|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02309 |
PLN02309 |
5'-adenylylsulfate reductase |
59-339 |
0e+00 |
|
5'-adenylylsulfate reductase
Pssm-ID: 215175 [Multi-domain] Cd Length: 457 Bit Score: 598.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 59 DLKVTKIGSLRLLNRTNVSAASLSLSGKRSS-VKALNVQSITKESIVASEVTEKLDV----VEVEDFEELAKRLENASPL 133
Cdd:PLN02309 20 ESKAKQIGSLRLLDRGGLSARAYSLSGKRSSaAKPLNAQPAARQAMIPSAATAVAEVpeeeGEVEDFEKLAKELENASPL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 134 EIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYGIRIEYMFPDAVEVQALV 213
Cdd:PLN02309 100 EIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRLFDAVEKHYGIRIEYMFPDAVEVQALV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 214 RNKGLFSFYEDGHQECCRIRKVRPLRRALKGLRAWITGQRKDQSPGTRSEIPVVQVDPVFEGLDGGVGSLVKWNPVANVE 293
Cdd:PLN02309 180 RNKGLFSFYEDGHQECCRVRKVRPLRRALKGLRAWITGQRKDQSPGTRAEVPVVQVDPVFEGLDGGPGSLVKWNPLANVT 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 334186800 294 GNDVWNFLRTMDVPVNTLHAAGYVSIGCEPCTRAVLPGQHEREGRW 339
Cdd:PLN02309 260 GNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCTRPVLPGQHEREGRW 305
|
|
| APS_reduc |
TIGR00424 |
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ... |
36-339 |
0e+00 |
|
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: 586.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 36 MALAINVSSSSSS-AISSSSFPSSDLKVTKIGSLRLLNRTNVSAASLSLSGKRSSVKALNVQSITKESIVASEVT----- 109
Cdd:TIGR00424 1 MALAVTSSSTAISgISLSRSGESTEAKAAQIGSFRLLDRPHTISPSVNLSRRRLSVKPLNAEPKRNESIVPSAATtvape 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 110 EKLDVVEVEDFEELAKRLENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFD 189
Cdd:TIGR00424 81 VEEKVVEVEDFEKLAKKLENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRFFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 190 TVEKHYGIRIEYMFPDAVEVQALVRNKGLFSFYEDGHQECCRIRKVRPLRRALKGLRAWITGQRKDQSPGTRSEIPVVQV 269
Cdd:TIGR00424 161 AVEKQYGIRIEYMFPDAVEVQALVRSKGLFSFYEDGHQECCRVRKVRPLRRALKGLKAWITGQRKDQSPGTRSEIPVVQV 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 270 DPVFEGLDGGVGSLVKWNPVANVEGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPCTRAVLPGQHEREGRW 339
Cdd:TIGR00424 241 DPVFEGLDGGVGSLVKWNPVANVEGKDVWNFLRTMDVPVNTLHAQGYVSIGCEPCTRPVLPGQHEREGRW 310
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
118-340 |
1.42e-77 |
|
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: 237.44 E-value: 1.42e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 118 EDFEELAKRLEnASPLEIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYG 196
Cdd:COG0175 8 DLLEELNAELE-AEAIEILREAAAEFGGRVVVSSSgGKDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDRLAERLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 197 IRIEYMFPDAVEVQALVRnKGLFSFYEDgHQECCRIRKVRPLRRALKGLR--AWITGQRKDQSPgTRSEIPVVQVDPVFE 274
Cdd:COG0175 87 LDLIVVRPEDAFAEQLAE-FGPPLFYRD-PRWCCKIRKVEPLKRALAGYDfdAWITGLRRDESP-TRAKEPVVEWDPVGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334186800 275 gldggvgsLVKWNPVANVEGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPCTRAVLPGQHEREGRWD 340
Cdd:COG0175 164 --------LIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWW 221
|
|
| PAPS_reductase |
cd23945 |
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ... |
132-320 |
6.03e-75 |
|
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: 6.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 132 PLEIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYGIRIEYMFPDAVEVQ 210
Cdd:cd23945 1 PLEILLWAAEEFGPKLVFATSfGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYGLNIEVYFPEGTEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 211 ALVRNKGL--FSFYEDGHQECCRIRKVRPLRRALKGLRAWITGQRKDQSPgTRSEIPVVQVDpvfegldgGVGSLVKWNP 288
Cdd:cd23945 81 EEALEGGLneFYLEDEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSP-TRANLPIVEVD--------EEGGLVKINP 151
|
170 180 190
....*....|....*....|....*....|..
