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Conserved domains on  [gi|2508160873|gb|WHP12237|]
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3-((4R)-4-hydroxycyclohexa-1,5-dien-1-yl)-2-oxopropanoate isomerase [Bacillus subtilis]

Protein Classification

cupin domain-containing protein( domain architecture ID 14449041)

cupin domain-containing protein such as Bacillus subtilis BacB that is involved in the synthesis of bacilysin, a non-ribosomally synthesized dipeptide antibiotic that is active against a wide range of bacteria and fungi

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
cupin_BacB_N cd20307
Bacillus subtilis bacilysin and related proteins, N-terminal cupin domain; This model ...
11-110 6.63e-54

Bacillus subtilis bacilysin and related proteins, N-terminal cupin domain; This model represents the N-terminal domain of bacilysin (BacB, also known as AerE in Microcystis aeruginosa), a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. Bacilysin is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF Aeruginosin biosynthesis gene cluster in Microcystis aeruginosa. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


:

Pssm-ID: 380441 [Multi-domain]  Cd Length: 100  Bit Score: 168.59  E-value: 6.63e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508160873  11 YFPTPKLIEWENGVRQYSTVRGDTEVLMSYVPPHTNVEPHQHKEVQIGMVVSGELMMTVGDVTRKMTALESAYIAPPHVP 90
Cdd:cd20307     1 FFPVPKTIKLENGVELYSFQCQDTVVQLSYIAPGAVVELHQHPESQIGMVLSGELEMNVGGVKKVMEPLQDVYVAPPNVP 80
                          90       100
                  ....*....|....*....|
gi 2508160873  91 HGARNDTDQEVIAIDIKRLK 110
Cdd:cd20307    81 HGAVNPSSEEAVGLDIKRLK 100
cupin_BacB_C cd10547
Bacillus subtilis bacilysin and related proteins, C-terminal cupin domain; This model ...
127-219 3.29e-49

Bacillus subtilis bacilysin and related proteins, C-terminal cupin domain; This model represents the C-terminal domain of bacilysin (BacB, also known as AerE in Microcystis aeruginosa), a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. Bacilysin is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF aeruginosin biosynthesis gene cluster in Microcystis aeruginosa. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


:

Pssm-ID: 380415 [Multi-domain]  Cd Length: 92  Bit Score: 156.27  E-value: 3.29e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508160873 127 KTRDLLPGMEVTFFVEDWVEIMLAKIPGnGGEMPFHKHRNEQIGICIGGGYDMTVEGCTVEMKFGTAYFCEPREDHGAIN 206
Cdd:cd10547     1 PTRDKITGLPCQFFVGSWFEIMISQIPP-GGKMPLHQHRGEQIGIILNGKYDMTVGGEEQELGYGKIYYAPPNVSHSGYN 79
                          90
                  ....*....|...
gi 2508160873 207 RSEKESKSINIFF 219
Cdd:cd10547    80 DSDETATLINIFI 92
 
Name Accession Description Interval E-value
cupin_BacB_N cd20307
Bacillus subtilis bacilysin and related proteins, N-terminal cupin domain; This model ...
11-110 6.63e-54

Bacillus subtilis bacilysin and related proteins, N-terminal cupin domain; This model represents the N-terminal domain of bacilysin (BacB, also known as AerE in Microcystis aeruginosa), a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. Bacilysin is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF Aeruginosin biosynthesis gene cluster in Microcystis aeruginosa. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380441 [Multi-domain]  Cd Length: 100  Bit Score: 168.59  E-value: 6.63e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508160873  11 YFPTPKLIEWENGVRQYSTVRGDTEVLMSYVPPHTNVEPHQHKEVQIGMVVSGELMMTVGDVTRKMTALESAYIAPPHVP 90
Cdd:cd20307     1 FFPVPKTIKLENGVELYSFQCQDTVVQLSYIAPGAVVELHQHPESQIGMVLSGELEMNVGGVKKVMEPLQDVYVAPPNVP 80
                          90       100
                  ....*....|....*....|
gi 2508160873  91 HGARNDTDQEVIAIDIKRLK 110
Cdd:cd20307    81 HGAVNPSSEEAVGLDIKRLK 100
cupin_BacB_C cd10547
Bacillus subtilis bacilysin and related proteins, C-terminal cupin domain; This model ...
127-219 3.29e-49

