|
Name |
Accession |
Description |
Interval |
E-value |
| PRK02090 |
PRK02090 |
phosphoadenylyl-sulfate reductase; |
6-244 |
7.12e-141 |
|
phosphoadenylyl-sulfate reductase;
Pssm-ID: 234997 Cd Length: 241 Bit Score: 394.20 E-value: 7.12e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 6 LNALNELPKVDRILALAETNAELEKLDAEGRIAWALDNLPGEYVLSSSFGIQAAVSLHLVNQIRPDIPVILTDTGYLFPE 85
Cdd:PRK02090 1 LNALNALPKADLALDLAELNAELEGASAQERLAWALENFGGRLALVSSFGAEDAVLLHLVAQVDPDIPVIFLDTGYLFPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 86 TYRFIDELTDKLKLNLKVYRATESAAWQEARYGKLWEQGVEGIEKYNDINKVEPMNRALKELNAqtWFAGLRREQSGSRA 165
Cdd:PRK02090 81 TYRFIDELTERLLLNLKVYRPDASAAEQEARYGGLWEQSVEDRDECCRIRKVEPLNRALAGLDA--WITGLRREQSGTRA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 166 NLPVLAIQRGVFKVLPIIDWDNRTIYQYLQKHGLKYHPLWDEGYLSVGDTHTTRKWESGMSEEETRFFG-LKRECGLHEG 244
Cdd:PRK02090 159 NLPVLEIDGGRFKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGRWWGgLKKECGLHEG 238
|
|
| PAPS_reductase |
TIGR02057 |
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ... |
21-242 |
1.69e-127 |
|
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: 359.92 E-value: 1.69e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 21 LAETNAELEKLDAEGRIAWALDNLPGEYVLSSSFGIQAAVSLHLVNQIR-PDIPVILTDTGYLFPETYRFIDELTDKLK- 98
Cdd:TIGR02057 1 LDELNEQLEKLTPQEIIAWSIVTFPHGLVQTSAFGIQALVTLHLLSSISePMIPVIFIDTLYHFPQTLTLKDELTKKYYq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 99 -LNLKVYRATESAAWQEARYGKLWEQGveGIEKYNDINKVEPMNRALKELNAQTWFAGLRREQSGSRANLPVLAI--QRG 175
Cdd:TIGR02057 81 tLNLYKYDGCESEADFEAKYGKLLWQK--DIEKYDYIAKVEPMQRALKELNASAWFTGRRRDQGSARANLPVIEIdeQNG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445961981 176 VFKVLPIIDWDNRTIYQYLQKHGLKYHPLWDEGYLSVGDTHTTRKWESGMSEEETRFFG-LKRECGLH 242
Cdd:TIGR02057 159 ILKVNPLIDWTFEQVYQYLDAHNVPYNPLLDQGYRSIGDYHSTRKVKEGEDERAGRWKGkLKTECGIH 226
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
15-241 |
1.08e-89 |
|
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: 264.40 E-value: 1.08e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 15 VDRILALAETNAELEKlDAEGRIAWALDNLPGEYVLSSSFGIQAAVSLHLVNQIRPDIPVILTDTGYLFPETYRFIDELT 94
Cdd:COG0175 4 ATLDDLLEELNAELEA-EAIEILREAAAEFGGRVVVSSSGGKDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 95 DKLKLNLKVYRATESAAWQEARYG-KLWEQgveGIEKYNDINKVEPMNRALKELNAQTWFAGLRREQSGSRANLPVLAI- 172
Cdd:COG0175 83 ERLGLDLIVVRPEDAFAEQLAEFGpPLFYR---DPRWCCKIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVVEWd 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445961981 173 -QRGVFKVLPIIDWDNRTIYQYLQKHGLKYHPLWDEGYLSVGDTHTTRKWESGMSEEETRFFGL---KRECGL 241
Cdd:COG0175 160 pVGGLIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWWDEekeRKECGL 232
|
|
| PAPS_reductase |
cd23945 |
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ... |
33-213 |
1.47e-81 |
|
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: 242.12 E-value: 1.47e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 33 AEGRIAWALDNLPGEYVLSSSFGIQAAVSLHLVNQIRPDIPVILTDTGYLFPETYRFIDELTDKLKLNLKVYRATESAAW 112
Cdd:cd23945 1 PLEILLWAAEEFGPKLVFATSFGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYGLNIEVYFPEGTEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 113 QEARYGKLWEQGVEGIEKYNDINKVEPMNRALKELNAQTWFAGLRREQSGSRANLPV--LAIQRGVFKVLPIIDWDNRTI 190
Cdd:cd23945 81 EEALEGGLNEFYLEDEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIveVDEEGGLVKINPLADWTWEDV 160
|
170 180
....*....|....*....|...
