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Conserved domains on  [gi|24584122|ref|NP_609653|]
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uncharacterized protein Dmel_CG16848 [Drosophila melanogaster]

Protein Classification

FAD synthase( domain architecture ID 19233630)

FAD (Flavin adenine dinucleotide) synthase catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme

CATH:  3.40.50.620
EC:  2.7.7.2
Gene Ontology:  GO:0005524|GO:0003919|GO:0006747
PubMed:  19375431|12012333
SCOP:  3001593

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 38-211 4.22e-93

FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; Flavin adenine dinucleotide synthase (FADS); EC 2.7.7.2) is involved in the biochemical pathway for converting riboflavin into FAD. By sequence comparison, bacterial and eukaryotic FMNAT enzymes belong to two different protein superfamilies and apparently utilize different sets of active-site residues to accomplish the same chemistry. This subfamily includes eukaryotic FMNATs, which are members of the 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase-like family belonging to the adenine nucleotide alpha hydrolase superfamily, which has conserved motifs different from those of nucleotidylyl transferases.


:

Pssm-ID: 467513 [Multi-domain]  Cd Length: 179  Bit Score: 271.32  E-value: 4.22e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122  38 KLEYTEEVIKRAMTLYKPNEMMLSFNGGKDCTVLLDILARMTP-----PSMPLGAVYVKSANPFEELEKFVDDCVQRYGL 112
Cdd:cd23948   1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKrkypsPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122 113 QLRRYEGVLKVAFEQLIAEDSQVKAIFLGCRRSDPESCNLYELEPTNNGWPAMMRIFPLLEWSYHDIWNYLRSNNLPYCC 192
Cdd:cd23948  81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYCS 160

                       170
                ....*....|....*....
gi 24584122 193 LYDQGYTSLGDRSSTRVNP 211
Cdd:cd23948 161 LYDQGYTSLGSVDNTLPNP 179
 
Name Accession Description Interval E-value
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 38-211 4.22e-93

FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; Flavin adenine dinucleotide synthase (FADS); EC 2.7.7.2) is involved in the biochemical pathway for converting riboflavin into FAD. By sequence comparison, bacterial and eukaryotic FMNAT enzymes belong to two different protein superfamilies and apparently utilize different sets of active-site residues to accomplish the same chemistry. This subfamily includes eukaryotic FMNATs, which are members of the 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase-like family belonging to the adenine nucleotide alpha hydrolase superfamily, which has conserved motifs different from those of nucleotidylyl transferases.


Pssm-ID: 467513 [Multi-domain]  Cd Length: 179  Bit Score: 271.32  E-value: 4.22e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122  38 KLEYTEEVIKRAMTLYKPNEMMLSFNGGKDCTVLLDILARMTP-----PSMPLGAVYVKSANPFEELEKFVDDCVQRYGL 112
Cdd:cd23948   1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKrkypsPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122 113 QLRRYEGVLKVAFEQLIAEDSQVKAIFLGCRRSDPESCNLYELEPTNNGWPAMMRIFPLLEWSYHDIWNYLRSNNLPYCC 192
Cdd:cd23948  81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYCS 160

                       170
                ....*....|....*....
gi 24584122 193 LYDQGYTSLGDRSSTRVNP 211
Cdd:cd23948 161 LYDQGYTSLGSVDNTLPNP 179
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 59-208 7.71e-34

Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine phosphosulfate (PAPS) reductase enzymes or PAPS sulfotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). It is also found in NodP nodulation protein P from Rhizobium which has ATP sulfurylase activity (sulfate adenylate transferase).


Pssm-ID: 396201 [Multi-domain]  Cd Length: 173  Bit Score: 120.09  E-value: 7.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122    59 MLSFNGGKDCTVLLDiLARMTPPSMPLgaVYVKSANPFEELEKFVDDCVQRYGLQL-----------------------R 115
Cdd:pfam01507   3 VVSFSGGKDSLVLLH-LASKAFPPGPV--IFIDTGYEFPETYEFVDELEEKYGLNLkvylpedsfaeginpegipsslyR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122   116 RYEGVLKVAFEQLIAEDSQVKAIFLGCRRSDPESCNLYELEPTNNGWPAMMRIFPLLEWSYHDIWNYLRSNNLPYCCLYD 195
Cdd:pfam01507  80 RCCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDGDFPKVIKVFPLLNWTETDVWQYILANNVPYNPLYD 159

