|
Name |
Accession |
Description |
Interval |
E-value |
| cysH |
TIGR00434 |
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ... |
29-238 |
4.81e-108 |
|
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: 310.18 E-value: 4.81e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 29 AYEILEWAYRTYGDSIVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFPkLRIEMKKPDLTLE 108
Cdd:TIGR00434 1 AQEIIAWAYVTFGGHLVYSTSFGIQGAVLLDLVSKISPDIPVIFLDTGYHFPETYELIDELTERYP-LNIKVYKPDLSLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 109 EQADKYNPALWKNNPNQCCYIRKIKPLEEVLGG--AVAWVSGLRRDQSPTRANTNFINKDERFKSVKVCPLIYWTEDEVW 186
Cdd:TIGR00434 80 EQAAKYGDKLWEQDPNKYDYLRKVEPMHRALKElhASAWFTGLRRDQGPSRANLSILNIDEKFGILKVLPLIDWTWKDVY 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 123661322 187 DYIKKHDLPYNALHDQHYPSIGCIPCTAPVFDSEDSRAGRWSNFDKTECGLH 238
Cdd:TIGR00434 160 QYIDAHNLPYNPLHDQGYPSIGDYHSTRPVKEGEDERAGRWKGKAKTECGLH 211
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
29-237 |
2.35e-103 |
|
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: 299.07 E-value: 2.35e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 29 AYEILEWAYRTYGDSIVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFpKLRIEMKKPDLTLE 108
Cdd:COG0175 21 AIEILREAAAEFGGRVVVSSSGGKDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDRLAERL-GLDLIVVRPEDAFA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 109 EQADKYNPALWKNNPNQCCYIRKIKPLEEVLGG--AVAWVSGLRRDQSPTRANTNFINKDERFKSVKVCPLIYWTEDEVW 186
Cdd:COG0175 100 EQLAEFGPPLFYRDPRWCCKIRKVEPLKRALAGydFDAWITGLRRDESPTRAKEPVVEWDPVGGLIKVNPLADWTELDVW 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 123661322 187 DYIKKHDLPYNALHDQHYPSIGCIPCTAPVFDSEDSRAGRWSNFDK--TECGL 237
Cdd:COG0175 180 AYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWWDEEKerKECGL 232
|
|
| PRK02090 |
PRK02090 |
phosphoadenylyl-sulfate reductase; |
25-243 |
5.40e-100 |
|
phosphoadenylyl-sulfate reductase;
Pssm-ID: 234997 Cd Length: 241 Bit Score: 290.97 E-value: 5.40e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 25 ATKGAYEILEWAYRTYGDSIVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFpKLRIEMKKPD 104
Cdd:PRK02090 24 EGASAQERLAWALENFGGRLALVSSFGAEDAVLLHLVAQVDPDIPVIFLDTGYLFPETYRFIDELTERL-LLNLKVYRPD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 105 LTLEEQADKYNPaLWKN---NPNQCCYIRKIKPLEEVLGGAVAWVSGLRRDQSPTRANTNFINKDErfKSVKVCPLIYWT 181
Cdd:PRK02090 103 ASAAEQEARYGG-LWEQsveDRDECCRIRKVEPLNRALAGLDAWITGLRREQSGTRANLPVLEIDG--GRFKINPLADWT 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123661322 182 EDEVWDYIKKHDLPYNALHDQHYPSIGCIPCTAPVFDSEDSRAGRWSNFDKTECGLHVADKP 243
Cdd:PRK02090 180 NEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGRWWGGLKKECGLHEGNLP 241
|
|
| PAPS_reductase |
cd23945 |
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ... |
31-208 |
2.04e-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: 229.02 E-value: 2.04e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 31 EILEWAYRTYGDSIVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFPkLRIEMKKPDLTLEEQ 110
Cdd:cd23945 3 EILLWAAEEFGPKLVFATSFGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYG-LNIEVYFPEGTEAEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 111 --ADKYNPALWK--NNPNQCCYIRKIKPLEEVLGGAVAWVSGLRRDQSPTRANTNFINKDERFKSVKVCPLIYWTEDEVW 186
Cdd:cd23945 82 eaLEGGLNEFYLedEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIVEVDEEGGLVKINPLADWTWEDVW 161
|
170 180
....*....|....*....|..