gi 445961981 191 YQYLQKHGLKYHPLWDEGYLSVG 213
Cdd:cd23945 161 WAYIREHDLPYNPLHDQGYPSIG 183
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
47-220 |
1.18e-73 |
|
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: 221.40 E-value: 1.18e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 47 EYVLSSSFGIQAAVSLHLVNQIRPDIPVILTDTGYLFPETYRFIDELTDKLKLNLKVYRATESAAWQEARYGKLWEQGve 126
Cdd:pfam01507 1 ELVVSFSGGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSSLY-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 127 giEKYNDINKVEPMNRALKELNAQTWFAGLRREQSGSRANLPVLAIQRG---VFKVLPIIDWDNRTIYQYLQKHGLKYHP 203
Cdd:pfam01507 79 --RRCCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDGDfpkVIKVFPLLNWTETDVWQYILANNVPYNP 156
|
170
....*....|....*..
gi 445961981 204 LWDEGYLSVGDTHTTRK 220
Cdd:pfam01507 157 LYDQGYRSIGCYPCTGP 173
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK02090 |
PRK02090 |
phosphoadenylyl-sulfate reductase; |
6-244 |
7.12e-141 |
|
phosphoadenylyl-sulfate reductase;
Pssm-ID: 234997 Cd Length: 241 Bit Score: 394.20 E-value: 7.12e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 6 LNALNELPKVDRILALAETNAELEKLDAEGRIAWALDNLPGEYVLSSSFGIQAAVSLHLVNQIRPDIPVILTDTGYLFPE 85
Cdd:PRK02090 1 LNALNALPKADLALDLAELNAELEGASAQERLAWALENFGGRLALVSSFGAEDAVLLHLVAQVDPDIPVIFLDTGYLFPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 86 TYRFIDELTDKLKLNLKVYRATESAAWQEARYGKLWEQGVEGIEKYNDINKVEPMNRALKELNAqtWFAGLRREQSGSRA 165
Cdd:PRK02090 81 TYRFIDELTERLLLNLKVYRPDASAAEQEARYGGLWEQSVEDRDECCRIRKVEPLNRALAGLDA--WITGLRREQSGTRA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 166 NLPVLAIQRGVFKVLPIIDWDNRTIYQYLQKHGLKYHPLWDEGYLSVGDTHTTRKWESGMSEEETRFFG-LKRECGLHEG 244
Cdd:PRK02090 159 NLPVLEIDGGRFKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGRWWGgLKKECGLHEG 238
|
|
| PAPS_reductase |
TIGR02057 |
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ... |
21-242 |
1.69e-127 |
|
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: 359.92 E-value: 1.69e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 21 LAETNAELEKLDAEGRIAWALDNLPGEYVLSSSFGIQAAVSLHLVNQIR-PDIPVILTDTGYLFPETYRFIDELTDKLK- 98
Cdd:TIGR02057 1 LDELNEQLEKLTPQEIIAWSIVTFPHGLVQTSAFGIQALVTLHLLSSISePMIPVIFIDTLYHFPQTLTLKDELTKKYYq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 99 -LNLKVYRATESAAWQEARYGKLWEQGveGIEKYNDINKVEPMNRALKELNAQTWFAGLRREQSGSRANLPVLAI--QRG 175
Cdd:TIGR02057 81 tLNLYKYDGCESEADFEAKYGKLLWQK--DIEKYDYIAKVEPMQRALKELNASAWFTGRRRDQGSARANLPVIEIdeQNG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445961981 176 VFKVLPIIDWDNRTIYQYLQKHGLKYHPLWDEGYLSVGDTHTTRKWESGMSEEETRFFG-LKRECGLH 242
Cdd:TIGR02057 159 ILKVNPLIDWTFEQVYQYLDAHNVPYNPLLDQGYRSIGDYHSTRKVKEGEDERAGRWKGkLKTECGIH 226
|
|
| cysH |
TIGR00434 |
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ... |
33-243 |
1.35e-119 |
|
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: 339.46 E-value: 1.35e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 33 AEGRIAWALDNLPGEYVLSSSFGIQAAVSLHLVNQIRPDIPVILTDTGYLFPETYRFIDELTDKLKLNLKVYRATESAAW 112
