|
Name |
Accession |
Description |
Interval |
E-value |
| PRK02090 |
PRK02090 |
phosphoadenylyl-sulfate reductase; |
11-252 |
6.37e-143 |
|
phosphoadenylyl-sulfate reductase;
Pssm-ID: 234997 Cd Length: 241 Bit Score: 399.98 E-value: 6.37e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 11 LSELLSLTKAEQSIRLAEINVELEMLSAQERVAWALQNLEGAHAVSSSFGIQAAVMLHLLSKQQADIPVILTDTGYLFPE 90
Cdd:PRK02090 1 LNALNALPKADLALDLAELNAELEGASAQERLAWALENFGGRLALVSSFGAEDAVLLHLVAQVDPDIPVIFLDTGYLFPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 91 TYQFIDELTKSLNLNLKVYRANESANWQEARYGKLWEQGIEGIEKYNKLNKVEPMRRALNELNVktWFSGLRREQSQSRA 170
Cdd:PRK02090 81 TYRFIDELTERLLLNLKVYRPDASAAEQEARYGGLWEQSVEDRDECCRIRKVEPLNRALAGLDA--WITGLRREQSGTRA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 171 GLPILSIQNGVFKFLPVVDWSNKDVHYYLKEHGLSYHPLWEQGYLSVGDTHTTQKWEPGMSEEETRFFG-LKRECGLHEE 249
Cdd:PRK02090 159 NLPVLEIDGGRFKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGRWWGgLKKECGLHEG 238
|
...
gi 762206547 250 DNE 252
Cdd:PRK02090 239 NLP 241
|
|
| PAPS_reductase |
TIGR02057 |
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ... |
26-247 |
2.58e-105 |
|
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: 304.45 E-value: 2.58e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 26 LAEINVELEMLSAQERVAWALQNLEGAHAVSSSFGIQAAVMLHLLSK-QQADIPVILTDTGYLFPETYQFIDELTKSLN- 103
Cdd:TIGR02057 1 LDELNEQLEKLTPQEIIAWSIVTFPHGLVQTSAFGIQALVTLHLLSSiSEPMIPVIFIDTLYHFPQTLTLKDELTKKYYq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 104 -LNLKVYRANESANWQEARYGKLWEQGieGIEKYNKLNKVEPMRRALNELNVKTWFSGLRREQSQSRAGLPILSI--QNG 180
Cdd:TIGR02057 81 tLNLYKYDGCESEADFEAKYGKLLWQK--DIEKYDYIAKVEPMQRALKELNASAWFTGRRRDQGSARANLPVIEIdeQNG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 762206547 181 VFKFLPVVDWSNKDVHYYLKEHGLSYHPLWEQGYLSVGDTHTTQKWEPGMSEEETRFFG-LKRECGLH 247
Cdd:TIGR02057 159 ILKVNPLIDWTFEQVYQYLDAHNVPYNPLLDQGYRSIGDYHSTRKVKEGEDERAGRWKGkLKTECGIH 226
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
25-246 |
6.49e-91 |
|
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: 268.25 E-value: 6.49e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 25 RLAEINVELEmLSAQERVAWALQNLEGAHAVSSSFGIQAAVMLHLLSKQQADIPVILTDTGYLFPETYQFIDELTKSLNL 104
Cdd:COG0175 9 LLEELNAELE-AEAIEILREAAAEFGGRVVVSSSGGKDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDRLAERLGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 105 NLKVYRANESANWQEARYG-KLWEQgieGIEKYNKLNKVEPMRRALNELNVKTWFSGLRREQSQSRAGLPILSI--QNGV 181
Cdd:COG0175 88 DLIVVRPEDAFAEQLAEFGpPLFYR---DPRWCCKIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVVEWdpVGGL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 762206547 182 FKFLPVVDWSNKDVHYYLKEHGLSYHPLWEQGYLSVGDTHTTQKWEPGMSEEETRFFGL---KRECGL 246
Cdd:COG0175 165 IKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWWDEekeRKECGL 232
|
|
| PAPS_reductase |
cd23945 |
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ... |
38-218 |
2.08e-85 |
|
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: 252.13 E-value: 2.08e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 38 AQERVAWALQNLEGAHAVSSSFGIQAAVMLHLLSKQQADIPVILTDTGYLFPETYQFIDELTKSLNLNLKVYRANESANW 117
Cdd:cd23945 1 PLEILLWAAEEFGPKLVFATSFGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYGLNIEVYFPEGTEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 118 QEARYGKLWEQGIEGIEKYNKLNKVEPMRRALNELNVKTWFSGLRREQSQSRAGLPI--LSIQNGVFKFLPVVDWSNKDV 195
Cdd:cd23945 81 EEALEGGLNEFYLEDEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIveVDEEGGLVKINPLADWTWEDV 160
|
170 180
....*....|....*....|...
