|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05253 |
PRK05253 |
sulfate adenylyltransferase subunit CysD; |
1-302 |
0e+00 |
|
sulfate adenylyltransferase subunit CysD;
Pssm-ID: 235375 Cd Length: 301 Bit Score: 653.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 1 MDQKRLTHLRQLEAESIHIIREVAAEFSNPVMMYSIGKDSSVMLHLARKAFYPGTLPFPLLHVDTGWKFSEMYEFRDRTA 80
Cdd:PRK05253 1 MDQYRLTHLDQLEAESIHILREVAAEFENPVMLYSIGKDSSVMLHLARKAFYPGKLPFPLLHVDTGWKFPEMIEFRDRRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 81 KAYGCELLVHKNPEGVAMGINPFVHGSAKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERIYSFRDRFHRWDP 160
Cdd:PRK05253 81 KELGLELIVHSNPEGIARGINPFRHGSAKHTNAMKTEGLKQALEKYGFDAAFGGARRDEEKSRAKERIFSFRDEFGQWDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 161 KNQRPELWHNYNGQINKGESIRVFPLSNWTEQDIWQYIWLENIDIVPLYLAAERPVLERDGMLMMIdDDRIDLQPGEVIK 240
Cdd:PRK05253 161 KNQRPELWNLYNGRINKGEHIRVFPLSNWTELDIWQYIERENIPIVPLYFAHERPVVERDGMLIMV-DDRMPLRPGEVVE 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1518978224 241 KRMVRFRTLGCWPLTGAVESNAQTLPEIIEEMLVSTTSERQGRVIDRDQAGSMELKKRQGYF 302
Cdd:PRK05253 240 ERMVRFRTLGCYPCTGAVESEAATLEEIIAEMLVTRTSERGGRAIDDDQEASMEKRKREGYF 301
|
|
| CysD |
TIGR02039 |
sulfate adenylyltransferase, small subunit; Metabolic assimilation of sulfur from inorganic ... |
9-302 |
0e+00 |
|
sulfate adenylyltransferase, small subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 131094 Cd Length: 294 Bit Score: 603.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 9 LRQLEAESIHIIREVAAEFSNPVMMYSIGKDSSVMLHLARKAFYPGTLPFPLLHVDTGWKFSEMYEFRDRTAKAYGCELL 88
Cdd:TIGR02039 1 LRALESEAIHIIREVAAEFERPVMLYSIGKDSSVLLHLARKAFYPGPLPFPLLHVDTGWKFREMIAFRDHMVAKYGLRLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 89 VHKNPEGVAMGINPFVHGSAKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERIYSFRDRFHRWDPKNQRPELW 168
Cdd:TIGR02039 81 VHSNEEGIADGINPFTEGSALHTDIMKTEALRQALDKNQFDAAFGGARRDEEKSRAKERIFSFRNAFHQWDPKKQRPELW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 169 HNYNGQINKGESIRVFPLSNWTEQDIWQYIWLENIDIVPLYLAAERPVLERDGMLMMIDDDRIDLQPGEVIKKRMVRFRT 248
Cdd:TIGR02039 161 NLYNGRISKGESVRVFPLSNWTELDIWRYIAAENIPIVPLYFAAKRPVVQRDGMLIMVDDVRMPLAPGEVVKERMVRFRT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1518978224 249 LGCWPLTGAVESNAQTLPEIIEEMLVSTTSERQGRVIDRDQAGSMELKKRQGYF 302
Cdd:TIGR02039 241 LGCYPLTGAIESDAATVEEIIAETAAARTSERQGRAIDRDQAASMEDKKREGYF 294
|
|
| Sulfate_adenylyltransferase_2 |
cd23946 |
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ... |
8-221 |
9.85e-161 |
|
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: 446.17 E-value: 9.85e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 8 HLRQLEAESIHIIREVAAEFSNPVMMYSIGKDSSVMLHLARKAFYPGTLPFPLLHVDTGWKFSEMYEFRDRTAKAYGCEL 87
