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Conserved domains on  [gi|16078927|ref|NP_389748|]
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oxalate decarboxylase (Mn2+-dependent); spore constituent [Bacillus subtilis subsp. subtilis str. 168]

Protein Classification

oxalate decarboxylase family bicupin( domain architecture ID 11496804)

oxalate decarboxylase family bicupin contains two cupin domains and is similar to Bacillus subtilis oxalate decarboxylases OxdC and OxdD that convert oxalate to formate and CO(2)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
bicupin_oxalic TIGR03404
bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins ...
 22-387 0e+00

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: 689.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927    22 DGAGAIDTGPRNIIRDIQNPNIFVPPVTDEGMIPNLRFSFSDAPMKLDHGGWSREITVRQLPISTAIAGVNMSLTAGGVR 101
Cdd:TIGR03404   1 GGLGATDPGPRNLARDKQNPDILAPPTTDHGSVPNLKWSFSDSHNRLENGGWAREVTVRDLPISTAIAGVNMRLEPGAIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927   102 ELHWHKQAEWAYMLLGRARITAVDQDGRNFIADVGPGDLWYFPAGIPHSIQGL-EHCEFLLVFDDGNFSEFSTLTISDWL 180
Cdd:TIGR03404  81 ELHWHKEAEWAYVLYGSCRITAVDENGRNYIDDVGAGDLWYFPPGIPHSLQGLdEGCEFLLVFDDGNFSEDGTFLVTDWL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927   181 AHTPKDVLSANFGVPENAFNSLPSEQVYIYQGNVPGSVASEDIQSPYGKVPMTFKHELLNQPPIQMPGGSVRIVDSSNFP 260
Cdd:TIGR03404 161 AHTPKDVLAKNFGVPESAFDNLPLKELYIFPGTVPGPLDEEAVTGPAGEVPGPFTYHLSEQKPKQVPGGTVRIADSTNFP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927   261 ISKTIAAALVQIEPGAMRELHWHPNSDEWQYYLTGQGRMTVFIGNGTARTFDYRAGDVGYVPSNAGHYIQNTGTETLWFL 340
Cdd:TIGR03404 241 VSKTIAAAIVTVEPGAMRELHWHPNADEWQYFIQGQARMTVFAAGGNARTFDYQAGDVGYVPRNMGHYVENTGDETLVFL 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 16078927   341 EMFKSNRYADVSLNQWMALTPKELVQSNLNAGSVMLDSLRKKKVPVV 387
Cdd:TIGR03404 321 EVFKADRFADVSLNQWLALTPPQLVAAHLNLDDEVIDSLKKEKQPVV 367
 
Name Accession Description Interval E-value
bicupin_oxalic TIGR03404
bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins ...
 22-387 0e+00

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: 689.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927    22 DGAGAIDTGPRNIIRDIQNPNIFVPPVTDEGMIPNLRFSFSDAPMKLDHGGWSREITVRQLPISTAIAGVNMSLTAGGVR 101
Cdd:TIGR03404   1 GGLGATDPGPRNLARDKQNPDILAPPTTDHGSVPNLKWSFSDSHNRLENGGWAREVTVRDLPISTAIAGVNMRLEPGAIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927   102 ELHWHKQAEWAYMLLGRARITAVDQDGRNFIADVGPGDLWYFPAGIPHSIQGL-EHCEFLLVFDDGNFSEFSTLTISDWL 180
Cdd:TIGR03404  81 ELHWHKEAEWAYVLYGSCRITAVDENGRNYIDDVGAGDLWYFPPGIPHSLQGLdEGCEFLLVFDDGNFSEDGTFLVTDWL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927   181 AHTPKDVLSANFGVPENAFNSLPSEQVYIYQGNVPGSVASEDIQSPYGKVPMTFKHELLNQPPIQMPGGSVRIVDSSNFP 260
Cdd:TIGR03404 161 AHTPKDVLAKNFGVPESAFDNLPLKELYIFPGTVPGPLDEEAVTGPAGEVPGPFTYHLSEQKPKQVPGGTVRIADSTNFP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927   261 ISKTIAAALVQIEPGAMRELHWHPNSDEWQYYLTGQGRMTVFIGNGTARTFDYRAGDVGYVPSNAGHYIQNTGTETLWFL 340
Cdd:TIGR03404 241 VSKTIAAAIVTVEPGAMRELHWHPNADEWQYFIQGQARMTVFAAGGNARTFDYQAGDVGYVPRNMGHYVENTGDETLVFL 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 16078927   341 EMFKSNRYADVSLNQWMALTPKELVQSNLNAGSVMLDSLRKKKVPVV 387
Cdd:TIGR03404 321 EVFKADRFADVSLNQWLALTPPQLVAAHLNLDDEVIDSLKKEKQPVV 367
cupin_OxDC_N cd20304
Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-terminal ...
 58-210 5.21e-106

Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-terminal cupin domain of oxalate decarboxylase (OxDC; EC 4.1.1.2), a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds with each domain containing one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380438  Cd Length: 155  Bit Score: 308.77  E-value: 5.21e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927  58 RFSFSDAPMKLDHGGWSREITVRQLPISTAIAGVNMSLTAGGVRELHWHKQAEWAYMLLGRARITAVDQDGRNFIADVGP 137
Cdd:cd20304   1 KFSFSDSHNRLESGGWAREVTVRDLPISTGIAGVNMRLEPGAIRELHWHAAAEWAYVLSGRCRITAVDPEGRSFIDDVGP 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16078927 138 GDLWYFPAGIPHSIQGL--EHCEFLLVFDDGNFSEFSTLTISDWLAHTPKDVLSANFGVPENAFNSLPSEQVYIY 210
Cdd:cd20304  81 GDLWYFPRGHPHSIQGLgpDGCEFLLVFDDGNFSEFGTFSITDWLAHTPKEVLAKNFGVPAEAFDNLPKKELYIF 155
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 264-366 3.46e-40

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: 138.56  E-value: 3.46e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927 264 TIAAALVQIEPGAMRELHWHPNSDEWQYYLTGQGRMTVFIGNGTARTFDYRAGDVGYVPSNAGHYIQNTGTETLWFLEMF 343
Cdd:COG2140   2 TLAGGLTVLEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGRARTVDVGPGDVVYVPPGYGHYIINTGDEPLVFLAVF 81

                        90       100
                ....*....|....*....|....*.
gi 16078927 344 KSNR---YADVSLNQWMALTPKELVQ 366
Cdd:COG2140  82 DDDAgsdYGTISLSGWLAHTPPEVLA 107
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 242-370 1.47e-31

Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant.


Pssm-ID: 214845 [Multi-domain]  Cd Length: 146  Bit Score: 117.00  E-value: 1.47e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927    242 PPIQMPGGSVRIVDSSNFPISKT--IAAALVQIEPGAMRELHWHPNSDEWQYYLTGQGRMTVFIGNGTAR-TFDYRAGDV 318
Cdd:smart00835   5 PDFSNEGGRLREADPTNFPALNGlgISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNGNKVyDARLREGDV 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 16078927    319 GYVPSNAGHYIQNTGTETLWFLeMFKSNRYADVSL----NQWMALTPKELVQSNLN 370
Cdd:smart00835  85 FVVPQGHPHFQVNSGDENLEFV-AFNTNDPNRRFFlagrNSVLRGLPPEVLAAAFG 139
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 236-373 2.55e-26

Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant.


