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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657623705  24 PGQIVSKTLAQNKHH-NVTLFAFDKNEEISAHDSSGDAMVTVLDGTGRITIGDTEHILHAGDCIVMPAKIPHAVYALERF 102
Cdd:COG1917    8 LTGVSVRVLADGEDElEVVRVTFEPGARTPWHSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGDE 87

                         90
                 ....*....|.
gi 657623705 103 KMLLIVLFTDA 113
Cdd:COG1917   88 PAVLLVVFSPG 98

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        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657623705  29 SKTLAQNKHHNVTLFAFDKNEEISAHDSSGDAMVTVLDGTGRITIGDTEHILHAGDCIVMPAKIPHAVYALERFKMLLI 107
Cdd:cd06983    1 SMALSNSDNVQISLFAFADGESVSEEEYFGDTLYYVLEGEAEITIGDEKHRLKAGDVLAVPAGVLHAIGGLGAFKLLQI 79

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        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657623705  24 PGqIVSKTLAQNKHHNVTLFAFDKNEEISAHDSSGDAMVTVLDGTGRITIGDTEHILHAGDCIVMPAKIPHAVYALE 100
Cdd:cd02238   14 PG-VRRKILAGGEKLMLVEVRFEKGAVVPLHSHPHEQIGYVLSGRFEFTIGGETRILKPGDSYYIPPNVPHGAEALE 89

Uncharacterized conserved protein, cupin superfamily [Function unknown];

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 657623705  53 AHdSSGDAMVTVLDGTGRITIGDTEHILHAGDCIVMPAKIPHAVY 97
Cdd:COG3837   46 AH-SAEEEFVYVLEGELTLRIGGEEYVLEPGDSVGFPAGVPHRLR 89

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657623705  16 LAEQVTYQPGQIVSKTLAQNKHHNVTLFAFDKNEEISAHDSSG-DAMVTVLDGTGRITIGDTEHILHAGDCIVMPAKIPH 94
Cdd:cd06122    5 LRDHARFSPEKMQKITLFESERLFCDLYCLEPGQSQKVHAHAGsDKVYFVLEGEGRFTVGDEERELGAGEAVLAPAGVPH 84

                 ..
gi 657623705  95 AV 96
Cdd:cd06122   85 GV 86

uncharacterized Methanocaldococcus jannaschii Moth_1897 and related proteins, cupin domain; This family includes archaeal and bacterial proteins homologous to Moth_1897, a Methanocaldococcus jannaschii 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 657623705  29 SKTLAQNKHHNVTLFAFDKNEEISAHDSSGDAMVTVLDGTGRITIGDTEHILHAGDCIVMPAKIPHAVYA 98
Cdd:cd06984    2 ARKLYDTEHAQIVHITLKPGESLKKHITPVDVFFYVLEGEGIVEIGEEKQEVEADTLIESPANIPHCLYN 71

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

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 657623705  40 VTLFAFDKNEEISAHDSSGDAMVTVLDGTGRITIGDT-----EHILHAGDCIVMPAKIPHAVYA 98
Cdd:cd06989   20 VVRLKFPAGYKIPPHTHPDDERVTVISGTFYLGMGDKfdeakAKALPAGSFFTLPAGTPHFAWA 83

AraC/XylS family transcriptional regulators similar to MmsR, N-terminal cupin domain; This family contains bacterial proteins containing an AraC/XylS family helix-turn-helix (HTH) DNA-binding domain C-terminal to a cupin domain, and may be possible transcriptional regulators. Included is MmsR, a bacterial transcriptional regulator thought to positively regulate the expression of the mmsAB operon. The mmsAB operon contains two structural genes involved in valine metabolism: mmsA which encodes methylmalonate-semialdehyde dehydrogenase, and mmsB which encodes 3-hydroxyisobutyrate dehydrogenase. The cupin domain of members of this subfamily does not contain a metal binding site.

