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Conserved domains on  [gi|1278577271|gb|PJA90944|]
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MAG: phosphoadenosine phosphosulfate reductase [Candidatus Levybacteria bacterium CG_4_9_14_3_um_filter_36_7]

Protein Classification

phosphoadenosine phosphosulfate reductase family protein( domain architecture ID 11415063)

phosphoadenosine phosphosulfate (PAPS) reductase family protein; similar to Escherichia coli CysH, a PAPS reductase which catalyzes the reduction of PAPS to phospho-adenosine-phosphate (PAP) and sulfite using thioredoxin as the electron donor, and to Rhizobium nodulation protein P which has ATP sulfurylase (sulfate adenylate transferase) activity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 5-212 4.06e-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: 196.22  E-value: 4.06e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271   5 QEKIANTKKILKQAEKKYGLNdIALAWKGGKDTTTLMHIIlcmYDGVIPYKVMFNDTTLEFPEMYKFIEKVAHQWNLNLl 84
Cdd:COG0175    15 AELEAEAIEILREAAAEFGGR-VVVSSSGGKDSTVLLHLA---AKFKPPIPVLFLDTGYEFPETYEFRDRLAERLGLDL- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  85 IERHSEEDLANYHKARGMVLKEEISR----RAKINSLNRALEKYKLKGYMLGIRRDENPARANEKYFS--PRPNHIRIHP 158
Cdd:COG0175    90 IVVRPEDAFAEQLAEFGPPLFYRDPRwcckIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVVEwdPVGGLIKVNP 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1278577271 159 LLDFTEEDVWNYIRLFNVPYSPLYDKGYRSIGEKPFTK--KSSGDERSGREQNKEK 212
Cdd:COG0175   170 LADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRavESGEDERAGRWWDEEK 225
 
Name Accession Description Interval E-value
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 5-212 4.06e-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: 196.22  E-value: 4.06e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271   5 QEKIANTKKILKQAEKKYGLNdIALAWKGGKDTTTLMHIIlcmYDGVIPYKVMFNDTTLEFPEMYKFIEKVAHQWNLNLl 84
Cdd:COG0175    15 AELEAEAIEILREAAAEFGGR-VVVSSSGGKDSTVLLHLA---AKFKPPIPVLFLDTGYEFPETYEFRDRLAERLGLDL- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  85 IERHSEEDLANYHKARGMVLKEEISR----RAKINSLNRALEKYKLKGYMLGIRRDENPARANEKYFS--PRPNHIRIHP 158
Cdd:COG0175    90 IVVRPEDAFAEQLAEFGPPLFYRDPRwcckIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVVEwdPVGGLIKVNP 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1278577271 159 LLDFTEEDVWNYIRLFNVPYSPLYDKGYRSIGEKPFTK--KSSGDERSGREQNKEK 212
Cdd:COG0175   170 LADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRavESGEDERAGRWWDEEK 225
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 27-190 6.06e-43

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: 142.44  E-value: 6.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  27 IALAWKGGKDTTTLMHIILCMYDgviPYKVMFNDTTLEFPEMYKFIEKVAHQWNLNLLIER--HSEEDLANYHKARGMvL 104
Cdd:pfam01507   2 LVVSFSGGKDSLVLLHLASKAFP---PGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLpeDSFAEGINPEGIPSS-L 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271 105 KEEISRRAKINSLNRALEKYKLKGYMLGIRRDENPARANEKYFSPR---PNHIRIHPLLDFTEEDVWNYIRLFNVPYSPL 181
Cdd:pfam01507  78 YRRCCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDgdfPKVIKVFPLLNWTETDVWQYILANNVPYNPL 157


                  ....*....
gi 1278577271 182 YDKGYRSIG 190
Cdd:pfam01507 158 YDQGYRSIG 166
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 7-192 3.08e-36

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: 125.71  E-value: 3.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271   7 KIANTKKILKQAEKKYGLNDIALAWKGGKDTTTLMHIILCMY-----DGVIPYKVMFNDTTLEFPEMYKFIEKVAHQWNL 81
Cdd:cd23948     1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALkrkypSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  82 NLlierhseedlanYHKARGMvlKEeisrrakinslnrALEKYK-----LKGYMLGIRRDEnPARANEKYFSPR----PN 152
Cdd:cd23948    81 DL------------ITIDGPM--KE-------------GLEELLkehpiIKAVFMGTRRTD-PHGENLKPFSPTdpgwPQ 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1278577271 153 HIRIHPLLDFTEEDVWNYIRLFNVPYSPLYDKGYRSIGEK 192
Cdd:cd23948   133 FMRVNPILDWSYHDVWEFLRTLNLPYCSLYDQGYTSLGSV 172
PRK05253 PRK05253
sulfate adenylyltransferase subunit CysD;
27-222 4.02e-36