Cdd:TIGR00434 1 AQEIIAWAYVTFGGHLVYSTSFGIQGAVLLDLVSKISPDIPVIFLDTGYHFPETYELIDELTERYPLNIKVYKPDLSLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 113 QEARYG-KLWEQgveGIEKYNDINKVEPMNRALKELNAQTWFAGLRREQSGSRANLPVLAIQR--GVFKVLPIIDWDNRT 189
Cdd:TIGR00434 81 QAAKYGdKLWEQ---DPNKYDYLRKVEPMHRALKELHASAWFTGLRRDQGPSRANLSILNIDEkfGILKVLPLIDWTWKD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 445961981 190 IYQYLQKHGLKYHPLWDEGYLSVGDTHTTRKWESGMSEEETRFFG-LKRECGLHE 243
Cdd:TIGR00434 158 VYQYIDAHNLPYNPLHDQGYPSIGDYHSTRPVKEGEDERAGRWKGkAKTECGLHE 212
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
15-241 |
1.08e-89 |
|
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: 264.40 E-value: 1.08e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 15 VDRILALAETNAELEKlDAEGRIAWALDNLPGEYVLSSSFGIQAAVSLHLVNQIRPDIPVILTDTGYLFPETYRFIDELT 94
Cdd:COG0175 4 ATLDDLLEELNAELEA-EAIEILREAAAEFGGRVVVSSSGGKDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 95 DKLKLNLKVYRATESAAWQEARYG-KLWEQgveGIEKYNDINKVEPMNRALKELNAQTWFAGLRREQSGSRANLPVLAI- 172
Cdd:COG0175 83 ERLGLDLIVVRPEDAFAEQLAEFGpPLFYR---DPRWCCKIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVVEWd 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445961981 173 -QRGVFKVLPIIDWDNRTIYQYLQKHGLKYHPLWDEGYLSVGDTHTTRKWESGMSEEETRFFGL---KRECGL 241
Cdd:COG0175 160 pVGGLIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWWDEekeRKECGL 232
|
|
| PAPS_reductase |
cd23945 |
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ... |
33-213 |
1.47e-81 |
|
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: 242.12 E-value: 1.47e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 33 AEGRIAWALDNLPGEYVLSSSFGIQAAVSLHLVNQIRPDIPVILTDTGYLFPETYRFIDELTDKLKLNLKVYRATESAAW 112
Cdd:cd23945 1 PLEILLWAAEEFGPKLVFATSFGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYGLNIEVYFPEGTEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 113 QEARYGKLWEQGVEGIEKYNDINKVEPMNRALKELNAQTWFAGLRREQSGSRANLPV--LAIQRGVFKVLPIIDWDNRTI 190
Cdd:cd23945 81 EEALEGGLNEFYLEDEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIveVDEEGGLVKINPLADWTWEDV 160
|
170 180
....*....|....*....|...
gi 445961981 191 YQYLQKHGLKYHPLWDEGYLSVG 213
Cdd:cd23945 161 WAYIREHDLPYNPLHDQGYPSIG 183
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
47-220 |
1.18e-73 |
|
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: 221.40 E-value: 1.18e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 47 EYVLSSSFGIQAAVSLHLVNQIRPDIPVILTDTGYLFPETYRFIDELTDKLKLNLKVYRATESAAWQEARYGKLWEQGve 126
Cdd:pfam01507 1 ELVVSFSGGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSSLY-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 127 giEKYNDINKVEPMNRALKELNAQTWFAGLRREQSGSRANLPVLAIQRG---VFKVLPIIDWDNRTIYQYLQKHGLKYHP 203
Cdd:pfam01507 79 --RRCCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDGDfpkVIKVFPLLNWTETDVWQYILANNVPYNP 156
|
170
....*....|....*..