Bacillus subtilis bacilysin and related proteins, C-terminal cupin domain; This model represents the C-terminal domain of bacilysin (BacB, also known as AerE in Microcystis aeruginosa), a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. Bacilysin is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF aeruginosin biosynthesis gene cluster in Microcystis aeruginosa. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380415 [Multi-domain]  Cd Length: 92  Bit Score: 156.27  E-value: 3.29e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508160873 127 KTRDLLPGMEVTFFVEDWVEIMLAKIPGnGGEMPFHKHRNEQIGICIGGGYDMTVEGCTVEMKFGTAYFCEPREDHGAIN 206
Cdd:cd10547     1 PTRDKITGLPCQFFVGSWFEIMISQIPP-GGKMPLHQHRGEQIGIILNGKYDMTVGGEEQELGYGKIYYAPPNVSHSGYN 79
                          90
                  ....*....|...
gi 2508160873 207 RSEKESKSINIFF 219
Cdd:cd10547    80 DSDETATLINIFI 92
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
22-106 4.63e-12

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 60.63  E-value: 4.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508160873  22 NGVRQYSTVRGDTEVLMSYV--PPHTNVEPHQHKEVQIGMVVSGELMMTVGDVTRKMTALESAYIaPPHVPHGARNDTDQ 99
Cdd:COG1917     9 TGVSVRVLADGEDELEVVRVtfEPGARTPWHSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFI-PPGVPHAFRNLGDE 87

                  ....*..
gi 2508160873 100 EVIAIDI 106
Cdd:COG1917    88 PAVLLVV 94
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
41-106 7.59e-11

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: 56.50  E-value: 7.59e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2508160873  41 VPPHTNVEPHQHK-EVQIGMVVSGELMMTVGDVTRKMTALESAYIaPPHVPHGARNDTDQEVIAIDI 106
Cdd:pfam07883   5 LPPGESSPPHRHPgEDEFFYVLEGEGELTVDGEEVVLKAGDSVYF-PAGVPHRFRNTGDEPARLLDV 70
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
156-222 9.09e-08

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 48.69  E-value: 9.09e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2508160873 156 GGEMPFHKHRNEQIGICIGGGYDMTVEGCTVEMKFGTAYFCEPREDHGAINRSEKESKSINIFFPPR 222
Cdd:COG1917    33 GARTPWHSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGDEPAVLLVVFSPGL 99
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
156-218 2.15e-07

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: 46.87  E-value: 2.15e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2508160873 156 GGEMPFHKHRNE-QIGICIGGGYDMTVEGCTVEMKFGTAYFCEPREDHGAINRSEKESKSINIF 218
Cdd:pfam07883   8 GESSPPHRHPGEdEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDVY 71
 
Name Accession Description Interval E-value
cupin_BacB_N cd20307
Bacillus subtilis bacilysin and related proteins, N-terminal cupin domain; This model ...
11-110 6.63e-54

Bacillus subtilis bacilysin and related proteins, N-terminal cupin domain; This model represents the N-terminal domain of bacilysin (BacB, also known as AerE in Microcystis aeruginosa), a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. Bacilysin is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF Aeruginosin biosynthesis gene cluster in Microcystis aeruginosa. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380441 [Multi-domain]  Cd Length: 100  Bit Score: 168.59  E-value: 6.63e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508160873  11 YFPTPKLIEWENGVRQYSTVRGDTEVLMSYVPPHTNVEPHQHKEVQIGMVVSGELMMTVGDVTRKMTALESAYIAPPHVP 90
Cdd:cd20307     1 FFPVPKTIKLENGVELYSFQCQDTVVQLSYIAPGAVVELHQHPESQIGMVLSGELEMNVGGVKKVMEPLQDVYVAPPNVP 80
                          90       100
                  ....*....|....*....|
gi 2508160873  91 HGARNDTDQEVIAIDIKRLK 110
Cdd:cd20307    81 HGAVNPSSEEAVGLDIKRLK 100
cupin_BacB_C cd10547
Bacillus subtilis bacilysin and related proteins, C-terminal cupin domain; This model ...
127-219 3.29e-49