                         170
                  ....*....|...
gi 24584122   196 QGYTSLGDRSSTR 208
Cdd:pfam01507 160 QGYRSIGCYPCTG 172
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 33-209 6.41e-23

3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439945 [Multi-domain]  Cd Length: 232  Bit Score: 93.37  E-value: 6.41e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122  33 DQLRDKLE-YTEEVIKRAMTLYKPNeMMLSFNGGKDCTVLLDILARMTPPsMPLgaVYV----KsanpFEELEKFVDDCV 107
Cdd:COG0175  11 EELNAELEaEAIEILREAAAEFGGR-VVVSSSGGKDSTVLLHLAAKFKPP-IPV--LFLdtgyE----FPETYEFRDRLA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122 108 QRYGLQLRRYE-------------------------GVLKV-AFEQLIAEDSQVkAIFLGCRRSdpES-----CNLYELE 156
Cdd:COG0175  83 ERLGLDLIVVRpedafaeqlaefgpplfyrdprwccKIRKVePLKRALAGYDFD-AWITGLRRD--ESptrakEPVVEWD 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 24584122 157 PTNNgwpaMMRIFPLLEWSYHDIWNYLRSNNLPYCCLYDQGYTSLGDRSSTRV 209
Cdd:COG0175 160 PVGG----LIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRA 208
cysH TIGR00434
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ...
 43-219 1.87e-12

phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of inorganic sulfate, is designated cysH in Bacteria and MET16 in Saccharomyces cerevisiae. Synonyms include phosphoadenosine phosphosulfate reductase, PAPS reductase, and PAPS reductase, thioredoxin-dependent. In a reaction requiring reduced thioredoxin and NADPH, it converts 3(prime)-phosphoadenylylsulfate (PAPS) to sulfite and adenosine 3(prime),5(prime) diphosphate (PAP). A related family of plant enzymes, scoring below the trusted cutoff, differs in having a thioredoxin-like C-terminal domain, not requiring thioredoxin, and in having a preference for 5(prime)-adenylylsulfate (APS) over PAPS. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 129526  Cd Length: 212  Bit Score: 64.42  E-value: 1.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122    43 EEVIKRAMTLYkPNEMMLSFNGGKDCTVLLDILARMTPpSMPLgaVYVKSANPFEELEKFVDDCVQRYGLQLRRYEGVLK 122
Cdd:TIGR00434   2 QEIIAWAYVTF-GGHLVYSTSFGIQGAVLLDLVSKISP-DIPV--IFLDTGYHFPETYELIDELTERYPLNIKVYKPDLS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122   123 VA----------FEQLIAEDSQVK---------------AIFLGCRRSD-PESCNLYELEPtnNGWPAMMRIFPLLEWSY 176
Cdd:TIGR00434  78 LAeqaakygdklWEQDPNKYDYLRkvepmhralkelhasAWFTGLRRDQgPSRANLSILNI--DEKFGILKVLPLIDWTW 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 24584122   177 HDIWNYLRSNNLPYCCLYDQGYTSLGDRSSTRvnPSLLAYDEK 219
Cdd:TIGR00434 156 KDVYQYIDAHNLPYNPLHDQGYPSIGDYHSTR--PVKEGEDER 196
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
170-208 1.85e-11

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 62.16  E-value: 1.85e-11
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 24584122  170 PLLEWSYHDIWNYLRSNNLPYCCLYDQGYTSLGDRSSTR 208
Cdd:PRK02090 174 PLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTR 212
 
Name Accession Description Interval E-value
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 38-211 4.22e-93

FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; Flavin adenine dinucleotide synthase (FADS); EC 2.7.7.2) is involved in the biochemical pathway for converting riboflavin into FAD. By sequence comparison, bacterial and eukaryotic FMNAT enzymes belong to two different protein superfamilies and apparently utilize different sets of active-site residues to accomplish the same chemistry. This subfamily includes eukaryotic FMNATs, which are members of the 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase-like family belonging to the adenine nucleotide alpha hydrolase superfamily, which has conserved motifs different from those of nucleotidylyl transferases.