                         10        20        30
                 ....*....|....*....|....*....|....*
gi 657623705  64 VLDGTGRITIGDTEHILHAGDCIVMPAKIPHAVYA 98
Cdd:cd06986   34 VLSGKGTFSVNGKTYHLKAGQGFLIPPGEPHSYGA 68

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 657623705  64 VLDGTGRITIGDTEHILHAGDCIVMPAKIPHAVYAL--ERFKMLLIV 108
Cdd:cd02214   46 ILEGEGTMEIDGEPREVGPGDAVLIPPGAVQRIENTgeEDLVFLCIC 92

gentisate 1,2-dioxygenase, 1-hydroxy-2-naphthoate dioxygenase, and salicylate 1,2-dioxygenase bicupin aromatic ring-cleaving dioxygenases, C-terminal cupin domain; This model represents the C-terminal cupin domains of three closely related bicupin aromatic ring-cleaving dioxygenases: gentisate 1,2-dioxygenase (GDO), salicylate 1,2-dioxygenase (SDO), and 1-hydroxy-2-naphthoate dioxygenase (NDO). GDO catalyzes the cleavage of the gentisate (2,5-dihydroxybenzoate) aromatic ring, a key step in the gentisate degradation pathway allowing soil bacteria to utilize 2,5-xylenol, 3,5-xylenol, and m-cresol as sole carbon and energy sources. NDO catalyzes the cleavage of 1-hydroxy-2-naphthoate as part of the bacterial phenanthrene degradation pathway. SDO is a ring cleavage dioxygenase from Pseudaminobacter salicylatoxidans that oxidizes salicylate to 2-oxohepta-3,5-dienedioic acid via a novel ring fission mechanism. SDO differs from other known GDO's and NDO's in its unique ability to oxidatively cleave many different salicylate, gentisate, and 1-hydroxy-2- naphthoate substrates with high catalytic efficiency. The active site of this enzyme is located in the N-terminal domain but could be influenced by changes in the C-terminal domain, which lacks the strictly conserved metal-binding residues found in other cupin domains and is thought to be an inactive vestigial remnant.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 657623705  53 AHDSSGDAMVTVLDGTGRITIGDTEHILHAGDCIVMPAKIPH 94
Cdd:cd06992   34 PHRSTASAVYHVVEGSGRTVIGGKTFEWEPGDVFVVPSWAWH 75

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.

                         10        20        30
                 ....*....|....*....|....*....|.
gi 657623705  64 VLDGTGRITIGDTEHILHAGDCIVMPAKIPH 94
Cdd:cd02222   43 VLRGKGVVVIGGEEYPVKPGDVVYIPPNEPH 73

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
                  ....*....|....*....|....*....|....*
gi 657623705   64 VLDGTGRITIGDTEHILHAGDCIVMPAKIPHAVYA 98
Cdd:pfam02311  29 IERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDYEP 63

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

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 657623705  47 KNEEISAHDSSGDAMVTVLDGTGRITIGDTEHILHAGDCIVMPAKIPHAVY 97
Cdd:cd10547   28 PGGKMPLHQHRGEQIGIILNGKYDMTVGGEEQELGYGKIYYAPPNVSHSGY 78

(S)-ureidoglycine aminohydrolase and related proteins, C-terminal cupin domain; This family includes the C-terminal cupin domain of (S)-Ureidoglycine aminohydrolase (UGlyAH), an enzyme that converts (S)-ureidoglycine into (S)-ureidoglycolate and ammonia, providing the final substrate to the ureide pathway. The ureide pathway has recently been identified as the metabolic route of purine catabolism in plants and some bacteria where, uric acid, which is a major product of the early stage of purine catabolism, is degraded into glyoxylate and ammonia via stepwise reactions by seven different enzymes. Thus, this pathway has a possible physiological role in mobilization of purine ring nitrogen for further assimilation. This enzyme from Arabidopsis thaliana(AtUGlyAH) has been shown to bind a Mn2+ ion,via the C-terminal cupin domain, which acts as a molecular anchor to bind (S)-ureidoglycine, and its binding mode dictates the enantioselectivity of the reaction. The structure of AtUGlyAH shows a bi-cupin fold with a conserved "jelly roll-like" beta-barrel fold and an octameric functional unit. Several structural homologs of UGlyAH, including the Escherichia coli ortholog YlbA (also known as GlxB6), also exhibit similar features.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 657623705  64 VLDGTGRITIGDTEHILHAGDCIVMPAKIPHAVYAL--ERFKMLL 106
Cdd:cd02212   42 MLEGQGIYRLGDDWYPVQAGDFIWMAPYCPQWFYALgrEPFRYLL 86