gi 123661322 187 DYIKKHDLPYNALHDQHYPSIG 208
Cdd:cd23945 162 AYIREHDLPYNPLHDQGYPSIG 183
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
44-215 |
2.37e-66 |
|
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: 202.91 E-value: 2.37e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 44 IVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFPkLRIEMKKPDLTLEEQADKYNPALWKNNp 123
Cdd:pfam01507 2 LVVSFSGGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYG-LNLKVYLPEDSFAEGINPEGIPSSLYR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 124 nQCCYIRKIKPLEEVLG--GAVAWVSGLRRDQSPTRANTNFINKDERF-KSVKVCPLIYWTEDEVWDYIKKHDLPYNALH 200
Cdd:pfam01507 80 -RCCRLRKVEPLKRALKelGFDAWFTGLRRDESPSRAKLPIVSIDGDFpKVIKVFPLLNWTETDVWQYILANNVPYNPLY 158
|
170
....*....|....*
gi 123661322 201 DQHYPSIGCIPCTAP 215
Cdd:pfam01507 159 DQGYRSIGCYPCTGP 173
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| cysH |
TIGR00434 |
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ... |
29-238 |
4.81e-108 |
|
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: 310.18 E-value: 4.81e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 29 AYEILEWAYRTYGDSIVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFPkLRIEMKKPDLTLE 108
Cdd:TIGR00434 1 AQEIIAWAYVTFGGHLVYSTSFGIQGAVLLDLVSKISPDIPVIFLDTGYHFPETYELIDELTERYP-LNIKVYKPDLSLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 109 EQADKYNPALWKNNPNQCCYIRKIKPLEEVLGG--AVAWVSGLRRDQSPTRANTNFINKDERFKSVKVCPLIYWTEDEVW 186
Cdd:TIGR00434 80 EQAAKYGDKLWEQDPNKYDYLRKVEPMHRALKElhASAWFTGLRRDQGPSRANLSILNIDEKFGILKVLPLIDWTWKDVY 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 123661322 187 DYIKKHDLPYNALHDQHYPSIGCIPCTAPVFDSEDSRAGRWSNFDKTECGLH 238
Cdd:TIGR00434 160 QYIDAHNLPYNPLHDQGYPSIGDYHSTRPVKEGEDERAGRWKGKAKTECGLH 211
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
29-237 |
2.35e-103 |
|
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: 299.07 E-value: 2.35e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 29 AYEILEWAYRTYGDSIVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFpKLRIEMKKPDLTLE 108
Cdd:COG0175 21 AIEILREAAAEFGGRVVVSSSGGKDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDRLAERL-GLDLIVVRPEDAFA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 109 EQADKYNPALWKNNPNQCCYIRKIKPLEEVLGG--AVAWVSGLRRDQSPTRANTNFINKDERFKSVKVCPLIYWTEDEVW 186
Cdd:COG0175 100 EQLAEFGPPLFYRDPRWCCKIRKVEPLKRALAGydFDAWITGLRRDESPTRAKEPVVEWDPVGGLIKVNPLADWTELDVW 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 123661322 187 DYIKKHDLPYNALHDQHYPSIGCIPCTAPVFDSEDSRAGRWSNFDK--TECGL 237
Cdd:COG0175 180 AYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWWDEEKerKECGL 232
|
|
| PRK02090 |
PRK02090 |
phosphoadenylyl-sulfate reductase; |
25-243 |
5.40e-100 |
|
phosphoadenylyl-sulfate reductase;
Pssm-ID: 234997 Cd Length: 241 Bit Score: 290.97 E-value: 5.40e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 25 ATKGAYEILEWAYRTYGDSIVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFpKLRIEMKKPD 104