Pssm-ID: 467513 [Multi-domain]  Cd Length: 179  Bit Score: 271.32  E-value: 4.22e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122  38 KLEYTEEVIKRAMTLYKPNEMMLSFNGGKDCTVLLDILARMTP-----PSMPLGAVYVKSANPFEELEKFVDDCVQRYGL 112
Cdd:cd23948   1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKrkypsPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122 113 QLRRYEGVLKVAFEQLIAEDSQVKAIFLGCRRSDPESCNLYELEPTNNGWPAMMRIFPLLEWSYHDIWNYLRSNNLPYCC 192
Cdd:cd23948  81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYCS 160

                       170
                ....*....|....*....
gi 24584122 193 LYDQGYTSLGDRSSTRVNP 211
Cdd:cd23948 161 LYDQGYTSLGSVDNTLPNP 179
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 59-208 7.71e-34

Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine phosphosulfate (PAPS) reductase enzymes or PAPS sulfotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). It is also found in NodP nodulation protein P from Rhizobium which has ATP sulfurylase activity (sulfate adenylate transferase).


Pssm-ID: 396201 [Multi-domain]  Cd Length: 173  Bit Score: 120.09  E-value: 7.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122    59 MLSFNGGKDCTVLLDiLARMTPPSMPLgaVYVKSANPFEELEKFVDDCVQRYGLQL-----------------------R 115
Cdd:pfam01507   3 VVSFSGGKDSLVLLH-LASKAFPPGPV--IFIDTGYEFPETYEFVDELEEKYGLNLkvylpedsfaeginpegipsslyR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122   116 RYEGVLKVAFEQLIAEDSQVKAIFLGCRRSDPESCNLYELEPTNNGWPAMMRIFPLLEWSYHDIWNYLRSNNLPYCCLYD 195
Cdd:pfam01507  80 RCCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDGDFPKVIKVFPLLNWTETDVWQYILANNVPYNPLYD 159

                         170
                  ....*....|...
gi 24584122   196 QGYTSLGDRSSTR 208
Cdd:pfam01507 160 QGYRSIGCYPCTG 172
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 33-209 6.41e-23

3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439945 [Multi-domain]  Cd Length: 232  Bit Score: 93.37  E-value: 6.41e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122  33 DQLRDKLE-YTEEVIKRAMTLYKPNeMMLSFNGGKDCTVLLDILARMTPPsMPLgaVYV----KsanpFEELEKFVDDCV 107
Cdd:COG0175  11 EELNAELEaEAIEILREAAAEFGGR-VVVSSSGGKDSTVLLHLAAKFKPP-IPV--LFLdtgyE----FPETYEFRDRLA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122 108 QRYGLQLRRYE-------------------------GVLKV-AFEQLIAEDSQVkAIFLGCRRSdpES-----CNLYELE 156
Cdd:COG0175  83 ERLGLDLIVVRpedafaeqlaefgpplfyrdprwccKIRKVePLKRALAGYDFD-AWITGLRRD--ESptrakEPVVEWD 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 24584122 157 PTNNgwpaMMRIFPLLEWSYHDIWNYLRSNNLPYCCLYDQGYTSLGDRSSTRV 209
Cdd:COG0175 160 PVGG----LIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRA 208
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 42-202 5.93e-16

Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8) is part of the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP).


Pssm-ID: 467510 [Multi-domain]  Cd Length: 183  Bit Score: 73.40  E-value: 5.93e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122  42 TEEVIKRAMTLYKPNeMMLSFNGGKDCTVLLDILARMTPPsmpLGAVYVKSANPFEELEKFVDDCVQRYGLQLR------ 115
Cdd:cd23945   1 PLEILLWAAEEFGPK-LVFATSFGAEDAVILDLLSKVRPD---IPVVFLDTGYLFPETYDLIDEVEARYGLNIEvyfpeg 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122 116 ---------------------RYEGVLKVAFEQLIAEDSQVKAIFLGCRRSD-PESCNL--YELEPTNNgwpaMMRIFPL 171
Cdd:cd23945  77 teaeeealegglnefyledeeRYDCCRKRKPFPLALALLGVKAWITGRRRDQsPTRANLpiVEVDEEGG----LVKINPL 152

                       170       180       190
                ....*....|....*....|....*....|.
gi 24584122 172 LEWSYHDIWNYLRSNNLPYCCLYDQGYTSLG 202
Cdd:cd23945 153 ADWTWEDVWAYIREHDLPYNPLHDQGYPSIG 183
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 44-202 8.78e-14

uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to Escherichia coli YbdN; This subgroup contains Escherichia coli YbdN and other phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8)-like proteins. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP).