gi 762206547 196 HYYLKEHGLSYHPLWEQGYLSVG 218
Cdd:cd23945 161 WAYIREHDLPYNPLHDQGYPSIG 183
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
53-225 |
2.54e-68 |
|
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: 208.69 E-value: 2.54e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 53 HAVSSSFGIQAAVMLHLLSKQQADIPVILTDTGYLFPETYQFIDELTKSLNLNLKVYRANESANWQEARYGKLWEQGieg 132
Cdd:pfam01507 2 LVVSFSGGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSSLY--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 133 iEKYNKLNKVEPMRRALNELNVKTWFSGLRREQSQSRAGLPILSIQNG---VFKFLPVVDWSNKDVHYYLKEHGLSYHPL 209
Cdd:pfam01507 79 -RRCCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDGDfpkVIKVFPLLNWTETDVWQYILANNVPYNPL 157
|
170
....*....|....*.
gi 762206547 210 WEQGYLSVGDTHTTQK 225
Cdd:pfam01507 158 YDQGYRSIGCYPCTGP 173
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK02090 |
PRK02090 |
phosphoadenylyl-sulfate reductase; |
11-252 |
6.37e-143 |
|
phosphoadenylyl-sulfate reductase;
Pssm-ID: 234997 Cd Length: 241 Bit Score: 399.98 E-value: 6.37e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 11 LSELLSLTKAEQSIRLAEINVELEMLSAQERVAWALQNLEGAHAVSSSFGIQAAVMLHLLSKQQADIPVILTDTGYLFPE 90
Cdd:PRK02090 1 LNALNALPKADLALDLAELNAELEGASAQERLAWALENFGGRLALVSSFGAEDAVLLHLVAQVDPDIPVIFLDTGYLFPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 91 TYQFIDELTKSLNLNLKVYRANESANWQEARYGKLWEQGIEGIEKYNKLNKVEPMRRALNELNVktWFSGLRREQSQSRA 170
Cdd:PRK02090 81 TYRFIDELTERLLLNLKVYRPDASAAEQEARYGGLWEQSVEDRDECCRIRKVEPLNRALAGLDA--WITGLRREQSGTRA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 171 GLPILSIQNGVFKFLPVVDWSNKDVHYYLKEHGLSYHPLWEQGYLSVGDTHTTQKWEPGMSEEETRFFG-LKRECGLHEE 249
Cdd:PRK02090 159 NLPVLEIDGGRFKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGRWWGgLKKECGLHEG 238
|
...
gi 762206547 250 DNE 252
Cdd:PRK02090 239 NLP 241
|
|
| PAPS_reductase |
TIGR02057 |
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ... |
26-247 |
2.58e-105 |
|
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: 304.45 E-value: 2.58e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 26 LAEINVELEMLSAQERVAWALQNLEGAHAVSSSFGIQAAVMLHLLSK-QQADIPVILTDTGYLFPETYQFIDELTKSLN- 103
Cdd:TIGR02057 1 LDELNEQLEKLTPQEIIAWSIVTFPHGLVQTSAFGIQALVTLHLLSSiSEPMIPVIFIDTLYHFPQTLTLKDELTKKYYq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 104 -LNLKVYRANESANWQEARYGKLWEQGieGIEKYNKLNKVEPMRRALNELNVKTWFSGLRREQSQSRAGLPILSI--QNG 180
Cdd:TIGR02057 81 tLNLYKYDGCESEADFEAKYGKLLWQK--DIEKYDYIAKVEPMQRALKELNASAWFTGRRRDQGSARANLPVIEIdeQNG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 762206547 181 VFKFLPVVDWSNKDVHYYLKEHGLSYHPLWEQGYLSVGDTHTTQKWEPGMSEEETRFFG-LKRECGLH 247
Cdd:TIGR02057 159 ILKVNPLIDWTFEQVYQYLDAHNVPYNPLLDQGYRSIGDYHSTRKVKEGEDERAGRWKGkLKTECGIH 226
|
|
| cysH |
TIGR00434 |
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ... |
38-248 |
4.98e-101 |
|
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: 293.23 E-value: 4.98e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 38 AQERVAWALQNLEGAHAVSSSFGIQAAVMLHLLSKQQADIPVILTDTGYLFPETYQFIDELTKSLNLNLKVYRANESANW 117