Bacillus subtilis bacilysin and related proteins, C-terminal cupin domain; This model represents the C-terminal domain of bacilysin (BacB, also known as AerE in Microcystis aeruginosa), a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. Bacilysin is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF aeruginosin biosynthesis gene cluster in Microcystis aeruginosa. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380415 [Multi-domain]  Cd Length: 92  Bit Score: 156.27  E-value: 3.29e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508160873 127 KTRDLLPGMEVTFFVEDWVEIMLAKIPGnGGEMPFHKHRNEQIGICIGGGYDMTVEGCTVEMKFGTAYFCEPREDHGAIN 206
Cdd:cd10547     1 PTRDKITGLPCQFFVGSWFEIMISQIPP-GGKMPLHQHRGEQIGIILNGKYDMTVGGEEQELGYGKIYYAPPNVSHSGYN 79
                          90
                  ....*....|...
gi 2508160873 207 RSEKESKSINIFF 219
Cdd:cd10547    80 DSDETATLINIFI 92
cupin_BacB cd06975
Bacillus subtilis bacilysin and related proteins, cupin domain; Bacilysin (BacB, also known as ...
16-108 3.28e-45

Bacillus subtilis bacilysin and related proteins, cupin domain; Bacilysin (BacB, also known as AerE in Microcystis aeruginosa) is a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. It is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF aeruginosin biosynthesis gene cluster in Microcystis aeruginosa.


Pssm-ID: 380380 [Multi-domain]  Cd Length: 93  Bit Score: 146.19  E-value: 3.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508160873  16 KLIEWENGVRQYSTVRGDTEVLMSYVPPHTNVEPHQHKEVQIGMVVSGELMMTVGDVTRKMTALESAYIAPPHVPHGARN 95
Cdd:cd06975     1 KTIKLETGVELQFFVGSWTEIMLSYIPPGAKMPLHQHREEQIGMILNGELEMTVGGEEQELEPLGDVYYAPPNVPHGAVN 80
                          90
                  ....*....|...
gi 2508160873  96 DTDQEVIAIDIKR 108
Cdd:cd06975    81 PSDETAVLLDIKR 93
cupin_BacB cd06975
Bacillus subtilis bacilysin and related proteins, cupin domain; Bacilysin (BacB, also known as ...
127-219 7.10e-41

Bacillus subtilis bacilysin and related proteins, cupin domain; Bacilysin (BacB, also known as AerE in Microcystis aeruginosa) is a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. It is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF aeruginosin biosynthesis gene cluster in Microcystis aeruginosa.


Pssm-ID: 380380 [Multi-domain]  Cd Length: 93  Bit Score: 135.01  E-value: 7.10e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508160873 127 KTRDLLPGMEVTFFVEDWVEIMLAKIPGnGGEMPFHKHRNEQIGICIGGGYDMTVEGCTVEMKF-GTAYFCEPREDHGAI 205
Cdd:cd06975     1 KTIKLETGVELQFFVGSWTEIMLSYIPP-GAKMPLHQHREEQIGMILNGELEMTVGGEEQELEPlGDVYYAPPNVPHGAV 79
                          90
                  ....*....|....
gi 2508160873 206 NRSEKESKSINIFF 219
Cdd:cd06975    80 NPSDETAVLLDIKR 93
cupin_BacB_C cd10547
Bacillus subtilis bacilysin and related proteins, C-terminal cupin domain; This model ...
35-106 4.03e-17

Bacillus subtilis bacilysin and related proteins, C-terminal cupin domain; This model represents the C-terminal domain of bacilysin (BacB, also known as AerE in Microcystis aeruginosa), a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. Bacilysin is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF aeruginosin biosynthesis gene cluster in Microcystis aeruginosa. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380415 [Multi-domain]  Cd Length: 92  Bit Score: 73.84  E-value: 4.03e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2508160873  35 EVLMSYVPPHTNVEPHQHKEVQIGMVVSGELMMTVGDVTRKMTaLESAYIAPPHVPHGARNDTDQEVIAIDI 106
Cdd:cd10547    20 EIMISQIPPGGKMPLHQHRGEQIGIILNGKYDMTVGGEEQELG-YGKIYYAPPNVSHSGYNDSDETATLINI 90
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
18-106 1.20e-14

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: 67.49  E-value: 1.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508160873  18 IEWE---NGVRQySTVRGDTEVLMSYV--PPHTNVEPHQHKEVQIGMVVSGELMMTVGDVTRKMTALESAYIaPPHVPHG 92
Cdd:cd02238     7 LPWEelgPGVRR-KILAGGEKLMLVEVrfEKGAVVPLHSHPHEQIGYVLSGRFEFTIGGETRILKPGDSYYI-PPNVPHG 84
                          90
                  ....*....|....
gi 2508160873  93 ARNDTDqeVIAIDI 106
Cdd:cd02238    85 AEALED--SVLLDV 96
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
22-106 4.63e-12

