|
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
|
|
|