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Conserved domains on  [gi|2055117442|sp|A0R0W2|]
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RecName: Full=Adenosine 5'-phosphosulfate reductase; Short=APS reductase; AltName: Full=5'-adenylylsulfate reductase; AltName: Full=Thioredoxin-dependent 5'-adenylylsulfate reductase

Protein Classification

adenylyl/phosphoadenylyl-sulfate reductase( domain architecture ID 10792199)

adenylyl/phosphoadenylyl-sulfate reductase catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS)/phosphoadenosine 5'-phosphosulfate (PAPS) using thioredoxin as the electron donor

CATH:  3.40.50.620
EC:  1.8.4.-
Gene Ontology:  GO:0016671|GO:0070814|GO:0019379|GO:0006790
PubMed:  9261082|17352498|12012333
SCOP:  4003838

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
1-236 7.54e-121

phosphoadenylyl-sulfate reductase;


:

Pssm-ID: 234997  Cd Length: 241  Bit Score: 343.36  E-value: 7.54e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442   1 MTDVTTSTENELRELAERGAAELADASAEELLRWTDEHFGGNYVVAS--NMQDAVLVEMAAKVRPGVDVLFLDTGYHFAE 78
Cdd:PRK02090    1 LNALNALPKADLALDLAELNAELEGASAQERLAWALENFGGRLALVSsfGAEDAVLLHLVAQVDPDIPVIFLDTGYLFPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  79 TIGTRDAVEAVYDVHVVNVTPERTVAEQDELLGKNLFA--RDPGECCRLRKVVPLTNALKGYSAWVTGIRRVEAPTRANA 156
Cdd:PRK02090   81 TYRFIDELTERLLLNLKVYRPDASAAEQEARYGGLWEQsvEDRDECCRIRKVEPLNRALAGLDAWITGLRREQSGTRANL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442 157 PLISWDNafGLVKINPIAAWTDEDMQNYIDANGILVNPLVYEGYPSIGCAPCTSKPIPGADPRSGRWAGLSKTECGLHVS 236
Cdd:PRK02090  161 PVLEIDG--GRFKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGRWWGGLKKECGLHEG 238
 
Name Accession Description Interval E-value
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
1-236 7.54e-121

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 343.36  E-value: 7.54e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442   1 MTDVTTSTENELRELAERGAAELADASAEELLRWTDEHFGGNYVVAS--NMQDAVLVEMAAKVRPGVDVLFLDTGYHFAE 78
Cdd:PRK02090    1 LNALNALPKADLALDLAELNAELEGASAQERLAWALENFGGRLALVSsfGAEDAVLLHLVAQVDPDIPVIFLDTGYLFPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  79 TIGTRDAVEAVYDVHVVNVTPERTVAEQDELLGKNLFA--RDPGECCRLRKVVPLTNALKGYSAWVTGIRRVEAPTRANA 156
Cdd:PRK02090   81 TYRFIDELTERLLLNLKVYRPDASAAEQEARYGGLWEQsvEDRDECCRIRKVEPLNRALAGLDAWITGLRREQSGTRANL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442 157 PLISWDNafGLVKINPIAAWTDEDMQNYIDANGILVNPLVYEGYPSIGCAPCTSKPIPGADPRSGRWAGLSKTECGLHVS 236
Cdd:PRK02090  161 PVLEIDG--GRFKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGRWWGGLKKECGLHEG 238
APS_reductase TIGR02055
thioredoxin-dependent adenylylsulfate APS reductase; This model describes recently identified ...
 47-233 4.14e-101

