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Conserved domains on  [gi|2064737281|ref|WP_217848497|]
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phosphoadenylyl-sulfate reductase [Pseudomonas muyukensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02309 super family cl33459
5'-adenylylsulfate reductase
 6-240 1.52e-124

5'-adenylylsulfate reductase


The actual alignment was detected with superfamily member PLN02309:

Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 361.03  E-value: 1.52e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281   6 DVAALAATYASKSPQEILKLAFEHFGDDLWISFSGAEDVVLVDMAWKLNKQVKVFSLDTGRLHPETYRFIDQVREQYNLP 85
Cdd:PLN02309   85 DFEKLAKELENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRLFDAVEKHYGIR 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  86 IEILSPDRDKLDPFVKEKGLFSFYKDGHGECCGIRKIEPLRRKLATVSAWATGQRRDQSPGTRSQVAALEVDSAF----S 161
Cdd:PLN02309  165 IEYMFPDAVEVQALVRNKGLFSFYEDGHQECCRVRKVRPLRRALKGLRAWITGQRKDQSPGTRAEVPVVQVDPVFegldG 244

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2064737281 162 TPErTLYKFNPLAQMTSEEVWGYIRMLELPYNSLHERGFISIGCEPCTRPVLPNQHEREGRWWWEESTQKECGLHAGNL 240
Cdd:PLN02309  245 GPG-SLVKWNPLANVTGNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCTRPVLPGQHEREGRWWWEDAKAKECGLHKGNI 322
 
Name Accession Description Interval E-value
PLN02309 PLN02309
5'-adenylylsulfate reductase
 6-240 1.52e-124

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 361.03  E-value: 1.52e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281   6 DVAALAATYASKSPQEILKLAFEHFGDDLWISFSGAEDVVLVDMAWKLNKQVKVFSLDTGRLHPETYRFIDQVREQYNLP 85
Cdd:PLN02309   85 DFEKLAKELENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRLFDAVEKHYGIR 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  86 IEILSPDRDKLDPFVKEKGLFSFYKDGHGECCGIRKIEPLRRKLATVSAWATGQRRDQSPGTRSQVAALEVDSAF----S 161
Cdd:PLN02309  165 IEYMFPDAVEVQALVRNKGLFSFYEDGHQECCRVRKVRPLRRALKGLRAWITGQRKDQSPGTRAEVPVVQVDPVFegldG 244

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2064737281 162 TPErTLYKFNPLAQMTSEEVWGYIRMLELPYNSLHERGFISIGCEPCTRPVLPNQHEREGRWWWEESTQKECGLHAGNL 240
Cdd:PLN02309  245 GPG-SLVKWNPLANVTGNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCTRPVLPGQHEREGRWWWEDAKAKECGLHKGNI 322
APS_reductase TIGR02055
thioredoxin-dependent adenylylsulfate APS reductase; This model describes recently identified ...
 39-235 8.82e-113

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: 321.33  E-value: 8.82e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  39 SGAEDVVLVDMAWKLNKQVKVFSLDTGRLHPETYRFIDQVREQYNLPIEILSPDRDKLDPFVKEKGLFSFYKDGHGECCG 118
Cdd:TIGR02055   1 LGAEDVVLVDLAAKVRPDVKVFFLDTGRLFKETYETIDQVRERYDILIDVLSPPPLTVEEQVKEYGLNLFYRSVPHECCG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281 119 IRKIEPLRRKLATVSAWATGQRRDQSPgTRSQVAALEVDSAFStpertLYKFNPLAQMTSEEVWGYIRMLELPYNSLHER 198
Cdd:TIGR02055  81 IRKVEPLKRALAGVSAWITGLRRDQSP-TRAQAPFLEIDEAFG-----LVKINPLADWTSEDVWEYIADNELPYNPLHDR 154

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2064737281 199 GFISIGCEPCTRPVLPNQHEREGRWWWEESTQKECGL 235
Cdd:TIGR02055 155 GYPSIGCEPCTRPVAPGEDPRAGRWWWEEAAKKECGL 191
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 6-235 3.82e-94