Cdd:PRK02090 24 EGASAQERLAWALENFGGRLALVSSFGAEDAVLLHLVAQVDPDIPVIFLDTGYLFPETYRFIDELTERL-LLNLKVYRPD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 105 LTLEEQADKYNPaLWKN---NPNQCCYIRKIKPLEEVLGGAVAWVSGLRRDQSPTRANTNFINKDErfKSVKVCPLIYWT 181
Cdd:PRK02090 103 ASAAEQEARYGG-LWEQsveDRDECCRIRKVEPLNRALAGLDAWITGLRREQSGTRANLPVLEIDG--GRFKINPLADWT 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123661322 182 EDEVWDYIKKHDLPYNALHDQHYPSIGCIPCTAPVFDSEDSRAGRWSNFDKTECGLHVADKP 243
Cdd:PRK02090 180 NEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGRWWGGLKKECGLHEGNLP 241
|
|
| APS_reductase |
TIGR02055 |
thioredoxin-dependent adenylylsulfate APS reductase; This model describes recently identified ... |
50-237 |
2.08e-97 |
|
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: 282.42 E-value: 2.08e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 50 FGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFPKLRIEMKKPDLTLEEQADKYNPALW-KNNPNQCCY 128
Cdd:TIGR02055 1 LGAEDVVLVDLAAKVRPDVKVFFLDTGRLFKETYETIDQVRERYDILIDVLSPPPLTVEEQVKEYGLNLFyRSVPHECCG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 129 IRKIKPLEEVLGGAVAWVSGLRRDQSPTRANTNFINKDERFKSVKVCPLIYWTEDEVWDYIKKHDLPYNALHDQHYPSIG 208
Cdd:TIGR02055 81 IRKVEPLKRALAGVSAWITGLRRDQSPTRAQAPFLEIDEAFGLVKINPLADWTSEDVWEYIADNELPYNPLHDRGYPSIG 160
|
170 180 190
....*....|....*....|....*....|.
gi 123661322 209 CIPCTAPVFDSEDSRAGRW--SNFDKTECGL 237
Cdd:TIGR02055 161 CEPCTRPVAPGEDPRAGRWwwEEAAKKECGL 191
|
|
| PAPS_reductase |
cd23945 |
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ... |
31-208 |
2.04e-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: 229.02 E-value: 2.04e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 31 EILEWAYRTYGDSIVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFPkLRIEMKKPDLTLEEQ 110
Cdd:cd23945 3 EILLWAAEEFGPKLVFATSFGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYG-LNIEVYFPEGTEAEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 111 --ADKYNPALWK--NNPNQCCYIRKIKPLEEVLGGAVAWVSGLRRDQSPTRANTNFINKDERFKSVKVCPLIYWTEDEVW 186
Cdd:cd23945 82 eaLEGGLNEFYLedEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIVEVDEEGGLVKINPLADWTWEDVW 161
|
170 180
....*....|....*....|..
gi 123661322 187 DYIKKHDLPYNALHDQHYPSIG 208
Cdd:cd23945 162 AYIREHDLPYNPLHDQGYPSIG 183
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
44-215 |
2.37e-66 |
|
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: 202.91 E-value: 2.37e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 44 IVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFPkLRIEMKKPDLTLEEQADKYNPALWKNNp 123
Cdd:pfam01507 2 LVVSFSGGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYG-LNLKVYLPEDSFAEGINPEGIPSSLYR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 124 nQCCYIRKIKPLEEVLG--GAVAWVSGLRRDQSPTRANTNFINKDERF-KSVKVCPLIYWTEDEVWDYIKKHDLPYNALH 200
Cdd:pfam01507 80 -RCCRLRKVEPLKRALKelGFDAWFTGLRRDESPSRAKLPIVSIDGDFpKVIKVFPLLNWTETDVWQYILANNVPYNPLY 158
|
170
....*....|....*