thioredoxin-dependent adenylylsulfate APS reductase; This model describes recently identified adenosine 5'-phosphosulfate (APS) reductase activity found in sulfate-assimilatory prokaryotes, thus separating it from the traditionally described phosphoadenosine 5'-phosphosulfate (PAPS) reductases found in bacteria and fungi. Homologous to PAPS reductase in enterobacteria, cyanobacteria, and yeast, APS reductase here clusters with, and demonstrates greater homology to plant APS reductase. Additionally, the presence of two conserved C-terminal motifs (CCXXRKXXPL _ SXGCXXCT) distinguishes APS substrate specificity and serves as a FeS cluster. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 273945  Cd Length: 191  Bit Score: 291.67  E-value: 4.14e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  47 SNMQDAVLVEMAAKVRPGVDVLFLDTGYHFAETIGTRDAVEAVYDVH-VVNVTPERTVAEQDELLGKNLFARD-PGECCR 124
Cdd:TIGR02055   1 LGAEDVVLVDLAAKVRPDVKVFFLDTGRLFKETYETIDQVRERYDILiDVLSPPPLTVEEQVKEYGLNLFYRSvPHECCG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442 125 LRKVVPLTNALKGYSAWVTGIRRVEAPTRANAPLISWDNAFGLVKINPIAAWTDEDMQNYIDANGILVNPLVYEGYPSIG 204
Cdd:TIGR02055  81 IRKVEPLKRALAGVSAWITGLRRDQSPTRAQAPFLEIDEAFGLVKINPLADWTSEDVWEYIADNELPYNPLHDRGYPSIG 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2055117442 205 CAPCTSKPIPGADPRSGRWAGLS--KTECGL 233
Cdd:TIGR02055 161 CEPCTRPVAPGEDPRAGRWWWEEaaKKECGL 191
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 8-233 9.59e-101

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: 292.14  E-value: 9.59e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442   8 TENELRELAERGAAELAdASAEELLRWTDEHFGGNYVVASNM--QDAVLVEMAAKVRPGVDVLFLDTGYHFAETIGTRDA 85
Cdd:COG0175     2 LPATLDDLLEELNAELE-AEAIEILREAAAEFGGRVVVSSSGgkDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  86 VEAVYDVHVVNVTPERTVAEQDELLGKNLFARDPGECCRLRKVVPLTNALKGYS--AWVTGIRRVEAPTRANAPLISWDN 163
Cdd:COG0175    81 LAERLGLDLIVVRPEDAFAEQLAEFGPPLFYRDPRWCCKIRKVEPLKRALAGYDfdAWITGLRRDESPTRAKEPVVEWDP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055117442 164 AFGLVKINPIAAWTDEDMQNYIDANGILVNPLVYEGYPSIGCAPCTSKPIPGADPRSGRWAGLSK--TECGL 233
Cdd:COG0175   161 VGGLIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWWDEEKerKECGL 232
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 28-204 8.60e-76

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: 227.09  E-value: 8.60e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  28 AEELLRWTDEHFGGNYVVASN--MQDAVLVEMAAKVRPGVDVLFLDTGYHFAETIGTRDAVEAVYDVHVVNVTPERTVAE 105
Cdd:cd23945     1 PLEILLWAAEEFGPKLVFATSfgAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYGLNIEVYFPEGTEAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442 106 QDELLGK----NLFARDPGECCRLRKVVPLTNALKGYSAWVTGIRRVEAPTRANAPLISWDNAFGLVKINPIAAWTDEDM 181
Cdd:cd23945    81 EEALEGGlnefYLEDEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIVEVDEEGGLVKINPLADWTWEDV 160

                         170       180
                  ....*....|....*....|...
gi 2055117442 182 QNYIDANGILVNPLVYEGYPSIG 204
Cdd:cd23945   161 WAYIREHDLPYNPLHDQGYPSIG 183
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 42-211 5.90e-62

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: 191.74  E-value: 5.90e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  42 NYVVASNMQDAVLVEMAAKVRPGVDVLFLDTGYHFAETIGTRDAVEAVYDVHVVNVTPERTVAEQDELLGKNLFARDpgE 121
Cdd:pfam01507   3 VVSFSGGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSSLYR--R 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442 122 CCRLRKVVPLTNALK--GYSAWVTGIRRVEAPTRANAPLISWDNAFG-LVKINPIAAWTDEDMQNYIDANGILVNPLVYE 198
Cdd:pfam01507  81 CCRLRKVEPLKRALKelGFDAWFTGLRRDESPSRAKLPIVSIDGDFPkVIKVFPLLNWTETDVWQYILANNVPYNPLYDQ 160

                         170
                  ....*....|...
gi 2055117442 199 GYPSIGCAPCTSK 211
Cdd:pfam01507 161 GYRSIGCYPCTGP 173
 
