2,4'-Dihydroxyacetophenone dioxygenase (DAD), cupin domain; 2,4'-Dihydroxyacetophenone dioxygenase (DAD) catalyzes the oxidation of 2,4'-dihydroxyacetophenone to 4-hydroxybenzoate and formate as part of the 4-hydroxyacetophenone catabolic pathway. This enzyme is a homo-tetramer containing one iron per molecule of enzyme. This enzyme is an unusual dioxygenase in that it cleaves a C-C bond in a substituent of the aromatic ring rather than within the ring itself. As a bacterial dioxygenase, DAD plays an important environmental role in the aerobic catabolism of aromatic compounds; expression of this enzyme in appropriately engineered microorganisms has the potential to use these aromatic pollutants as a carbon source and thus remove them from the environment. 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 490300141  25 PWLPMDASLPGLAIKYLHINVADDEMTVLLKMPVGLALPRHRHDGAVFVYTLQGEWRYREYDWIARPGSAVLEPAGSHHT 104
Cdd:cd20302    1 DWVPWTPLGPGVWFKPLRFDPETGEWVVLLRVPPGGSLPRHRHTGPVHAYTLSGSWRYLEHDWVATAGSYVYEPAGSIHT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 490300141 105 PEALasETGAVVTFNVMRGDLVLLDDAGRETARENCRVAL 144
Cdd:cd20302   81 LVVP--EEEETIVLFIVQGALIFLDEDGNVIGVEDAFTLL 118

2,4'-Dihydroxyacetophenone dioxygenase (DAD), cupin domain; 2,4'-Dihydroxyacetophenone dioxygenase (DAD) catalyzes the oxidation of 2,4'-dihydroxyacetophenone to 4-hydroxybenzoate and formate as part of the 4-hydroxyacetophenone catabolic pathway. This enzyme is a homo-tetramer containing one iron per molecule of enzyme. This enzyme is an unusual dioxygenase in that it cleaves a C-C bond in a substituent of the aromatic ring rather than within the ring itself. As a bacterial dioxygenase, DAD plays an important environmental role in the aerobic catabolism of aromatic compounds; expression of this enzyme in appropriately engineered microorganisms has the potential to use these aromatic pollutants as a carbon source and thus remove them from the environment. 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 490300141  25 PWLPMDASLPGLAIKYLHINVADDEMTVLLKMPVGLALPRHRHDGAVFVYTLQGEWRYREYDWIARPGSAVLEPAGSHHT 104
Cdd:cd20302    1 DWVPWTPLGPGVWFKPLRFDPETGEWVVLLRVPPGGSLPRHRHTGPVHAYTLSGSWRYLEHDWVATAGSYVYEPAGSIHT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 490300141 105 PEALasETGAVVTFNVMRGDLVLLDDAGRETARENCRVAL 144
Cdd:cd20302   81 LVVP--EEEETIVLFIVQGALIFLDEDGNVIGVEDAFTLL 118

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490300141  28 PMDASLPGLAIKYLHINvADDEMTVLLKMPVGLALPRHRHDGAVFVYTLQGEWRYR--EYDWIARPGSAVLEPAGSHHTP 105
Cdd:COG1917    3 LAEIALTGVSVRVLADG-EDELEVVRVTFEPGARTPWHSHPGEELIYVLEGEGEVEvgGEEYELKPGDVVFIPPGVPHAF 81