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: 275.57  E-value: 3.82e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281   6 DVAALAATYASkSPQEILKLAFEHFGDDLWISFS-GAEDVVLVDMAWKLNKQVKVFSLDTGRLHPETYRFIDQVREQYNL 84
Cdd:COG0175     9 LLEELNAELEA-EAIEILREAAAEFGGRVVVSSSgGKDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDRLAERLGL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  85 PIEILSPDRDKLDPFVkEKGLFSFYKDgHGECCGIRKIEPLRRKLATVS--AWATGQRRDQSPgTRSQVAALEVDsafst 162
Cdd:COG0175    88 DLIVVRPEDAFAEQLA-EFGPPLFYRD-PRWCCKIRKVEPLKRALAGYDfdAWITGLRRDESP-TRAKEPVVEWD----- 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064737281 163 PERTLYKFNPLAQMTSEEVWGYIRMLELPYNSLHERGFISIGCEPCTRPVLPNQHEREGRWWWEESTQKECGL 235
Cdd:COG0175   160 PVGGLIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWWDEEKERKECGL 232
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 19-204 2.64e-72

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: 218.62  E-value: 2.64e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  19 PQEILKLAFEHFGDDL-WISFSGAEDVVLVDMAWKLNKQVKVFSLDTGRLHPETYRFIDQVREQYNLPIEILSPDRDKLD 97
Cdd:cd23945     1 PLEILLWAAEEFGPKLvFATSFGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYGLNIEVYFPEGTEAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  98 PFVKEKGL--FSFYKDGHGECCGIRKIEPLRRKLATVSAWATGQRRDQSPgTRSQVAALEVDSafstpERTLYKFNPLAQ 175
Cdd:cd23945    81 EEALEGGLneFYLEDEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSP-TRANLPIVEVDE-----EGGLVKINPLAD 154

                         170       180
                  ....*....|....*....|....*....
gi 2064737281 176 MTSEEVWGYIRMLELPYNSLHERGFISIG 204
Cdd:cd23945   155 WTWEDVWAYIREHDLPYNPLHDQGYPSIG 183
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 34-211 7.06e-62

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: 191.74  E-value: 7.06e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  34 LWISFS-GAEDVVLVDMAWKLNKQVKVFSLDTGRLHPETYRFIDQVREQYNLPIEILSPDRDKLDPFVKEKGLFSFYkdg 112
Cdd:pfam01507   2 LVVSFSgGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSSLY--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281 113 hGECCGIRKIEPLRRKLAT--VSAWATGQRRDQSPgTRSQVAALEVDSAFStperTLYKFNPLAQMTSEEVWGYIRMLEL 190
Cdd:pfam01507  79 -RRCCRLRKVEPLKRALKElgFDAWFTGLRRDESP-SRAKLPIVSIDGDFP----KVIKVFPLLNWTETDVWQYILANNV 152

                         170       180
                  ....*....|....*....|.
gi 2064737281 191 PYNSLHERGFISIGCEPCTRP 211
Cdd:pfam01507 153 PYNPLYDQGYRSIGCYPCTGP 173
 
Name Accession Description Interval E-value
PLN02309 PLN02309
5'-adenylylsulfate reductase
 6-240 1.52e-124

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 361.03  E-value: 1.52e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281   6 DVAALAATYASKSPQEILKLAFEHFGDDLWISFSGAEDVVLVDMAWKLNKQVKVFSLDTGRLHPETYRFIDQVREQYNLP 85
Cdd:PLN02309   85 DFEKLAKELENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRLFDAVEKHYGIR 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  86 IEILSPDRDKLDPFVKEKGLFSFYKDGHGECCGIRKIEPLRRKLATVSAWATGQRRDQSPGTRSQVAALEVDSAF----S 161
Cdd:PLN02309  165 IEYMFPDAVEVQALVRNKGLFSFYEDGHQECCRVRKVRPLRRALKGLRAWITGQRKDQSPGTRAEVPVVQVDPVFegldG 244

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2064737281 162 TPErTLYKFNPLAQMTSEEVWGYIRMLELPYNSLHERGFISIGCEPCTRPVLPNQHEREGRWWWEESTQKECGLHAGNL 240
Cdd:PLN02309  245 GPG-SLVKWNPLANVTGNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCTRPVLPGQHEREGRWWWEDAKAKECGLHKGNI 322
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
1-241 5.21e-120