Cdd:cd23946 1 HLRQLEAESIHIIREVAAEFSNPVMLYSIGKDSSVMLHLARKAFYPGKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 88 LVHKNPEGVAMGINPFVHGSAKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERIYSFRDRFHRWDPKNQRPEL 167
Cdd:cd23946 81 IVHVNPDGVEAGINPFTHGSAKHTDIMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSNHRWDPKNQRPEL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1518978224 168 WHNYNGQINKGESIRVFPLSNWTEQDIWQYIWLENIDIVPLYLAAERPVLERDG 221
Cdd:cd23946 161 WNQYNGRVKKGESIRVFPLSNWTELDIWQYIYLENIPIVPLYFAAERPVIERDG 214
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
5-300 |
1.23e-84 |
|
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: 254.00 E-value: 1.23e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 5 RLTHL-RQLEAESIHIIREVAAEFS-NPVMMYSIGKDSSVMLHLARKAfypgTLPFPLLHVDTGWKFSEMYEFRDRTAKA 82
Cdd:COG0175 9 LLEELnAELEAEAIEILREAAAEFGgRVVVSSSGGKDSTVLLHLAAKF----KPPIPVLFLDTGYEFPETYEFRDRLAER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 83 YGCELLVHKNPEGVAM-----GINPFVHGSAKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERIYSfrdrfhr 157
Cdd:COG0175 85 LGLDLIVVRPEDAFAEqlaefGPPLFYRDPRWCCKIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVVE------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 158 WDPknqrpelwhnyngqinKGESIRVFPLSNWTEQDIWQYIWLENIDIVPLYlaaerpvlerdgmlmmidddridlqpge 237
Cdd:COG0175 158 WDP----------------VGGLIKVNPLADWTELDVWAYIRREDLPYNPLY---------------------------- 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1518978224 238 vikkrMVRFRTLGCWPLTGAVESNaqtlpeiieEMlvsttsERQGRVIDRDqagsmELKKRQG 300
Cdd:COG0175 194 -----DQGYPSIGCAPCTRAVESG---------ED------ERAGRWWDEE-----KERKECG 231
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
29-257 |
2.91e-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: 222.94 E-value: 2.91e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 29 NPVMMYSIGKDSSVMLHLARKAFYPGtlpfPLLHVDTGWKFSEMYEFRDRTAKAYGCELLVHKNPEGVAMGINPFVHGSA 108
Cdd:pfam01507 1 ELVVSFSGGKDSLVLLHLASKAFPPG----PVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 109 ---KHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERIYSFRDRFHRwdpknqrpelwhnyngqinkgeSIRVFP 185
Cdd:pfam01507 77 lyrRCCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDGDFPK----------------------VIKVFP 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1518978224 186 LSNWTEQDIWQYIWLENIDIVPLYLAAerpvlerdgmlmmidddridlqpgevikkrmvrFRTLGCWPLTGA 257
Cdd:pfam01507 135 LLNWTETDVWQYILANNVPYNPLYDQG---------------------------------YRSIGCYPCTGP 173
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05253 |
PRK05253 |
sulfate adenylyltransferase subunit CysD; |
1-302 |
0e+00 |
|
sulfate adenylyltransferase subunit CysD;
Pssm-ID: 235375 Cd Length: 301 Bit Score: 653.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 1 MDQKRLTHLRQLEAESIHIIREVAAEFSNPVMMYSIGKDSSVMLHLARKAFYPGTLPFPLLHVDTGWKFSEMYEFRDRTA 80