Pssm-ID: 395138  Cd Length: 151  Bit Score: 102.80  E-value: 2.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927   236 HELLNQPP-IQMPGGSVRIVDSSNFPISKT--IAAALVQIEPGAMRELHWHPNSDEWQYYLTGQGRM-TVFIGNG-TART 310
Cdd:pfam00190   1 LNLLEPGPtYNPEGGRVTTVNSKNLPGLNTlgISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVgFVVPGNGnRVFH 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16078927   311 FDYRAGDVGYVPSNAGHYIQNTGTETLWFLEMFKSNRYADVS----LNQWMALTPKELVQSNLNAGS 373
Cdd:pfam00190  81 KVLREGDVFVVPQGLPHFQYNIGDEPAVAFVAFDTNNPGNQSilagGFSSLPALPPEVLAKAFQLAG 147
PRK04190 PRK04190
glucose-6-phosphate isomerase; Provisional
 268-340 2.04e-04

glucose-6-phosphate isomerase; Provisional


Pssm-ID: 179774  Cd Length: 191  Bit Score: 41.94  E-value: 2.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927  268 ALVQIEPGA------MRELHWHPNSDEWQYY--LTGQGRMTVFIGNGTARTFDYRAGDVGYVPSNAGHYIQNTGTETLWF 339
Cdd:PRK04190  71 GTTRLYPGKvgdeyfMTKGHFHAKADRAEIYygLKGKGLMLLQDPEGEARWIEMEPGTVVYVPPYWAHRSVNTGDEPLVF 150


                 .
gi 16078927  340 L 340
Cdd:PRK04190 151 L 151
 
Name Accession Description Interval E-value
bicupin_oxalic TIGR03404
bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins ...
 22-387 0e+00

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: 689.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927    22 DGAGAIDTGPRNIIRDIQNPNIFVPPVTDEGMIPNLRFSFSDAPMKLDHGGWSREITVRQLPISTAIAGVNMSLTAGGVR 101
Cdd:TIGR03404   1 GGLGATDPGPRNLARDKQNPDILAPPTTDHGSVPNLKWSFSDSHNRLENGGWAREVTVRDLPISTAIAGVNMRLEPGAIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927   102 ELHWHKQAEWAYMLLGRARITAVDQDGRNFIADVGPGDLWYFPAGIPHSIQGL-EHCEFLLVFDDGNFSEFSTLTISDWL 180
Cdd:TIGR03404  81 ELHWHKEAEWAYVLYGSCRITAVDENGRNYIDDVGAGDLWYFPPGIPHSLQGLdEGCEFLLVFDDGNFSEDGTFLVTDWL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927   181 AHTPKDVLSANFGVPENAFNSLPSEQVYIYQGNVPGSVASEDIQSPYGKVPMTFKHELLNQPPIQMPGGSVRIVDSSNFP 260
Cdd:TIGR03404 161 AHTPKDVLAKNFGVPESAFDNLPLKELYIFPGTVPGPLDEEAVTGPAGEVPGPFTYHLSEQKPKQVPGGTVRIADSTNFP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927   261 ISKTIAAALVQIEPGAMRELHWHPNSDEWQYYLTGQGRMTVFIGNGTARTFDYRAGDVGYVPSNAGHYIQNTGTETLWFL 340
Cdd:TIGR03404 241 VSKTIAAAIVTVEPGAMRELHWHPNADEWQYFIQGQARMTVFAAGGNARTFDYQAGDVGYVPRNMGHYVENTGDETLVFL 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 16078927   341 EMFKSNRYADVSLNQWMALTPKELVQSNLNAGSVMLDSLRKKKVPVV 387
Cdd:TIGR03404 321 EVFKADRFADVSLNQWLALTPPQLVAAHLNLDDEVIDSLKKEKQPVV 367
cupin_OxDC_N cd20304
Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-terminal ...
 58-210 5.21e-106

Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-terminal cupin domain of oxalate decarboxylase (OxDC; EC 4.1.1.2), a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds with each domain containing one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380438  Cd Length: 155  Bit Score: 308.77  E-value: 5.21e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927  58 RFSFSDAPMKLDHGGWSREITVRQLPISTAIAGVNMSLTAGGVRELHWHKQAEWAYMLLGRARITAVDQDGRNFIADVGP 137
Cdd:cd20304   1 KFSFSDSHNRLESGGWAREVTVRDLPISTGIAGVNMRLEPGAIRELHWHAAAEWAYVLSGRCRITAVDPEGRSFIDDVGP 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16078927 138 GDLWYFPAGIPHSIQGL--EHCEFLLVFDDGNFSEFSTLTISDWLAHTPKDVLSANFGVPENAFNSLPSEQVYIY 210
Cdd:cd20304  81 GDLWYFPRGHPHSIQGLgpDGCEFLLVFDDGNFSEFGTFSITDWLAHTPKEVLAKNFGVPAEAFDNLPKKELYIF 155
cupin_OxDC_C cd20305
Oxalate decarboxylase (OxDC), C-terminal cupin domain; This model represents the C-terminal ...
 233-384 1.55e-96

Oxalate decarboxylase (OxDC), C-terminal cupin domain; This model represents the C-terminal cupin domain of oxalate decarboxylase (OxDC; EC 4.1.1.2), a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds with each domain containing one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380439 [Multi-domain]  Cd Length: 153  Bit Score: 284.48  E-value: 1.55e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927 233 TFKHELLNQPPIQMP-GGSVRIVDSSNFPISKTIAAALVQIEPGAMRELHWHPNSDEWQYYLTGQGRMTVFIGNGTARTF 311
Cdd:cd20305   1 PHTFRLLAQPPIKVPaGGSVRIVDSKNFPISTTIAAALVTLEPGALRELHWHPNADEWQYYISGKARMTVFASGGRARTF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16078927 312 DYRAGDVGYVPSNAGHYIQNTGTETLWFLEMFKSNRYADVSLNQWMALTPKELVQSNLNAGSVMLDSLRKKKV 384
Cdd:cd20305  81 DFQAGDVGYVPRGYGHYIENTGDEPLEFLEVFNSGRYQDISLSQWLALTPPDLVAAHLGLPDDTIAKLPKKKQ 153
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 242-383 9.18e-56

Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds and both domains are included in this alignment. Each OxDC cupin domain contains one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380367 [Multi-domain]  Cd Length: 145  Bit Score: 179.98  E-value: 9.18e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927 242 PPIQMPGGSVRIVDSSNFPISKTIAAALVQIEPGAMRELHWHPNSDEWQYYLTGQGRMTVFIGNGTARTFDYRAGDVGYV 321
Cdd:cd02240   4 PIEENAGGSVRIATVTNFPISKDLSSALVRVAPGAMRELHWHPNTAEWQYVISGSARVTVFDEDGRFETFNLGAGDVGYV 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16078927 322 PSNAGHYIQNTGTETLWFLEMFKSNRYADVSLNQWMALTPKELVQSNLNAGSVMLDSLRKKK 383
Cdd:cd02240  84 PSGSGHHIENIGDEDAEFLLIFDDGTFADVSLPWWLAMTPEEVLAATLDLGKFIDALPKAKH 145
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 71-206 8.30e-43

Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds and both domains are included in this alignment. Each OxDC cupin domain contains one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380367 [Multi-domain]  Cd Length: 145  Bit Score: 146.47  E-value: 8.30e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927  71 GGWSREITVRQLPISTAIAGVNMSLTAGGVRELHWHK-QAEWAYMLLGRARITAVDQDGRNFIADVGPGDLWYFPAGIPH 149
Cdd:cd02240  10 GGSVRIATVTNFPISKDLSSALVRVAPGAMRELHWHPnTAEWQYVISGSARVTVFDEDGRFETFNLGAGDVGYVPSGSGH 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16078927 150 SIQ--GLEHCEFLLVFDDGNFSEFStltISDWLAHTPKDVLSANFGVPENAFNsLPSEQ 206
Cdd:cd02240  90 HIEniGDEDAEFLLIFDDGTFADVS---LPWWLAMTPEEVLAATLDLGKFIDA-LPKAK 144
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 264-366 3.46e-40

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: 138.56  E-value: 3.46e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927 264 TIAAALVQIEPGAMRELHWHPNSDEWQYYLTGQGRMTVFIGNGTARTFDYRAGDVGYVPSNAGHYIQNTGTETLWFLEMF 343
Cdd:COG2140   2 TLAGGLTVLEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGRARTVDVGPGDVVYVPPGYGHYIINTGDEPLVFLAVF 81

                        90       100
                ....*....|....*....|....*.
gi 16078927 344 KSNR---YADVSLNQWMALTPKELVQ 366
Cdd:COG2140  82 DDDAgsdYGTISLSGWLAHTPPEVLA 107
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 87-189 4.68e-37

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: 130.47  E-value: 4.68e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927  87 AIAGVNMSLTAGGVRELHWH-KQAEWAYMLLGRARITAVDQDGRNFIADVGPGDLWYFPAGIPHSIQGL--EHCEFLLVF 163
Cdd:COG2140   2 TLAGGLTVLEPGGVREEHWHpNAAEWYYVLSGEARMTVQDPPGRARTVDVGPGDVVYVPPGYGHYIINTgdEPLVFLAVF 81

                        90       100
                ....*....|....*....|....*.
gi 16078927 164 DDGNFSEFSTLTISDWLAHTPKDVLS 189
Cdd:COG2140  82 DDDAGSDYGTISLSGWLAHTPPEVLA 107
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 242-370 1.47e-31

Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant.


Pssm-ID: 214845 [Multi-domain]  Cd Length: 146  Bit Score: 117.00  E-value: 1.47e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927    242 PPIQMPGGSVRIVDSSNFPISKT--IAAALVQIEPGAMRELHWHPNSDEWQYYLTGQGRMTVFIGNGTAR-TFDYRAGDV 318
Cdd:smart00835   5 PDFSNEGGRLREADPTNFPALNGlgISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNGNKVyDARLREGDV 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 16078927    319 GYVPSNAGHYIQNTGTETLWFLeMFKSNRYADVSL----NQWMALTPKELVQSNLN 370
Cdd:smart00835  85 FVVPQGHPHFQVNSGDENLEFV-AFNTNDPNRRFFlagrNSVLRGLPPEVLAAAFG 139
cupin_OxDC_N cd20304
Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-terminal ...
 235-384 2.63e-30

Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-terminal cupin domain of oxalate decarboxylase (OxDC; EC 4.1.1.2), a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds with each domain containing one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380438  Cd Length: 155  Bit Score: 113.86  E-value: 2.63e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927 235 KHELLNQPPIQMPGGSVRIVDSSNFPISKTIAAALVQIEPGAMRELHWHpNSDEWQYYLTGQGRMTVFIGNGTARTFDYR 314
Cdd:cd20304   1 KFSFSDSHNRLESGGWAREVTVRDLPISTGIAGVNMRLEPGAIRELHWH-AAAEWAYVLSGRCRITAVDPEGRSFIDDVG 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16078927 315 AGDVGYVPSNAGHYIQNTGTETLWFLEMFKSNRYAD---VSLNQWMALTPKELVQSNLNAGSVMLDSLRKKKV 384
Cdd:cd20304  80 PGDLWYFPRGHPHSIQGLGPDGCEFLLVFDDGNFSEfgtFSITDWLAHTPKEVLAKNFGVPAEAFDNLPKKEL 152
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 242-367 4.59e-28

Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and eukaryotic cupin domains of proteins homologous to oxalate decarboxylase (OxDC; EC 4.1.1.2) such as MSMEG_2254, a putative OxDC from Mycobacterium smegmatis. OxDC is a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds with each domain containing one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues.


Pssm-ID: 380440 [Multi-domain]  Cd Length: 151  Bit Score: 107.68  E-value: 4.59e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927 242 PPIQMPGGSVRIVDSSNFPISKTIAAALVQIEPGAMRELHWHPNSDEWQYYLTGQGRMTVFIGNGTARTFDYRAGDVGYV 321
Cdd:cd20306  11 PFFESEGGSIRQATADQLPVLKGLSIYRLRLSPGGIREPHWHPNANELGYVISGEARVSILDPTGSLDTFTVKPGQVVFI 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 16078927 322 PSNAGHYIQNTGTETLWFLEMFKSNRYADVSLNQWMALTPKELVQS 367
Cdd:cd20306  91 PQGWLHWIENVGDEEAHLLIFFNHETPEDIGLSDSLRATPPEVLGN 136
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 236-373 2.55e-26

Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant.


Pssm-ID: 395138  Cd Length: 151  Bit Score: 102.80  E-value: 2.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927   236 HELLNQPP-IQMPGGSVRIVDSSNFPISKT--IAAALVQIEPGAMRELHWHPNSDEWQYYLTGQGRM-TVFIGNG-TART 310
Cdd:pfam00190   1 LNLLEPGPtYNPEGGRVTTVNSKNLPGLNTlgISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVgFVVPGNGnRVFH 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16078927   311 FDYRAGDVGYVPSNAGHYIQNTGTETLWFLEMFKSNRYADVS----LNQWMALTPKELVQSNLNAGS 373
Cdd:pfam00190  81 KVLREGDVFVVPQGLPHFQYNIGDEPAVAFVAFDTNNPGNQSilagGFSSLPALPPEVLAKAFQLAG 147
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 55-198 9.16e-25

Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and eukaryotic cupin domains of proteins homologous to oxalate decarboxylase (OxDC; EC 4.1.1.2) such as MSMEG_2254, a putative OxDC from Mycobacterium smegmatis. OxDC is a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds with each domain containing one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues.