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 60.63  E-value: 4.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508160873  22 NGVRQYSTVRGDTEVLMSYV--PPHTNVEPHQHKEVQIGMVVSGELMMTVGDVTRKMTALESAYIaPPHVPHGARNDTDQ 99
Cdd:COG1917     9 TGVSVRVLADGEDELEVVRVtfEPGARTPWHSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFI-PPGVPHAFRNLGDE 87

                  ....*..
gi 2508160873 100 EVIAIDI 106
Cdd:COG1917    88 PAVLLVV 94
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
41-106 7.59e-11

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: 56.50  E-value: 7.59e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2508160873  41 VPPHTNVEPHQHK-EVQIGMVVSGELMMTVGDVTRKMTALESAYIaPPHVPHGARNDTDQEVIAIDI 106
Cdd:pfam07883   5 LPPGESSPPHRHPgEDEFFYVLEGEGELTVDGEEVVLKAGDSVYF-PAGVPHRFRNTGDEPARLLDV 70
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
129-222 5.78e-10

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: 54.78  E-value: 5.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508160873 129 RDLLPGMEVTFFVED----WVEIMLAKipgnGGEMPFHKHRNEQIGICIGGGYDMTVEGCTVEMKFGTAYFCEPREDHGA 204
Cdd:cd02238    10 EELGPGVRRKILAGGeklmLVEVRFEK----GAVVPLHSHPHEQIGYVLSGRFEFTIGGETRILKPGDSYYIPPNVPHGA 85
                          90
                  ....*....|....*...
gi 2508160873 205 INRseKESKSINIFFPPR 222
Cdd:cd02238    86 EAL--EDSVLLDVFSPPR 101
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
7-106 4.13e-09

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 52.84  E-value: 4.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508160873   7 MQELYFPTPKLIEWEnGVRQYSTVRGDTEVLMSYVPPHTNVEPHQHKEV-QIGMVVSGELMMTVGDVTRKMTALESAYIa 85
Cdd:COG0662     1 MQDVNIEELKAIGWG-SYEVLGEGGERLSVKRITVPPGAELSLHVHPHRdEFFYVLEGTGEVTIGDEEVELKAGDSVYI- 78
                          90       100
                  ....*....|....*....|.
gi 2508160873  86 PPHVPHGARNDTDQEVIAIDI 106
Cdd:COG0662    79 PAGVPHRLRNPGDEPLELLEV 99
cupin_DddK cd06988
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ...
41-106 1.34e-08

Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes mostly bacterial proteins homologous to dimethylsulfoniopropionate lyase DddK from marine bacterium Pelagibacter. DddK cleaves dimethylsulfoniopropionate (DMSP), the organic osmolyte and antioxidant produced in marine environments, and yields acrylate and the climate-active gas dimethyl sulfide (DMS). DddK contains a double-stranded beta-helical motif which utilizes various divalent metal ions as cofactors for catalytic activity; however, nickel, an abundant metal ion in marine environments, confers the highest DMSP lyase activity. Also included in this family is Plu4264, a Photorhabdus luminescens manganese-containing cupin shown to have similar metal binding site to TM1287 decarboxylase, but two very different substrate binding pockets. The Plu4264 binding pocket shows a cavity and substrate entry point more than twice as large as and more hydrophobic than TM1287, suggesting that Plu4264 accepts a substrate that is significantly larger than that of TM1287, a putative oxalate decarboxylase. Thus, the function of Plu4264 could be similar to that of TM1287 but with a larger, less charged substrate. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380393 [Multi-domain]  Cd Length: 76  Bit Score: 50.31  E-value: 1.34e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2508160873  41 VPPHTNVEPHQHKEVQIGMVVSGELMMTVGDVTRKMTALESAYIaPPHVPHGARNDTDQEVIAIDI 106
Cdd:cd06988     9 VRPGTTSTPHSHHEYEIFIVISGKGIVVVDGEREPVKAGDVVYI-PPGTEHYVKNDGDEDFEFYSI 73
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
156-222 9.09e-08

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 48.69  E-value: 9.09e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2508160873 156 GGEMPFHKHRNEQIGICIGGGYDMTVEGCTVEMKFGTAYFCEPREDHGAINRSEKESKSINIFFPPR 222
Cdd:COG1917    33 GARTPWHSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGDEPAVLLVVFSPGL 99
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
156-218 2.15e-07

