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        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446919928  1 MNDDQIQLFKANGDFIWHEHPNTDKLFIVLEGEMFIDFRDGQVKVSKGEMFIVPRGVEHKPFTEKESHIMLVEP 74
Cdd:cd02226  21 VNDQVVKLAKLKGEFVWHKHDDEDELFLVLEGELTIDFRDRDVTLGPGEFFVVPKGVEHRPVAEEETVVLLIEP 94

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        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446919928  1 MNDDQIQLFKANGDFIWHEHPNTDKLFIVLEGEMFIDFRDGQVKVSKGEMFIVPRGVEHKPFTEKESHIMLVEP 74
Cdd:cd02226  21 VNDQVVKLAKLKGEFVWHKHDDEDELFLVLEGELTIDFRDRDVTLGPGEFFVVPKGVEHRPVAEEETVVLLIEP 94

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

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446919928   6 IQLFKANGDFIWHEHPNTDKLFIVLEGEMFIDFRDGQVKVSKGEMFIVPRGVEHKP 61
Cdd:pfam07883  2 LVTLPPGESSPPHRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRF 57

3-hydroxyanthranilate 3,4-dioxygenase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919928   7 QLFKaNGDFI------------WHEHPnTDKLFIVLEGEMFIDFRDG----QVKVSKGEMFIVPRGVEHKPFTEKESHIM 70
Cdd:PRK13264  28 QIWQ-DSDFIvmvvggpnartdFHYDP-GEEFFYQLEGDMYLKVQEDgkrrDVPIREGEMFLLPPHVPHSPQREAGSIGL 105

                 ....*..
gi 446919928  71 LVEPKRE 77
Cdd:PRK13264 106 VIERKRP 112

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        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446919928  1 MNDDQIQLFKANGDFIWHEHPNTDKLFIVLEGEMFIDFRDGQVKVSKGEMFIVPRGVEHKPFTEKESHIMLVEP 74
Cdd:cd02226  21 VNDQVVKLAKLKGEFVWHKHDDEDELFLVLEGELTIDFRDRDVTLGPGEFFVVPKGVEHRPVAEEETVVLLIEP 94

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

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446919928   6 IQLFKANGDFIWHEHPNTDKLFIVLEGEMFIDFRDGQVKVSKGEMFIVPRGVEHKP 61
Cdd:pfam07883  2 LVTLPPGESSPPHRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRF 57

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
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446919928    9 FKANGDFIWHEHPNTDKLFIVLEGEMFI-------DFRDGQVKVSKGEMFIVPRGVEH 59
Cdd:pfam00190  40 LAPGGMNPPHWHPNATEILYVLQGRGRVgfvvpgnGNRVFHKVLREGDVFVVPQGLPH 97

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
                 ....*....|....*....|....*....|....*....|....*....
gi 446919928  13 GDFIW-HEHPNTDKLFIVLEGEMFIDFRDGQVKVSKGEMFIVPRGVEHK 60
Cdd:cd06991   29 GERVSeHYHPYSEEFLYVVRGRLVVRVDGEPVVLEAGEALLVPRGVRHR 77

Uncharacterized conserved protein, cupin superfamily [Function unknown];

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 446919928  17 WHEHPNTDKLFIVLEGEMFIDFRDGQVKVSKGEMFIVPRGVEH 59
Cdd:COG3837   44 YHAHSAEEEFVYVLEGELTLRIGGEEYVLEPGDSVGFPAGVPH 86

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
                 ....*....|....*....|....*....|....*....|....*...
gi 446919928  18 HEHPNTDKLFIVLEGEM---FIDFRDGQV---KVSKGEMFIVPRGVEH 59
Cdd:cd02241   86 HTHPRATELLYVVEGTLyvgFVDENGNRLftkTLNPGDVFVFPQGLIH 133

Desulfitobacterium hafniense dsy2733 and related proteins, cupin domain; This family includes bacterial proteins homologous to dsy2733, a Desulfitobacterium hafniense 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
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 446919928  5 QIQLFK-ANGDFIWHEHPNTDKLFIVLEGEMFIDFRDGQVKVSKGEMFIVPRGVEH 59
Cdd:cd06983  11 QISLFAfADGESVSEEEYFGDTLYYVLEGEAEITIGDEKHRLKAGDVLAVPAGVLH 66

acireductone dioxygenase (ARD), cupin domain; Acireductone dioxygenase (ARD; also known as 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase) catalyzes the oxidation of 1,2-dihydroxy-3-keto-5-methylthiopentene to yield two different products depending on which active site metal is present (Fe2+ or Ni2+) as part of the methionine salvage pathway. The ARD apo-enzyme, obtained after the metal is removed, is catalytically inactive. The Fe(II)-ARD reaction yields an alpha-keto acid and formic acid, while Ni(II)-ARD instead catalyzes a shunt out of the methionine salvage pathway, yielding methylthiocarboxylic acid, formic acid, and CO. ARD belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 446919928  29 VLEGEMFIDFRDGQ-----VKVSKGEMFIVPRGVEH 59
Cdd:cd02232   75 ILDGSGYFDVRDKDdewirILVEKGDLIVVPAGIYH 110

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446919928  16 IWHEHPNTDKLFIVLEGE--MFIDfrDGQVKVSKGEMFIVPRGVEHK 60
Cdd:cd02214   33 LPHRLKGSEEVYYILEGEgtMEID--GEPREVGPGDAVLIPPGAVQR 77

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 446919928   15 FIWHEHPNTdKLFIVLEGEMFIDFRDGQVKVSKGEMFIVPRGVEH 59
Cdd:pfam02311  16 FPPHVHDFY-VIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPH 59

Streptomyces resistomycificus RemF cyclase and related proteins, cupin domain; RemF cyclase is a manganese-containing polyketide cyclase present in bacteria that is involved in the biosynthesis of resistomycin, the aromatic pentacyclic metabolite in Streptomyces resistomycificus. Structure of this enzyme shows a cupin fold with a conserved "jelly roll-like" beta-barrel fold that forms a homodimer. It contains an unusual octahedral zinc-binding site in a large hydrophobic pocket that may represent the active site. The zinc ion, coordinated to four histidine side chains and two water molecules, could act as a Lewis acid in the aldol condensation reaction catalyzed by RemF, reminiscent of class II aldolases.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 446919928 18 HEHPNTDKLFIVLEGEMFIDFRDGQVKVSKGEMFIVPRGVEH 59
Cdd:cd06979  34 HYHEDWEETIYGLEGSVTLTLPGKTVEVGPGDSIFIPRGEVH 75

Bacillus subtilis YjlB and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to YjlB, a Bacillus subtilis protein of unknown function with a cupin beta barrel fold. 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. 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446919928   7 QLFKANG----------DFiWHEHPNTDKLFIVLEGEMFIDF--RDGQ-VKVSKGEMFIVPRGVEHK 60
Cdd:cd02219   34 ALFEANGwtpqwrngiyDY-HHYHSTTHEVLGVASGSATLQLggPGGVeVTVEAGDVVVLPAGVGHK 99