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 235375  Cd Length: 301  Bit Score: 128.72  E-value: 4.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  27 IALAWKGGKDTTTLMHiiLCM---YDGVIPYKVMFNDTTLEFPEMYKFIEKVAHQWNLNLLIeRHSEEDLAnyhkaRGMV 103
Cdd:PRK05253   30 PVMLYSIGKDSSVMLH--LARkafYPGKLPFPLLHVDTGWKFPEMIEFRDRRAKELGLELIV-HSNPEGIA-----RGIN 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271 104 ----LKEEISRRAKINSLNRALEKYKLKGYMLGIRRDENPARANEKYFSPR------------P-------------NHI 154
Cdd:PRK05253  102 pfrhGSAKHTNAMKTEGLKQALEKYGFDAAFGGARRDEEKSRAKERIFSFRdefgqwdpknqrPelwnlyngrinkgEHI 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271 155 RIHPLLDFTEEDVWNYIRLFNVPYSPLY------------------DKGYRSIGEKPFTKK----SSGD----------- 201
Cdd:PRK05253  182 RVFPLSNWTELDIWQYIERENIPIVPLYfaherpvverdgmlimvdDRMPLRPGEVVEERMvrfrTLGCypctgavesea 261

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1278577271 202 ----------------ERSGREQNK--EKMMEKLRQMGY 222
Cdd:PRK05253  262 atleeiiaemlvtrtsERGGRAIDDdqEASMEKRKREGY 300
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 2-206 1.85e-17

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: 80.06  E-value: 1.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271   2 QTLQEKIANTK--KILKQAEKKYGlNDIALAWKGGKDTTTLMHIILCMYdgviPYKVMFNDTTLEFPEMYKFIEKVAHQW 79
Cdd:TIGR00424  92 EKLAKKLENASplEIMDKALEKFG-NDIAIAFSGAEDVALIEYAHLTGR----PFRVFSLDTGRLNPETYRFFDAVEKQY 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  80 NLNLLIERHSEEDLANYHKARGMVL-----KEEISRRAKINSLNRALEKykLKGYMLGIRRDENPA-RANEKYFSPRP-- 151
Cdd:TIGR00424 167 GIRIEYMFPDAVEVQALVRSKGLFSfyedgHQECCRVRKVRPLRRALKG--LKAWITGQRKDQSPGtRSEIPVVQVDPvf 244

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278577271 152 --------NHIRIHPLLDFTEEDVWNYIRLFNVPYSPLYDKGYRSIGEKPFTKK--SSGDERSGR 206
Cdd:TIGR00424 245 egldggvgSLVKWNPVANVEGKDVWNFLRTMDVPVNTLHAQGYVSIGCEPCTRPvlPGQHEREGR 309
 
Name Accession Description Interval E-value
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 5-212 4.06e-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: 196.22  E-value: 4.06e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271   5 QEKIANTKKILKQAEKKYGLNdIALAWKGGKDTTTLMHIIlcmYDGVIPYKVMFNDTTLEFPEMYKFIEKVAHQWNLNLl 84
Cdd:COG0175    15 AELEAEAIEILREAAAEFGGR-VVVSSSGGKDSTVLLHLA---AKFKPPIPVLFLDTGYEFPETYEFRDRLAERLGLDL- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  85 IERHSEEDLANYHKARGMVLKEEISR----RAKINSLNRALEKYKLKGYMLGIRRDENPARANEKYFS--PRPNHIRIHP 158
Cdd:COG0175    90 IVVRPEDAFAEQLAEFGPPLFYRDPRwcckIRKVEPLKRALAGYDFDAWITGLRRDESPTRAKEPVVEwdPVGGLIKVNP 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1278577271 159 LLDFTEEDVWNYIRLFNVPYSPLYDKGYRSIGEKPFTK--KSSGDERSGREQNKEK 212
Cdd:COG0175   170 LADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRavESGEDERAGRWWDEEK 225
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 27-190 6.06e-43

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: 142.44  E-value: 6.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  27 IALAWKGGKDTTTLMHIILCMYDgviPYKVMFNDTTLEFPEMYKFIEKVAHQWNLNLLIER--HSEEDLANYHKARGMvL 104
Cdd:pfam01507   2 LVVSFSGGKDSLVLLHLASKAFP---PGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLpeDSFAEGINPEGIPSS-L 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271 105 KEEISRRAKINSLNRALEKYKLKGYMLGIRRDENPARANEKYFSPR---PNHIRIHPLLDFTEEDVWNYIRLFNVPYSPL 181
Cdd:pfam01507  78 YRRCCRLRKVEPLKRALKELGFDAWFTGLRRDESPSRAKLPIVSIDgdfPKVIKVFPLLNWTETDVWQYILANNVPYNPL 157


                  ....*....
gi 1278577271 182 YDKGYRSIG 190
Cdd:pfam01507 158 YDQGYRSIG 166
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 7-192 3.08e-36