Cdd:TIGR00434 1 AQEIIAWAYVTFGGHLVYSTSFGIQGAVLLDLVSKISPDIPVIFLDTGYHFPETYELIDELTERYPLNIKVYKPDLSLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 118 QEARYG-KLWEQgieGIEKYNKLNKVEPMRRALNELNVKTWFSGLRREQSQSRAGLPILSIQ--NGVFKFLPVVDWSNKD 194
Cdd:TIGR00434 81 QAAKYGdKLWEQ---DPNKYDYLRKVEPMHRALKELHASAWFTGLRRDQGPSRANLSILNIDekFGILKVLPLIDWTWKD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 762206547 195 VHYYLKEHGLSYHPLWEQGYLSVGDTHTTQKWEPGMSEEETRFFG-LKRECGLHE 248
Cdd:TIGR00434 158 VYQYIDAHNLPYNPLHDQGYPSIGDYHSTRPVKEGEDERAGRWKGkAKTECGLHE 212
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
25-246 |
6.49e-91 |
|
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: 268.25 E-value: 6.49e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 25 RLAEINVELEmLSAQERVAWALQNLEGAHAVSSSFGIQAAVMLHLLSKQQADIPVILTDTGYLFPETYQFIDELTKSLNL 104
Cdd:COG0175 9 LLEELNAELE-AEAIEILREAAAEFGGRVVVSSSGGKDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDRLAERLGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 105 NLKVYRANESANWQEARYG-KLWEQgieGIEKYNKLNKVEPMRRALNELNVKTWFSGLRREQSQSRAGLPILSI--QNGV 181
Cdd:COG0175 88 DLIVVRPEDAFAEQLAEFGpPLFYR---DPRWCCKIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVVEWdpVGGL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 762206547 182 FKFLPVVDWSNKDVHYYLKEHGLSYHPLWEQGYLSVGDTHTTQKWEPGMSEEETRFFGL---KRECGL 246
Cdd:COG0175 165 IKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWWDEekeRKECGL 232
|
|
| PAPS_reductase |
cd23945 |
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ... |
38-218 |
2.08e-85 |
|
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: 252.13 E-value: 2.08e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 38 AQERVAWALQNLEGAHAVSSSFGIQAAVMLHLLSKQQADIPVILTDTGYLFPETYQFIDELTKSLNLNLKVYRANESANW 117
Cdd:cd23945 1 PLEILLWAAEEFGPKLVFATSFGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYGLNIEVYFPEGTEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 118 QEARYGKLWEQGIEGIEKYNKLNKVEPMRRALNELNVKTWFSGLRREQSQSRAGLPI--LSIQNGVFKFLPVVDWSNKDV 195
Cdd:cd23945 81 EEALEGGLNEFYLEDEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIveVDEEGGLVKINPLADWTWEDV 160
|
170 180
....*....|....*....|...
gi 762206547 196 HYYLKEHGLSYHPLWEQGYLSVG 218
Cdd:cd23945 161 WAYIREHDLPYNPLHDQGYPSIG 183
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
53-225 |
2.54e-68 |
|
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: 208.69 E-value: 2.54e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 53 HAVSSSFGIQAAVMLHLLSKQQADIPVILTDTGYLFPETYQFIDELTKSLNLNLKVYRANESANWQEARYGKLWEQGieg 132
Cdd:pfam01507 2 LVVSFSGGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSSLY--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 133 iEKYNKLNKVEPMRRALNELNVKTWFSGLRREQSQSRAGLPILSIQNG---VFKFLPVVDWSNKDVHYYLKEHGLSYHPL 209
Cdd:pfam01507 79 -RRCCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDGDfpkVIKVFPLLNWTETDVWQYILANNVPYNPL 157
|
170
....*....|....*.