Pssm-ID: 467512 [Multi-domain]  Cd Length: 206  Bit Score: 68.19  E-value: 8.78e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122  44 EVIKRAMTLYKPneMMLSFNGGKDCTVLLdILARMT--PPSMPLGAVYVKSANPFEELEKFVDDCVQRYGLQL------- 114
Cdd:cd23947   3 ERIRKVFEEFDP--VIVSFSGGKDSLVLL-HLALEAlrRLRKDVYVVFIDTGIEFPETIDFVEKLAETLGLDVeaarppl 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122 115 --------------------------RRYEGVLKV-AFEQLIAEDSQVKAI-FLGCRRSdpESCNLYELEPTNNGW---- 162
Cdd:cd23947  80 flewltsnfqpqwdpiwdnpppprdyRWCCDELKLePFTKWLKEKKPEGVLlLVGIRAD--ESLNRAKRPRVYRKYgwrn 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 24584122 163 ---PAMMRIFPLLEWSYHDIWNYLRSNNLPYCCLYDQGYTSLG 202
Cdd:cd23947 158 stlPGQIVAYPIKDWSVEDVWLYILRHGLPYNPLYDLGFDRGG 200
cysH TIGR00434
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ...
 43-219 1.87e-12

phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of inorganic sulfate, is designated cysH in Bacteria and MET16 in Saccharomyces cerevisiae. Synonyms include phosphoadenosine phosphosulfate reductase, PAPS reductase, and PAPS reductase, thioredoxin-dependent. In a reaction requiring reduced thioredoxin and NADPH, it converts 3(prime)-phosphoadenylylsulfate (PAPS) to sulfite and adenosine 3(prime),5(prime) diphosphate (PAP). A related family of plant enzymes, scoring below the trusted cutoff, differs in having a thioredoxin-like C-terminal domain, not requiring thioredoxin, and in having a preference for 5(prime)-adenylylsulfate (APS) over PAPS. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 129526  Cd Length: 212  Bit Score: 64.42  E-value: 1.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122    43 EEVIKRAMTLYkPNEMMLSFNGGKDCTVLLDILARMTPpSMPLgaVYVKSANPFEELEKFVDDCVQRYGLQLRRYEGVLK 122
Cdd:TIGR00434   2 QEIIAWAYVTF-GGHLVYSTSFGIQGAVLLDLVSKISP-DIPV--IFLDTGYHFPETYELIDELTERYPLNIKVYKPDLS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122   123 VA----------FEQLIAEDSQVK---------------AIFLGCRRSD-PESCNLYELEPtnNGWPAMMRIFPLLEWSY 176
Cdd:TIGR00434  78 LAeqaakygdklWEQDPNKYDYLRkvepmhralkelhasAWFTGLRRDQgPSRANLSILNI--DEKFGILKVLPLIDWTW 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 24584122   177 HDIWNYLRSNNLPYCCLYDQGYTSLGDRSSTRvnPSLLAYDEK 219
Cdd:TIGR00434 156 KDVYQYIDAHNLPYNPLHDQGYPSIGDYHSTR--PVKEGEDER 196
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
170-208 1.85e-11

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 62.16  E-value: 1.85e-11
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 24584122  170 PLLEWSYHDIWNYLRSNNLPYCCLYDQGYTSLGDRSSTR 208
Cdd:PRK02090 174 PLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTR 212
Sulfate_adenylyltransferase_2 cd23946
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ...
 56-194 1.21e-08

Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in the sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN, coupled to ATP hydrolysis by CysD. CysD belongs to the ATP pyrophosphatase (ATP PPase) family of proteins, members of which include PAPS reductase, GMP synthetase, asparagine synthetase, and NAD(+) synthetase. This subunit is responsible for directly forming APS under control of the G protein. A modified version of the P loop (PP-loop), the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues.