Cdd:PRK05253 1 MDQYRLTHLDQLEAESIHILREVAAEFENPVMLYSIGKDSSVMLHLARKAFYPGKLPFPLLHVDTGWKFPEMIEFRDRRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 81 KAYGCELLVHKNPEGVAMGINPFVHGSAKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERIYSFRDRFHRWDP 160
Cdd:PRK05253 81 KELGLELIVHSNPEGIARGINPFRHGSAKHTNAMKTEGLKQALEKYGFDAAFGGARRDEEKSRAKERIFSFRDEFGQWDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 161 KNQRPELWHNYNGQINKGESIRVFPLSNWTEQDIWQYIWLENIDIVPLYLAAERPVLERDGMLMMIdDDRIDLQPGEVIK 240
Cdd:PRK05253 161 KNQRPELWNLYNGRINKGEHIRVFPLSNWTELDIWQYIERENIPIVPLYFAHERPVVERDGMLIMV-DDRMPLRPGEVVE 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1518978224 241 KRMVRFRTLGCWPLTGAVESNAQTLPEIIEEMLVSTTSERQGRVIDRDQAGSMELKKRQGYF 302
Cdd:PRK05253 240 ERMVRFRTLGCYPCTGAVESEAATLEEIIAEMLVTRTSERGGRAIDDDQEASMEKRKREGYF 301
|
|
| CysD |
TIGR02039 |
sulfate adenylyltransferase, small subunit; Metabolic assimilation of sulfur from inorganic ... |
9-302 |
0e+00 |
|
sulfate adenylyltransferase, small subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 131094 Cd Length: 294 Bit Score: 603.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 9 LRQLEAESIHIIREVAAEFSNPVMMYSIGKDSSVMLHLARKAFYPGTLPFPLLHVDTGWKFSEMYEFRDRTAKAYGCELL 88
Cdd:TIGR02039 1 LRALESEAIHIIREVAAEFERPVMLYSIGKDSSVLLHLARKAFYPGPLPFPLLHVDTGWKFREMIAFRDHMVAKYGLRLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 89 VHKNPEGVAMGINPFVHGSAKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERIYSFRDRFHRWDPKNQRPELW 168
Cdd:TIGR02039 81 VHSNEEGIADGINPFTEGSALHTDIMKTEALRQALDKNQFDAAFGGARRDEEKSRAKERIFSFRNAFHQWDPKKQRPELW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 169 HNYNGQINKGESIRVFPLSNWTEQDIWQYIWLENIDIVPLYLAAERPVLERDGMLMMIDDDRIDLQPGEVIKKRMVRFRT 248
Cdd:TIGR02039 161 NLYNGRISKGESVRVFPLSNWTELDIWRYIAAENIPIVPLYFAAKRPVVQRDGMLIMVDDVRMPLAPGEVVKERMVRFRT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1518978224 249 LGCWPLTGAVESNAQTLPEIIEEMLVSTTSERQGRVIDRDQAGSMELKKRQGYF 302
Cdd:TIGR02039 241 LGCYPLTGAIESDAATVEEIIAETAAARTSERQGRAIDRDQAASMEDKKREGYF 294
|
|
| PRK12563 |
PRK12563 |
sulfate adenylyltransferase subunit CysD; |
2-302 |
0e+00 |
|
sulfate adenylyltransferase subunit CysD;
Pssm-ID: 237138 Cd Length: 312 Bit Score: 546.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 2 DQKRLTHLRQLEAESIHIIREVAAEFSNPVMMYSIGKDSSVMLHLARKAFYPGTLPFPLLHVDTGWKFSEMYEFRDRTAK 81
Cdd:PRK12563 12 STSRMGHLDRLEAESIHILREVVAECSKPVMLYSIGKDSVVMLHLAMKAFRPTRPPFPLLHVDTTWKFREMIDFRDRRAK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 82 AYGCELLVHKNPEGVAMGINPFVHGSAKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERIYSFRDRFHRWDPK 161
Cdd:PRK12563 92 ELGLDLVVHHNPDGIARGIVPFRHGSALHTDVAKTQGLKQALDHHGFDAAIGGARRDEEKSRAKERIFSFRSAFHRWDPK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 162 NQRPELWHNYNGQINKGESIRVFPLSNWTEQDIWQYIWLENIDIVPLYLAAERPVLERDGMLMMIDDDRIDLQPGEVIKK 241