gi 334186800 289 VANVEGNDVWNFLRTMDVPVNTLHAAGYVSIG 320
Cdd:cd23945 152 LADWTWEDVWAYIREHDLPYNPLHDQGYPSIG 183
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
147-327 |
2.63e-58 |
|
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: 185.96 E-value: 2.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 147 IAIAFS-GAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYGIRIEYMFPDAVEVQALVRNKGLFSFYedg 225
Cdd:pfam01507 2 LVVSFSgGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSSLY--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 226 hQECCRIRKVRPLRRALK--GLRAWITGQRKDQSPgTRSEIPVVQVDPVFEGLdggvgslVKWNPVANVEGNDVWNFLRT 303
Cdd:pfam01507 79 -RRCCRLRKVEPLKRALKelGFDAWFTGLRRDESP-SRAKLPIVSIDGDFPKV-------IKVFPLLNWTETDVWQYILA 149
|
170 180
....*....|....*....|....
gi 334186800 304 MDVPVNTLHAAGYVSIGCEPCTRA 327
Cdd:pfam01507 150 NNVPYNPLYDQGYRSIGCYPCTGP 173
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02309 |
PLN02309 |
5'-adenylylsulfate reductase |
59-339 |
0e+00 |
|
5'-adenylylsulfate reductase
Pssm-ID: 215175 [Multi-domain] Cd Length: 457 Bit Score: 598.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 59 DLKVTKIGSLRLLNRTNVSAASLSLSGKRSS-VKALNVQSITKESIVASEVTEKLDV----VEVEDFEELAKRLENASPL 133
Cdd:PLN02309 20 ESKAKQIGSLRLLDRGGLSARAYSLSGKRSSaAKPLNAQPAARQAMIPSAATAVAEVpeeeGEVEDFEKLAKELENASPL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 134 EIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYGIRIEYMFPDAVEVQALV 213
Cdd:PLN02309 100 EIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRLFDAVEKHYGIRIEYMFPDAVEVQALV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 214 RNKGLFSFYEDGHQECCRIRKVRPLRRALKGLRAWITGQRKDQSPGTRSEIPVVQVDPVFEGLDGGVGSLVKWNPVANVE 293
Cdd:PLN02309 180 RNKGLFSFYEDGHQECCRVRKVRPLRRALKGLRAWITGQRKDQSPGTRAEVPVVQVDPVFEGLDGGPGSLVKWNPLANVT 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 334186800 294 GNDVWNFLRTMDVPVNTLHAAGYVSIGCEPCTRAVLPGQHEREGRW 339
Cdd:PLN02309 260 GNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCTRPVLPGQHEREGRW 305
|
|
| APS_reduc |
TIGR00424 |
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ... |
36-339 |
0e+00 |
|
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: 586.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 36 MALAINVSSSSSS-AISSSSFPSSDLKVTKIGSLRLLNRTNVSAASLSLSGKRSSVKALNVQSITKESIVASEVT----- 109
Cdd:TIGR00424 1 MALAVTSSSTAISgISLSRSGESTEAKAAQIGSFRLLDRPHTISPSVNLSRRRLSVKPLNAEPKRNESIVPSAATtvape 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 110 EKLDVVEVEDFEELAKRLENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFD 189
Cdd:TIGR00424 81 VEEKVVEVEDFEKLAKKLENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRFFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 190 TVEKHYGIRIEYMFPDAVEVQALVRNKGLFSFYEDGHQECCRIRKVRPLRRALKGLRAWITGQRKDQSPGTRSEIPVVQV 269
Cdd:TIGR00424 161 AVEKQYGIRIEYMFPDAVEVQALVRSKGLFSFYEDGHQECCRVRKVRPLRRALKGLKAWITGQRKDQSPGTRSEIPVVQV 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 270 DPVFEGLDGGVGSLVKWNPVANVEGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPCTRAVLPGQHEREGRW 339
Cdd:TIGR00424 241 DPVFEGLDGGVGSLVKWNPVANVEGKDVWNFLRTMDVPVNTLHAQGYVSIGCEPCTRPVLPGQHEREGRW 310
|
|
| PRK02090 |
PRK02090 |
phosphoadenylyl-sulfate reductase; |
118-339 |
2.91e-92 |
|
phosphoadenylyl-sulfate reductase;
Pssm-ID: 234997 Cd Length: 241 Bit Score: 275.18 E-value: 2.91e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 118 EDFEELAKRLENASPLEIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYG 196
Cdd:PRK02090 14 LDLAELNAELEGASAQERLAWALENFGGRLALVSSfGAEDAVLLHLVAQVDPDIPVIFLDTGYLFPETYRFIDELTERLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 197 IRIEYMFPDAVEVQALVRNKGLFSFYEDGHQECCRIRKVRPLRRALKGLRAWITGQRKDQSPgTRSEIPVVQVDpvfegl 276