                         90
                 ....*....|...
gi 490300141 106 EALASETGAVVTF 118
Cdd:COG1917   82 RNLGDEPAVLLVV 94

2,4'-Dihydroxyacetophenone dioxygenase (DAD), cupin domain; 2,4'-Dihydroxyacetophenone dioxygenase (DAD) catalyzes the oxidation of 2,4'-dihydroxyacetophenone to 4-hydroxybenzoate and formate as part of the 4-hydroxyacetophenone catabolic pathway. This enzyme is a homo-tetramer containing one iron per molecule of enzyme. This enzyme is an unusual dioxygenase in that it cleaves a C-C bond in a substituent of the aromatic ring rather than within the ring itself. As a bacterial dioxygenase, DAD plays an important environmental role in the aerobic catabolism of aromatic compounds; expression of this enzyme in appropriately engineered microorganisms has the potential to use these aromatic pollutants as a carbon source and thus remove them from the environment. 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 490300141  25 PWLPMDASLPGLAIKYLHINVADDEMTVLLKMPVGLALPRHRHDGAVFVYTLQGEWRYREYDWIARPGSAVLEPAGSHHT 104
Cdd:cd20302    1 DWVPWTPLGPGVWFKPLRFDPETGEWVVLLRVPPGGSLPRHRHTGPVHAYTLSGSWRYLEHDWVATAGSYVYEPAGSIHT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 490300141 105 PEALasETGAVVTFNVMRGDLVLLDDAGRETARENCRVAL 144
Cdd:cd20302   81 LVVP--EEEETIVLFIVQGALIFLDEDGNVIGVEDAFTLL 118

ChrR Cupin-like domain; Members of this family are part of the cupin superfamily. This family includes the transcriptional activator ChrR.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490300141   25 PWLPMDAslPGLAIKYLH-INVADDEMTVLLKMPVGLALPRHRHDGAVFVYTLQGEWRYREYDWiaRPGSAVLEPAGSHH 103
Cdd:pfam12973   1 PWVPSPV--PGVERKPLHrDGGEKARATSLVRYAPGSRFPAHRHPGGEEILVLEGVFSDEHGDY--PAGTYLRNPPGSSH 76

                          90
                  ....*....|..
gi 490300141  104 TPealASETGAV 115
Cdd:pfam12973  77 AP---FSEEGCT 85

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        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490300141  44 NVADDEMTVLL-KMPVGLALPRHRHDGAVFVYTLQGEWRY-------REYdwiaRPGSAVLEPAGSHHTPEALASET 112
Cdd:cd02234   13 NIPGKEVTVLLvTYPPGAASPPHRHPGFVFAYVLEGEVRSqvnggppRVY----KAGESFYEPPGAHHRVSRNASAT 85

Marinobacter hydrocarbonoclasticus anti-ECFsigma factor ChrR, and similar proteins; 2 heterologous tandem repeats of cupin domain; This family contains bacterial anti-sigma factor such as ChrR from Marinobacter hydrocarbonoclasticus. Anti-sigma factor ChrR is a member of the ZAS (Zn2+ anti-sigma) subfamily of group IV anti-sigmas. It inhibits transcriptional activity by binding to the ECF sigma factor E (sigmaE), an essential factor to mount a transcriptional response to a singlet oxygen and for viability when carotenoids are limiting. This protein family likely contains two distinct homologous functional domains belonging to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490300141  22 DDRPWLPmdASLPGLAIKYLHinVADDEMTVLLKMPVGLALPRHRHDGAVFVYTLQGEWR--YREYDwiarPGSAVLEPA 99
Cdd:cd20303   10 RDADWVP--GPVPGVERLPLH--RFGAEATALVRWAPGTRFPPHSHPGGEEILVLEGTFSdeHGDYP----AGTWLRNPH 81

                         90
                 ....*....|....*..
gi 490300141 100 GSHHTPEalaSETGAVV 116
Cdd:cd20303   82 GSRHAPF---SEEGCTL 95

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490300141  52 VLLKMPVGLALPRHRHDGA-VFVYTLQGEWRYREYDW---IARPGSAVLEPAGSHHTPEALASE 111
Cdd:cd02208    2 SVVTLPPGTSSPPHWHPEQdEIFYVLSGEGELTLDDGetvELKAGDIVLIPPGVPHSFVNTSDE 65

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490300141  40 YLHINVADDEMTV-LLKMPVGLALPRHRH-DGAVFVYTLQGEWR--YREYDWIARPGSAVLEPAGSHHTPEALASETGAV 115
Cdd:COG0662   17 YEVLGEGGERLSVkRITVPPGAELSLHVHpHRDEFFYVLEGTGEvtIGDEEVELKAGDSVYIPAGVPHRLRNPGDEPLEL 96

                         90
                 ....*....|....*....
gi 490300141 116 VTfnVMRGDLVLLDDAGRE 134
Cdd:COG0662   97 LE--VQAPAYLGEDDIVRE 113