|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05253 |
PRK05253 |
sulfate adenylyltransferase subunit CysD; |
15-308 |
0e+00 |
|
sulfate adenylyltransferase subunit CysD;
Pssm-ID: 235375 Cd Length: 301 Bit Score: 527.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 15 PRLAELEAEAIDIIRQTAGQFDRPALLFSGGKDSVVVLELAKRAFAPAGIPLELLHVNTGHNFPEVIEFRDKIAAQPGIK 94
Cdd:PRK05253 7 THLDQLEAESIHILREVAAEFENPVMLYSIGKDSSVMLHLARKAFYPGKLPFPLLHVDTGWKFPEMIEFRDRRAKELGLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 95 LHVAKVQDWIDSGVLTERADG--TRNPLQTVPLVETIANRGYDAVLGGARRDEEKARAKERVFSVRDSFGGWDPRRQRPE 172
Cdd:PRK05253 87 LIVHSNPEGIARGINPFRHGSakHTNAMKTEGLKQALEKYGFDAAFGGARRDEEKSRAKERIFSFRDEFGQWDPKNQRPE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 173 LWGLYNGRHAAGENVRVFPISNWTEADVWAYIEARDIELPPIYFAHEREVFNRGGMWLAPGEWGGPRDGETLEVRTVRYR 252
Cdd:PRK05253 167 LWNLYNGRINKGEHIRVFPLSNWTELDIWQYIERENIPIVPLYFAHERPVVERDGMLIMVDDRMPLRPGEVVEERMVRFR 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 896167334 253 TVGDMSCTGAVESTATTIAEVMEELRTSKLTERGATRADDKlSESSMEDRKKEGYF 308
Cdd:PRK05253 247 TLGCYPCTGAVESEAATLEEIIAEMLVTRTSERGGRAIDDD-QEASMEKRKREGYF 301
|
|
| CysD |
TIGR02039 |
sulfate adenylyltransferase, small subunit; Metabolic assimilation of sulfur from inorganic ... |
17-308 |
1.45e-147 |
|
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: 416.06 E-value: 1.45e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 17 LAELEAEAIDIIRQTAGQFDRPALLFSGGKDSVVVLELAKRAFAPAGIPLELLHVNTGHNFPEVIEFRDKIAAQPGIKLH 96
Cdd:TIGR02039 1 LRALESEAIHIIREVAAEFERPVMLYSIGKDSSVLLHLARKAFYPGPLPFPLLHVDTGWKFREMIAFRDHMVAKYGLRLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 97 VAKVQDWIDSGV--LTERADGTRNPLQTVPLVETIANRGYDAVLGGARRDEEKARAKERVFSVRDSFGGWDPRRQRPELW 174
Cdd:TIGR02039 81 VHSNEEGIADGInpFTEGSALHTDIMKTEALRQALDKNQFDAAFGGARRDEEKSRAKERIFSFRNAFHQWDPKKQRPELW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 175 GLYNGRHAAGENVRVFPISNWTEADVWAYIEARDIELPPIYFAHEREVFNRGGMWLAPG-EWGGPRDGETLEVRTVRYRT 253
Cdd:TIGR02039 161 NLYNGRISKGESVRVFPLSNWTELDIWRYIAAENIPIVPLYFAAKRPVVQRDGMLIMVDdVRMPLAPGEVVKERMVRFRT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 896167334 254 VGDMSCTGAVESTATTIAEVMEELRTSKLTERgATRADDKLSESSMEDRKKEGYF 308
Cdd:TIGR02039 241 LGCYPLTGAIESDAATVEEIIAETAAARTSER-QGRAIDRDQAASMEDKKREGYF 294
|
|
| Sulfate_adenylyltransferase_2 |
cd23946 |
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ... |
17-227 |
7.07e-82 |
|
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: 246.64 E-value: 7.07e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 17 LAELEAEAIDIIRQTAGQFDRPALLFSGGKDSVVVLELAKRAFAPAGIPLELLHVNTGHNFPEVIEFRDKIAAQPGIKLH 96
Cdd:cd23946 2 LRQLEAESIHIIREVAAEFSNPVMLYSIGKDSSVMLHLARKAFYPGKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 97 VAKVQDWIDSGV--LTERADGTRNPLQTVPLVETIANRGYDAVLGGARRDEEKARAKERVFSVRDSFGGWDPRRQRPELW 174
Cdd:cd23946 82 VHVNPDGVEAGInpFTHGSAKHTDIMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSNHRWDPKNQRPELW 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 896167334 175 GLYNGRHAAGENVRVFPISNWTEADVWAYIEARDIELPPIYFAHEREVFNRGG 227
Cdd:cd23946 162 NQYNGRVKKGESIRVFPLSNWTELDIWQYIYLENIPIVPLYFAAERPVIERDG 214
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
18-306 |
1.56e-63 |
|
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: 200.46 E-value: 1.56e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 18 AELEAEAIDIIRQTAGQF-DRPALLFSGGKDSVVVLELAKRAfapaGIPLELLHVNTGHNFPEVIEFRDKIAAQPGIKLH 96