gi 445961981 204 LWDEGYLSVGDTHTTRK 220
Cdd:pfam01507 157 LYDQGYRSIGCYPCTGP 173
|
|
| APS_reduc |
TIGR00424 |
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ... |
3-244 |
1.96e-17 |
|
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: 80.83 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 3 KLDLNALNELPKV-DRILALAETNAELEKLDAEGRI------AWALDNLPGEYVLSSS---FGIQAAVSL---------- 62
Cdd:TIGR00424 53 RLSVKPLNAEPKRnESIVPSAATTVAPEVEEKVVEVedfeklAKKLENASPLEIMDKAlekFGNDIAIAFsgaedvalie 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 63 --HLVNqiRPdIPVILTDTGYLFPETYRFIDELTDKLKLNLKvYRATESAAWQE-ARYGKLWEQGVEGIEKYNDINKVEP 139
Cdd:TIGR00424 133 yaHLTG--RP-FRVFSLDTGRLNPETYRFFDAVEKQYGIRIE-YMFPDAVEVQAlVRSKGLFSFYEDGHQECCRVRKVRP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 140 MNRALKELNAqtWFAGLRREQS-GSRANLPVLAIQRgVFKVL-----------PIIDWDNRTIYQYLQKHGLKYHPLWDE 207
Cdd:TIGR00424 209 LRRALKGLKA--WITGQRKDQSpGTRSEIPVVQVDP-VFEGLdggvgslvkwnPVANVEGKDVWNFLRTMDVPVNTLHAQ 285
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 445961981 208 GYLSVGDTHTTRKWESGMSEEETRFF---GLKRECGLHEG 244
Cdd:TIGR00424 286 GYVSIGCEPCTRPVLPGQHEREGRWWwedAKAKECGLHKG 325
|
|
| PAPS_reductase-like_YbdN |
cd23947 |
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ... |
60-209 |
3.48e-17 |
|
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: 77.05 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 60 VSLHLVN----QIRPDIPVILTDTGYLFPETYRFIDELTDKLKLNLKVYRATESAAWQEARYGKLWEQGVEGIEKY---- 131
Cdd:cd23947 27 VLLHLALealrRLRKDVYVVFIDTGIEFPETIDFVEKLAETLGLDVEAARPPLFLEWLTSNFQPQWDPIWDNPPPPrdyr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 132 --NDINKVEPMNRALKELNAQTW--FAGLRREQSGSRANLPVLAIQR--------GVFKVLPIIDWDNRTIYQYLQKHGL 199
Cdd:cd23947 107 wcCDELKLEPFTKWLKEKKPEGVllLVGIRADESLNRAKRPRVYRKYgwrnstlpGQIVAYPIKDWSVEDVWLYILRHGL 186
|
170
....*....|
gi 445961981 200 KYHPLWDEGY 209
Cdd:cd23947 187 PYNPLYDLGF 196
|
|
| PLN02309 |
PLN02309 |
5'-adenylylsulfate reductase |
78-244 |
5.40e-16 |
|
5'-adenylylsulfate reductase
Pssm-ID: 215175 [Multi-domain] Cd Length: 457 Bit Score: 76.37 E-value: 5.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 78 DTGYLFPETYRFIDELTDKLKLNLKvYRATESAAWQE-ARYGKLWEQGVEGIEKYNDINKVEPMNRALKELNAqtWFAGL 156
Cdd:PLN02309 142 DTGRLNPETYRLFDAVEKHYGIRIE-YMFPDAVEVQAlVRNKGLFSFYEDGHQECCRVRKVRPLRRALKGLRA--WITGQ 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 157 RREQS-GSRANLPVLAIQRgVF-----------KVLPIIDWDNRTIYQYLQKHGLKYHPLWDEGYLSVGDTHTTRKWESG 224
Cdd:PLN02309 219 RKDQSpGTRAEVPVVQVDP-VFegldggpgslvKWNPLANVTGNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCTRPVLPG 297
|
170 180
....*....|....*....|...