gi 123661322 201 DQHYPSIGCIPCTAP 215
Cdd:pfam01507 159 DQGYRSIGCYPCTGP 173
|
|
| PAPS_reductase |
TIGR02057 |
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ... |
29-238 |
1.65e-61 |
|
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: 192.74 E-value: 1.65e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 29 AYEILEWAYRTYGDSIVYSCSFGAESMVLIDLIYQI-KPDAQIVFLDTDLHFQETYDLIDRVKEHFpKLRIEMKKPD--L 105
Cdd:TIGR02057 13 PQEIIAWSIVTFPHGLVQTSAFGIQALVTLHLLSSIsEPMIPVIFIDTLYHFPQTLTLKDELTKKY-YQTLNLYKYDgcE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 106 TLEEQADKYNPALWKNNPNQCCYIRKIKPLEEVLG--GAVAWVSGLRRDQSPTRANTNFINKDERFKSVKVCPLIYWTED 183
Cdd:TIGR02057 92 SEADFEAKYGKLLWQKDIEKYDYIAKVEPMQRALKelNASAWFTGRRRDQGSARANLPVIEIDEQNGILKVNPLIDWTFE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 123661322 184 EVWDYIKKHDLPYNALHDQHYPSIGCIPCTAPVFDSEDSRAGRWSNFDKTECGLH 238
Cdd:TIGR02057 172 QVYQYLDAHNVPYNPLLDQGYRSIGDYHSTRKVKEGEDERAGRWKGKLKTECGIH 226
|
|
| APS_reduc |
TIGR00424 |
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ... |
31-238 |
1.97e-40 |
|
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: 144.39 E-value: 1.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 31 EILEWAYRTYGDSIVYSCSfGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFpKLRIEMKKPDlTLEEQ 110
Cdd:TIGR00424 105 EIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRFFDAVEKQY-GIRIEYMFPD-AVEVQ 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 111 ADKYNPAL---WKNNPNQCCYIRKIKPLEEVLGGAVAWVSGLRRDQSP-TRANTNFINKDERFKSVK--VCPLIYWTE-- 182
Cdd:TIGR00424 182 ALVRSKGLfsfYEDGHQECCRVRKVRPLRRALKGLKAWITGQRKDQSPgTRSEIPVVQVDPVFEGLDggVGSLVKWNPva 261
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123661322 183 ----DEVWDYIKKHDLPYNALHDQHYPSIGCIPCTAPVFDSEDSRAGR--WSNFDKTECGLH 238
Cdd:TIGR00424 262 nvegKDVWNFLRTMDVPVNTLHAQGYVSIGCEPCTRPVLPGQHEREGRwwWEDAKAKECGLH 323
|
|
| PLN02309 |
PLN02309 |
5'-adenylylsulfate reductase |
31-238 |
3.39e-40 |
|
5'-adenylylsulfate reductase
Pssm-ID: 215175 [Multi-domain] Cd Length: 457 Bit Score: 143.78 E-value: 3.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 31 EILEWAYRTYGDSIVYSCSfGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFpKLRIEMKKPDlTLEEQ 110
Cdd:PLN02309 100 EIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRLFDAVEKHY-GIRIEYMFPD-AVEVQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 111 A---DKYNPALWKNNPNQCCYIRKIKPLEEVLGGAVAWVSGLRRDQSP-TRANTNFINKDERFKS--------VKVCPLI 178
Cdd:PLN02309 177 AlvrNKGLFSFYEDGHQECCRVRKVRPLRRALKGLRAWITGQRKDQSPgTRAEVPVVQVDPVFEGldggpgslVKWNPLA 256
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123661322 179 YWTEDEVWDYIKKHDLPYNALHDQHYPSIGCIPCTAPVFDSEDSRAGRWSNFDKT--ECGLH 238
Cdd:PLN02309 257 NVTGNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCTRPVLPGQHEREGRWWWEDAKakECGLH 318
|
|
| PAPS_reductase-like_YbdN |
cd23947 |
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ... |
29-212 |
1.31e-23 |
|