Cdd:PRK02090 94 LNLKVYRPDASAAEQEARYGGLWEQSVEDRDECCRIRKVEPLNRALAGLDAWITGLRREQSG-TRANLPVLEID------ 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334186800 277 dggvGSLVKWNPVANVEGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPCTRAVLPGQHEREGRW 339
Cdd:PRK02090 167 ----GGRFKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGRW 225
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
118-340 |
1.42e-77 |
|
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: 237.44 E-value: 1.42e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 118 EDFEELAKRLEnASPLEIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYG 196
Cdd:COG0175 8 DLLEELNAELE-AEAIEILREAAAEFGGRVVVSSSgGKDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDRLAERLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 197 IRIEYMFPDAVEVQALVRnKGLFSFYEDgHQECCRIRKVRPLRRALKGLR--AWITGQRKDQSPgTRSEIPVVQVDPVFE 274
Cdd:COG0175 87 LDLIVVRPEDAFAEQLAE-FGPPLFYRD-PRWCCKIRKVEPLKRALAGYDfdAWITGLRRDESP-TRAKEPVVEWDPVGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334186800 275 gldggvgsLVKWNPVANVEGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPCTRAVLPGQHEREGRWD 340
Cdd:COG0175 164 --------LIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWW 221
|
|
| APS_reductase |
TIGR02055 |
thioredoxin-dependent adenylylsulfate APS reductase; This model describes recently identified ... |
152-339 |
3.92e-77 |
|
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: 234.66 E-value: 3.92e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 152 SGAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYGIRIEYMFPDAVEVQALVRNKGLFSFYEDGHQECCR 231
Cdd:TIGR02055 1 LGAEDVVLVDLAAKVRPDVKVFFLDTGRLFKETYETIDQVRERYDILIDVLSPPPLTVEEQVKEYGLNLFYRSVPHECCG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 232 IRKVRPLRRALKGLRAWITGQRKDQSPgTRSEIPVVQVDpvfegldgGVGSLVKWNPVANVEGNDVWNFLRTMDVPVNTL 311
Cdd:TIGR02055 81 IRKVEPLKRALAGVSAWITGLRRDQSP-TRAQAPFLEID--------EAFGLVKINPLADWTSEDVWEYIADNELPYNPL 151
|
170 180
....*....|....*....|....*...
gi 334186800 312 HAAGYVSIGCEPCTRAVLPGQHEREGRW 339
Cdd:TIGR02055 152 HDRGYPSIGCEPCTRPVAPGEDPRAGRW 179
|
|
| PAPS_reductase |
cd23945 |
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ... |
132-320 |
6.03e-75 |
|
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: 6.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 132 PLEIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYGIRIEYMFPDAVEVQ 210
Cdd:cd23945 1 PLEILLWAAEEFGPKLVFATSfGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYGLNIEVYFPEGTEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 211 ALVRNKGL--FSFYEDGHQECCRIRKVRPLRRALKGLRAWITGQRKDQSPgTRSEIPVVQVDpvfegldgGVGSLVKWNP 288
Cdd:cd23945 81 EEALEGGLneFYLEDEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSP-TRANLPIVEVD--------EEGGLVKINP 151
|
170 180 190
....*....|....*....|....*....|..
gi 334186800 289 VANVEGNDVWNFLRTMDVPVNTLHAAGYVSIG 320
Cdd:cd23945 152 LADWTWEDVWAYIREHDLPYNPLHDQGYPSIG 183
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
147-327 |
2.63e-58 |
|
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: 185.96 E-value: 2.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 147 IAIAFS-GAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYGIRIEYMFPDAVEVQALVRNKGLFSFYedg 225
Cdd:pfam01507 2 LVVSFSgGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSSLY--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 226 hQECCRIRKVRPLRRALK--GLRAWITGQRKDQSPgTRSEIPVVQVDPVFEGLdggvgslVKWNPVANVEGNDVWNFLRT 303
Cdd:pfam01507 79 -RRCCRLRKVEPLKRALKelGFDAWFTGLRRDESP-SRAKLPIVSIDGDFPKV-------IKVFPLLNWTETDVWQYILA 149
|
170 180
....*....|....*....|....