gi 445961981 225 MSEEETRFF---GLKRECGLHEG 244
Cdd:PLN02309 298 QHEREGRWWwedAKAKECGLHKG 320
|
|
| PRK08557 |
PRK08557 |
hypothetical protein; Provisional |
48-213 |
2.09e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 181465 [Multi-domain] Cd Length: 417 Bit Score: 71.71 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 48 YVLSSSF--GIQAAVSLHLVNQIRPDIPVILTDTGYLFPETYRFIDELTDKLKLNLKVYRATEsaAWQEarygkLWEQGV 125
Cdd:PRK08557 182 YAINASFsgGKDSSVSTLLAKEVIPDLEVIFIDTGLEYPETINYVKDFAKKYDLNLDTLDGDN--FWEN-----LEKEGI 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 126 EGIEKY--NDINKVEPMNRALKELNAQT---WFAGLRREQSGSRANLP------VLAIQRGVFkvlPIIDWDNRTIYQYL 194
Cdd:PRK08557 255 PTKDNRwcNSACKLMPLKEYLKKKYGNKkvlTIDGSRKYESFTRANLDyerksgFIDFQTNVF---PILDWNSLDIWSYI 331
|
170
....*....|....*....
gi 445961981 195 QKHGLKYHPLWDEGYLSVG 213
Cdd:PRK08557 332 YLNDILYNPLYDKGFERIG 350
|
|
| PRK13794 |
PRK13794 |
hypothetical protein; Provisional |
71-213 |
8.12e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 237509 [Multi-domain] Cd Length: 479 Bit Score: 58.14 E-value: 8.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 71 DIPVILTDTGYLFPETYRFIDELTDklKLNLKVYRATESAAWQearygKLWEQGVEGIEKY--NDINKVEPmnraLKELN 148
Cdd:PRK13794 274 NFPVLFNDTGLEFPETLENVEDVEK--HYGLEIIRTKSEEFWE-----KLEEYGPPARDNRwcSEVCKLEP----LGKLI 342
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445961981 149 AQTW------FAGLRREQSGSRANLPVLAIQRGVFK---VLPIIDWDNRTIYQYLQKHGLKYHPLWDEGYLSVG 213
Cdd:PRK13794 343 DEKYegeclsFVGQRKYESFNRSKKPRIWRNPYIKKqilAAPILHWTAMHVWIYLFREKAPYNKLYEQGFDRIG 416
|
|
| PRK13795 |
PRK13795 |
hypothetical protein; Provisional |
43-213 |
1.03e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 58.08 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 43 NLPgeYVLSSSFGIQAAVSLHLVNQIRPDIPVILTDTGYLFPETYRFIDELTDKLKLNLKVYRATESaawqearygkLWE 122
Cdd:PRK13795 243 NLP--VSVSFSGGKDSLVVLDLAREALKDFKAFFNNTGLEFPETVENVKEVAEEYGIELIEADAGDA----------FWR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 123 QgvegIEKYN----------DINKVEPMNRALKELNAQTW--FAGLRREQSGSRANL------PVLAIQRGVFkvlPIID 184
Cdd:PRK13795 311 A----VEKFGppardyrwccKVCKLGPITRAIKENFPKGCltFVGQRKYESFSRAKSprvwrnPWVPNQIGAS---PIQD 383
|
170 180
....*....|....*....|....*....
gi 445961981 185 WDNRTIYQYLQKHGLKYHPLWDEGYLSVG 213
Cdd:PRK13795 384 WTALEVWLYIFWRKLPYNPLYERGFDRIG 412
|
|
| Sulfate_adenylyltransferase_2 |
cd23946 |
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ... |
53-205 |
1.22e-09 |
|
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: 56.35 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 53 SFGIQAAVSLHLVNQI----RPDIPVILTDTGYLFPETYRFIDELTDKLKLNLKVYRATESAawqearygklwEQGV--- 125
Cdd:cd23946 28 SIGKDSSVMLHLARKAfypgKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDLIVHVNPDGV-----------EAGInpf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 126 -EGIEKYNDINKVEPMNRALKELNAQTWFAGLRREQSGSRANLPVLAI-----------QR--------GVFK------V 179
Cdd:cd23946 97 tHGSAKHTDIMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFrdsnhrwdpknQRpelwnqynGRVKkgesirV 176
|
170 180
....*....|....*....|....*.