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 341.43  E-value: 5.21e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281   1 MSQPFDVAALAATYASKSPQEILKLAFEHFGDDL-WISFSGAEDVVLVDMAWKLNKQVKVFSLDTGRLHPETYRFIDQVR 79
Cdd:PRK02090   10 ADLALDLAELNAELEGASAQERLAWALENFGGRLaLVSSFGAEDAVLLHLVAQVDPDIPVIFLDTGYLFPETYRFIDELT 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  80 EQYNLPIEILSPDRDKLDPFVKEKGLFSFYKDGHGECCGIRKIEPLRRKLATVSAWATGQRRDQSPgTRSQVAALEVDsa 159
Cdd:PRK02090   90 ERLLLNLKVYRPDASAAEQEARYGGLWEQSVEDRDECCRIRKVEPLNRALAGLDAWITGLRREQSG-TRANLPVLEID-- 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281 160 fstpeRTLYKFNPLAQMTSEEVWGYIRMLELPYNSLHERGFISIGCEPCTRPVLPNQHEREGRWWweESTQKECGLHAGN 239
Cdd:PRK02090  167 -----GGRFKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGRWW--GGLKKECGLHEGN 239


                  ..
gi 2064737281 240 LI 241
Cdd:PRK02090  240 LP 241
APS_reductase TIGR02055
thioredoxin-dependent adenylylsulfate APS reductase; This model describes recently identified ...
 39-235 8.82e-113

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: 321.33  E-value: 8.82e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  39 SGAEDVVLVDMAWKLNKQVKVFSLDTGRLHPETYRFIDQVREQYNLPIEILSPDRDKLDPFVKEKGLFSFYKDGHGECCG 118
Cdd:TIGR02055   1 LGAEDVVLVDLAAKVRPDVKVFFLDTGRLFKETYETIDQVRERYDILIDVLSPPPLTVEEQVKEYGLNLFYRSVPHECCG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281 119 IRKIEPLRRKLATVSAWATGQRRDQSPgTRSQVAALEVDSAFStpertLYKFNPLAQMTSEEVWGYIRMLELPYNSLHER 198
Cdd:TIGR02055  81 IRKVEPLKRALAGVSAWITGLRRDQSP-TRAQAPFLEIDEAFG-----LVKINPLADWTSEDVWEYIADNELPYNPLHDR 154

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2064737281 199 GFISIGCEPCTRPVLPNQHEREGRWWWEESTQKECGL 235
Cdd:TIGR02055 155 GYPSIGCEPCTRPVAPGEDPRAGRWWWEEAAKKECGL 191
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 6-240 1.32e-109

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: 323.51  E-value: 1.32e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281   6 DVAALAATYASKSPQEILKLAFEHFGDDLWISFSGAEDVVLVDMAWKLNKQVKVFSLDTGRLHPETYRFIDQVREQYNLP 85
Cdd:TIGR00424  90 DFEKLAKKLENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRFFDAVEKQYGIR 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  86 IEILSPDRDKLDPFVKEKGLFSFYKDGHGECCGIRKIEPLRRKLATVSAWATGQRRDQSPGTRSQVAALEVDSAFSTPE- 164
Cdd:TIGR00424 170 IEYMFPDAVEVQALVRSKGLFSFYEDGHQECCRVRKVRPLRRALKGLKAWITGQRKDQSPGTRSEIPVVQVDPVFEGLDg 249

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2064737281 165 --RTLYKFNPLAQMTSEEVWGYIRMLELPYNSLHERGFISIGCEPCTRPVLPNQHEREGRWWWEESTQKECGLHAGNL 240
Cdd:TIGR00424 250 gvGSLVKWNPVANVEGKDVWNFLRTMDVPVNTLHAQGYVSIGCEPCTRPVLPGQHEREGRWWWEDAKAKECGLHKGNI 327
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 6-235 3.82e-94

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: 275.57  E-value: 3.82e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281   6 DVAALAATYASkSPQEILKLAFEHFGDDLWISFS-GAEDVVLVDMAWKLNKQVKVFSLDTGRLHPETYRFIDQVREQYNL 84
Cdd:COG0175     9 LLEELNAELEA-EAIEILREAAAEFGGRVVVSSSgGKDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDRLAERLGL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  85 PIEILSPDRDKLDPFVkEKGLFSFYKDgHGECCGIRKIEPLRRKLATVS--AWATGQRRDQSPgTRSQVAALEVDsafst 162
Cdd:COG0175    88 DLIVVRPEDAFAEQLA-EFGPPLFYRD-PRWCCKIRKVEPLKRALAGYDfdAWITGLRRDESP-TRAKEPVVEWD----- 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064737281 163 PERTLYKFNPLAQMTSEEVWGYIRMLELPYNSLHERGFISIGCEPCTRPVLPNQHEREGRWWWEESTQKECGL 235
Cdd:COG0175   160 PVGGLIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWWDEEKERKECGL 232
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 19-204 2.64e-72