gi 762206547 210 WEQGYLSVGDTHTTQK 225
Cdd:pfam01507 158 YDQGYRSIGCYPCTGP 173
|
|
| PAPS_reductase-like_YbdN |
cd23947 |
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ... |
38-214 |
5.75e-19 |
|
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: 82.05 E-value: 5.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 38 AQERVAWALQNLEgAHAVSSSFGIQAAVMLHL----LSKQQADIPVILTDTGYLFPETYQFIDELTKSLNLNLKVYRANE 113
Cdd:cd23947 1 ALERIRKVFEEFD-PVIVSFSGGKDSLVLLHLaleaLRRLRKDVYVVFIDTGIEFPETIDFVEKLAETLGLDVEAARPPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 114 SANWqEARYGKLWEQGIEGIE----KYNKLN---KVEPMRRALNEL---NVKTWFsGLRREQSQSRAGLPIL-------- 175
Cdd:cd23947 80 FLEW-LTSNFQPQWDPIWDNPppprDYRWCCdelKLEPFTKWLKEKkpeGVLLLV-GIRADESLNRAKRPRVyrkygwrn 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 762206547 176 SIQNGVFKFLPVVDWSNKDVHYYLKEHGLSYHPLWEQGY 214
Cdd:cd23947 158 STLPGQIVAYPIKDWSVEDVWLYILRHGLPYNPLYDLGF 196
|
|
| APS_reduc |
TIGR00424 |
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ... |
26-256 |
8.36e-19 |
|
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: 85.07 E-value: 8.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 26 LAEINVELEMLSAQ--ERVAWALQN---LEGAHAVSSSFGIQAAVML------------HLLSKQqadIPVILTDTGYLF 88
Cdd:TIGR00424 76 TVAPEVEEKVVEVEdfEKLAKKLENaspLEIMDKALEKFGNDIAIAFsgaedvalieyaHLTGRP---FRVFSLDTGRLN 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 89 PETYQFIDELTKSLNLNLKvYRANESANWQE-ARYGKLWEQGIEGIEKYNKLNKVEPMRRALNELnvKTWFSGLRREQSQ 167
Cdd:TIGR00424 153 PETYRFFDAVEKQYGIRIE-YMFPDAVEVQAlVRSKGLFSFYEDGHQECCRVRKVRPLRRALKGL--KAWITGQRKDQSP 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 168 -SRAGLPILSIQ-------NGV---FKFLPVVDWSNKDVHYYLKEHGLSYHPLWEQGYLSVGDTHTTQKWEPGMSEEETR 236
Cdd:TIGR00424 230 gTRSEIPVVQVDpvfegldGGVgslVKWNPVANVEGKDVWNFLRTMDVPVNTLHAQGYVSIGCEPCTRPVLPGQHEREGR 309
|
250 260
....*....|....*....|....*.
gi 762206547 237 FF---GLKRECGLHE---EDNEQDGS 256
Cdd:TIGR00424 310 WWwedAKAKECGLHKgniKEETLDGA 335
|
|
| PLN02309 |
PLN02309 |
5'-adenylylsulfate reductase |
83-257 |
5.99e-17 |
|
5'-adenylylsulfate reductase
Pssm-ID: 215175 [Multi-domain] Cd Length: 457 Bit Score: 79.83 E-value: 5.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 83 DTGYLFPETYQFIDELTKSLNLNLKvYRANESANWQE-ARYGKLWEQGIEGIEKYNKLNKVEPMRRALNELnvKTWFSGL 161
Cdd:PLN02309 142 DTGRLNPETYRLFDAVEKHYGIRIE-YMFPDAVEVQAlVRNKGLFSFYEDGHQECCRVRKVRPLRRALKGL--RAWITGQ 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 162 RREQSQ-SRAGLPILSIqNGVF-----------KFLPVVDWSNKDVHYYLKEHGLSYHPLWEQGYLSVGDTHTTQKWEPG 229
Cdd:PLN02309 219 RKDQSPgTRAEVPVVQV-DPVFegldggpgslvKWNPLANVTGNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCTRPVLPG 297
|
170 180 190
....*....|....*....|....*....|.