Cdd:COG0175 15 AELEAEAIEILREAAAEFgGRVVVSSSGGKDSTVLLHLAAKF----KPPIPVLFLDTGYEFPETYEFRDRLAERLGLDLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 97 VAKVQDWIDSGVL-------TERADGTRNPLQTVPLVETIANRGYDAVLGGARRDEEKARAKERVFSvrdsfggWDPRrq 169
Cdd:COG0175 91 VVRPEDAFAEQLAefgpplfYRDPRWCCKIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVVE-------WDPV-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 170 rpelwglyngrhaaGENVRVFPISNWTEADVWAYIEARDIELPPIYFaherevfnrggmwlapgewggprdgetlevrtV 249
Cdd:COG0175 162 --------------GGLIKVNPLADWTELDVWAYIRREDLPYNPLYD--------------------------------Q 195
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 896167334 250 RYRTVGDMSCTGAVESTattiaevmEELRtskltergATRADDKLSEssmedRKKEG 306
Cdd:COG0175 196 GYPSIGCAPCTRAVESG--------EDER--------AGRWWDEEKE-----RKECG 231
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
37-262 |
6.91e-45 |
|
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: 150.52 E-value: 6.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 37 RPALLFSGGKDSVVVLELAKRAFAPAgiplELLHVNTGHNFPEVIEFRDKIAAQPGIKLHVAKVQDWIDSGVLTERADGT 116
Cdd:pfam01507 1 ELVVSFSGGKDSLVLLHLASKAFPPG----PVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 117 -----RNPLQTVPLVETIANRGYDAVLGGARRDEEKARAKERVFSVRDSFGGwdprrqrpelwglyngrhaageNVRVFP 191
Cdd:pfam01507 77 lyrrcCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDGDFPK----------------------VIKVFP 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896167334 192 ISNWTEADVWAYIEARDIELPPIYFAHerevfnrggmwlapgewggprdgetlevrtvrYRTVGDMSCTGA 262
Cdd:pfam01507 135 LLNWTETDVWQYILANNVPYNPLYDQG--------------------------------YRSIGCYPCTGP 173
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05253 |
PRK05253 |
sulfate adenylyltransferase subunit CysD; |
15-308 |
0e+00 |
|
sulfate adenylyltransferase subunit CysD;
Pssm-ID: 235375 Cd Length: 301 Bit Score: 527.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 15 PRLAELEAEAIDIIRQTAGQFDRPALLFSGGKDSVVVLELAKRAFAPAGIPLELLHVNTGHNFPEVIEFRDKIAAQPGIK 94
Cdd:PRK05253 7 THLDQLEAESIHILREVAAEFENPVMLYSIGKDSSVMLHLARKAFYPGKLPFPLLHVDTGWKFPEMIEFRDRRAKELGLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 95 LHVAKVQDWIDSGVLTERADG--TRNPLQTVPLVETIANRGYDAVLGGARRDEEKARAKERVFSVRDSFGGWDPRRQRPE 172
Cdd:PRK05253 87 LIVHSNPEGIARGINPFRHGSakHTNAMKTEGLKQALEKYGFDAAFGGARRDEEKSRAKERIFSFRDEFGQWDPKNQRPE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 173 LWGLYNGRHAAGENVRVFPISNWTEADVWAYIEARDIELPPIYFAHEREVFNRGGMWLAPGEWGGPRDGETLEVRTVRYR 252
Cdd:PRK05253 167 LWNLYNGRINKGEHIRVFPLSNWTELDIWQYIERENIPIVPLYFAHERPVVERDGMLIMVDDRMPLRPGEVVEERMVRFR 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 896167334 253 TVGDMSCTGAVESTATTIAEVMEELRTSKLTERGATRADDKlSESSMEDRKKEGYF 308
Cdd:PRK05253 247 TLGCYPCTGAVESEAATLEEIIAEMLVTRTSERGGRAIDDD-QEASMEKRKREGYF 301
|
|
| CysD |
TIGR02039 |
sulfate adenylyltransferase, small subunit; Metabolic assimilation of sulfur from inorganic ... |
17-308 |
1.45e-147 |
|
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: 416.06 E-value: 1.45e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 17 LAELEAEAIDIIRQTAGQFDRPALLFSGGKDSVVVLELAKRAFAPAGIPLELLHVNTGHNFPEVIEFRDKIAAQPGIKLH 96