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: 218.62  E-value: 2.64e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  19 PQEILKLAFEHFGDDL-WISFSGAEDVVLVDMAWKLNKQVKVFSLDTGRLHPETYRFIDQVREQYNLPIEILSPDRDKLD 97
Cdd:cd23945     1 PLEILLWAAEEFGPKLvFATSFGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYGLNIEVYFPEGTEAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  98 PFVKEKGL--FSFYKDGHGECCGIRKIEPLRRKLATVSAWATGQRRDQSPgTRSQVAALEVDSafstpERTLYKFNPLAQ 175
Cdd:cd23945    81 EEALEGGLneFYLEDEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSP-TRANLPIVEVDE-----EGGLVKINPLAD 154

                         170       180
                  ....*....|....*....|....*....
gi 2064737281 176 MTSEEVWGYIRMLELPYNSLHERGFISIG 204
Cdd:cd23945   155 WTWEDVWAYIREHDLPYNPLHDQGYPSIG 183
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 34-211 7.06e-62

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: 191.74  E-value: 7.06e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  34 LWISFS-GAEDVVLVDMAWKLNKQVKVFSLDTGRLHPETYRFIDQVREQYNLPIEILSPDRDKLDPFVKEKGLFSFYkdg 112
Cdd:pfam01507   2 LVVSFSgGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSSLY--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281 113 hGECCGIRKIEPLRRKLAT--VSAWATGQRRDQSPgTRSQVAALEVDSAFStperTLYKFNPLAQMTSEEVWGYIRMLEL 190
Cdd:pfam01507  79 -RRCCRLRKVEPLKRALKElgFDAWFTGLRRDESP-SRAKLPIVSIDGDFP----KVIKVFPLLNWTETDVWQYILANNV 152

                         170       180
                  ....*....|....*....|.
gi 2064737281 191 PYNSLHERGFISIGCEPCTRP 211
Cdd:pfam01507 153 PYNPLYDQGYRSIGCYPCTGP 173
cysH TIGR00434
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ...
 19-236 5.36e-58

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: 183.06  E-value: 5.36e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  19 PQEILKLAFEHFGDDLWISFS-GAEDVVLVDMAWKLNKQVKVFSLDTGRLHPETYRFIDQVREQYNLPIEILSPDrDKLD 97
Cdd:TIGR00434   1 AQEIIAWAYVTFGGHLVYSTSfGIQGAVLLDLVSKISPDIPVIFLDTGYHFPETYELIDELTERYPLNIKVYKPD-LSLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  98 PFVKEKGLFsFYKDGHGECCGIRKIEPLRRKLA--TVSAWATGQRRDQSPgTRSQVAALEVDSAFStpertLYKFNPLAQ 175
Cdd:TIGR00434  80 EQAAKYGDK-LWEQDPNKYDYLRKVEPMHRALKelHASAWFTGLRRDQGP-SRANLSILNIDEKFG-----ILKVLPLID 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2064737281 176 MTSEEVWGYIRMLELPYNSLHERGFISIGCEPCTRPVLPNQHEREGRWWWEESTqkECGLH 236
Cdd:TIGR00434 153 WTWKDVYQYIDAHNLPYNPLHDQGYPSIGDYHSTRPVKEGEDERAGRWKGKAKT--ECGLH 211
PAPS_reductase TIGR02057
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ...
 18-236 8.67e-43

phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an electron donor, phosphoadenosine phosphosulfate reductase catalyzes the reduction of 3'-phosphoadenylylsulfate (PAPS) to sulfite and phospho-adenosine-phosphate (PAP). Found in enterobacteria, cyanobacteria, and yeast, PAPS reductase is related to a group of plant (TIGR00424) and bacterial (TIGR02055) enzymes preferring 5'-adenylylsulfate (APS) over PAPS as a substrate for reduction to sulfite. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 131112  Cd Length: 226  Bit Score: 144.59  E-value: 8.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  18 SPQEILKLAFEHFGDDLWISFS-GAEDVVLVDMAWKLNKQ-VKVFSLDTGRLHPETYRFIDQVREQYNLPIEI-LSPDRD 94
Cdd:TIGR02057  12 TPQEIIAWSIVTFPHGLVQTSAfGIQALVTLHLLSSISEPmIPVIFIDTLYHFPQTLTLKDELTKKYYQTLNLyKYDGCE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  95 KLDPFVKEKGLFSFYKDGHGECcGIRKIEPLRRKLA--TVSAWATGQRRDQSpGTRSQVAALEVDSafstpERTLYKFNP 172
Cdd:TIGR02057  92 SEADFEAKYGKLLWQKDIEKYD-YIAKVEPMQRALKelNASAWFTGRRRDQG-SARANLPVIEIDE-----QNGILKVNP 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2064737281 173 LAQMTSEEVWGYIRMLELPYNSLHERGFISIGCEPCTRPVLPNQHEREGRwwWEESTQKECGLH 236
Cdd:TIGR02057 165 LIDWTFEQVYQYLDAHNVPYNPLLDQGYRSIGDYHSTRKVKEGEDERAGR--WKGKLKTECGIH 226
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 20-210 1.21e-25

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: 99.77  E-value: 1.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  20 QEILKLAFEHFgDDLWISFSGAED-VVLVDMAW----KLNKQVKVFSLDTGRLHPETYRFIDQVREQYNLPIEILSPDRD 94
Cdd:cd23947     2 LERIRKVFEEF-DPVIVSFSGGKDsLVLLHLALealrRLRKDVYVVFIDTGIEFPETIDFVEKLAETLGLDVEAARPPLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  95 ---------KLDPFVKEKGLFSFYKDGhgeCCGIRKIEPLRRKLATVSAWAT----GQRRDQSPGTRSQVAALEVDSAFS 161
Cdd:cd23947    81 lewltsnfqPQWDPIWDNPPPPRDYRW---CCDELKLEPFTKWLKEKKPEGVlllvGIRADESLNRAKRPRVYRKYGWRN 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2064737281 162 TPERTLYKFNPLAQMTSEEVWGYIRMLELPYNSLHERGFISIGCEPCTR 210
Cdd:cd23947   158 STLPGQIVAYPIKDWSVEDVWLYILRHGLPYNPLYDLGFDRGGCLVCPR 206
PRK13795 PRK13795
hypothetical protein; Provisional
 36-208 2.79e-15

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 74.65  E-value: 2.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  36 ISFSGAED--VVLvDMAWKLNKQVKVFSLDTGRLHPETYRFIDQVREQYNLPIEILS--------------PDRD----- 94
Cdd:PRK13795  248 VSFSGGKDslVVL-DLAREALKDFKAFFNNTGLEFPETVENVKEVAEEYGIELIEADagdafwravekfgpPARDyrwcc 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  95 ---KLDPFVKEKGlfSFYKDGHGECCGIRKIEPLRR-KLATVSawatgqrrdQSPGTRSQVAAlevdsafstpertlykf 170
Cdd:PRK13795  327 kvcKLGPITRAIK--ENFPKGCLTFVGQRKYESFSRaKSPRVW---------RNPWVPNQIGA----------------- 378

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2064737281 171 NPLAQMTSEEVWGYIRMLELPYNSLHERGFISIGCEPC 208
Cdd:PRK13795  379 SPIQDWTALEVWLYIFWRKLPYNPLYERGFDRIGCWLC 416
PRK13794 PRK13794
hypothetical protein; Provisional
 36-208 1.24e-13

hypothetical protein; Provisional


Pssm-ID: 237509 [Multi-domain]  Cd Length: 479  Bit Score: 69.70  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  36 ISFSGAED--VVLVDMAWKLNKQVKVFSLDTGRLHPETYRFIDQVREQYNLPIEILS-------------PDRD------ 94
Cdd:PRK13794  252 VAYSGGKDslATLLLALKALGINFPVLFNDTGLEFPETLENVEDVEKHYGLEIIRTKseefwekleeygpPARDnrwcse 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  95 --KLDP---FVKEK---GLFSFykdghgecCGIRKIEPLRRklatvsawATGQRRDQSPGTRSQVAALevdsafstpert 166
Cdd:PRK13794  332 vcKLEPlgkLIDEKyegECLSF--------VGQRKYESFNR--------SKKPRIWRNPYIKKQILAA------------ 383