gi 334186800 304 MDVPVNTLHAAGYVSIGCEPCTRA 327
Cdd:pfam01507 150 NNVPYNPLYDQGYRSIGCYPCTGP 173
|
|
| cysH |
TIGR00434 |
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ... |
132-339 |
6.96e-42 |
|
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: 144.93 E-value: 6.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 132 PLEIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYGIRIEYMFPD--AVE 208
Cdd:TIGR00434 1 AQEIIAWAYVTFGGHLVYSTSfGIQGAVLLDLVSKISPDIPVIFLDTGYHFPETYELIDELTERYPLNIKVYKPDlsLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 209 VQALVRNKglfsFYEDGHQECCRIRKVRPLRRALKGL--RAWITGQRKDQSPgTRSEIPVVQVDPVFEgldggvgsLVKW 286
Cdd:TIGR00434 81 QAAKYGDK----LWEQDPNKYDYLRKVEPMHRALKELhaSAWFTGLRRDQGP-SRANLSILNIDEKFG--------ILKV 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 334186800 287 NPVANVEGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPCTRAVLPGQHEREGRW 339
Cdd:TIGR00434 148 LPLIDWTWKDVYQYIDAHNLPYNPLHDQGYPSIGDYHSTRPVKEGEDERAGRW 200
|
|
| PAPS_reductase-like_YbdN |
cd23947 |
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ... |
133-326 |
2.56e-14 |
|
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: 70.88 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 133 LEIMDKALEKFgNDIAIAFSGAED--VAL---IEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYGIRIEYMFPD-- 205
Cdd:cd23947 2 LERIRKVFEEF-DPVIVSFSGGKDslVLLhlaLEALRRLRKDVYVVFIDTGIEFPETIDFVEKLAETLGLDVEAARPPlf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 206 ------AVEVQALVRNKGL-FSFYEDGhqeCCRIRKVRPLRRALKGLR----AWITGQRKDQSPgTRSEIPVVQvdpvfe 274
Cdd:cd23947 81 lewltsNFQPQWDPIWDNPpPPRDYRW---CCDELKLEPFTKWLKEKKpegvLLLVGIRADESL-NRAKRPRVY------ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 334186800 275 gldGGVGSLVKWNPVANV-------EGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPCTR 326
Cdd:cd23947 151 ---RKYGWRNSTLPGQIVaypikdwSVEDVWLYILRHGLPYNPLYDLGFDRGGCLVCPR 206
|
|
| PRK13795 |
PRK13795 |
hypothetical protein; Provisional |
113-324 |
2.35e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 49.22 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 113 DVVEVEDfEELAKRLENAspLEIMDKALEKFGNDIAIAFSGAED--VALieyaHLT---GRPYRVFSLDTGRLNPETYRL 187
Cdd:PRK13795 215 DAIEANR-KHLEEKEKEA--VNFIRGVAEKYNLPVSVSFSGGKDslVVL----DLAreaLKDFKAFFNNTGLEFPETVEN 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 188 FDTVEKHYGIRIEYM-----FPDAVEVqalvrnkglFSFYEDGHQECCRIRKVRPLRRALK--GLRAWIT--GQRKDQSp 258
Cdd:PRK13795 288 VKEVAEEYGIELIEAdagdaFWRAVEK---------FGPPARDYRWCCKVCKLGPITRAIKenFPKGCLTfvGQRKYES- 357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334186800 259 GTRSEIPVVQVDPVfegldggVGSLVKWNPVANVEGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPC 324
Cdd:PRK13795 358 FSRAKSPRVWRNPW-------VPNQIGASPIQDWTALEVWLYIFWRKLPYNPLYERGFDRIGCWLC 416
|
|
| FAD_synthase |
cd23948 |
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ... |
133-320 |
3.66e-06 |
|
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; Flavin adenine dinucleotide synthase (FADS); EC 2.7.7.2) is involved in the biochemical pathway for converting riboflavin into FAD. By sequence comparison, bacterial and eukaryotic FMNAT enzymes belong to two different protein superfamilies and apparently utilize different sets of active-site residues to accomplish the same chemistry. This subfamily includes eukaryotic FMNATs, which are members of the 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase-like family belonging to the adenine nucleotide alpha hydrolase superfamily, which has conserved motifs different from those of nucleotidylyl transferases.