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: 46.87  E-value: 2.15e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2508160873 156 GGEMPFHKHRNE-QIGICIGGGYDMTVEGCTVEMKFGTAYFCEPREDHGAINRSEKESKSINIF 218
Cdd:pfam07883   8 GESSPPHRHPGEdEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDVY 71
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
40-106 4.86e-07

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: 45.94  E-value: 4.86e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2508160873  40 YVPPHTNVEPHQHKEV-QIGMVVSGELMMTVGDV-TRKMTALESAYIaPPHVPHGARNDTDQEVIAIDI 106
Cdd:cd02208     5 TLPPGTSSPPHWHPEQdEIFYVLSGEGELTLDDGeTVELKAGDIVLI-PPGVPHSFVNTSDEPAVFLVV 72
cupin_XRE_C cd02209
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ...
35-104 5.58e-07

XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; This family contains transcriptional regulators containing an N-terminal XRE (Xenobiotic Response Element) family helix-turn-helix (HTH) DNA-binding domain and a C-terminal cupin domain. Included in this family is Escherichia coli transcription factor SutR (YdcN) that plays a regulatory role in sulfur utilization; it regulates a set of genes involved in the generation of sulfate and its reduction, the synthesis of cysteine, the synthesis of enzymes containing Fe-S as cofactors, and the modification of tRNA with use of sulfur-containing substrates. This family belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380339 [Multi-domain]  Cd Length: 90  Bit Score: 46.35  E-value: 5.58e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2508160873  35 EVLMSYVPPH-TNVEPHQHKEVQIGMVVSGELMMTVGDVTRKMTALESAYIaPPHVPHGARNDTDQEVIAI 104
Cdd:cd02209    17 EPFLVTLPPGgSGGEPYSHEGEEFGYVLEGELELTVGGETYVLEAGDSIYF-DSDVPHRYRNPGDEPARVL 86
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
41-104 1.64e-05

Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to MJ1618, a Methanocaldococcus jannaschii protein of unknown function with a cupin beta barrel domain. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion.


Pssm-ID: 380344 [Multi-domain]  Cd Length: 100  Bit Score: 42.50  E-value: 1.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2508160873  41 VPPHTNVEPHQHKEV-QIGMVVSGELMMTVGDVTRKMTALESAYIaPPHVPHGARN--DTDQEVIAI 104
Cdd:cd02214    26 VPPGESTLPHRLKGSeEVYYILEGEGTMEIDGEPREVGPGDAVLI-PPGAVQRIENtgEEDLVFLCI 91
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
40-100 2.10e-04

Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to Thermotoga maritima TM1459, a manganese-containing cupin that has been shown to cleave C=C bonds in the presence of alkylperoxide as oxidant in vitro. Its biological function is still unknown. This family also includes Halorhodospira halophila Hhal_0468. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer.


Pssm-ID: 380351 [Multi-domain]  Cd Length: 91  Bit Score: 38.97  E-value: 2.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2508160873  40 YVPPHTNvePHQHkEVqigMVVSGELMMTVGDVTRKMTALESAYIaPPHVPHGARNDTDQE 100
Cdd:cd02222    29 HTPLHTH--PWEH-EV---YVLRGKGVVVIGGEEYPVKPGDVVYI-PPNEPHQFRNTGDEP 82
cupin_TTHA0104 cd06122
Thermus thermophilus TTHA0104 and related proteins, cupin domain; This family contains ...
49-102 3.81e-04

Thermus thermophilus TTHA0104 and related proteins, cupin domain; This family contains bacterial proteins including TTHA0104 (also called TT1209), a putative antibiotic synthesis protein from Thermus thermophilus. TTHA0104 is a cupin-like protein. The 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).