Cdd:PRK12563 172 AQRPELWSLYNARLRRGESLRVFPLSNWTELDVWQYIAREKIPLVPLYFAKRRPVVERDGLLIMVDDERTPLRPGETPQQ 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1518978224 242 RMVRFRTLGCWPLTGAVESNAQTLPEIIEEMLVSTTSERQGRVIDRDQAGSMELKKRQGYF 302
Cdd:PRK12563 252 RKVRFRTLGCYPLTGAVESDADTVEKIIQEMAVTRISERQGRMIDQDSAASMEKKKKEGYF 312
|
|
| Sulfate_adenylyltransferase_2 |
cd23946 |
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ... |
8-221 |
9.85e-161 |
|
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: 446.17 E-value: 9.85e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 8 HLRQLEAESIHIIREVAAEFSNPVMMYSIGKDSSVMLHLARKAFYPGTLPFPLLHVDTGWKFSEMYEFRDRTAKAYGCEL 87
Cdd:cd23946 1 HLRQLEAESIHIIREVAAEFSNPVMLYSIGKDSSVMLHLARKAFYPGKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 88 LVHKNPEGVAMGINPFVHGSAKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERIYSFRDRFHRWDPKNQRPEL 167
Cdd:cd23946 81 IVHVNPDGVEAGINPFTHGSAKHTDIMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSNHRWDPKNQRPEL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1518978224 168 WHNYNGQINKGESIRVFPLSNWTEQDIWQYIWLENIDIVPLYLAAERPVLERDG 221
Cdd:cd23946 161 WNQYNGRVKKGESIRVFPLSNWTELDIWQYIYLENIPIVPLYFAAERPVIERDG 214
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
5-300 |
1.23e-84 |
|
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: 254.00 E-value: 1.23e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 5 RLTHL-RQLEAESIHIIREVAAEFS-NPVMMYSIGKDSSVMLHLARKAfypgTLPFPLLHVDTGWKFSEMYEFRDRTAKA 82
Cdd:COG0175 9 LLEELnAELEAEAIEILREAAAEFGgRVVVSSSGGKDSTVLLHLAAKF----KPPIPVLFLDTGYEFPETYEFRDRLAER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 83 YGCELLVHKNPEGVAM-----GINPFVHGSAKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERIYSfrdrfhr 157
Cdd:COG0175 85 LGLDLIVVRPEDAFAEqlaefGPPLFYRDPRWCCKIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVVE------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 158 WDPknqrpelwhnyngqinKGESIRVFPLSNWTEQDIWQYIWLENIDIVPLYlaaerpvlerdgmlmmidddridlqpge 237
Cdd:COG0175 158 WDP----------------VGGLIKVNPLADWTELDVWAYIRREDLPYNPLY---------------------------- 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1518978224 238 vikkrMVRFRTLGCWPLTGAVESNaqtlpeiieEMlvsttsERQGRVIDRDqagsmELKKRQG 300
Cdd:COG0175 194 -----DQGYPSIGCAPCTRAVESG---------ED------ERAGRWWDEE-----KERKECG 231
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
29-257 |
2.91e-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: 222.94 E-value: 2.91e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 29 NPVMMYSIGKDSSVMLHLARKAFYPGtlpfPLLHVDTGWKFSEMYEFRDRTAKAYGCELLVHKNPEGVAMGINPFVHGSA 108
Cdd:pfam01507 1 ELVVSFSGGKDSLVLLHLASKAFPPG----PVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 109 ---KHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERIYSFRDRFHRwdpknqrpelwhnyngqinkgeSIRVFP 185