Pssm-ID: 467511  Cd Length: 214  Bit Score: 53.66  E-value: 1.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122  56 NEMMLsFNGGKDCTVLLDILAR-MTPPSMPLGAVYVKSANPFEELEKFVDDCVQRYGLQLRRYEG--------------- 119
Cdd:cd23946  22 NPVML-YSIGKDSSVMLHLARKaFYPGKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDLIVHVNpdgveaginpfthgs 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122 120 -----VLKVAFEQLIAEDSQVKAIFLGCRRSDPESC---NLYELEPTNNGW------PAM-------------MRIFPLL 172
Cdd:cd23946 101 akhtdIMKTEGLKQALDKYGFDAAFGGARRDEEKSRakeRVYSFRDSNHRWdpknqrPELwnqyngrvkkgesIRVFPLS 180

                       170       180
                ....*....|....*....|..
gi 24584122 173 EWSYHDIWNYLRSNNLPYCCLY 194
Cdd:cd23946 181 NWTELDIWQYIYLENIPIVPLY 202
PRK08557 PRK08557
hypothetical protein; Provisional
 30-202 7.47e-07

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 49.37  E-value: 7.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122   30 ESNDQLRDKLE-YTEEVIKRAMTLYKPN--EMMLSFNGGKDCTVLlDILARMTPPSMPlgAVYVKSANPFEELEKFVDDC 106
Cdd:PRK08557 153 EKNKERIEKLEeNSLSILKDYIEKYKNKgyAINASFSGGKDSSVS-TLLAKEVIPDLE--VIFIDTGLEYPETINYVKDF 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122  107 VQRYGLQLRRYEGvlKVAFEQLIAE----------DSQVKAIFL-----------------GCRRSDPESCNLYELEPTN 159
Cdd:PRK08557 230 AKKYDLNLDTLDG--DNFWENLEKEgiptkdnrwcNSACKLMPLkeylkkkygnkkvltidGSRKYESFTRANLDYERKS 307

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 24584122  160 NGWPAMMRIFPLLEWSYHDIWNYLRSNNLPYCCLYDQGYTSLG 202
Cdd:PRK08557 308 GFIDFQTNVFPILDWNSLDIWSYIYLNDILYNPLYDKGFERIG 350
PRK13795 PRK13795
hypothetical protein; Provisional
 27-202 3.24e-06

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 47.68  E-value: 3.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122   27 EKSESNDQLRDKLEYTEEVIKRAMTLYK--PNEMML----SFNGGKDCTVLLDILARmtppsmPLGAVYVKSANP---FE 97
Cdd:PRK13795 209 GRATLEDAIEANRKHLEEKEKEAVNFIRgvAEKYNLpvsvSFSGGKDSLVVLDLARE------ALKDFKAFFNNTgleFP 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122   98 ELEKFVDDCVQRYGLQLRRYEG-----------------------VLKVA-FEQLIAEDSQVKAI-FLGCRRSdpESCNL 152
Cdd:PRK13795 283 ETVENVKEVAEEYGIELIEADAgdafwravekfgppardyrwcckVCKLGpITRAIKENFPKGCLtFVGQRKY--ESFSR 360

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24584122  153 YELEPT-NNGW-PAMMRIFPLLEWSYHDIWNYLRSNNLPYCCLYDQGYTSLG 202
Cdd:PRK13795 361 AKSPRVwRNPWvPNQIGASPIQDWTALEVWLYIFWRKLPYNPLYERGFDRIG 412
PRK12563 PRK12563
sulfate adenylyltransferase subunit CysD;
56-194 7.97e-06

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 237138  Cd Length: 312  Bit Score: 45.93  E-value: 7.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122   56 NEMMLsFNGGKDCTVLLDILA---RMTPPSMPLgaVYVKSANPFEELEKFVDDCVQRYGLQLRRY---EGVLK------- 122
Cdd:PRK12563  39 KPVML-YSIGKDSVVMLHLAMkafRPTRPPFPL--LHVDTTWKFREMIDFRDRRAKELGLDLVVHhnpDGIARgivpfrh 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122  123 -----------VAFEQLIaEDSQVKAIFLGCRRSD-------------------------PESCNLYE--LEPTNNgwpa 164
Cdd:PRK12563 116 gsalhtdvaktQGLKQAL-DHHGFDAAIGGARRDEeksrakerifsfrsafhrwdpkaqrPELWSLYNarLRRGES---- 190