Name Accession Description Interval E-value
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
1-236 7.54e-121

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 343.36  E-value: 7.54e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442   1 MTDVTTSTENELRELAERGAAELADASAEELLRWTDEHFGGNYVVAS--NMQDAVLVEMAAKVRPGVDVLFLDTGYHFAE 78
Cdd:PRK02090    1 LNALNALPKADLALDLAELNAELEGASAQERLAWALENFGGRLALVSsfGAEDAVLLHLVAQVDPDIPVIFLDTGYLFPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  79 TIGTRDAVEAVYDVHVVNVTPERTVAEQDELLGKNLFA--RDPGECCRLRKVVPLTNALKGYSAWVTGIRRVEAPTRANA 156
Cdd:PRK02090   81 TYRFIDELTERLLLNLKVYRPDASAAEQEARYGGLWEQsvEDRDECCRIRKVEPLNRALAGLDAWITGLRREQSGTRANL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442 157 PLISWDNafGLVKINPIAAWTDEDMQNYIDANGILVNPLVYEGYPSIGCAPCTSKPIPGADPRSGRWAGLSKTECGLHVS 236
Cdd:PRK02090  161 PVLEIDG--GRFKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGRWWGGLKKECGLHEG 238
APS_reductase TIGR02055
thioredoxin-dependent adenylylsulfate APS reductase; This model describes recently identified ...
 47-233 4.14e-101

thioredoxin-dependent adenylylsulfate APS reductase; This model describes recently identified adenosine 5'-phosphosulfate (APS) reductase activity found in sulfate-assimilatory prokaryotes, thus separating it from the traditionally described phosphoadenosine 5'-phosphosulfate (PAPS) reductases found in bacteria and fungi. Homologous to PAPS reductase in enterobacteria, cyanobacteria, and yeast, APS reductase here clusters with, and demonstrates greater homology to plant APS reductase. Additionally, the presence of two conserved C-terminal motifs (CCXXRKXXPL _ SXGCXXCT) distinguishes APS substrate specificity and serves as a FeS cluster. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 273945  Cd Length: 191  Bit Score: 291.67  E-value: 4.14e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  47 SNMQDAVLVEMAAKVRPGVDVLFLDTGYHFAETIGTRDAVEAVYDVH-VVNVTPERTVAEQDELLGKNLFARD-PGECCR 124
Cdd:TIGR02055   1 LGAEDVVLVDLAAKVRPDVKVFFLDTGRLFKETYETIDQVRERYDILiDVLSPPPLTVEEQVKEYGLNLFYRSvPHECCG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442 125 LRKVVPLTNALKGYSAWVTGIRRVEAPTRANAPLISWDNAFGLVKINPIAAWTDEDMQNYIDANGILVNPLVYEGYPSIG 204
Cdd:TIGR02055  81 IRKVEPLKRALAGVSAWITGLRRDQSPTRAQAPFLEIDEAFGLVKINPLADWTSEDVWEYIADNELPYNPLHDRGYPSIG 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2055117442 205 CAPCTSKPIPGADPRSGRWAGLS--KTECGL 233
Cdd:TIGR02055 161 CEPCTRPVAPGEDPRAGRWWWEEaaKKECGL 191
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 8-233 9.59e-101

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: 292.14  E-value: 9.59e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442   8 TENELRELAERGAAELAdASAEELLRWTDEHFGGNYVVASNM--QDAVLVEMAAKVRPGVDVLFLDTGYHFAETIGTRDA 85
Cdd:COG0175     2 LPATLDDLLEELNAELE-AEAIEILREAAAEFGGRVVVSSSGgkDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  86 VEAVYDVHVVNVTPERTVAEQDELLGKNLFARDPGECCRLRKVVPLTNALKGYS--AWVTGIRRVEAPTRANAPLISWDN 163
Cdd:COG0175    81 LAERLGLDLIVVRPEDAFAEQLAEFGPPLFYRDPRWCCKIRKVEPLKRALAGYDfdAWITGLRRDESPTRAKEPVVEWDP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055117442 164 AFGLVKINPIAAWTDEDMQNYIDANGILVNPLVYEGYPSIGCAPCTSKPIPGADPRSGRWAGLSK--TECGL 233
Cdd:COG0175   161 VGGLIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWWDEEKerKECGL 232
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 28-204 8.60e-76