Cdd:pfam01507 77 lyrRCCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDGDFPK----------------------VIKVFP 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1518978224 186 LSNWTEQDIWQYIWLENIDIVPLYLAAerpvlerdgmlmmidddridlqpgevikkrmvrFRTLGCWPLTGA 257
Cdd:pfam01507 135 LLNWTETDVWQYILANNVPYNPLYDQG---------------------------------YRSIGCYPCTGP 173
|
|
| PAPS_reductase-like_YbdN |
cd23947 |
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ... |
16-209 |
6.09e-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: 93.99 E-value: 6.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 16 SIHIIREVAAEFSNPVMMYSIGKDSSVMLHLARKAFYPGTLPFPLLHVDTGWKFSEMYEFRDRTAKAYGCELLVHKNP-- 93
Cdd:cd23947 1 ALERIRKVFEEFDPVIVSFSGGKDSLVLLHLALEALRRLRKDVYVVFIDTGIEFPETIDFVEKLAETLGLDVEAARPPlf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 94 -----EGVAMGINPFVHGSAKH------TDIMKTEGLKQALN-KYGFDAAFG-GARRDEEKSRAKEriysfrdrfhrwdP 160
Cdd:cd23947 81 lewltSNFQPQWDPIWDNPPPPrdyrwcCDELKLEPFTKWLKeKKPEGVLLLvGIRADESLNRAKR-------------P 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1518978224 161 KNQRPELWHNyngqINKGESIRVFPLSNWTEQDIWQYIWLENIDIVPLY 209
Cdd:cd23947 148 RVYRKYGWRN----STLPGQIVAYPIKDWSVEDVWLYILRHGLPYNPLY 192
|
|
| PAPS_reductase |
cd23945 |
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ... |
19-209 |
1.02e-18 |
|
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: 81.87 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 19 IIREVAAEFSNPVMMYSIGKDSSVMLHLARKAFypgtLPFPLLHVDTGWKFSEMYEFRDRTAKAYGCELLVHKNPEGVAM 98
Cdd:cd23945 5 LLWAAEEFGPKLVFATSFGAEDAVILDLLSKVR----PDIPVVFLDTGYLFPETYDLIDEVEARYGLNIEVYFPEGTEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 99 ------GINPF-VHGSAKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERIYSfrdrfhrWDPKNQRpelwhny 171
Cdd:cd23945 81 eealegGLNEFyLEDEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIVE-------VDEEGGL------- 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 1518978224 172 ngqinkgesIRVFPLSNWTEQDIWQYIWLENIDIVPLY 209
Cdd:cd23945 147 ---------VKINPLADWTWEDVWAYIREHDLPYNPLH 175
|
|
| PRK13795 |
PRK13795 |
hypothetical protein; Provisional |
7-209 |
3.56e-17 |
|
hypothetical protein; Provisional
Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 81.58 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 7 THLRQLEAESIHIIREVAAEFSNPVMM-YSIGKDSSVMLHLARKAFypgtLPFPLLHVDTGWKFSEMYEFRDRTAKAYGC 85
Cdd:PRK13795 222 KHLEEKEKEAVNFIRGVAEKYNLPVSVsFSGGKDSLVVLDLAREAL----KDFKAFFNNTGLEFPETVENVKEVAEEYGI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 86 ELLVHKNPEGVAMGINPF------------VHGSAKHTDIMKTEGLKQALnkygfdaAFGGARRDEEKSRAKeriysfrd 153
Cdd:PRK13795 298 ELIEADAGDAFWRAVEKFgppardyrwcckVCKLGPITRAIKENFPKGCL-------TFVGQRKYESFSRAK-------- 362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1518978224 154 rfhrwdpknqRPELWHNY--NGQINkgesirVFPLSNWTEQDIWQYIWLENIDIVPLY 209
Cdd:PRK13795 363 ----------SPRVWRNPwvPNQIG------ASPIQDWTALEVWLYIFWRKLPYNPLY 404