Pssm-ID: 380440 [Multi-domain]  Cd Length: 151  Bit Score: 98.82  E-value: 9.16e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927  55 PNLRFSFSDAPMKLDHGGWSREITVRQLPISTAIAGVNMSLTAGGVRELHWHKQA-EWAYMLLGRARITAVDQDGRNFIA 133
Cdd:cd20306   1 PHLFSLEDSNPFFESEGGSIRQATADQLPVLKGLSIYRLRLSPGGIREPHWHPNAnELGYVISGEARVSILDPTGSLDTF 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16078927 134 DVGPGDLWYFPAGIPHSIQ--GLEHCEFLLVFDDGNFSEFStltISDWLAHTPKDVLSANFGVPENA 198
Cdd:cd20306  81 TVKPGQVVFIPQGWLHWIEnvGDEEAHLLIFFNHETPEDIG---LSDSLRATPPEVLGNTYGVDAFF 144
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 71-197 1.52e-19

Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant.


Pssm-ID: 214845 [Multi-domain]  Cd Length: 146  Bit Score: 84.25  E-value: 1.52e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927     71 GGWSREITVRQLPISTaiaGVNMS-----LTAGGVRELHWHKQA-EWAYMLLGRARITAVD-QDGRNFIADVGPGDLWYF 143
Cdd:smart00835  11 GGRLREADPTNFPALN---GLGISaarvnLEPGGMLPPHYHPRAtELLYVVRGEGRVGVVDpNGNKVYDARLREGDVFVV 87

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927    144 PAGIPHSI-----QGLEHceflLVFDDGNFSEFSTLT-ISDWLAHTPKDVLSANFGVPEN 197
Cdd:smart00835  88 PQGHPHFQvnsgdENLEF----VAFNTNDPNRRFFLAgRNSVLRGLPPEVLAAAFGVSAE 143
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 71-194 8.65e-18

Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant.


Pssm-ID: 395138  Cd Length: 151  Bit Score: 79.69  E-value: 8.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927    71 GGWSREITVRQLPI--STAIAGVNMSLTAGGVRELHWHKQA-EWAYMLLGRARITAVD--QDGRNFIADVGPGDLWYFPA 145
Cdd:pfam00190  14 GGRVTTVNSKNLPGlnTLGISAARVDLAPGGMNPPHWHPNAtEILYVLQGRGRVGFVVpgNGNRVFHKVLREGDVFVVPQ 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 16078927   146 GIPHSIQGLEH---CEFLLVFDDGNFSEFSTLTISDWLAHTPKDVLSANFGV 194
Cdd:pfam00190  94 GLPHFQYNIGDepaVAFVAFDTNNPGNQSILAGGFSSLPALPPEVLAKAFQL 145
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 268-340 1.31e-13

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: 66.39  E-value: 1.31e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16078927 268 ALVQIEPGAMRELHWHPNSDEWQYYLTGQGRMTvfIGNgtaRTFDYRAGDVGYVPSNAGHYIQNTGTETLWFL 340
Cdd:cd02214  22 AHARVPPGESTLPHRLKGSEEVYYILEGEGTME--IDG---EPREVGPGDAVLIPPGAVQRIENTGEEDLVFL 89
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 268-343 2.33e-12

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: 61.89  E-value: 2.33e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16078927   268 ALVQIEPGAMRELHWHPNSDEWQYYLTGQGRMTVfigNGtaRTFDYRAGDVGYVPSNAGHYIQNTGTETLWFLEMF 343
Cdd:pfam07883   1 GLVTLPPGESSPPHRHPGEDEFFYVLEGEGELTV---DG--EEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDVY 71
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
247-343 7.36e-12

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 61.70  E-value: 7.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927 247 PGGSVRIVDSSNfpisKTIAAALVQIEPGAMRELHWHPNSDEWQYYLTGQGRMTVfigNGtaRTFDYRAGDVGYVPSNAG 326
Cdd:COG0662  13 GWGSYEVLGEGG----ERLSVKRITVPPGAELSLHVHPHRDEFFYVLEGTGEVTI---GD--EEVELKAGDSVYIPAGVP 83

                        90
                ....*....|....*..
gi 16078927 327 HYIQNTGTETLWFLEMF 343
Cdd:COG0662  84 HRLRNPGDEPLELLEVQ 100
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 267-337 6.43e-11

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: 57.88  E-value: 6.43e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16078927 267 AALVQIEPGAMRELHWHPNSDEWQYYLTGQGRMTVFIGngtaRTFDYRAGDVGYVPSNAGHYIQNTGTETL 337
Cdd:cd02208   1 ISVVTLPPGTSSPPHWHPEQDEIFYVLSGEGELTLDDG----ETVELKAGDIVLIPPGVPHSFVNTSDEPA 67
cupin_OxOx cd02241
Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3. ...
 234-335 4.46e-09

Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3.4) catalyzes the manganese-dependent oxidative decarboxylation of oxalate to carbon dioxide and hydrogen peroxide (H2O2). It is widespread in fungi and various plant tissues and may play a role in plant signaling and defense. This enzyme has been employed in a widely used assay for detecting urinary oxalate levels. Also, the gene encoding OxOx from barley roots has been expressed in oilseed rape in order to provide a defense against externally supplied oxalic acid. In germin, the predominant protein produced during the early phase of wheat germination, it is believed that H2O2 production is employed as a defense mechanism in response to infection by pathogens. Germin is also a marker of growth onset in cell walls in germinating cereals. The H2O2 produced by OxOx, together with the Ca2+ released by degradation of calcium oxalate, are thought to mediate cell wall cross-linking at high concentrations. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380368  Cd Length: 191  Bit Score: 55.68  E-value: 4.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927 234 FKHELLNQPPIQMP--GGSVRIVDSSNFPISKT--IAAALVQIEPGAMRELHWHPNSDEWQYYLtgQGRMTV-FIGNGTA 308
Cdd:cd02241  35 FVFDFLNPPGNTSNplGGSVTLANVANFPALNGlgISMARGDLAPCGVNPPHTHPRATELLYVV--EGTLYVgFVDENGN 112

                        90       100
                ....*....|....*....|....*....
gi 16078927 309 RTF--DYRAGDVGYVPSNAGHYIQNTGTE 335
Cdd:cd02241 113 RLFtkTLNPGDVFVFPQGLIHFQFNPGCE 141
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
239-343 7.48e-09

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 52.93  E-value: 7.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927 239 LNQPPIQMPGGSVRIVdssnFPISKTIAAALVQIEPGAMRELHWHPNSdewQYYLTGQGRMTVFIGNgtaRTFDYRAGDV 318
Cdd:COG1917   1 MRLAEIALTGVSVRVL----ADGEDELEVVRVTFEPGARTPWHSHPGE---ELIYVLEGEGEVEVGG---EEYELKPGDV 70

                        90       100
                ....*....|....*....|....*
gi 16078927 319 GYVPSNAGHYIQNTGTETLWFLEMF 343
Cdd:COG1917  71 VFIPPGVPHAFRNLGDEPAVLLVVF 95
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 93-163 4.91e-08

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: 49.79  E-value: 4.91e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16078927  93 MSLTAGGVRELHWH-KQAEWAYMLLGRARITAVDQDGRNfiadVGPGDLWYFPAGIPHSIQGLEHCEFLLVF 163
Cdd:cd02208   4 VTLPPGTSSPPHWHpEQDEIFYVLSGEGELTLDDGETVE----LKAGDIVLIPPGVPHSFVNTSDEPAVFLV 71
cupin_TM1287-like cd02221
Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial ...
 268-340 6.63e-08

Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial proteins homologous to TM1287 decarboxylase, a Thermotoga maritima manganese-containing cupin thought to catalyze the conversion of oxalate to formate and carbon dioxide, due to its similarity to oxalate decarboxylase (OXDC) from Bacillus subtilis. TM1287 shows a cupin fold with a conserved "jelly roll-like" beta-barrel fold and forms a homodimer.