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: 94.38 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 29 AYEILEWAYRTyGDSIVYSCSFGAESMVLIDL----IYQIKPDAQIVFLDTDLHFQETYDLIDRVKEhFPKLRIEMKKPD 104
Cdd:cd23947 1 ALERIRKVFEE-FDPVIVSFSGGKDSLVLLHLaleaLRRLRKDVYVVFIDTGIEFPETIDFVEKLAE-TLGLDVEAARPP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 105 LTLE---EQADKYNPALWKNNP-----NQCCYIRKIKPLEEVL----GGAVAWVSGLRRDQSPTRANTNFINKDERFKS- 171
Cdd:cd23947 79 LFLEwltSNFQPQWDPIWDNPPpprdyRWCCDELKLEPFTKWLkekkPEGVLLLVGIRADESLNRAKRPRVYRKYGWRNs 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 123661322 172 -----VKVCPLIYWTEDEVWDYIKKHDLPYNALHDQHYPSIGCIPC 212
Cdd:cd23947 159 tlpgqIVAYPIKDWSVEDVWLYILRHGLPYNPLYDLGFDRGGCLVC 204
|
|
| PRK13794 |
PRK13794 |
hypothetical protein; Provisional |
70-214 |
3.29e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 237509 [Multi-domain] Cd Length: 479 Bit Score: 71.24 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 70 IVFLDTDLHFQETYDLIDRVKEHF--PKLRIEMKKPDLTLEEQADKYNPALWknnpnqCCYIRKIKPLEEVL-----GGA 142
Cdd:PRK13794 277 VLFNDTGLEFPETLENVEDVEKHYglEIIRTKSEEFWEKLEEYGPPARDNRW------CSEVCKLEPLGKLIdekyeGEC 350
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123661322 143 VAWVsGLRRDQSPTRANTNFINKDERF-KSVKVCPLIYWTEDEVWDYIKKHDLPYNALHDQHYPSIGCIPCTA 214
Cdd:PRK13794 351 LSFV-GQRKYESFNRSKKPRIWRNPYIkKQILAAPILHWTAMHVWIYLFREKAPYNKLYEQGFDRIGCFMCPA 422
|
|
| PRK13795 |
PRK13795 |
hypothetical protein; Provisional |
40-214 |
1.72e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 66.17 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 40 YGDSIVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFpKLRIEMKKPDLTLEEQADKYNP--- 116
Cdd:PRK13795 242 YNLPVSVSFSGGKDSLVVLDLAREALKDFKAFFNNTGLEFPETVENVKEVAEEY-GIELIEADAGDAFWRAVEKFGPpar 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 117 -ALWknnpnqCCYIRKIKP----LEEVLGGAVAWVSGLRRDQSPTRANTNFINKDErF--KSVKVCPLIYWTEDEVWDYI 189
Cdd:PRK13795 321 dYRW------CCKVCKLGPitraIKENFPKGCLTFVGQRKYESFSRAKSPRVWRNP-WvpNQIGASPIQDWTALEVWLYI 393
|
170 180
....*....|....*....|....*
gi 123661322 190 KKHDLPYNALHDQHYPSIGCIPCTA 214
Cdd:PRK13795 394 FWRKLPYNPLYERGFDRIGCWLCPS 418
|
|
| PRK08557 |
PRK08557 |
hypothetical protein; Provisional |
27-214 |
9.18e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 181465 [Multi-domain] Cd Length: 417 Bit Score: 64.00 E-value: 9.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 27 KGAYEILEWAYRTY---GDSIVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETydlIDRVKEHfpklrieMKKP 103
Cdd:PRK08557 164 ENSLSILKDYIEKYknkGYAINASFSGGKDSSVSTLLAKEVIPDLEVIFIDTGLEYPET---INYVKDF-------AKKY 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 104 DLTLEE-QADKYNPALWKNN-PNQ----CCYIRKIKPLEEVL-----GGAVAWVSGLRRDQSPTRANTNFiNKDERF--K 170
Cdd:PRK08557 234 DLNLDTlDGDNFWENLEKEGiPTKdnrwCNSACKLMPLKEYLkkkygNKKVLTIDGSRKYESFTRANLDY-ERKSGFidF 312
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 123661322 171 SVKVCPLIYWTEDEVWDYIKKHDLPYNALHDQHYPSIGCIPCTA 214