|
|
| PRK02090 |
PRK02090 |
phosphoadenylyl-sulfate reductase; |
7-198 |
8.24e-15 |
|
phosphoadenylyl-sulfate reductase;
Pssm-ID: 234997 Cd Length: 241 Bit Score: 72.18 E-value: 8.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 7 THLRQLEAEsiHIIREVAAEF-SNPVMMYSIGKDSSVMLHLARKAfYPGTlpfPLLHVDTGWKFSEMYEFRDRTAKAYGC 85
Cdd:PRK02090 21 AELEGASAQ--ERLAWALENFgGRLALVSSFGAEDAVLLHLVAQV-DPDI---PVIFLDTGYLFPETYRFIDELTERLLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 86 ELLV-HKNPEGVAM-----GIN-PFVHGSAKHTDIMKTEGLKQALNkyGFDAAFGGARRDEEKSRAKERIYSF-RDRFhr 157
Cdd:PRK02090 95 NLKVyRPDASAAEQearygGLWeQSVEDRDECCRIRKVEPLNRALA--GLDAWITGLRREQSGTRANLPVLEIdGGRF-- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1518978224 158 wdpknqrpelwhnyngQINkgesirvfPLSNWTEQDIWQYI 198
Cdd:PRK02090 171 ----------------KIN--------PLADWTNEDVWAYL 187
|
|
| cysH |
TIGR00434 |
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ... |
31-209 |
2.53e-14 |
|
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: 70.59 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 31 VMMYSIGKDSSVMLHLARKAFYPGTLPFpllhVDTGWKFSEMYEFRDRTAKAYGCELLVHKNPEGVA-----MGINPFVH 105
Cdd:TIGR00434 17 VYSTSFGIQGAVLLDLVSKISPDIPVIF----LDTGYHFPETYELIDELTERYPLNIKVYKPDLSLAeqaakYGDKLWEQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 106 GSAKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERIYSFRDRFhrwdpknqrpelwhnyngqinkgESIRVFP 185
Cdd:TIGR00434 93 DPNKYDYLRKVEPMHRALKELHASAWFTGLRRDQGPSRANLSILNIDEKF-----------------------GILKVLP 149
|
170 180
....*....|....*....|....
gi 1518978224 186 LSNWTEQDIWQYIWLENIDIVPLY 209
Cdd:TIGR00434 150 LIDWTWKDVYQYIDAHNLPYNPLH 173
|
|
| FAD_synthase |
cd23948 |
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ... |
15-209 |
5.28e-13 |
|
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: 66.01 E-value: 5.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 15 ESIHIIREVAAEFSNPVMMYSI--GKDSSVMLHLARKAF---YPGTL-PFPLLHVDTGWKFSEMYEFRDRTAKAYGCELL 88
Cdd:cd23948 4 SALEVIEEALDKYGPEEIAISFngGKDCTVLLHLLRAALkrkYPSPLtPLKALYIKSPDPFPEVEEFVEDTAKRYNLDLI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 89 VHKNPegvamginpfvhgsakhtdiMKtEGLKQALNKYG-FDAAFGGARRDeeksrakeriysfrdrfhrwDP--KNQRP 165
Cdd:cd23948 84 TIDGP--------------------MK-EGLEELLKEHPiIKAVFMGTRRT--------------------DPhgENLKP 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1518978224 166 ELW--HNYNgqinkgESIRVFPLSNWTEQDIWQYIWLENIDIVPLY 209
Cdd:cd23948 123 FSPtdPGWP------QFMRVNPILDWSYHDVWEFLRTLNLPYCSLY 162
|
|
| PRK13794 |
PRK13794 |
hypothetical protein; Provisional |
13-209 |
3.49e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 237509 [Multi-domain] Cd Length: 479 Bit Score: 66.61 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 13 EAESIHIIREVAAEFSNPVMM-YSIGKDSSVMLHLARKAFypgTLPFPLLHVDTGWKFSEMYEFRDRTAKAYGCELLVHK 91