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: 227.09  E-value: 8.60e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  28 AEELLRWTDEHFGGNYVVASN--MQDAVLVEMAAKVRPGVDVLFLDTGYHFAETIGTRDAVEAVYDVHVVNVTPERTVAE 105
Cdd:cd23945     1 PLEILLWAAEEFGPKLVFATSfgAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYGLNIEVYFPEGTEAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442 106 QDELLGK----NLFARDPGECCRLRKVVPLTNALKGYSAWVTGIRRVEAPTRANAPLISWDNAFGLVKINPIAAWTDEDM 181
Cdd:cd23945    81 EEALEGGlnefYLEDEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIVEVDEEGGLVKINPLADWTWEDV 160

                         170       180
                  ....*....|....*....|...
gi 2055117442 182 QNYIDANGILVNPLVYEGYPSIG 204
Cdd:cd23945   161 WAYIREHDLPYNPLHDQGYPSIG 183
cysH TIGR00434
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ...
 28-234 6.12e-70

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: 213.11  E-value: 6.12e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  28 AEELLRWTDEHFGGNYVVASN--MQDAVLVEMAAKVRPGVDVLFLDTGYHFAETIGTRDAVEAVYDVHVVNVTPERTVAE 105
Cdd:TIGR00434   1 AQEIIAWAYVTFGGHLVYSTSfgIQGAVLLDLVSKISPDIPVIFLDTGYHFPETYELIDELTERYPLNIKVYKPDLSLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442 106 QDELLGKNLFARDPGECCRLRKVVPLTNALKGY--SAWVTGIRRVEAPTRANAPLISWDNAFGLVKINPIAAWTDEDMQN 183
Cdd:TIGR00434  81 QAAKYGDKLWEQDPNKYDYLRKVEPMHRALKELhaSAWFTGLRRDQGPSRANLSILNIDEKFGILKVLPLIDWTWKDVYQ 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2055117442 184 YIDANGILVNPLVYEGYPSIGCAPCTSKPIPGADPRSGRWAGLSKTECGLH 234
Cdd:TIGR00434 161 YIDAHNLPYNPLHDQGYPSIGDYHSTRPVKEGEDERAGRWKGKAKTECGLH 211
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 42-211 5.90e-62

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: 191.74  E-value: 5.90e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  42 NYVVASNMQDAVLVEMAAKVRPGVDVLFLDTGYHFAETIGTRDAVEAVYDVHVVNVTPERTVAEQDELLGKNLFARDpgE 121
Cdd:pfam01507   3 VVSFSGGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSSLYR--R 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442 122 CCRLRKVVPLTNALK--GYSAWVTGIRRVEAPTRANAPLISWDNAFG-LVKINPIAAWTDEDMQNYIDANGILVNPLVYE 198
Cdd:pfam01507  81 CCRLRKVEPLKRALKelGFDAWFTGLRRDESPSRAKLPIVSIDGDFPkVIKVFPLLNWTETDVWQYILANNVPYNPLYDQ 160

                         170
                  ....*....|...
gi 2055117442 199 GYPSIGCAPCTSK 211
Cdd:pfam01507 161 GYRSIGCYPCTGP 173
PAPS_reductase TIGR02057
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ...
 21-234 3.35e-54

phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an electron donor, phosphoadenosine phosphosulfate reductase catalyzes the reduction of 3'-phosphoadenylylsulfate (PAPS) to sulfite and phospho-adenosine-phosphate (PAP). Found in enterobacteria, cyanobacteria, and yeast, PAPS reductase is related to a group of plant (TIGR00424) and bacterial (TIGR02055) enzymes preferring 5'-adenylylsulfate (APS) over PAPS as a substrate for reduction to sulfite. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 131112  Cd Length: 226  Bit Score: 173.48  E-value: 3.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  21 AELADASAEELLRWTDEHFGGNYVVAS--NMQDAVLVEMAAKVR-PGVDVLFLDTGYHFAETIGTRDAVEAVY--DVHVV 95
Cdd:TIGR02057   6 EQLEKLTPQEIIAWSIVTFPHGLVQTSafGIQALVTLHLLSSISePMIPVIFIDTLYHFPQTLTLKDELTKKYyqTLNLY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  96 NVTPERTVAEQDELLGKNLFARDPGECCRLRKVVPLTNALK--GYSAWVTGIRRVEAPTRANAPLISWDNAFGLVKINPI 173
Cdd:TIGR02057  86 KYDGCESEADFEAKYGKLLWQKDIEKYDYIAKVEPMQRALKelNASAWFTGRRRDQGSARANLPVIEIDEQNGILKVNPL 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2055117442 174 AAWTDEDMQNYIDANGILVNPLVYEGYPSIGCAPCTSKPIPGADPRSGRWAGLSKTECGLH 234
Cdd:TIGR02057 166 IDWTFEQVYQYLDAHNVPYNPLLDQGYRSIGDYHSTRKVKEGEDERAGRWKGKLKTECGIH 226
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 17-234 3.33e-42

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: 149.01  E-value: 3.33e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  17 ERGAAELADASAEELLRWTDEHFGGNYVVA-SNMQDAVLVEMAAKVRPGVDVLFLDTGYHFAETIGTRDAVEAVYDVHVV 95
Cdd:TIGR00424  92 EKLAKKLENASPLEIMDKALEKFGNDIAIAfSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRFFDAVEKQYGIRIE 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  96 NVTPErTVAEQDELLGKNLFA-RDPG--ECCRLRKVVPLTNALKGYSAWVTGIRRVEAP-TRANAPLISWDNAF------ 165
Cdd:TIGR00424 172 YMFPD-AVEVQALVRSKGLFSfYEDGhqECCRVRKVRPLRRALKGLKAWITGQRKDQSPgTRSEIPVVQVDPVFegldgg 250

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2055117442 166 --GLVKINPIAAWTDEDMQNYIDANGILVNPLVYEGYPSIGCAPCTSKPIPGADPRSGR--WAGLSKTECGLH 234
Cdd:TIGR00424 251 vgSLVKWNPVANVEGKDVWNFLRTMDVPVNTLHAQGYVSIGCEPCTRPVLPGQHEREGRwwWEDAKAKECGLH 323
PLN02309 PLN02309
5'-adenylylsulfate reductase
 7-234 5.04e-41

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 145.70  E-value: 5.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442   7 STENELRELAERGAAELADASAEELLRWTDEHFGGNYVVA-SNMQDAVLVEMAAKVRPGVDVLFLDTGYHFAETIGTRDA 85
Cdd:PLN02309   77 PEEEGEVEDFEKLAKELENASPLEIMDKALEKFGNDIAIAfSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRLFDA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  86 VEAVYDVHVVNVTPErTVAEQDELLGKNLFA-RDPG--ECCRLRKVVPLTNALKGYSAWVTGIRRVEAP-TRANAPLISW 161
Cdd:PLN02309  157 VEKHYGIRIEYMFPD-AVEVQALVRNKGLFSfYEDGhqECCRVRKVRPLRRALKGLRAWITGQRKDQSPgTRAEVPVVQV 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442 162 DNAF--------GLVKINPIAAWTDEDMQNYIDANGILVNPLVYEGYPSIGCAPCTSKPIPGADPRSGRW---AGLSKtE 230
Cdd:PLN02309  236 DPVFegldggpgSLVKWNPLANVTGNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCTRPVLPGQHEREGRWwweDAKAK-E 314


                  ....
gi 2055117442 231 CGLH 234
Cdd:PLN02309  315 CGLH 318
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 30-208 9.78e-20