Cdd:TIGR02039 1 LRALESEAIHIIREVAAEFERPVMLYSIGKDSSVLLHLARKAFYPGPLPFPLLHVDTGWKFREMIAFRDHMVAKYGLRLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 97 VAKVQDWIDSGV--LTERADGTRNPLQTVPLVETIANRGYDAVLGGARRDEEKARAKERVFSVRDSFGGWDPRRQRPELW 174
Cdd:TIGR02039 81 VHSNEEGIADGInpFTEGSALHTDIMKTEALRQALDKNQFDAAFGGARRDEEKSRAKERIFSFRNAFHQWDPKKQRPELW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 175 GLYNGRHAAGENVRVFPISNWTEADVWAYIEARDIELPPIYFAHEREVFNRGGMWLAPG-EWGGPRDGETLEVRTVRYRT 253
Cdd:TIGR02039 161 NLYNGRISKGESVRVFPLSNWTELDIWRYIAAENIPIVPLYFAAKRPVVQRDGMLIMVDdVRMPLAPGEVVKERMVRFRT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 896167334 254 VGDMSCTGAVESTATTIAEVMEELRTSKLTERgATRADDKLSESSMEDRKKEGYF 308
Cdd:TIGR02039 241 LGCYPLTGAIESDAATVEEIIAETAAARTSER-QGRAIDRDQAASMEDKKREGYF 294
|
|
| PRK12563 |
PRK12563 |
sulfate adenylyltransferase subunit CysD; |
15-308 |
3.53e-124 |
|
sulfate adenylyltransferase subunit CysD;
Pssm-ID: 237138 Cd Length: 312 Bit Score: 357.56 E-value: 3.53e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 15 PRLAELEAEAIDIIRQTAGQFDRPALLFSGGKDSVVVLELAKRAFAPAGIPLELLHVNTGHNFPEVIEFRDKIAAQPGIK 94
Cdd:PRK12563 17 GHLDRLEAESIHILREVVAECSKPVMLYSIGKDSVVMLHLAMKAFRPTRPPFPLLHVDTTWKFREMIDFRDRRAKELGLD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 95 LHVAKVQDWIDSGV--LTERADGTRNPLQTVPLVETIANRGYDAVLGGARRDEEKARAKERVFSVRDSFGGWDPRRQRPE 172
Cdd:PRK12563 97 LVVHHNPDGIARGIvpFRHGSALHTDVAKTQGLKQALDHHGFDAAIGGARRDEEKSRAKERIFSFRSAFHRWDPKAQRPE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 173 LWGLYNGRHAAGENVRVFPISNWTEADVWAYIEARDIELPPIYFAHEREVFNRGGMWLAPGEWGGP-RDGETLEVRTVRY 251
Cdd:PRK12563 177 LWSLYNARLRRGESLRVFPLSNWTELDVWQYIAREKIPLVPLYFAKRRPVVERDGLLIMVDDERTPlRPGETPQQRKVRF 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 896167334 252 RTVGDMSCTGAVESTATTIAEVMEELRTSKLTERGAtRADDKLSESSMEDRKKEGYF 308
Cdd:PRK12563 257 RTLGCYPLTGAVESDADTVEKIIQEMAVTRISERQG-RMIDQDSAASMEKKKKEGYF 312
|
|
| Sulfate_adenylyltransferase_2 |
cd23946 |
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ... |
17-227 |
7.07e-82 |
|
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: 246.64 E-value: 7.07e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 17 LAELEAEAIDIIRQTAGQFDRPALLFSGGKDSVVVLELAKRAFAPAGIPLELLHVNTGHNFPEVIEFRDKIAAQPGIKLH 96
Cdd:cd23946 2 LRQLEAESIHIIREVAAEFSNPVMLYSIGKDSSVMLHLARKAFYPGKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 97 VAKVQDWIDSGV--LTERADGTRNPLQTVPLVETIANRGYDAVLGGARRDEEKARAKERVFSVRDSFGGWDPRRQRPELW 174
Cdd:cd23946 82 VHVNPDGVEAGInpFTHGSAKHTDIMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDSNHRWDPKNQRPELW 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 896167334 175 GLYNGRHAAGENVRVFPISNWTEADVWAYIEARDIELPPIYFAHEREVFNRGG 227
Cdd:cd23946 162 NQYNGRVKKGESIRVFPLSNWTELDIWQYIYLENIPIVPLYFAAERPVIERDG 214
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
18-306 |
1.56e-63 |
|
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: 200.46 E-value: 1.56e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 18 AELEAEAIDIIRQTAGQF-DRPALLFSGGKDSVVVLELAKRAfapaGIPLELLHVNTGHNFPEVIEFRDKIAAQPGIKLH 96
Cdd:COG0175 15 AELEAEAIEILREAAAEFgGRVVVSSSGGKDSTVLLHLAAKF----KPPIPVLFLDTGYEFPETYEFRDRLAERLGLDLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 97 VAKVQDWIDSGVL-------TERADGTRNPLQTVPLVETIANRGYDAVLGGARRDEEKARAKERVFSvrdsfggWDPRrq 169
Cdd:COG0175 91 VVRPEDAFAEQLAefgpplfYRDPRWCCKIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVVE-------WDPV-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 170 rpelwglyngrhaaGENVRVFPISNWTEADVWAYIEARDIELPPIYFaherevfnrggmwlapgewggprdgetlevrtV 249
