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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221902  29 DSDPLQDFCVGDLKASPSINGFPCK--SSVSASDFFFSGLGGPLNTSTPNGVAVSPANVLTFPGLNTLGLSMNNVEFAPG 106
Cdd:cd02241   1 DPDPLQDFCVADLSSPRTPNGYPCKdpALVTADDFVFDFLNPPGNTSNPLGGSVTLANVANFPALNGLGISMARGDLAPC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221902 107 GVNPPHSHPRATEAGVVIEGSVFVGFLTTN-NTLFSKVLNAGEMFVVPRGLVHFQWNVGKVKARLITSFNSQLPGSAVLP 185
Cdd:cd02241  81 GVNPPHTHPRATELLYVVEGTLYVGFVDENgNRLFTKTLNPGDVFVFPQGLIHFQFNPGCEPAVFVAAFNSEDPGTQQIA 160

                       170       180       190
                ....*....|....*....|....*....|...
gi 15221902 186 STLFGSNPtiPNAVLTKTFRTDDVTVNKLKSKF 218
Cdd:cd02241 161 QALFGLPP--PDDVLAAAFGLDGAQVEKLKSKF 191

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221902  29 DSDPLQDFCVGDLKASPSINGFPCK--SSVSASDFFFSGLGGPLNTSTPNGVAVSPANVLTFPGLNTLGLSMNNVEFAPG 106
Cdd:cd02241   1 DPDPLQDFCVADLSSPRTPNGYPCKdpALVTADDFVFDFLNPPGNTSNPLGGSVTLANVANFPALNGLGISMARGDLAPC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221902 107 GVNPPHSHPRATEAGVVIEGSVFVGFLTTN-NTLFSKVLNAGEMFVVPRGLVHFQWNVGKVKARLITSFNSQLPGSAVLP 185
Cdd:cd02241  81 GVNPPHTHPRATELLYVVEGTLYVGFVDENgNRLFTKTLNPGDVFVFPQGLIHFQFNPGCEPAVFVAAFNSEDPGTQQIA 160

                       170       180       190
                ....*....|....*....|....*....|...
gi 15221902 186 STLFGSNPtiPNAVLTKTFRTDDVTVNKLKSKF 218
Cdd:cd02241 161 QALFGLPP--PDDVLAAAFGLDGAQVEKLKSKF 191

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221902     69 PLNTSTPNGVAVSPANVLTFPGLNTLGLSMNNVEFAPGGVNPPHSHPRATEAGVVIEGSVFVGFLTTN-NTLFSKVLNAG 147
Cdd:smart00835   3 PRPDFSNEGGRLREADPTNFPALNGLGISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNgNKVYDARLREG 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15221902    148 EMFVVPRGLVHFQWNVGKVKARLItSFNSQLPGSAVLPSTLFGSNPTIPNAVLTKTFRTDDVTV 211
Cdd:smart00835  83 DVFVVPQGHPHFQVNSGDENLEFV-AFNTNDPNRRFFLAGRNSVLRGLPPEVLAAAFGVSAEEV 145

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221902  29 DSDPLQDFCVGDLKASPSINGFPCK--SSVSASDFFFSGLGGPLNTSTPNGVAVSPANVLTFPGLNTLGLSMNNVEFAPG 106
Cdd:cd02241   1 DPDPLQDFCVADLSSPRTPNGYPCKdpALVTADDFVFDFLNPPGNTSNPLGGSVTLANVANFPALNGLGISMARGDLAPC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221902 107 GVNPPHSHPRATEAGVVIEGSVFVGFLTTN-NTLFSKVLNAGEMFVVPRGLVHFQWNVGKVKARLITSFNSQLPGSAVLP 185
Cdd:cd02241  81 GVNPPHTHPRATELLYVVEGTLYVGFVDENgNRLFTKTLNPGDVFVFPQGLIHFQFNPGCEPAVFVAAFNSEDPGTQQIA 160

                       170       180       190
                ....*....|....*....|....*....|...
gi 15221902 186 STLFGSNPtiPNAVLTKTFRTDDVTVNKLKSKF 218
Cdd:cd02241 161 QALFGLPP--PDDVLAAAFGLDGAQVEKLKSKF 191

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221902     69 PLNTSTPNGVAVSPANVLTFPGLNTLGLSMNNVEFAPGGVNPPHSHPRATEAGVVIEGSVFVGFLTTN-NTLFSKVLNAG 147
Cdd:smart00835   3 PRPDFSNEGGRLREADPTNFPALNGLGISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNgNKVYDARLREG 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15221902    148 EMFVVPRGLVHFQWNVGKVKARLItSFNSQLPGSAVLPSTLFGSNPTIPNAVLTKTFRTDDVTV 211
Cdd:smart00835  83 DVFVVPQGHPHFQVNSGDENLEFV-AFNTNDPNRRFFLAGRNSVLRGLPPEVLAAAFGVSAEEV 145

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221902  80 VSPANVLTFPGLNtlGLSMNNVEFAPGGVNPPHSHPRATEAGVVIEGSVFVGFLTTNNTLFSKVLNAGEMFVVPRGLVHF 159
Cdd:cd02240  13 VRIATVTNFPISK--DLSSALVRVAPGAMRELHWHPNTAEWQYVISGSARVTVFDEDGRFETFNLGAGDVGYVPSGSGHH 90