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2064737281 167 lykfnPLAQMTSEEVWGYIRMLELPYNSLHERGFISIGCEPC 208
Cdd:PRK13794  384 -----PILHWTAMHVWIYLFREKAPYNKLYEQGFDRIGCFMC 420
PRK08557 PRK08557
hypothetical protein; Provisional
 21-208 3.07e-10

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 59.38  E-value: 3.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  21 EILKLAFEHFGDDLWI---SFSGAED-VVLVDMAWKLNKQVKVFSLDTGRLHPETYRFIDQVREQYNLPIEILspDRDKL 96
Cdd:PRK08557  168 SILKDYIEKYKNKGYAinaSFSGGKDsSVSTLLAKEVIPDLEVIFIDTGLEYPETINYVKDFAKKYDLNLDTL--DGDNF 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  97 DPFVKEKGLFSfyKDGHGeCCGIRKIEPLRRKLATVSAWAT-----GQRRDQSpGTRSQVAaLEVDSAFSTPERTLYkfn 171
Cdd:PRK08557  246 WENLEKEGIPT--KDNRW-CNSACKLMPLKEYLKKKYGNKKvltidGSRKYES-FTRANLD-YERKSGFIDFQTNVF--- 317

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2064737281 172 PLAQMTSEEVWGYIRMLELPYNSLHERGFISIGCEPC 208
Cdd:PRK08557  318 PILDWNSLDIWSYIYLNDILYNPLYDKGFERIGCYLC 354
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 21-204 1.26e-07

FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; Flavin adenine dinucleotide synthase (FADS); EC 2.7.7.2) is involved in the biochemical pathway for converting riboflavin into FAD. By sequence comparison, bacterial and eukaryotic FMNAT enzymes belong to two different protein superfamilies and apparently utilize different sets of active-site residues to accomplish the same chemistry. This subfamily includes eukaryotic FMNATs, which are members of the 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase-like family belonging to the adenine nucleotide alpha hydrolase superfamily, which has conserved motifs different from those of nucleotidylyl transferases.


Pssm-ID: 467513 [Multi-domain]  Cd Length: 179  Bit Score: 50.21  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  21 EILKLAFEHFG-DDLWISFSGAED-VVLVDM---AWKLNKQVKVFSLDTgrLH-------PETYRFIDQVREQYNLPIEI 88
Cdd:cd23948     7 EVIEEALDKYGpEEIAISFNGGKDcTVLLHLlraALKRKYPSPLTPLKA--LYikspdpfPEVEEFVEDTAKRYNLDLIT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  89 LSPDrdkldpfVKEkGLFSfYKDGHGECCGIrkieplrrklatvsawATGQRRDqSPGTRSQvaalevdSAFST-----P 163
Cdd:cd23948    85 IDGP-------MKE-GLEE-LLKEHPIIKAV----------------FMGTRRT-DPHGENL-------KPFSPtdpgwP 131

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2064737281 164 ErtLYKFNPLAQMTSEEVWGYIRMLELPYNSLHERGFISIG 204
Cdd:cd23948   132 Q--FMRVNPILDWSYHDVWEFLRTLNLPYCSLYDQGYTSLG 170
Sulfate_adenylyltransferase_2 cd23946
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ...
 22-196 4.21e-03

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: 37.48  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  22 ILKLAFEHFGDDLWISFSGAEDVVLVDMAWKLNKQVK----VFSLDTGRLHPETYRFIDQVREQYNLPIEIlspdrdKLD 97
Cdd:cd23946    12 IIREVAAEFSNPVMLYSIGKDSSVMLHLARKAFYPGKppfpLLHVDTTWKFREMIEFRDRVAKEYGLDLIV------HVN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064737281  98 PFVKEKGLFSFYKdGHGECCGIRKIEPLRRKLAT--VSAWATGQRRDQSpGTRSQVAALEVDSAFST-------PER-TL 167
Cdd:cd23946    86 PDGVEAGINPFTH-GSAKHTDIMKTEGLKQALDKygFDAAFGGARRDEE-KSRAKERVYSFRDSNHRwdpknqrPELwNQ 163

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2064737281 168 YKFN----------PLAQMTSEEVWGYIRMLELPYNSLH 196
Cdd:cd23946   164 YNGRvkkgesirvfPLSNWTELDIWQYIYLENIPIVPLY 202
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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