Cdd:COG0175 162 --------------GGLIKVNPLADWTELDVWAYIRREDLPYNPLYD--------------------------------Q 195
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 896167334 250 RYRTVGDMSCTGAVESTattiaevmEELRtskltergATRADDKLSEssmedRKKEG 306
Cdd:COG0175 196 GYPSIGCAPCTRAVESG--------EDER--------AGRWWDEEKE-----RKECG 231
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
37-262 |
6.91e-45 |
|
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: 150.52 E-value: 6.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 37 RPALLFSGGKDSVVVLELAKRAFAPAgiplELLHVNTGHNFPEVIEFRDKIAAQPGIKLHVAKVQDWIDSGVLTERADGT 116
Cdd:pfam01507 1 ELVVSFSGGKDSLVLLHLASKAFPPG----PVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 117 -----RNPLQTVPLVETIANRGYDAVLGGARRDEEKARAKERVFSVRDSFGGwdprrqrpelwglyngrhaageNVRVFP 191
Cdd:pfam01507 77 lyrrcCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDGDFPK----------------------VIKVFP 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896167334 192 ISNWTEADVWAYIEARDIELPPIYFAHerevfnrggmwlapgewggprdgetlevrtvrYRTVGDMSCTGA 262
Cdd:pfam01507 135 LLNWTETDVWQYILANNVPYNPLYDQG--------------------------------YRSIGCYPCTGP 173
|
|
| PAPS_reductase-like_YbdN |
cd23947 |
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ... |
28-222 |
2.04e-24 |
|
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: 97.85 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 28 IRQTAGQFDRPALLFSGGKDSVVVLELAKRAFAPAGIPLELLHVNTGHNFPEVIEFRDKIAAQPGIKLHVAKV---QDWI 104
Cdd:cd23947 5 IRKVFEEFDPVIVSFSGGKDSLVLLHLALEALRRLRKDVYVVFIDTGIEFPETIDFVEKLAETLGLDVEAARPplfLEWL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 105 DSGVLTERADGTRNPLQTVP---------------LVETIANRGYdAVLGGARRDEEKARAKErvfsvrdsfggwdPRRQ 169
Cdd:cd23947 85 TSNFQPQWDPIWDNPPPPRDyrwccdelklepftkWLKEKKPEGV-LLLVGIRADESLNRAKR-------------PRVY 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 896167334 170 RPELWglyngRHAAGENVRVF-PISNWTEADVWAYIEARDIELPPIYF-AHEREV 222
Cdd:cd23947 151 RKYGW-----RNSTLPGQIVAyPIKDWSVEDVWLYILRHGLPYNPLYDlGFDRGG 200
|
|
| PRK13795 |
PRK13795 |
hypothetical protein; Provisional |
17-232 |
1.07e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 86.20 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 17 LAELEAEAIDIIRQTAGQFDRP-ALLFSGGKDSVVVLELAKRAFApagiPLELLHVNTGHNFPEVIEFRDKIAAQPGIKL 95
Cdd:PRK13795 224 LEEKEKEAVNFIRGVAEKYNLPvSVSFSGGKDSLVVLDLAREALK----DFKAFFNNTGLEFPETVENVKEVAEEYGIEL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 96 HVAKVQD--WIDSGVLTERADGTR---NPLQTVPLVETIANRGYDAVLG--GARRDEEKARAK-ERVfsvrdsfggWdpr 167
Cdd:PRK13795 300 IEADAGDafWRAVEKFGPPARDYRwccKVCKLGPITRAIKENFPKGCLTfvGQRKYESFSRAKsPRV---------W--- 367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896167334 168 rQRPelWglyngrhAAGEnVRVFPISNWTEADVWAYIEARDIELPPIYfahEREvFNRGGMWLAP 232
Cdd:PRK13795 368 -RNP--W-------VPNQ-IGASPIQDWTALEVWLYIFWRKLPYNPLY---ERG-FDRIGCWLCP 417
|
|
| PAPS_reductase |
cd23945 |
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ... |
24-209 |
3.58e-17 |
|
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: 77.64 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 24 AIDIIRQTAGQFDRPALLFSGGKDSVVVLELAKRAFAPAGIplelLHVNTGHNFPEVIEFRDKIAAQPGIKLHVAK---- 99