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15221902 160 QWNVGKVKARLITSFNSQLPGSAVLPStlFGSNptIPNAVLTKTFRTDDVTVNKLKSK 217
Cdd:cd02240  91 IENIGDEDAEFLLIFDDGTFADVSLPW--WLAM--TPEEVLAATLDLGKFIDALPKAK 144

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221902  96 LSMNNVEFAPGGVNPPHSHPrATEAGVVIEGSVFVgflTTNNTLFskVLNAGEMFVVPRGLVHFQWNVGKVKARLITSFN 175
Cdd:COG1917  23 LEVVRVTFEPGARTPWHSHP-GEELIYVLEGEGEV---EVGGEEY--ELKPGDVVFIPPGVPHAFRNLGDEPAVLLVVFS 96

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

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221902  95 GLSMNNVEFAPGGVNPPHSHPRATEAGVVIEGSvfvGFLTTNNTLFskVLNAGEMFVVPRGLVHFQWNVGKVKARLI 171
Cdd:COG0662  26 RLSVKRITVPPGAELSLHVHPHRDEFFYVLEGT---GEVTIGDEEV--ELKAGDSVYIPAGVPHRLRNPGDEPLELL 97

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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221902 101 VEFAPGGVNPPHSHPRATEAGVVIEGSVFVgfltTNNTLFSKVLNAGEMFVVPRGLVHFQWNVGKVKARLI 171
Cdd:cd02208   4 VTLPPGTSSPPHWHPEQDEIFYVLSGEGEL----TLDDGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFL 70

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.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15221902  96 LSMNNVEFAPGGVNPPHSHPRaTEAGVVIEGS--VFVGflttNNTlfsKVLNAGEMFVVPRGLVH 158
Cdd:cd02238  27 LMLVEVRFEKGAVVPLHSHPH-EQIGYVLSGRfeFTIG----GET---RILKPGDSYYIPPNVPH 83

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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15221902 101 VE-FAPGGVNPPHSHPRATEAGVVIEGSvfvGFLTTNNTLFSkvLNAGEMFVVPRGLVHFQWNVGKVKARLIT 172
Cdd:cd06987  32 VEiFDPGGRTPPNTHPAAHEMFFVLAGE---GRAYCDGQRVP--LRPGDALVVPPGSEHVIENTGSGRLYCLT 99

Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial proteins homologous to YdbB, a Bacillus subtilis protein of unknown function. It also includes protein Nmb1881 From Neisseria meningitidis, also of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 15221902 112 HSHPRATEAGVVIEGSVFVGFLTTnntlfSKVLNAGEMFVVPRGLVH 158
Cdd:cd02226  38 HKHDDEDELFLVLEGELTIDFRDR-----DVTLGPGEFFVVPKGVEH 79

Bradyrhizobium japonicum BLR7677 and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to BLR7677, a Bradyrhizobium japonicum 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.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15221902 101 VEFAPGGVNPPHSHPRATeAGVVIEGSVfvgflttnntLF------SKVLNAGEMFVVPRGLVH 158
Cdd:cd02234  24 VTYPPGAASPPHRHPGFV-FAYVLEGEV----------RSqvnggpPRVYKAGESFYEPPGAHH 76

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221902  78 VAVSPANVLTFPGLntlglsMNNVEFAPGGVNPPHSHPRATEAGVVIEGSVFVgflTTNNTLFskVLNAGEMFVVPRGLV 157
Cdd:cd06991   7 ILLSPKTVGATSGF------MGTLTLAPGERVSEHYHPYSEEFLYVVRGRLVV---RVDGEPV--VLEAGEALLVPRGVR 75

                        90
                ....*....|....
gi 15221902 158 HFQWNVGKVKARLI 171
Cdd:cd06991  76 HRLENAGDEPARLV 89

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.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15221902 104 APGGVNPPHSHPRATEAGVVIEGSVFVgflTTNNTlfSKVLNAGEMFVVPRGLVH-FQ 160
Cdd:cd02215  40 PKGDAIPPHYHKRHHETFYVLEGRLQL---WLDGE--SRLLTPGDFASVPPGTIHaYR 92

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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15221902  80 VSPANVLTFPGLNTLGLSMNNVEFAPGGVNPPHSHPRATEAGVVIEGSVFVGFLTTNN-TLFSKVLNAGEMFVVPRGLV 157
Cdd:cd20285   3 VTERTSNDFPILKSLNLLASSISLEEGAMFVPHYYSKAIVILVVNEGRAHIQVVGPKGyESYDAELSKGDVFVVPAAFP 81

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221902  74 TPNGVAVSPANVLTFPGLNTLGLSMNNVEFAPGGVNPPHSHPRATEAGVVIEGSVFVGFLTTN-NTLFSKVLNAGEMFVV 152
Cdd:cd02243   4 VPRGGRITTLNSFKLPILRFVGLSAERVKLEPNAMFAPHWNANAHQVIYVTRGSGRVQVVGDNgKRVLDGEVREGQLLVV 83

                ....*
gi 15221902 153 PRGLV 157
Cdd:cd02243  84 PQFFA 88