gi 762206547 230 MSEEETRFF---GLKRECGLHEEDNEQDGSG 257
Cdd:PLN02309 298 QHEREGRWWwedAKAKECGLHKGNIKEEDNG 328
|
|
| PRK13794 |
PRK13794 |
hypothetical protein; Provisional |
64-218 |
2.37e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 237509 [Multi-domain] Cd Length: 479 Bit Score: 63.15 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 64 AVMLHLLSKQQADIPVILTDTGYLFPETYQFIDELTKSLNLNLKVYRANESanWQearygKLWEQGIEGIEKY--NKLNK 141
Cdd:PRK13794 262 ATLLLALKALGINFPVLFNDTGLEFPETLENVEDVEKHYGLEIIRTKSEEF--WE-----KLEEYGPPARDNRwcSEVCK 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 142 VEPMRRALNElnvkTW------FSGLRREQSQSRAGLP-----------ILSiqngvfkfLPVVDWSNKDVHYYLKEHGL 204
Cdd:PRK13794 335 LEPLGKLIDE----KYegeclsFVGQRKYESFNRSKKPriwrnpyikkqILA--------APILHWTAMHVWIYLFREKA 402
|
170
....*....|....
gi 762206547 205 SYHPLWEQGYLSVG 218
Cdd:PRK13794 403 PYNKLYEQGFDRIG 416
|
|
| Sulfate_adenylyltransferase_2 |
cd23946 |
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ... |
58-179 |
3.26e-11 |
|
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: 60.97 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 58 SFGIQAAVMLHLLSKQ----QADIPVILTDTGYLFPETYQFIDELTKSLNLNLKVYRanesaNWqearygKLWEQGI--- 130
Cdd:cd23946 28 SIGKDSSVMLHLARKAfypgKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDLIVHV-----NP------DGVEAGInpf 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 762206547 131 -EGIEKYNKLNKVEPMRRALNELNVKTWFSGLRREQSQSRAGLPILSIQN 179
Cdd:cd23946 97 tHGSAKHTDIMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRD 146
|
|
| PRK13795 |
PRK13795 |
hypothetical protein; Provisional |
54-218 |
9.47e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 61.55 E-value: 9.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 54 AVSSSFGIQAAVMLHLLSKQQADIPVILTDTGYLFPETYQFIDELTKSLNLNLKVYRANESanwqearygkLWEQgiegI 133
Cdd:PRK13795 247 SVSFSGGKDSLVVLDLAREALKDFKAFFNNTGLEFPETVENVKEVAEEYGIELIEADAGDA----------FWRA----V 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 134 EKYN----------KLNKVEPMRRALNELNVKTW--FSGLRREQSQSRAGLPILSiQN-------GVFkflPVVDWSNKD 194
Cdd:PRK13795 313 EKFGppardyrwccKVCKLGPITRAIKENFPKGCltFVGQRKYESFSRAKSPRVW-RNpwvpnqiGAS---PIQDWTALE 388
|
170 180
....*....|....*....|....
gi 762206547 195 VHYYLKEHGLSYHPLWEQGYLSVG 218
Cdd:PRK13795 389 VWLYIFWRKLPYNPLYERGFDRIG 412
|
|
| PRK08557 |
PRK08557 |
hypothetical protein; Provisional |
55-218 |
3.51e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 181465 [Multi-domain] Cd Length: 417 Bit Score: 59.38 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 55 VSSSFGIQAAVMLHLLSKQQADIPVILTDTGYLFPETYQFIDELTKSLNLNLKVYRANESanWQEarygkLWEQGIEGIE 134
Cdd:PRK08557 186 ASFSGGKDSSVSTLLAKEVIPDLEVIFIDTGLEYPETINYVKDFAKKYDLNLDTLDGDNF--WEN-----LEKEGIPTKD 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 135 KY--NKLNKVEPMRRALNELN----VKTwFSGLRREQSQSRAGLP------ILSIQNGVFkflPVVDWSNKDVHYYLKEH 202
Cdd:PRK08557 259 NRwcNSACKLMPLKEYLKKKYgnkkVLT-IDGSRKYESFTRANLDyerksgFIDFQTNVF---PILDWNSLDIWSYIYLN 334
|
170
....*....|....*.