Cdd:cd23945 2 LEILLWAAEEFGPKLVFATSFGAEDAVILDLLSKVRPDIPV----VFLDTGYLFPETYDLIDEVEARYGLNIEVYFpegt 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 100 -VQDWIDSGVLTERADGTRNPLQTVPLVETIANR----GYDAVLGGARRDEEKARAKERVFsvrdsfgGWDPRRQRpelw 174
Cdd:cd23945 78 eAEEEALEGGLNEFYLEDEERYDCCRKRKPFPLAlallGVKAWITGRRRDQSPTRANLPIV-------EVDEEGGL---- 146
|
170 180 190
....*....|....*....|....*....|....*
gi 896167334 175 glyngrhaagenVRVFPISNWTEADVWAYIEARDI 209
Cdd:cd23945 147 ------------VKINPLADWTWEDVWAYIREHDL 169
|
|
| FAD_synthase |
cd23948 |
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ... |
23-212 |
2.59e-16 |
|
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: 75.25 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 23 EAIDIIRQTAGQF--DRPALLFSGGKDSVVVLELA----KRAFAPAGIPLELLHVNTGHNFPEVIEFRDKIAAQPGIKLH 96
Cdd:cd23948 4 SALEVIEEALDKYgpEEIAISFNGGKDCTVLLHLLraalKRKYPSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNLDLI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 97 VakvqdwIDSGVlterADGTRNPLQTVPLVEtianrgydAVLGGARRDEEKARaKERVFSVRDSfgGWdprrqrPELwgl 176
Cdd:cd23948 84 T------IDGPM----KEGLEELLKEHPIIK--------AVFMGTRRTDPHGE-NLKPFSPTDP--GW------PQF--- 133
|
170 180 190
....*....|....*....|....*....|....*.
gi 896167334 177 yngrhaagenVRVFPISNWTEADVWAYIeaRDIELP 212
Cdd:cd23948 134 ----------MRVNPILDWSYHDVWEFL--RTLNLP 157
|
|
| PRK02090 |
PRK02090 |
phosphoadenylyl-sulfate reductase; |
1-264 |
7.39e-16 |
|
phosphoadenylyl-sulfate reductase;
Pssm-ID: 234997 Cd Length: 241 Bit Score: 75.26 E-value: 7.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 1 MTSSTTVSVQNRLDPRLAELE-AEAIDIIRQTAGQF-DRPALLFSGGKDSVVVLELAKRAFApaGIPLELLhvNTGHNFP 78
Cdd:PRK02090 4 LNALPKADLALDLAELNAELEgASAQERLAWALENFgGRLALVSSFGAEDAVLLHLVAQVDP--DIPVIFL--DTGYLFP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 79 EVIEFRDKIAAQPGIKLHVAKVQ------------DWIDSGVLTERADGTR--NPLQTvplvetiANRGYDAVLGGARRD 144
Cdd:PRK02090 80 ETYRFIDELTERLLLNLKVYRPDasaaeqearyggLWEQSVEDRDECCRIRkvEPLNR-------ALAGLDAWITGLRRE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 145 EEKARAKERVFSvrdsfggWDPRRqrpelwglyngrhaagenVRVFPISNWTEADVWAYIEARDieLPPiyfaHerEVFN 224
Cdd:PRK02090 153 QSGTRANLPVLE-------IDGGR------------------FKINPLADWTNEDVWAYLKEHD--LPY----H--PLVD 199
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 896167334 225 RGgmwlapgewggprdgetlevrtvrYRTVGDMSCTGAVE 264
Cdd:PRK02090 200 QG------------------------YPSIGCEPCTRPVE 215
|
|
| PRK08557 |
PRK08557 |
hypothetical protein; Provisional |
16-232 |
1.36e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 181465 [Multi-domain] Cd Length: 417 Bit Score: 70.55 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 16 RLAELEAEAIDIIRQTAGQFDRPALL----FSGGKDSVVVLELAKRAfapagIP-LELLHVNTGHNFPEVIEFRDKIAAQ 90
Cdd:PRK08557 158 RIEKLEENSLSILKDYIEKYKNKGYAinasFSGGKDSSVSTLLAKEV-----IPdLEVIFIDTGLEYPETINYVKDFAKK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 91 PGIKLHVAKVQDWID----SGVLTERADGTRNPLQTVPLVETIANR-GYDAVL--GGARRDEEKARAK---ERVFSVRDS 160
Cdd:PRK08557 233 YDLNLDTLDGDNFWEnlekEGIPTKDNRWCNSACKLMPLKEYLKKKyGNKKVLtiDGSRKYESFTRANldyERKSGFIDF 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896167334 161 fggwdprrqrpelwglyngrhaageNVRVFPISNWTEADVWAYIEARDIELPPIYfaheREVFNRGGMWLAP 232
Cdd:PRK08557 313 -------------------------QTNVFPILDWNSLDIWSYIYLNDILYNPLY----DKGFERIGCYLCP 355
|
|
| PRK13794 |
PRK13794 |
hypothetical protein; Provisional |
17-232 |