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: 83.59  E-value: 9.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  30 ELLRWTDEHFGGNYVVASNMQD-AVLVEMAAKV----RPGVDVLFLDTGYHFAETIGTRDAVEAVYDVHVVNVTPERT-- 102
Cdd:cd23947     3 ERIRKVFEEFDPVIVSFSGGKDsLVLLHLALEAlrrlRKDVYVVFIDTGIEFPETIDFVEKLAETLGLDVEAARPPLFle 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442 103 ------VAEQDELLGKNLFARDPGECCRLRKVVPLTNALK-----GYSAWVtGIRRVEAPTRANAPLI----SWDNAF-- 165
Cdd:cd23947    83 wltsnfQPQWDPIWDNPPPPRDYRWCCDELKLEPFTKWLKekkpeGVLLLV-GIRADESLNRAKRPRVyrkyGWRNSTlp 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2055117442 166 GLVKINPIAAWTDEDMQNYIDANGILVNPLVYEGYPSIGCAPC 208
Cdd:cd23947   162 GQIVAYPIKDWSVEDVWLYILRHGLPYNPLYDLGFDRGGCLVC 204
PRK08557 PRK08557
hypothetical protein; Provisional
 52-210 4.21e-13

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 67.86  E-value: 4.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  52 AVLVEMAAKVRPGVDVLFLDTGYHFAETIGTRDAVEAVYDVHVVNVTPERTvaeQDELLGKNLFARDPGECCRLRKVVPL 131
Cdd:PRK08557  195 SVSTLLAKEVIPDLEVIFIDTGLEYPETINYVKDFAKKYDLNLDTLDGDNF---WENLEKEGIPTKDNRWCNSACKLMPL 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442 132 TNALK---GYSAWVT--GIRRVEAPTRANaplISWDNAFGLV--KIN--PIAAWTDEDMQNYIDANGILVNPLVYEGYPS 202
Cdd:PRK08557  272 KEYLKkkyGNKKVLTidGSRKYESFTRAN---LDYERKSGFIdfQTNvfPILDWNSLDIWSYIYLNDILYNPLYDKGFER 348


                  ....*...
gi 2055117442 203 IGCAPCTS 210
Cdd:PRK08557  349 IGCYLCPS 356
PRK13794 PRK13794
hypothetical protein; Provisional
 65-210 6.43e-11

hypothetical protein; Provisional


Pssm-ID: 237509 [Multi-domain]  Cd Length: 479  Bit Score: 61.22  E-value: 6.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  65 VDVLFLDTGYHFAETIGTRDAVEAVYDVHVVNVTPE---RTVAEQdellgkNLFARDPGECCRLRKVVPL-----TNALK 136
Cdd:PRK13794  275 FPVLFNDTGLEFPETLENVEDVEKHYGLEIIRTKSEefwEKLEEY------GPPARDNRWCSEVCKLEPLgklidEKYEG 348

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2055117442 137 GYSAWVtGIRRVEAPTRANAPLIsWDNAFGLVKIN--PIAAWTDEDMQNYIDANGILVNPLVYEGYPSIGCAPCTS 210
Cdd:PRK13794  349 ECLSFV-GQRKYESFNRSKKPRI-WRNPYIKKQILaaPILHWTAMHVWIYLFREKAPYNKLYEQGFDRIGCFMCPA 422
PRK13795 PRK13795
hypothetical protein; Provisional
 52-210 4.10e-10

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 59.24  E-value: 4.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  52 AVLVeMAAKVRPGVDVLFLDTGYHFAETIGTRDAVEAVYDVHVVNVTPERTVAEQDELLGKNlfARDPGECCRLRKVVPL 131
Cdd:PRK13795  258 VVLD-LAREALKDFKAFFNNTGLEFPETVENVKEVAEEYGIELIEADAGDAFWRAVEKFGPP--ARDYRWCCKVCKLGPI 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442 132 TNALK-----GYSAWVtGIRRVEAPTRANAPLIsWDNAF--GLVKINPIAAWTDEDMQNYIDANGILVNPLVYEGYPSIG 204
Cdd:PRK13795  335 TRAIKenfpkGCLTFV-GQRKYESFSRAKSPRV-WRNPWvpNQIGASPIQDWTALEVWLYIFWRKLPYNPLYERGFDRIG 412


                  ....*.
gi 2055117442 205 CAPCTS 210
Cdd:PRK13795  413 CWLCPS 418
PRK05253 PRK05253
sulfate adenylyltransferase subunit CysD;
52-209 6.80e-09