Pssm-ID: 380350 [Multi-domain]  Cd Length: 93  Bit Score: 49.77  E-value: 6.63e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16078927 268 ALVQIEPGAMRELHWHPNSDEWQYYLTGQGrmtVFIGNGTarTFDYRAGDVGYVPSNAGHYIQNTGTETLWFL 340
Cdd:cd02221  22 ARVTLPPGSSIGYHQHEGEFEIYYILSGEG---LYTDNGK--EYEVKAGDVTFTRDGESHGIENTGDEDLVFI 89
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 93-163 8.81e-08

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: 48.79  E-value: 8.81e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16078927    93 MSLTAGGVRELHWHK-QAEWAYMLLGRARITavdQDGRNFIadVGPGDLWYFPAGIPHSIQ--GLEHCEFLLVF 163
Cdd:pfam07883   3 VTLPPGESSPPHRHPgEDEFFYVLEGEGELT---VDGEEVV--LKAGDSVYFPAGVPHRFRntGDEPARLLDVY 71
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
91-166 9.43e-08

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 49.85  E-value: 9.43e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16078927  91 VNMSLTAGGVRELHWHKQAEWAYMLLGRARITAvdqDGRNFIadVGPGDLWYFPAGIPHSIQGLEH--CEFLLVFDDG 166
Cdd:COG1917  26 VRVTFEPGARTPWHSHPGEELIYVLEGEGEVEV---GGEEYE--LKPGDVVFIPPGVPHAFRNLGDepAVLLVVFSPG 98
cupin_MAE_RS03005 cd06987
Microcystis aeruginosa MAE_RS03005 and related proteins, cupin domain; This family includes ...
 247-342 1.46e-07

Microcystis aeruginosa MAE_RS03005 and related proteins, cupin domain; This family includes bacterial and some eukaryotic proteins homologous to MAE_RS03005, a Microcystis aeruginosa 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: 380392 [Multi-domain]  Cd Length: 122  Bit Score: 49.57  E-value: 1.46e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927 247 PGGSVR---IVDSSNFPISKTIAaalVQI-EPGAMRELHWHPNSDEWQYYLTGQGRMTVfigNGtaRTFDYRAGDVGYVP 322
Cdd:cd06987   9 PGDTNRlalLFDPEGDGVPFTVV---VEIfDPGGRTPPNTHPAAHEMFFVLAGEGRAYC---DG--QRVPLRPGDALVVP 80

                        90       100
                ....*....|....*....|
gi 16078927 323 SNAGHYIQNTGTETLWFLEM 342
Cdd:cd06987  81 PGSEHVIENTGSGRLYCLTL 100
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
263-350 2.56e-07

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 48.86  E-value: 2.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927 263 KTIAAALVQIEPGAM-RELHWHPNSDEWqYYLTgQGRMTVFIGNGTartFDYRAGDVGYVPSNAGHYIQNTGTETLWFLE 341
Cdd:COG3837  26 TRLGVNLITLPPGASsSPYHAHSAEEEF-VYVL-EGELTLRIGGEE---YVLEPGDSVGFPAGVPHRLRNRGDEPARYLV 100


                ....*....
gi 16078927 342 MFKSNRYAD 350
Cdd:COG3837 101 VGTRAPYPD 109
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 269-340 2.66e-07

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: 48.22  E-value: 2.66e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16078927 269 LVQIEPGAMRELHWHPNsDEWQYYLTGQGRmtVFIGNGTartFDYRAGDVGYVPSNAGHYIQNTGTETLWFL 340
Cdd:cd02222  21 YFEIEPGGHTPLHTHPW-EHEVYVLRGKGV--VVIGGEE---YPVKPGDVVYIPPNEPHQFRNTGDEPLGFL 86
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
93-163 4.63e-07

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 48.21  E-value: 4.63e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16078927  93 MSLTAGGVRELHWH-KQAEWAYMLLGRARITavdQDGRNFiaDVGPGDLWYFPAGIPHSI--QGLEHCEFLLVF 163
Cdd:COG0662  32 ITVPPGAELSLHVHpHRDEFFYVLEGTGEVT---IGDEEV--ELKAGDSVYIPAGVPHRLrnPGDEPLELLEVQ 100
cupin_SPO2919-like cd02224
Silicibacter pomeroyi SPO2919 and related proteins, uncharacterized sugar phosphate isomerase ...
 263-341 4.78e-07

Silicibacter pomeroyi SPO2919 and related proteins, uncharacterized sugar phosphate isomerase with a cupin domain; This family includes proteins similar to sugar phosphate isomerase SPO2919 from Silicibacter pomeroyi and Afe_0303 from Acidithiobacillus ferrooxidans, but are as yet uncharacterized. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer.


Pssm-ID: 380353 [Multi-domain]  Cd Length: 105  Bit Score: 47.87  E-value: 4.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927 263 KTIAAALVQIEPGAMR-ELHWHPNSDEWQYYLTGQGRMTVfigNGTARTFdyRAGD-VGYVP-SNAGHYIQNTGTETLWF 339
Cdd:cd02224  15 TQLGVNLERLPPGARSsPRHWHSAEEEFVYVLSGEGTLRL---DGEEVLP--RPGDfVGFPAgTGVAHQLINRSDEPLVY 89


                ..
gi 16078927 340 LE 341
Cdd:cd02224  90 LV 91
cupin_11S_legumin_C cd02243
11S legumin seed storage globulin, C-terminal cupin domain; This family contains the ...
 248-324 8.37e-07

11S legumin seed storage globulin, C-terminal cupin domain; This family contains the C-terminal domains of 11S legumin seed storage proteins that supply nutrition for seed germination, such as glycinin and legumin, including many common food allergens such as the peanut major allergen Ara h 3, almond allergen Pru du 6, Pecan allergen Car i 4, hazelnut nut allergen Cor a 9, Brazil nut allergen Ber e 2, cashew allergen Ana o 2, pistachio allergen Pis v 2/5, and walnut allergen Jug n/r 4. These plant seed storage globulins have tandem cupin-like beta-barrel folds (referred to as a bicupin). They are synthesized as propeptides in the endoplasmic reticulum and transported to the secretory vesicles as a homotrimer. The propeptides are processed as they are sorted in the secretory vesicles. The homotrimer binds another homotrimer to form a homohexamer with 32-point symmetry formed by a face-to-face stacking of the two trimers. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380370  Cd Length: 155  Bit Score: 48.24  E-value: 8.37e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927 248 GGSVRIVDSSNFPISKTI--AAALVQIEPGAMRELHWHPNSDEWQYYLTGQGRMTVfIGNGTARTFD--YRAGDVGYVPS 323
Cdd:cd02243   7 GGRITTLNSFKLPILRFVglSAERVKLEPNAMFAPHWNANAHQVIYVTRGSGRVQV-VGDNGKRVLDgeVREGQLLVVPQ 85