2.56e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 237509 [Multi-domain] Cd Length: 479 Bit Score: 63.92 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 17 LAELEAEAIDIIRQTAGQFDRPALL-FSGGKDSVVVLELAKRAFapaGIPLELLHVNTGHNFPEVIEFRDKIAAQPGIKL 95
Cdd:PRK13794 228 LDKYERNSIGFIRNTAEKINKPVTVaYSGGKDSLATLLLALKAL---GINFPVLFNDTGLEFPETLENVEDVEKHYGLEI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 96 HVAKVQD-WIDsgvLTERADGTRN------PLQTVPLVETIANRGYDAVLG--GARRDEEKARAKervfsvrdsfggwdp 166
Cdd:PRK13794 305 IRTKSEEfWEK---LEEYGPPARDnrwcseVCKLEPLGKLIDEKYEGECLSfvGQRKYESFNRSK--------------- 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896167334 167 rrqRPELWglyNGRH------AAgenvrvfPISNWTEADVWAYIEARDIELPPIYfaheREVFNRGGMWLAP 232
Cdd:PRK13794 367 ---KPRIW---RNPYikkqilAA-------PILHWTAMHVWIYLFREKAPYNKLY----EQGFDRIGCFMCP 421
|
|
| PRK08576 |
PRK08576 |
hypothetical protein; Provisional |
20-235 |
2.95e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 236300 [Multi-domain] Cd Length: 438 Bit Score: 54.32 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 20 LEAEAIDIIRQTAGqfDRPALLFSGGKDSVVVLELAKRAFApagiPLELLHVNTGHNFPEVIEFRDKIAAQPGIKLhvak 99
Cdd:PRK08576 221 FEKASIKFLRKFEE--WTVIVPWSGGKDSTAALLLAKKAFG----DVTAVYVDTGYEMPLTDEYVEKVAEKLGVDL---- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 100 VQDWIDSGVLTERAdgtrnPLQT----------VPLVETIANRGYDAVLGGARRDEEKARAKERvfsvrdsfggwDPRRQ 169
Cdd:PRK08576 291 IRAGVDVPMPIEKY-----GMPThsnrwctklkVEALEEAIRELEDGLLVVGDRDGESARRRLR-----------PPVVE 354
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896167334 170 RPELWGLYngrhaagenVRVFPISNWTEADVWAYIEARDIELPPIYFaherEVFNRGGMWLAPG--EW 235
Cdd:PRK08576 355 RKTNFGKI---------LVVMPIKFWSGAMVQLYILMNGLELNPLYY----KGFYRLGCYICPSlrSW 409
|
|
| cysH |
TIGR00434 |
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ... |
24-222 |
3.24e-06 |
|
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: 47.09 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 24 AIDIIRQTAGQFdrPALLF---SGGKDSVVVLELAKRAFAPAGIPLellhVNTGHNFPEVIEFRDKIAAQPGIKLHVAKV 100
Cdd:TIGR00434 1 AQEIIAWAYVTF--GGHLVystSFGIQGAVLLDLVSKISPDIPVIF----LDTGYHFPETYELIDELTERYPLNIKVYKP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 101 ------QDWIDSGVLTERADGTRNPLQTV-PLVETIANRGYDAVLGGARRDEEKARAKERVFSVRDSFGgwdprrqrpel 173
Cdd:TIGR00434 75 dlslaeQAAKYGDKLWEQDPNKYDYLRKVePMHRALKELHASAWFTGLRRDQGPSRANLSILNIDEKFG----------- 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 896167334 174 wglyngrhaageNVRVFPISNWTEADVWAYIEARDIELPPIYFAHEREV 222
Cdd:TIGR00434 144 ------------ILKVLPLIDWTWKDVYQYIDAHNLPYNPLHDQGYPSI 180
|
|
| TilS |
COG0037 |
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ... |
42-102 |
8.23e-06 |
|
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439807 [Multi-domain] Cd Length: 235 Bit Score: 45.98 E-value: 8.23e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896167334 42 FSGGKDSVVVLELAKRAFAPAGIPLELLHVNtgHNFPEVIEFRD----KIAAQPGIKLHVAKVQD 102
Cdd:COG0037 22 VSGGKDSLALLHLLAKLRRRLGFELVAVHVD--HGLREESDEDAefvaELCEELGIPLHVVRVDV 84
|
|
| APS_reduc |
TIGR00424 |
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ... |
19-209 |
1.45e-05 |
|
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: 46.16 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 19 ELE-AEAIDIIRQTAGQF-DRPALLFSGGKDsVVVLELAKRAfapaGIPLELLHVNTGHNFPEVIEFRDKIAAQPGIKLH 96