gi 445961981 180 LPIIDWDNRTIYQYLQKHGLKYHPLW 205
Cdd:cd23946 177 FPLSNWTELDIWQYIYLENIPIVPLY 202
|
|
| PRK12563 |
PRK12563 |
sulfate adenylyltransferase subunit CysD; |
49-205 |
2.96e-07 |
|
sulfate adenylyltransferase subunit CysD;
Pssm-ID: 237138 Cd Length: 312 Bit Score: 50.17 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 49 VLSSSFGIQAAVSLHLVNQI----RPDIPVILTDTGYLFPETYRFIDELTDKLKLNLKVYRATESAAwqearygklweQG 124
Cdd:PRK12563 41 VMLYSIGKDSVVMLHLAMKAfrptRPPFPLLHVDTTWKFREMIDFRDRRAKELGLDLVVHHNPDGIA-----------RG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 125 V----EGIEKYNDINKVEPMNRALKELNAQTWFAGLRREQSGSRANLPVLAI-----------QR--------------G 175
Cdd:PRK12563 110 IvpfrHGSALHTDVAKTQGLKQALDHHGFDAAIGGARRDEEKSRAKERIFSFrsafhrwdpkaQRpelwslynarlrrgE 189
|
170 180 190
....*....|....*....|....*....|
gi 445961981 176 VFKVLPIIDWDNRTIYQYLQKHGLKYHPLW 205
Cdd:PRK12563 190 SLRVFPLSNWTELDVWQYIAREKIPLVPLY 219
|
|
| FAD_synthase |
cd23948 |
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ... |
179-220 |
7.57e-06 |
|
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: 45.20 E-value: 7.57e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 445961981 179 VLPIIDWDNRTIYQYLQKHGLKYHPLWDEGYLSVGDTHTTRK 220
Cdd:cd23948 136 VNPILDWSYHDVWEFLRTLNLPYCSLYDQGYTSLGSVDNTLP 177
|
|
| PRK05253 |
PRK05253 |
sulfate adenylyltransferase subunit CysD; |
69-165 |
1.75e-05 |
|
sulfate adenylyltransferase subunit CysD;
Pssm-ID: 235375 Cd Length: 301 Bit Score: 44.74 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 69 RPDIPVILTDTGYLFPETYRFIDELTDKLKLNLKVYRATESAAwqearYGKLWEQGveGIEKYNDINKVEPMNRALKELN 148
Cdd:PRK05253 55 KLPFPLLHVDTGWKFPEMIEFRDRRAKELGLELIVHSNPEGIA-----RGINPFRH--GSAKHTNAMKTEGLKQALEKYG 127
|
90
....*....|....*..
gi 445961981 149 AQTWFAGLRREQSGSRA 165
Cdd:PRK05253 128 FDAAFGGARRDEEKSRA 144
|
|
| PRK08576 |
PRK08576 |
hypothetical protein; Provisional |
71-222 |
5.74e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 236300 [Multi-domain] Cd Length: 438 Bit Score: 43.53 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445961981 71 DIPVILTDTGYLFPETYRFIDELTDKLKLNLkvYRATESAAWQEARYGKLWEQgvegiEKYNDINKVEPMNRALKELNAQ 150
Cdd:PRK08576 260 DVTAVYVDTGYEMPLTDEYVEKVAEKLGVDL--IRAGVDVPMPIEKYGMPTHS-----NRWCTKLKVEALEEAIRELEDG 332
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445961981 151 TWFAGLRREQSGSRANLPVL----AIQRGVFKVLPIIDWDNRTIYQYLQKHGLKYHPLWDEGYLSVGDT--HTTRKWE 222
Cdd:PRK08576 333 LLVVGDRDGESARRRLRPPVverkTNFGKILVVMPIKFWSGAMVQLYILMNGLELNPLYYKGFYRLGCYicPSLRSWE 410
|
|
| AANH-like |
cd01986 |
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ... |
49-93 |
7.02e-03 |
|
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.
Pssm-ID: 467490 [Multi-domain] Cd Length: 74 Bit Score: 34.35 E-value: 7.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 445961981 49 VLSSSFGIQAAVSLHLVNQIRPDIPVILT--DTGYLFPETYRFIDEL 93
Cdd:cd01986 2 VVGYSGGKDSSVALHLASRLGRKAEVAVVhiDHGIGFKEEAESVASI 48
|
|
| |