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 235375  Cd Length: 301  Bit Score: 54.76  E-value: 6.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  52 AVLVEMAAK-VRPG---VDVLFLDTGYHFAETIGTRDAVEAVYD----VHVVnvtpERTVAEqdellGKNLFARDPGECC 123
Cdd:PRK05253   41 SVMLHLARKaFYPGklpFPLLHVDTGWKFPEMIEFRDRRAKELGleliVHSN----PEGIAR-----GINPFRHGSAKHT 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442 124 RLRKVVPLTNAL--KGYSAWVTGIRRVEAPTRANAPLISWDNAFG----------L-------------VKINPIAAWTD 178
Cdd:PRK05253  112 NAMKTEGLKQALekYGFDAAFGGARRDEEKSRAKERIFSFRDEFGqwdpknqrpeLwnlyngrinkgehIRVFPLSNWTE 191

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2055117442 179 EDMQNYIDANGILVNPLVY-----------------------EG---------YPSIGCAPCT 209
Cdd:PRK05253  192 LDIWQYIERENIPIVPLYFaherpvverdgmlimvddrmplrPGevveermvrFRTLGCYPCT 254
Sulfate_adenylyltransferase_2 cd23946
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ...
 25-197 8.50e-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: 50.96  E-value: 8.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  25 DASAEELLRWTDEHFGGNYVVASNMQD-AVLVEMAAKV----RPGVDVLFLDTGYHFAETIGTRDAVEAVYDVH-VVNVT 98
Cdd:cd23946     6 EAESIHIIREVAAEFSNPVMLYSIGKDsSVMLHLARKAfypgKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDlIVHVN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  99 PERTVAeqdellGKNLFARDPGECCRLRKVVPLTNALK--GYSAWVTGIRRVEAPTRANAPLIS---------------- 160
Cdd:cd23946    86 PDGVEA------GINPFTHGSAKHTDIMKTEGLKQALDkyGFDAAFGGARRDEEKSRAKERVYSfrdsnhrwdpknqrpe 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2055117442 161 -WDNAFGLVK------INPIAAWTDEDMQNYIDANGILVNPLVY 197
Cdd:cd23946   160 lWNQYNGRVKkgesirVFPLSNWTELDIWQYIYLENIPIVPLYF 203
PRK08576 PRK08576
hypothetical protein; Provisional
 123-210 2.24e-07

hypothetical protein; Provisional


Pssm-ID: 236300 [Multi-domain]  Cd Length: 438  Bit Score: 50.85  E-value: 2.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442 123 CRLRKVVPLTNALKGYS--AWVTGIRRVEAPTRANAPLISWDNA--FGLVKINPIAAWTDEDMQNYIDANGILVNPLVYE 198
Cdd:PRK08576  314 CTKLKVEALEEAIRELEdgLLVVGDRDGESARRRLRPPVVERKTnfGKILVVMPIKFWSGAMVQLYILMNGLELNPLYYK 393

                          90
                  ....*....|..
gi 2055117442 199 GYPSIGCAPCTS 210
Cdd:PRK08576  394 GFYRLGCYICPS 405
PRK12563 PRK12563
sulfate adenylyltransferase subunit CysD;
53-197 2.56e-05

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 237138  Cd Length: 312  Bit Score: 44.39  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442  53 VLVEMAAKV----RPGVDVLFLDTGYHFAETIGTRD--AVEAVYDVhVVNVTPERTVAeqdellGKNLFARDPGECCRLR 126
Cdd:PRK12563   52 VMLHLAMKAfrptRPPFPLLHVDTTWKFREMIDFRDrrAKELGLDL-VVHHNPDGIAR------GIVPFRHGSALHTDVA 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055117442 127 KVVPLTNALK--GYSAWVTGIRRVEAPTRANAPLISWDNAFGL-----------------------VKINPIAAWTDEDM 181
Cdd:PRK12563  125 KTQGLKQALDhhGFDAAIGGARRDEEKSRAKERIFSFRSAFHRwdpkaqrpelwslynarlrrgesLRVFPLSNWTELDV 204

                         170
                  ....*....|....*.
gi 2055117442 182 QNYIDANGILVNPLVY 197
Cdd:PRK12563  205 WQYIAREKIPLVPLYF 220
 
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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