Cdd:TIGR00424 97 KLEnASPLEIMDKALEKFgNDIAIAFSGAED-VALIEYAHLT----GRPFRVFSLDTGRLNPETYRFFDAVEKQYGIRIE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 97 -----VAKVQDWIDS-GVLTERADGTRN--------PLQTvplvetiANRGYDAVLGGARRDEEKA-RAKERVFSVRDSF 161
Cdd:TIGR00424 172 ymfpdAVEVQALVRSkGLFSFYEDGHQEccrvrkvrPLRR-------ALKGLKAWITGQRKDQSPGtRSEIPVVQVDPVF 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 896167334 162 GGWDprrqrpelwglyngrHAAGENVRVFPISNWTEADVWAYIEARDI 209
Cdd:TIGR00424 245 EGLD---------------GGVGSLVKWNPVANVEGKDVWNFLRTMDV 277
|
|
| QueC |
pfam06508 |
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ... |
41-114 |
1.04e-04 |
|
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis of 7-carboxy-7-deazaguanine. They catalyze the conversion of 7-deaza-7-carboxyguanine to preQ0.
Pssm-ID: 428982 [Multi-domain] Cd Length: 210 Bit Score: 42.60 E-value: 1.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896167334 41 LFSGGKDSVVVLELAKRAFApagiPLELLHVNTGHNFPEVIEFRDKIAAQPGIKLHVAKVQ---DWIDSGVLTERAD 114
Cdd:pfam06508 5 LLSGGLDSTTCLAWAKKEGY----EVYALSFDYGQRHRKELECAKKIAKALGVEHKILDLDflkQIGGSALTDDSIE 77
|
|
| AANH-like |
cd01986 |
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ... |
38-88 |
1.96e-04 |
|
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.
Pssm-ID: 467490 [Multi-domain] Cd Length: 74 Bit Score: 39.36 E-value: 1.96e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 896167334 38 PALLFSGGKDSVVVLELAKRAFapAGIPLELLHVNTGHNFPEVIEFRDKIA 88
Cdd:cd01986 1 VVVGYSGGKDSSVALHLASRLG--RKAEVAVVHIDHGIGFKEEAESVASIA 49
|
|
| TilS_N |
cd01992 |
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ... |
42-113 |
2.63e-04 |
|
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine synthase (EC 6.3.4.19), also called tRNA(Ile)-2-lysyl-cytidine synthase or tRNA(Ile)-lysidine synthetase, catalyzes the ligation of lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. This subfamily belongs to the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This domain has a strongly conserved motif SGGXD at the N-terminus.
Pssm-ID: 467496 [Multi-domain] Cd Length: 185 Bit Score: 41.04 E-value: 2.63e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896167334 42 FSGGKDSVVVLELAKRAFAPAGIPLELLHVNtgHNF----PEVIEFRDKIAAQPGIKLHVAKVQDWIDSGVLTERA 113
Cdd:cd01992 6 VSGGPDSMALLHLLKELRPKLGLKLVAVHVD--HGLreesAEEAQFVAKLCKKLGIPLHILTVTEAPKSGGNLEAA 79
|
|
| ATP_bind_3 |
pfam01171 |
PP-loop family; This family of proteins belongs to the PP-loop superfamily. |
42-101 |
4.28e-04 |
|
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
Pssm-ID: 426097 [Multi-domain] Cd Length: 178 Bit Score: 40.30 E-value: 4.28e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896167334 42 FSGGKDSVVVLELAKRAFAPAGIPLELLHVNtgHNF----PEVIEFRDKIAAQPGIKLHVAKVQ 101
Cdd:pfam01171 3 VSGGPDSMALLYLLAKLKIKLGIELTAAHVN--HGLreesDREAEHVQALCRQLGIPLEILRVD 64
|
|
| CTU1-like |
cd01713 |
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ... |
36-119 |
7.28e-04 |
|
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human cytoplasmic tRNA 2-thiolation protein 1, also called cytosolic thiouridylase subunit 1 (CTU1), ATP-binding domain-containing protein 3 (ATPBD3), cancer-associated gene protein, or cytoplasmic tRNA adenylyltransferase 1. CTU1 plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). It directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. The CTU1-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.