                .
gi 16078927 324 N 324
Cdd:cd02243  86 F 86
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 91-163 1.85e-05

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: 43.23  E-value: 1.85e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16078927  91 VNMSLTAGGVRELHWHKQAEWAYMLLGRARITAvdqDGRNFIadVGPGDLWYFPAGIPHSIQGLEHCEFLLVF 163
Cdd:cd02238  30 VEVRFEKGAVVPLHSHPHEQIGYVLSGRFEFTI---GGETRI--LKPGDSYYIPPNVPHGAEALEDSVLLDVF 97
RmlC COG4101
Uncharacterized conserved protein, RmlC-like cupin domain [General function prediction only];
84-149 2.56e-05

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


Pssm-ID: 443277  Cd Length: 146  Bit Score: 43.80  E-value: 2.56e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16078927  84 ISTAIAG---VNMSLT---AGGVRELHWHKQAEWA-YMLLGRARItaVDQDGRNFIADVGPGDLWYFPAGIPH 149
Cdd:COG4101  36 ISAETVGstgLWMGLVtipPGARAKAHHHGEHETAiYVLSGRAET--RYGERLEHRVVTEPGDFIFIPPGVPH 106
cupin_TcmJ-like cd06991
TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of ...
 248-336 2.59e-05

TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of the tetracenomycin (TCM) polyketide synthase (PKS) type II complex in Streptomyces glaucescens. TcmJ is a quinone-forming monooxygenase involved in the modification of aromatic polyketides synthesized by polyketide synthases of types II and III. Orthologs of TcmJ include the Streptomyces BenD (benastatin biosynthetic pathway), the Streptomyces olivaceus ElmJ (polyketide antibiotic elloramycin biosynthetic pathway), the Actinomadura hibisca PdmL (pradimicin biosynthetic pathway), the Streptomyces cyaneus CurC (curamycin biosynthetic pathway), the Streptomyces rishiriensis Lct30 (lactonamycin biosynthetic pathway), and the Streptomyces WhiE II (spore pigment polyketide biosynthetic pathway). Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380396 [Multi-domain]  Cd Length: 105  Bit Score: 42.67  E-value: 2.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927 248 GGSVRIVDSsnfPisKTIAA-----ALVQIEPGAMRELHWHPNSDEWQYYLtgQGRMTVFIgNGTarTFDYRAGDVGYVP 322
Cdd:cd06991   2 GGDLRILLS---P--KTVGAtsgfmGTLTLAPGERVSEHYHPYSEEFLYVV--RGRLVVRV-DGE--PVVLEAGEALLVP 71

                        90
                ....*....|....
gi 16078927 323 SNAGHYIQNTGTET 336
Cdd:cd06991  72 RGVRHRLENAGDEP 85
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
90-162 4.64e-05

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 42.31  E-value: 4.64e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16078927  90 GVNMS-LTAGG-VRELHWH-KQAEWAYMLLGRarITAVDQDGRnfiADVGPGDLWYFPAGIPHSIQ--GLEHCEFLLV 162
Cdd:COG3837  29 GVNLItLPPGAsSSPYHAHsAEEEFVYVLEGE--LTLRIGGEE---YVLEPGDSVGFPAGVPHRLRnrGDEPARYLVV 101
cupin_DddK cd06988
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ...
 272-339 6.14e-05

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: 41.07  E-value: 6.14e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16078927 272 IEPGAMRELHWHpNSDEWQYYLTGQGRMTVfigNGTARTFdyRAGDVGYVPSNAGHYIQNTGTETLWF 339
Cdd:cd06988   9 VRPGTTSTPHSH-HEYEIFIVISGKGIVVV---DGEREPV--KAGDVVYIPPGTEHYVKNDGDEDFEF 70
cupin_HP0902-like cd02230
Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes ...
 113-162 9.80e-05

Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes prokaryotic and archaeal proteins homologous to HP0902, a functionally uncharacterized protein from Helicobacter pylori and Spy1581, a protein of unknown function from Streptococcus pyogenes. These proteins demonstrate all-beta cupin folds that cannot bind metal ions due to the absence of a metal-binding histidine that is conserved in many metallo-cupins. HP0902 is able to bind bacterial endotoxin lipopolysaccharides (LPS) through its surface-exposed loops, where metal-binding sites are usually found in other metallo-cupins, and thus may have a putative role in H. pylori pathogenicity.


Pssm-ID: 380358 [Multi-domain]  Cd Length: 83  Bit Score: 40.57  E-value: 9.80e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 16078927 113 YMLLGRARITAVDQDgrnfiADVGPGDLWYFPAGIPHSIQGLEHCEFLLV 162
Cdd:cd02230  36 QVLEGEAEFTIGGET-----VTLKAGELIVMPANVPHALKAEEDFKMLLT 80
cupin_BLR2406-like cd02210
Bradyrhizobium japonicum BLR2406 and related proteins, cupin domain; This family includes ...
 97-149 1.48e-04

Bradyrhizobium japonicum BLR2406 and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to BLR2406, a Bradyrhizobium japonicum protein of unknown function with a cupin beta barrel domain. Proteins in this subfamily appear to align closest to RmlC carbohydrate epimerase which is involved in dTDP-L-rhamnose production, and belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380340 [Multi-domain]  Cd Length: 98  Bit Score: 40.58  E-value: 1.48e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 16078927  97 AGGVRELHWHKQAEWA-YMLLGRARItaVDQDGRNFIADVGPGDLWYFPAGIPH 149
Cdd:cd02210  20 PGARTGAHHHGEHETAiYVLSGRAET--RYGDRLEHRAEAGPGDFIYIPPGVPH 71
cupin_TM1112-like cd02227
Thermotoga maritima TM1112 and related proteins, cupin domain; This family includes bacterial ...
 99-146 1.82e-04

Thermotoga maritima TM1112 and related proteins, cupin domain; This family includes bacterial and plant proteins homologous to TM1112, a Thermotoga maritima protein of unknown function with a cupin beta barrel domain. TM1112 (also known as DUF861) is a subfamily of RmlC-like cupins with a conserved "jelly roll-like" beta-barrel fold; structures indicate that a monomer is the biologically-relevant form.