Cdd:PRK13794 232 ERNSIGFIRNTAEKINKPVTVaYSGGKDSLATLLLALKAL---GINFPVLFNDTGLEFPETLENVEDVEKHYGLEIIRTK 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 92 NPEgvamginpFVHGSAKH----------TDIMKTEGLKQAL-NKYGFDA-AFGGARRDEEKSRAKeriysfrdrfhrwd 159
Cdd:PRK13794 309 SEE--------FWEKLEEYgppardnrwcSEVCKLEPLGKLIdEKYEGEClSFVGQRKYESFNRSK-------------- 366
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1518978224 160 pknqRPELWHNYNgqINKgeSIRVFPLSNWTEQDIWQYIWLENIDIVPLY 209
Cdd:PRK13794 367 ----KPRIWRNPY--IKK--QILAAPILHWTAMHVWIYLFREKAPYNKLY 408
|
|
| AANH-like |
cd01986 |
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ... |
30-100 |
1.61e-08 |
|
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: 50.53 E-value: 1.61e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1518978224 30 PVMMYSIGKDSSVMLHLARKAFYPgtLPFPLLHVDTGWKFSEMYEFRDRTAKAYGCELLVHKNPEGVAMGI 100
Cdd:cd01986 1 VVVGYSGGKDSSVALHLASRLGRK--AEVAVVHIDHGIGFKEEAESVASIARRSILKKLAEKGARAIATGV 69
|
|
| PRK08557 |
PRK08557 |
hypothetical protein; Provisional |
3-209 |
7.34e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 181465 [Multi-domain] Cd Length: 417 Bit Score: 53.22 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 3 QKRLTHLRQLEAESIHIIREVAAEFSNPVMM----YSIGKDSSVMLHLARKAFYPGTLPFpllhVDTGWKFSEMYEFRDR 78
Cdd:PRK08557 153 EKNKERIEKLEENSLSILKDYIEKYKNKGYAinasFSGGKDSSVSTLLAKEVIPDLEVIF----IDTGLEYPETINYVKD 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 79 TAKAYGCELLVHK--------NPEGVAMGINPFVHGSAKhtdimkTEGLKQALNK-YGFDAAF--GGARRDEEKSRAK-- 145
Cdd:PRK08557 229 FAKKYDLNLDTLDgdnfwenlEKEGIPTKDNRWCNSACK------LMPLKEYLKKkYGNKKVLtiDGSRKYESFTRANld 302
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1518978224 146 -ERIYSFRDrfhrwdpknqrpelwhnynGQINkgesirVFPLSNWTEQDIWQYIWLENIDIVPLY 209
Cdd:PRK08557 303 yERKSGFID-------------------FQTN------VFPILDWNSLDIWSYIYLNDILYNPLY 342
|
|
| PRK08576 |
PRK08576 |
hypothetical protein; Provisional |
9-231 |
4.46e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 236300 [Multi-domain] Cd Length: 438 Bit Score: 50.85 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 9 LRQLEAESIHIIREVaaEFSNPVMMYSIGKDSSVMLHLARKAFYPGTlpfpLLHVDTGWKFSEMYEFRDRTAKAYGCELL 88
Cdd:PRK08576 218 LEAFEKASIKFLRKF--EEWTVIVPWSGGKDSTAALLLAKKAFGDVT----AVYVDTGYEMPLTDEYVEKVAEKLGVDLI 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 89 VhknpEGVAMGINPFVHGSAKHTD----IMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKeriysfrdrfhrwdpknqR 164
Cdd:PRK08576 292 R----AGVDVPMPIEKYGMPTHSNrwctKLKVEALEEAIRELEDGLLVVGDRDGESARRRL------------------R 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518978224 165 PELWHNYNgqiNKGESIRVFPLSNWTEQDIWQYIWLENIDIVPLY--------------LAA-ERPVLERDGMLMMIDDD 229
Cdd:PRK08576 350 PPVVERKT---NFGKILVVMPIKFWSGAMVQLYILMNGLELNPLYykgfyrlgcyicpsLRSwEIELLKRLPVLPLILKK 426
|
..
gi 1518978224 230 RI 231
Cdd:PRK08576 427 RP 428
|
|
| |