Pssm-ID: 467486 Cd Length: 208 Bit Score: 39.88 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 36 DRPALLFSGGKDSVVVL----ELAKRafAPAGIPLELLHVNTGHNF--PEVIEFRDKIAAQPGIKLHVAKVQD----WID 105
Cdd:cd01713 19 DRVAVGLSGGKDSTVLLyvlkELNKR--HDYGVELIAVTIDEGIKGyrDDSLEAARKLAEEYGIPLEIVSFEDefgfTLD 96
|
90
....*....|....
gi 896167334 106 SGVLTerADGTRNP 119
Cdd:cd01713 97 ELIVG--KGGKKNA 108
|
|
| TtcA-like |
cd24138 |
tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) ... |
36-112 |
1.21e-03 |
|
tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) 2-sulfurtransferase, also called two-thiocytidine biosynthesis protein A or tRNA 2-thiocytidine biosynthesis protein TtcA, catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). TtcA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus.
Pssm-ID: 467514 [Multi-domain] Cd Length: 187 Bit Score: 39.18 E-value: 1.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896167334 36 DRPALLFSGGKDSVVVLELAK--RAFAPAGIPLELLHVNTGhnFPEVIEFRDKIAAQPGIKLHVAKVQDWIDSGVLTER 112
Cdd:cd24138 9 DRILVGLSGGKDSLTLLHLLEelKRRAPIKFELVAVTVDPG--YPGYRPPREELAEILEELGEILEDEESEIIIIEKER 85
|
|
| lysidine_TilS_N |
TIGR02432 |
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ... |
42-101 |
2.59e-03 |
|
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble position of a tRNA must discriminate between G and A of mRNA are AUA (Ile) vs. AUG (Met) and UGA (stop) vs. UGG (Trp). In all bacteria, the wobble position of the tRNA(Ile) recognizing AUA is lysidine, a lysine derivative of cytidine. This family describes a protein domain found, apparently, in all bacteria in a single copy. Eukaryotic sequences appear to be organellar. The domain archictecture of this protein family is variable; some, including characterized proteins of E. coli and B. subtilis known to be tRNA(Ile)-lysidine synthetase, include a conserved 50-residue domain that many other members lack. This protein belongs to the ATP-binding PP-loop family ( pfam01171). It appears in the literature and protein databases as TilS, YacA, and putative cell cycle protein MesJ (a misnomer). [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 274129 [Multi-domain] Cd Length: 189 Bit Score: 38.38 E-value: 2.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896167334 42 FSGGKDSVVVLELAKRAFAPAGIPLELLHVNtgHNF----PEVIEFRDKIAAQPGIKLHVAKVQ 101
Cdd:TIGR02432 6 VSGGVDSMALLHLLLKLQPKIKIKLIAAHVD--HGLrpesDEEAEFVQQFCRKLNIPLEIKKVD 67
|
|
| TtuA-like |
cd01993 |
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ... |
43-119 |
2.95e-03 |
|
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) 2-sulfurtransferase, also called tRNA thiouridine synthetase TtuA, catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T). TtuA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus.
Pssm-ID: 467497 [Multi-domain] Cd Length: 190 Bit Score: 38.08 E-value: 2.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896167334 43 SGGKDSVVVLELAKRafapAGIPLELLHVNTG-HNFPE-VIEFRDKIAAQPGIKLHVAKVQDWIDSGVlTERADGTRNP 119
Cdd:cd01993 16 SGGKDSLALLAVLKK----LGYNVEALYINLGiGEYSEkSEEVVKKLAEKLNLPLHVVDLKEEYGLGI-PELAKKSRRP 89
|
|
| COG2117 |
COG2117 |
Predicted subunit of tRNA(5-methylaminomethyl-2-thiouridylate) methyltransferase, contains the ... |
39-144 |
3.96e-03 |
|
Predicted subunit of tRNA(5-methylaminomethyl-2-thiouridylate) methyltransferase, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; Predicted subunit of tRNA(5-methylaminomethyl-2-thiouridylate) methyltransferase, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 441720 Cd Length: 196 Bit Score: 37.88 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896167334 39 ALLFSGGKDSVVVLELAKRAFAPagiplELLHVNTGHNfpEVIEFRDKIAAQPGIKLHVAKvqdwIDSGVLTE-----RA 113
Cdd:COG2117 3 AVLYSGGKDSSLAALLLERFYDV-----ELVTANFGIT--DSWKHAREAAEALGFPHRVLE----LDRGVLEEavdmiIE 71
|
90 100 110
....*....|....*....|....*....|....
gi 896167334 114 DG-TRNPLQTVPL--VETIANRGYDAVLGGARRD 144
Cdd:COG2117 72 DGyPRNGIQYVHEhaLEALADLEYDAIADGTRRD 105
|
|
| |