Pssm-ID: 380356 [Multi-domain]  Cd Length: 69  Bit Score: 39.49  E-value: 1.82e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 16078927  99 GVRELHWH-KQAEWAYMLLGRARITavDQDGRnfIADVGPGDLWYFPAG 146
Cdd:cd02227   8 TPGKFPWNyDEDEFCYILEGEVRVT--PEDGE--PVTFKAGDLVVFPAG 52
cupin_PMI_typeII_C cd02213
Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal ...
 270-341 1.82e-04

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: 41.00  E-value: 1.82e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16078927 270 VQIEPGAMRELHWHPNSDEWQYYLTGQGRMTVfigNGtaRTFDYRAGDVGYVPSNAGHYIQNTGTETLWFLE 341
Cdd:cd02213  45 LTVNPGKRLSLQRHHHRSEHWVVVSGTAEVTL---DG--KEKLLKEGESIYIPKGTKHRLENPGKIPLEIIE 111
cupin_TTHA0104 cd06122
Thermus thermophilus TTHA0104 and related proteins, cupin domain; This family contains ...
 273-340 1.83e-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: 40.23  E-value: 1.83e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16078927 273 EPGAMRELHWHPNSDEWQYYLTGQGRMTVfiGNgtaRTFDYRAGDVGYVPSNAGHYIQNTGTETLWFL 340
Cdd:cd06122  35 EPGQSQKVHAHAGSDKVYFVLEGEGRFTV--GD---EERELGAGEAVLAPAGVPHGVRNTGAERLVLL 97
PRK04190 PRK04190
glucose-6-phosphate isomerase; Provisional
 268-340 2.04e-04

glucose-6-phosphate isomerase; Provisional


Pssm-ID: 179774  Cd Length: 191  Bit Score: 41.94  E-value: 2.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927  268 ALVQIEPGA------MRELHWHPNSDEWQYY--LTGQGRMTVFIGNGTARTFDYRAGDVGYVPSNAGHYIQNTGTETLWF 339
Cdd:PRK04190  71 GTTRLYPGKvgdeyfMTKGHFHAKADRAEIYygLKGKGLMLLQDPEGEARWIEMEPGTVVYVPPYWAHRSVNTGDEPLVF 150


                 .
gi 16078927  340 L 340
Cdd:PRK04190 151 L 151
cupin_QDO_N_C cd02215
quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known ...
 103-171 5.58e-04

quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known as quercetin 2,3-dioxygenase, 2,3QD, QDO and YxaG; EC 1.13.11.24), a mononuclear copper-dependent dioxygenase that catalyzes the cleavage of the flavonol quercetin (5,7,3',4'-tetrahydroxyflavonol) heterocyclic ring to produce 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon monoxide. Bacillus subtilis quercetin 2,3-dioxygenase (QDO) is a homodimer that shows oxygenase activity with several divalent metals such as Mn2+, Co2+, Fe2+, and Cu2+, although the preferred one appears to be Mn2+. The dioxygen binds to the metal ion of the Cu-QDO-quercetin complex, yielding a Cu2+-superoxo quercetin radical intermediate, which then forms a Cu2+-alkylperoxo complex which then evolves into endoperoxide intermediate that decomposes to the product. Quercetinase is a bicupin with two tandem cupin beta-barrel domains, both of which are included in this alignment model. The pirins, which also belong to the cupin domain family, have been shown to catalyze a reaction involving quercetin and may have a function similar to that of quercetinase.


Pssm-ID: 380345 [Multi-domain]  Cd Length: 122  Bit Score: 39.44  E-value: 5.58e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16078927 103 LHWHKQA-EWAYMLLGRARITaVDQDGRnfiaDVGPGDLWYFPAGIPHSIQGLEHC-EFLLVFDDGNFSEF 171
Cdd:cd02215  47 PHYHKRHhETFYVLEGRLQLW-LDGESR----LLTPGDFASVPPGTIHAYRMLSPDtRFLGVITPGGFERF 112
cupin_BacB cd06975
Bacillus subtilis bacilysin and related proteins, cupin domain; Bacilysin (BacB, also known as ...
 269-343 1.31e-03

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: 37.56  E-value: 1.31e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16078927 269 LVQIEPGAMRELHWHPNSdewQ--YYLTGQGRMTVfigNGTARTFDYrAGDVGYVPSNAGHYIQNTGTETLWFLEMF 343
Cdd:cd06975  23 LSYIPPGAKMPLHQHREE---QigMILNGELEMTV---GGEEQELEP-LGDVYYAPPNVPHGAVNPSDETAVLLDIK 92
cupin_XcTcmJ-like cd07006
Xanthomonas campestris XcTcmJ and related proteins, cupin domain; This family includes ...
 283-337 1.47e-03

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


Pssm-ID: 380409 [Multi-domain]  Cd Length: 89  Bit Score: 37.34  E-value: 1.47e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16078927 283 HPNSDEWQYYLTGQGRMTVfigNGtaRTFDYRAGDVGYVPSNAGHYIQNTGTETL 337
Cdd:cd07006  30 HRGSDQWLYVVSGSGEAIV---EG--ERVALKPGSLLLIEAGETHEIRNTGDEPL 79
COG3450 COG3450
Predicted enzyme of the cupin superfamily [General function prediction only];
104-146 2.02e-03

Predicted enzyme of the cupin superfamily [General function prediction only];


Pssm-ID: 442673  Cd Length: 108  Bit Score: 37.65  E-value: 2.02e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 16078927 104 HWH-KQAEWAYMLLGRARITavDQDGRnfIADVGPGDLWYFPAG 146
Cdd:COG3450  51 RWDyDEDEFCYILEGRVTVT--DDDGE--PVEFGAGDSFVFPAG 90
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 268-327 3.31e-03

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: 36.68  E-value: 3.31e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16078927 268 ALVQIEPGAMRELHWHPNSdewQY-YLTgQGRMTVFIGNgtaRTFDYRAGDVGYVPSNAGH 327
Cdd:cd02238  30 VEVRFEKGAVVPLHSHPHE---QIgYVL-SGRFEFTIGG---ETRILKPGDSYYIPPNVPH 83
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 78-152 3.45e-03

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: 36.73  E-value: 3.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927  78 TVRQLPISTAIAGVNMSLT-----AGGVRELHWHK-QAEWAYMLLGRARITaVDQDGRnfiaDVGPGDLWYFPAGIPHSI 151
Cdd:cd02214   4 LIRELLHPDNDGDPRYSLAharvpPGESTLPHRLKgSEEVYYILEGEGTME-IDGEPR----EVGPGDAVLIPPGAVQRI 78


                .
gi 16078927 152 Q 152
Cdd:cd02214  79 E 79
cupin_BLR2406-like cd02210
Bradyrhizobium japonicum BLR2406 and related proteins, cupin domain; This family includes ...
 262-327 3.87e-03

Bradyrhizobium japonicum BLR2406 and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to BLR2406, a Bradyrhizobium japonicum protein of unknown function with a cupin beta barrel domain. Proteins in this subfamily appear to align closest to RmlC carbohydrate epimerase which is involved in dTDP-L-rhamnose production, and belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380340 [Multi-domain]  Cd Length: 98  Bit Score: 36.34  E-value: 3.87e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16078927 262 SKTIAAALVQIEPGAMRELHWHPNSDEWQYYLTGQGRMtvFIGNGTARTFDYRAGDVGYVPSNAGH 327
Cdd:cd02210   8 AKGLWMGVVTIPPGARTGAHHHGEHETAIYVLSGRAET--RYGDRLEHRAEAGPGDFIYIPPGVPH 71
cupin_OxOx cd02241
Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3. ...
 59-202 4.18e-03

Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3.4) catalyzes the manganese-dependent oxidative decarboxylation of oxalate to carbon dioxide and hydrogen peroxide (H2O2). It is widespread in fungi and various plant tissues and may play a role in plant signaling and defense. This enzyme has been employed in a widely used assay for detecting urinary oxalate levels. Also, the gene encoding OxOx from barley roots has been expressed in oilseed rape in order to provide a defense against externally supplied oxalic acid. In germin, the predominant protein produced during the early phase of wheat germination, it is believed that H2O2 production is employed as a defense mechanism in response to infection by pathogens. Germin is also a marker of growth onset in cell walls in germinating cereals. The H2O2 produced by OxOx, together with the Ca2+ released by degradation of calcium oxalate, are thought to mediate cell wall cross-linking at high concentrations. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380368  Cd Length: 191  Bit Score: 37.96  E-value: 4.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927  59 FSFSDAPMKLD--HGGWSREITVRQLPistAIAGVNMSLT-----AGGVRELHWHKQA-EWAYMLLGRarITA--VD-QD 127
Cdd:cd02241  37 FDFLNPPGNTSnpLGGSVTLANVANFP---ALNGLGISMArgdlaPCGVNPPHTHPRAtELLYVVEGT--LYVgfVDeNG 111

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16078927 128 GRNFIADVGPGDLWYFPAGIPHSIQ--GLEHCEFLLVFDDGNfseFSTLTISDWLAHT--PKDVLSANFGVPENAFNSL 202
Cdd:cd02241 112 NRLFTKTLNPGDVFVFPQGLIHFQFnpGCEPAVFVAAFNSED---PGTQQIAQALFGLppPDDVLAAAFGLDGAQVEKL 187
cupin_7S_11S_C cd20285
7S and 11S seed storage globulin, C-terminal cupin domain; This family contains the C-terminal ...
 249-324 4.40e-03

7S and 11S seed storage globulin, C-terminal cupin domain; This family contains the C-terminal cupin domains of 7S and 11S seed storage proteins. The 7S globulins include soybean allergen beta-conglycinin, peanut allergen conarachin (Ara h 1), walnut allergen Jug r 2, and lentil allergen Len c 1. Proteins in this family perform various functions, including a role in sucrose binding, desiccation, defense against microbes and oxidative stress. The 11S globulins include many common food allergens such as the peanut major allergen Ara h 3, almond allergen Pru du 6, pecan allergen Car i 4, hazelnut nut allergen Cor a 9, Brazil nut allergen Ber e 2, cashew allergen Ana o 2, pistachio allergen Pis v 2/5, and walnut allergen Jug n/r 4. These plant seed storage globulins have tandem cupin-like beta-barrel folds (referred to as a bicupin). Storage proteins are the cause of well-known allergic reactions to peanuts and cereals. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380420  Cd Length: 109  Bit Score: 36.82  E-value: 4.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927 249 GSVRIVDSSNFPISK--TIAAALVQIEPGAMRELHWHPNSDEWQYYLTGQGRMTVFIGNGTaRTFD--YRAGDVGYVPSN 324
Cdd:cd20285   1 GNVTERTSNDFPILKslNLLASSISLEEGAMFVPHYYSKAIVILVVNEGRAHIQVVGPKGY-ESYDaeLSKGDVFVVPAA 79
cupin_BLL4011-like cd02235
Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes ...
 268-337 7.56e-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: 35.63  E-value: 7.56e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16078927 268 ALVQIEPGAMRELHWHPnSDEWQYYLTGQGRMTVfigNGTA-RTFdyRAGDVGYVPSNAGHYIQNTGTETL 337
Cdd:cd02235  22 VRVEIPPGAVAGRHTHP-GEESGYVLEGSLELEV---DGQPpVTL--KAGDSFFIPAGTVHNAKNVGSGPA 86
cupin_PGI cd02218
cupin-type phosphoglucose isomerase; The cupin-type phosphoglucose isomerase (also called ...
 272-337 8.25e-03

cupin-type phosphoglucose isomerase; The cupin-type phosphoglucose isomerase (also called cupin-like glucose-6-phosphate isomerase or cPGI; EC 5.3.1.9) family is found in archaea and certain prokaryotes where they catalyze the reversible aldose-ketose isomerization of glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P) as part of a unique variation of the Embden-Meyerhof glycolytic pathway. Cupin-PGIs represent a separate lineage in the evolution of phosphoglucose isomerases. Pyrococcus furiosus phosphoglucose isomerase (PfPGI) has been shown to be a metal-containing enzyme which catalyzes the interconversion of glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P). These domains have a cupin beta-barrel fold capable of homodimerization.


Pssm-ID: 380347  Cd Length: 168  Bit Score: 36.77  E-value: 8.25e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16078927 272 IEPGAM-REL-----HWHPNSDEWQYY--LTGQGRM---TVFIGNgtARTFDYRAGDVGYVPSNAGHYIQNTGTETL 337
Cdd:cd02218  52 IYPGKVgDEYfktkgHYHAKRDYPEVYevLSGEGLLllqKEDVGE--VILVEAKPGDKVYIPPGYAHRTINTGDEPL 126
cupin_yp_001338853-like cd07008
Klebsiella pneumoniae yp_001338853.1 and related proteins, cupin domain; This family includes ...
 252-340 8.64e-03

Klebsiella pneumoniae yp_001338853.1 and related proteins, cupin domain; This family includes bacterial proteins homologous to Klebsiella pneumoniae yp_001338853.1, an uncharacterized conserved protein with double-stranded beta-helix domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380411 [Multi-domain]  Cd Length: 101  Bit Score: 35.69  E-value: 8.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078927 252 RIVDSSNF-----------PISKTIAAALV--QIEPGAMRELHWHPNSDEWQYYLTGQGrmTVFIGNGTARTFDyrAGDV 318
Cdd:cd07008   1 RIFDVAEFvqfsdeepirsVITETDDSAIVvwHVKPGQEIAAHIHPHGQDTWIVLSGEG--EYLLGDGQTVPIK--AGDI 76

                        90       100
                ....*....|....*....|..
gi 16078927 319 GYVPSNAGHYIQNTGTETLWFL 340
Cdd:cd07008  77 VIAPAGQVHGARNTGDEPLVFV 98
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 104-152 9.13e-03

AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization domain of the bacterial gene regulatory protein AraC. The domain is found in conjunction with the helix-turn-helix (HTH) DNA-binding motif pfam00165. This domain is distantly related to the Cupin domain pfam00190.


Pssm-ID: 396749 [Multi-domain]  Cd Length: 134  Bit Score: 36.26  E-value: 9.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 16078927   104 HWHKQAEWAYMLLGRARITAvdqDGRNFiaDVGPGDLWYFPAGIPHSIQ 152
Cdd:pfam02311  19 HVHDFYVIGYIERGVGRFRL---NGRTY--HLGPGDLFLLPPGEPHDYE 62
 
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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