 91  Bit Score: 110.73  E-value: 2.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806016548 468 TFTVTrYTSASEVSVRIIAPSFTTHSFGMNQRMVVLKlvgVTQMNGDTYYATIVGPSTAQIAPSGYYMLFVVHAGIPSSG 547
Cdd:pfam09118  11 TFTVT-FGVAGNVKVSLIRPGFVTHSVNMGQRLVFLD---VTSTGGTGYTVTVTAPPNPNIAPPGYYMLFVVDNGVPSVG 86


                  ....*
gi 1806016548 548 LWVQV 552
Cdd:pfam09118  87 KWVRV 91
E_set_GO_C cd02851
C-terminal Early set domain associated with the catalytic domain of galactose oxidase; E or ...
 445-552 4.80e-25

C-terminal Early set domain associated with the catalytic domain of galactose oxidase; E or "early" set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalyzing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active center necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.


Pssm-ID: 199882  Cd Length: 103  Bit Score: 99.24  E-value: 4.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806016548 445 DQVRPNIQYMSSDILGYRVFSyITFTVTRytsASEVSVRIIAPSFTTHSFGMNQRMVVLKLVGvtqmNGDTYYATIVGPS 524
Cdd:cd02851     3 GAPRPTITSAPKTVGYGQTFT-VTVSGPG---GGIVRVTLVRPGFVTHSFNMGQRLVKLPVTG----SGGDYTVTVTAPP 74

                          90       100
                  ....*....|....*....|....*....
gi 1806016548 525 TAQIAPSGYYMLFVVHA-GIPSSGLWVQV 552
Cdd:cd02851    75 NANVAPPGYYMLFVVNAdGVPSVAKWVRV 103
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
93-185 5.61e-05

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 45.15  E-value: 5.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806016548  93 TAHSLIYDITTNSFRPLMVQTDTWCSSASVLPNGTLVQTGGFNDGERN--IRMFTPCWDEtcdWNEFPgYLSQRRWYATN 170
Cdd:COG3055    89 LNDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGGWDDGGNVawVEVYDPATGT---WTQLA-PLPTPRDHLAA 164

                          90
                  ....*....|....*
gi 1806016548 171 QILPDGRVIVVGGRR 185
Cdd:COG3055   165 AVLPDGKILVIGGRN 179
 
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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