Pssm-ID: 380377 [Multi-domain]  Cd Length: 102  Bit Score: 38.69  E-value: 3.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2508160873  49 PHQHKEV-QIGMVVSGELMMTVGDVTRKMTALESAyIAPPHVPHGARNDTDQEVI 102
Cdd:cd06122    42 VHAHAGSdKVYFVLEGEGRFTVGDEERELGAGEAV-LAPAGVPHGVRNTGAERLV 95
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
156-218 1.35e-03

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: 36.31  E-value: 1.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2508160873 156 GGEMPFHKHRN-EQIGICI-GGGYDMTVEGCTVEMKFGTAYFCEPREDHGAINRSEKESKSINIF 218
Cdd:cd02208     9 GTSSPPHWHPEqDEIFYVLsGEGELTLDDGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVVS 73
cupin_DRT102 cd06989
Arabidopsis thaliana DRT102 and related proteins, cupin domain; This family includes bacterial ...
41-102 1.71e-03

Arabidopsis thaliana DRT102 and related proteins, cupin domain; This family includes bacterial and eukaryotic proteins homologous to DNA-damage-repair/toleration protein DRT102 found in Arabidopsis thaliana. DRT102 may be involved in DNA repair from UV damage. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380394  Cd Length: 97  Bit Score: 36.74  E-value: 1.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2508160873  41 VPPHTNVEPHQHKEVQIGMVVSGELMMTVGDV--TRKMTALE--SAYIAPPHVPHGARNDtDQEVI 102
Cdd:cd06989    25 FPAGYKIPPHTHPDDERVTVISGTFYLGMGDKfdEAKAKALPagSFFTLPAGTPHFAWAK-DEETV 89
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
156-211 2.32e-03

Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to Thermotoga maritima TM1459, a manganese-containing cupin that has been shown to cleave C=C bonds in the presence of alkylperoxide as oxidant in vitro. Its biological function is still unknown. This family also includes Halorhodospira halophila Hhal_0468. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer.


Pssm-ID: 380351 [Multi-domain]  Cd Length: 91  Bit Score: 36.27  E-value: 2.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2508160873 156 GGEMPFHKHRNEQIGICIGGGYDMTVEGCTVEMKFGTAYFCEPREDHGAINRSEKE 211
Cdd:cd02222    27 GGHTPLHTHPWEHEVYVLRGKGVVVIGGEEYPVKPGDVVYIPPNEPHQFRNTGDEP 82
cupin_PMI_typeII_C cd02213
Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal ...
60-109 3.49e-03

Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal cupin domain of mannose-6-phosphate isomerases (MPIs) which have been classified broadly into two groups, type I and type II, based on domain organization. This family contains type II phosphomannose isomerase (also known as PMI-GDP, phosphomannose isomerase/GDP-D-mannose pyrophosphorylase), a bifunctional enzyme with two domains that catalyze the first and third steps in the GDP-mannose pathway in which fructose 6-phosphate is converted to GDP-D-mannose. The N-terminal domain catalyzes the first and rate-limiting step, the isomerization from D-fructose-6-phosphate to D-mannose-6-phosphate, while the C-terminal cupin domain (represented in this alignment model) converts mannose 1-phosphate to GDP-D-mannose in the final step of the reaction. Although these two domains occur together in one protein in most organisms, they occur as separate proteins in certain cyanobacterial organisms. Also, although type I and type II MPIs have no overall sequence similarity, they share a conserved catalytic motif.


Pssm-ID: 380343 [Multi-domain]  Cd Length: 126  Bit Score: 36.38  E-value: 3.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2508160873  60 VVSGELMMTVGDVTRKMTALESAYIaPPHVPHGARNDTDQ--EVIAI---------DIKRL 109
Cdd:cd02213    67 VVSGTAEVTLDGKEKLLKEGESIYI-PKGTKHRLENPGKIplEIIEVqtgeylgedDIVRL 126
cupin_BLL4011-like cd02235
Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes ...
41-101 5.29e-03

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: 35.25  E-value: 5.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2508160873  41 VPPHTNVEPHQHKEVQIGMVVSGELMMTV-GDVTRKMTALESAYIaPPHVPHGARNDTDQEV 101
Cdd:cd02235    26 IPPGAVAGRHTHPGEESGYVLEGSLELEVdGQPPVTLKAGDSFFI-PAGTVHNAKNVGSGPA 86
RmlC COG4101
Uncharacterized conserved protein, RmlC-like cupin domain [General function prediction only];
41-104 9.97e-03

Uncharacterized conserved protein, RmlC-like cupin domain [General function prediction only];


Pssm-ID: 443277  Cd Length: 146  Bit Score: 35.33  E-value: 9.97e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2508160873  41 VPPHTNVEPHQHKEVQIGM-VVSGELMMTVGD---VTRKMTALESAYIaPPHVPHGARN-DTDQEVIAI 104
Cdd:COG4101    53 IPPGARAKAHHHGEHETAIyVLSGRAETRYGErleHRVVTEPGDFIFI-PPGVPHQEINlSDTEPAVAV 120
 
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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