                        170       180       190
                 ....*....|....*....|....*....|
gi 24584122  165 mMRIFPLLEWSYHDIWNYLRSNNLPYCCLY 194
Cdd:PRK12563 191 -LRVFPLSNWTELDVWQYIAREKIPLVPLY 219
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 24-208 1.21e-05

5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the assimilation of inorganic sulfate, is closely related to the thioredoxin-dependent PAPS reductase of Bacteria (CysH) and Saccharomyces cerevisiae. However, it has its own C-terminal thioredoxin-like domain and is not thioredoxin-dependent. Also, it has a substrate preference for 5'-adenylylsulfate (APS) over 3'-phosphoadenylylsulfate (PAPS) so the pathway does not require an APS kinase (CysC) to convert APS to PAPS. Arabidopsis thaliana appears to have three isozymes, all able to complement E. coli CysH mutants (even in backgrounds lacking thioredoxin or APS kinase) but likely localized to different compartments in Arabidopsis. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 273072 [Multi-domain]  Cd Length: 463  Bit Score: 45.78  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122    24 PPVEKS----ESNDQLRDKLEYTE--EVIKRAMTLYKpNEMMLSFNGGKDctVLLDILARMTPPSMPLGAVYVKSANPfe 97
Cdd:TIGR00424  79 PEVEEKvvevEDFEKLAKKLENASplEIMDKALEKFG-NDIAIAFSGAED--VALIEYAHLTGRPFRVFSLDTGRLNP-- 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122    98 ELEKFVDDCVQRYGLQ-------------LRRYEGVLKVaFEQLIAEDSQVKAI------------FLGCRRSDPESCNL 152
Cdd:TIGR00424 154 ETYRFFDAVEKQYGIRieymfpdavevqaLVRSKGLFSF-YEDGHQECCRVRKVrplrralkglkaWITGQRKDQSPGTR 232

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24584122   153 YEL---------EPTNNGWPAMMRIFPLLEWSYHDIWNYLRSNNLPYCCLYDQGYTSLGDRSSTR 208
Cdd:TIGR00424 233 SEIpvvqvdpvfEGLDGGVGSLVKWNPVANVEGKDVWNFLRTMDVPVNTLHAQGYVSIGCEPCTR 297
PRK05253 PRK05253
sulfate adenylyltransferase subunit CysD;
59-194 1.40e-05

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 235375  Cd Length: 301  Bit Score: 45.13  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122   59 MLsFNGGKDCTVLLDiLAR-----MTPPsMPLgaVYVKSANPFEELEKFVDDCVQRYGLQLRRY---EGV---------- 120
Cdd:PRK05253  32 ML-YSIGKDSSVMLH-LARkafypGKLP-FPL--LHVDTGWKFPEMIEFRDRRAKELGLELIVHsnpEGIarginpfrhg 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584122  121 -------LK-VAFEQLIAE---DsqvkAIFLGCRRsD--------------------------PESCNLYeleptnNGWP 163
Cdd:PRK05253 107 sakhtnaMKtEGLKQALEKygfD----AAFGGARR-DeeksrakerifsfrdefgqwdpknqrPELWNLY------NGRI 175

                        170       180       190
                 ....*....|....*....|....*....|....
gi 24584122  164 AM---MRIFPLLEWSYHDIWNYLRSNNLPYCCLY 194
Cdd:PRK05253 176 NKgehIRVFPLSNWTELDIWQYIERENIPIVPLY 209
PLN02309 PLN02309
5'-adenylylsulfate reductase
 170-208 6.23e-03

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 37.46  E-value: 6.23e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 24584122  170 PLLEWSYHDIWNYLRSNNLPYCCLYDQGYTSLGDRSSTR 208
Cdd:PLN02309 254 PLANVTGNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCTR 292
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 59-105 9.04e-03

adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


Pssm-ID: 467490 [Multi-domain]  Cd Length: 74  Bit Score: 34.35  E-value: 9.04e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 24584122  59 MLSFNGGKDCTVLLDILARmTPPSMPLGAVYVKSANPFEELEKFVDD 105
Cdd:cd01986   2 VVGYSGGKDSSVALHLASR-LGRKAEVAVVHIDHGIGFKEEAESVAS 47
 
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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