Cdd:PRK08557 313 QTNVFPILDWNSLDIWSYIYLNDILYNPLYDKGFERIGCYLCPS 356
|
|
| FAD_synthase |
cd23948 |
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ... |
174-208 |
1.98e-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: 49.44 E-value: 1.98e-07
10 20 30
....*....|....*....|....*....|....*
gi 123661322 174 VCPLIYWTEDEVWDYIKKHDLPYNALHDQHYPSIG 208
Cdd:cd23948 136 VNPILDWSYHDVWEFLRTLNLPYCSLYDQGYTSLG 170
|
|
| Sulfate_adenylyltransferase_2 |
cd23946 |
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ... |
32-200 |
4.41e-07 |
|
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: 49.03 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 32 ILEWAYRTYGDSIVYScSFGAESMVLIDL----IYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFPKLRIEMKKPDLTl 107
Cdd:cd23946 12 IIREVAAEFSNPVMLY-SIGKDSSVMLHLarkaFYPGKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDLIVHVNPDGV- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 108 eeqADKYNPalWKNNPNQCCYIRKIKPLEEVLG--GAVAWVSGLRRDQSPTRANT---NFINKDERF------------- 169
Cdd:cd23946 90 ---EAGINP--FTHGSAKHTDIMKTEGLKQALDkyGFDAAFGGARRDEEKSRAKErvySFRDSNHRWdpknqrpelwnqy 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 123661322 170 -------KSVKVCPLIYWTEDEVWDYIKKHDLPYNALH 200
Cdd:cd23946 165 ngrvkkgESIRVFPLSNWTELDIWQYIYLENIPIVPLY 202
|
|
| PRK12563 |
PRK12563 |
sulfate adenylyltransferase subunit CysD; |
49-216 |
9.55e-05 |
|
sulfate adenylyltransferase subunit CysD;
Pssm-ID: 237138 Cd Length: 312 Bit Score: 42.85 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 49 SFGAESMVLIDL----IYQIKPDAQIVFLDTDLHFQETYDLIDRVkehfpklrieMKKPDLTL------EEQADKYNP-- 116
Cdd:PRK12563 45 SIGKDSVVMLHLamkaFRPTRPPFPLLHVDTTWKFREMIDFRDRR----------AKELGLDLvvhhnpDGIARGIVPfr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 117 ---ALWKNnpnqccyIRKIKPLEEVLG--GAVAWVSGLRRDQSPTRANTN-FINKDE----------------------R 168
Cdd:PRK12563 115 hgsALHTD-------VAKTQGLKQALDhhGFDAAIGGARRDEEKSRAKERiFSFRSAfhrwdpkaqrpelwslynarlrR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 169 FKSVKVCPLIYWTEDEVWDYIKKHDLPYNALH------------------DQHYP---------------SIGCIPCTAP 215
Cdd:PRK12563 188 GESLRVFPLSNWTELDVWQYIAREKIPLVPLYfakrrpvverdgllimvdDERTPlrpgetpqqrkvrfrTLGCYPLTGA 267
|
.
gi 123661322 216 V 216
Cdd:PRK12563 268 V 268
|
|
| PRK08576 |
PRK08576 |
hypothetical protein; Provisional |
67-214 |
2.99e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 236300 [Multi-domain] Cd Length: 438 Bit Score: 41.60 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 67 DAQIVFLDTDLHFQETYDLIDRVKEhfpKLRIEMKKPDLTLEEQADKYN-PalwkNNPNQCCYIRKIKPLEEVLG----G 141
Cdd:PRK08576 260 DVTAVYVDTGYEMPLTDEYVEKVAE---KLGVDLIRAGVDVPMPIEKYGmP----THSNRWCTKLKVEALEEAIReledG 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 142 AVawVSGLRRDQSPTR--------ANTNFINKDErfksvkVCPLIYWTEDEVWDYIKKHDLPYNALHDQHYPSIGCIPCT 213
Cdd:PRK08576 333 LL--VVGDRDGESARRrlrppvveRKTNFGKILV------VMPIKFWSGAMVQLYILMNGLELNPLYYKGFYRLGCYICP 404
|
.
gi 123661322 214 A 214
Cdd:PRK08576 405 S 405
|
|
|