Pssm-ID: 467513 [Multi-domain] Cd Length: 179 Bit Score: 46.75 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 133 LEIMDKALEKFGND-IAIAFSGAED-VALIeyaHLTgrpYRVFsldtGRLNPETYRLFDTVekhYgIRIEYMFPdavEVQ 210
Cdd:cd23948 6 LEVIEEALDKYGPEeIAISFNGGKDcTVLL---HLL---RAAL----KRKYPSPLTPLKAL---Y-IKSPDPFP---EVE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 211 ALVrnkglfsfyedghQECCR------IRKVRPLRRALKGL-------RAWITGQRKDqSPGTRSEIPVVQVDPvfegld 277
Cdd:cd23948 69 EFV-------------EDTAKrynldlITIDGPMKEGLEELlkehpiiKAVFMGTRRT-DPHGENLKPFSPTDP------ 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 334186800 278 ggvgslvKW------NPVANVEGNDVWNFLRTMDVPVNTLHAAGYVSIG 320
Cdd:cd23948 129 -------GWpqfmrvNPILDWSYHDVWEFLRTLNLPYCSLYDQGYTSLG 170
|
|
| PRK13794 |
PRK13794 |
hypothetical protein; Provisional |
117-324 |
4.02e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 237509 [Multi-domain] Cd Length: 479 Bit Score: 48.13 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 117 VEDFEELAKRLENASpLEIMDKALEKFGNDIAIAFSGAED--VALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKH 194
Cdd:PRK13794 221 VEANKNVLDKYERNS-IGFIRNTAEKINKPVTVAYSGGKDslATLLLALKALGINFPVLFNDTGLEFPETLENVEDVEKH 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 195 YGIRIeymfpdavevqalVRNKGLfSFYEDGHQE---------CCRIRKVRPLRRAL-----KGLRAWItGQRKDQSpGT 260
Cdd:PRK13794 300 YGLEI-------------IRTKSE-EFWEKLEEYgppardnrwCSEVCKLEPLGKLIdekyeGECLSFV-GQRKYES-FN 363
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334186800 261 RSEIPVVQVDPVfegldggVGSLVKWNPVANVEGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPC 324
Cdd:PRK13794 364 RSKKPRIWRNPY-------IKKQILAAPILHWTAMHVWIYLFREKAPYNKLYEQGFDRIGCFMC 420
|
|
| Sulfate_adenylyltransferase_2 |
cd23946 |
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ... |
125-314 |
5.09e-05 |
|
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: 43.64 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 125 KRLENASpLEIMDKALEKFGNdIAIAFSGAEDVA----LIEYAHLTGR-PYRVFSLDTGRLNPETYRLFDTVEKHYGIR- 198
Cdd:cd23946 3 RQLEAES-IHIIREVAAEFSN-PVMLYSIGKDSSvmlhLARKAFYPGKpPFPLLHVDTTWKFREMIEFRDRVAKEYGLDl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 199 IEYMFPDAVEvqalvrnKGLFSFYEdGHQECCRIRKVRPLRRALK--GLRAWITGQRKDQSpGTRSEIPVVQVDPVFEGL 276
Cdd:cd23946 81 IVHVNPDGVE-------AGINPFTH-GSAKHTDIMKTEGLKQALDkyGFDAAFGGARRDEE-KSRAKERVYSFRDSNHRW 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 334186800 277 DG---------------GVGSLVKWNPVANVEGNDVWNFLRTMDVPVNTLHAA 314
Cdd:cd23946 152 DPknqrpelwnqyngrvKKGESIRVFPLSNWTELDIWQYIYLENIPIVPLYFA 204
|
|
| PRK08557 |
PRK08557 |
hypothetical protein; Provisional |
117-328 |
2.92e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 181465 [Multi-domain] Cd Length: 417 Bit Score: 42.43 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 117 VEDFEELAKRLENASpLEIMDKALEKFGND---IAIAFSGAEDVALIEY-AHLTGRPYRVFSLDTGRLNPETYRLFDTVE 192
Cdd:PRK08557 152 LEKNKERIEKLEENS-LSILKDYIEKYKNKgyaINASFSGGKDSSVSTLlAKEVIPDLEVIFIDTGLEYPETINYVKDFA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 193 KHYGIRIEYMFPDavevqalvrnkglfSFYEDGHQE---------CCRIRKVRPLRRALKGLRAW-----ITGQRKDQSp 258
Cdd:PRK08557 231 KKYDLNLDTLDGD--------------NFWENLEKEgiptkdnrwCNSACKLMPLKEYLKKKYGNkkvltIDGSRKYES- 295
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186800 259 GTRSEIPvvqvdpvFEGLDGGVGSLVKWNPVANVEGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPCTRAV 328
Cdd:PRK08557 296 FTRANLD-------YERKSGFIDFQTNVFPILDWNSLDIWSYIYLNDILYNPLYDKGFERIGCYLCPSAL 358
|
|
| |