gi 762206547 203 GLSYHPLWEQGYLSVG 218
Cdd:PRK08557 335 DILYNPLYDKGFERIG 350
|
|
| FAD_synthase |
cd23948 |
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ... |
41-225 |
1.15e-07 |
|
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: 50.21 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 41 RVAWALQNLEGA------HAVSSSF--GIQAAVMLHLL--------SKQQADIPVILTDTGYLFPETYQFIDELTKSLNL 104
Cdd:cd23948 1 KVKSALEVIEEAldkygpEEIAISFngGKDCTVLLHLLraalkrkyPSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 105 NLKVYRanesanwqearygklweqgiegiekynklnkvEPMRRALNEL-----NVKTWFSGLRR---------EQSQSRA 170
Cdd:cd23948 81 DLITID--------------------------------GPMKEGLEELlkehpIIKAVFMGTRRtdphgenlkPFSPTDP 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 762206547 171 GLPilsiqngvfKFL---PVVDWSNKDVHYYLKEHGLSYHPLWEQGYLSVGDTHTTQK 225
Cdd:cd23948 129 GWP---------QFMrvnPILDWSYHDVWEFLRTLNLPYCSLYDQGYTSLGSVDNTLP 177
|
|
| PRK08576 |
PRK08576 |
hypothetical protein; Provisional |
25-218 |
2.84e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 236300 [Multi-domain] Cd Length: 438 Bit Score: 50.85 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 25 RLAEINVELemLSAQERVAWA-LQNLEGAHA-VSSSFGIQAAVMLHLLSKQQADIPVILTDTGYLFPETYQFIDELTKSL 102
Cdd:PRK08576 209 KLIEANREV--LEAFEKASIKfLRKFEEWTViVPWSGGKDSTAALLLAKKAFGDVTAVYVDTGYEMPLTDEYVEKVAEKL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 103 NLNLkvYRANESANWQearygklweqgiegIEKY----------NKLnKVEPMRRALNELNVKTWFSGLRREQSQSRAGL 172
Cdd:PRK08576 287 GVDL--IRAGVDVPMP--------------IEKYgmpthsnrwcTKL-KVEALEEAIRELEDGLLVVGDRDGESARRRLR 349
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 762206547 173 PILSIQNGVFKFLPVVD----WSNKDVHYYLKEHGLSYHPLWEQGYLSVG 218
Cdd:PRK08576 350 PPVVERKTNFGKILVVMpikfWSGAMVQLYILMNGLELNPLYYKGFYRLG 399
|
|
| PRK12563 |
PRK12563 |
sulfate adenylyltransferase subunit CysD; |
58-178 |
4.03e-07 |
|
sulfate adenylyltransferase subunit CysD;
Pssm-ID: 237138 Cd Length: 312 Bit Score: 50.17 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 58 SFGIQAAVMLHLLSKQ----QADIPVILTDTGYLFPETYQFIDELTKSLNLNLKVYRANESAnwqearygklwEQGI--- 130
Cdd:PRK12563 45 SIGKDSVVMLHLAMKAfrptRPPFPLLHVDTTWKFREMIDFRDRRAKELGLDLVVHHNPDGI-----------ARGIvpf 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 762206547 131 -EGIEKYNKLNKVEPMRRALNELNVKTWFSGLRREQSQSRAGLPILSIQ 178
Cdd:PRK12563 114 rHGSALHTDVAKTQGLKQALDHHGFDAAIGGARRDEEKSRAKERIFSFR 162
|
|
| PRK05253 |
PRK05253 |
sulfate adenylyltransferase subunit CysD; |
64-170 |
4.67e-07 |
|
sulfate adenylyltransferase subunit CysD;
Pssm-ID: 235375 Cd Length: 301 Bit Score: 49.75 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762206547 64 AVMLHLLSKqqA------DIPVILTDTGYLFPETYQFIDELTKSLNLNLKVYRanesaNWQEARYGKLWEQGieGIEKYN 137
Cdd:PRK05253 41 SVMLHLARK--AfypgklPFPLLHVDTGWKFPEMIEFRDRRAKELGLELIVHS-----NPEGIARGINPFRH--GSAKHT 111
|
90 100 110
....*....|....*....|....*....|...
gi 762206547 138 KLNKVEPMRRALNELNVKTWFSGLRREQSQSRA 170
Cdd:PRK05253 112 NAMKTEGLKQALEKYGFDAAFGGARRDEEKSRA 144
|
|
| AANH-like |
cd01986 |
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ... |
53-98 |
3.15e-04 |
|
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: 38.20 E-value: 3.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 762206547 53 HAVSSSFGIQAAVMLHLLSKQQADIPVILT--DTGYLFPETYQFIDEL 98
Cdd:cd01986 1 VVVGYSGGKDSSVALHLASRLGRKAEVAVVhiDHGIGFKEEAESVASI 48
|
|
| |