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: 125.71  E-value: 3.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271   7 KIANTKKILKQAEKKYGLNDIALAWKGGKDTTTLMHIILCMY-----DGVIPYKVMFNDTTLEFPEMYKFIEKVAHQWNL 81
Cdd:cd23948     1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALkrkypSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  82 NLlierhseedlanYHKARGMvlKEeisrrakinslnrALEKYK-----LKGYMLGIRRDEnPARANEKYFSPR----PN 152
Cdd:cd23948    81 DL------------ITIDGPM--KE-------------GLEELLkehpiIKAVFMGTRRTD-PHGENLKPFSPTdpgwPQ 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1278577271 153 HIRIHPLLDFTEEDVWNYIRLFNVPYSPLYDKGYRSIGEK 192
Cdd:cd23948   133 FMRVNPILDWSYHDVWEFLRTLNLPYCSLYDQGYTSLGSV 172
PRK05253 PRK05253
sulfate adenylyltransferase subunit CysD;
27-222 4.02e-36

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 235375  Cd Length: 301  Bit Score: 128.72  E-value: 4.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  27 IALAWKGGKDTTTLMHiiLCM---YDGVIPYKVMFNDTTLEFPEMYKFIEKVAHQWNLNLLIeRHSEEDLAnyhkaRGMV 103
Cdd:PRK05253   30 PVMLYSIGKDSSVMLH--LARkafYPGKLPFPLLHVDTGWKFPEMIEFRDRRAKELGLELIV-HSNPEGIA-----RGIN 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271 104 ----LKEEISRRAKINSLNRALEKYKLKGYMLGIRRDENPARANEKYFSPR------------P-------------NHI 154
Cdd:PRK05253  102 pfrhGSAKHTNAMKTEGLKQALEKYGFDAAFGGARRDEEKSRAKERIFSFRdefgqwdpknqrPelwnlyngrinkgEHI 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271 155 RIHPLLDFTEEDVWNYIRLFNVPYSPLY------------------DKGYRSIGEKPFTKK----SSGD----------- 201
Cdd:PRK05253  182 RVFPLSNWTELDIWQYIERENIPIVPLYfaherpvverdgmlimvdDRMPLRPGEVVEERMvrfrTLGCypctgavesea 261

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1278577271 202 ----------------ERSGREQNK--EKMMEKLRQMGY 222
Cdd:PRK05253  262 atleeiiaemlvtrtsERGGRAIDDdqEASMEKRKREGY 300
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
55-212 1.91e-33

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 120.33  E-value: 1.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  55 KVMFNDTTLEFPEMYKFIEKVAHQWNLNLLIER--HSE-EDLANYHK--ARGMVLKEEISRRAKINSLNRALEKYKlkGY 129
Cdd:PRK02090   68 PVIFLDTGYLFPETYRFIDELTERLLLNLKVYRpdASAaEQEARYGGlwEQSVEDRDECCRIRKVEPLNRALAGLD--AW 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271 130 MLGIRRDENPARANEKYFSPRPNHIRIHPLLDFTEEDVWNYIRLFNVPYSPLYDKGYRSIGEKPFTKK-SSG-DERSGRE 207
Cdd:PRK02090  146 ITGLRREQSGTRANLPVLEIDGGRFKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPvEPGeDERAGRW 225


                  ....*
gi 1278577271 208 QNKEK 212
Cdd:PRK02090  226 WGGLK 230
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 25-190 8.97e-29

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: 107.09  E-value: 8.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  25 NDIALAWKGGKDTTTLMHIILcMYDG--VIPYKVMFNDTTLEFPEMYKFIEKVAHQWNLNLLIERHS--EEDLANYHKAR 100
Cdd:cd23947    13 DPVIVSFSGGKDSLVLLHLAL-EALRrlRKDVYVVFIDTGIEFPETIDFVEKLAETLGLDVEAARPPlfLEWLTSNFQPQ 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271 101 GMVLKEEI---------SRRAKINSLNRALEKYKLKGY--MLGIRRDENPARANEKYF--------SPRPNHIRIHPLLD 161
Cdd:cd23947    92 WDPIWDNPppprdyrwcCDELKLEPFTKWLKEKKPEGVllLVGIRADESLNRAKRPRVyrkygwrnSTLPGQIVAYPIKD 171

                         170       180
                  ....*....|....*....|....*....
gi 1278577271 162 FTEEDVWNYIRLFNVPYSPLYDKGYRSIG 190
Cdd:cd23947   172 WSVEDVWLYILRHGLPYNPLYDLGFDRGG 200
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 11-190 1.06e-27

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: 103.83  E-value: 1.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  11 TKKILKQAEKKYGlNDIALAWKGGKDTTTLMHIILCMYDGVipyKVMFNDTTLEFPEMYKFIEKVAHQWNLNLLI---ER 87
Cdd:cd23945     1 PLEILLWAAEEFG-PKLVFATSFGAEDAVILDLLSKVRPDI---PVVFLDTGYLFPETYDLIDEVEARYGLNIEVyfpEG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  88 HSEEDLANYHKARGMVLKEE-----ISRRaKINSLNRALEKYKlkgYML-GIRRDENPARANEKYFS--PRPNHIRIHPL 159
Cdd:cd23945    77 TEAEEEALEGGLNEFYLEDEerydcCRKR-KPFPLALALLGVK---AWItGRRRDQSPTRANLPIVEvdEEGGLVKINPL 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1278577271 160 LDFTEEDVWNYIRLFNVPYSPLYDKGYRSIG 190
Cdd:cd23945   153 ADWTWEDVWAYIREHDLPYNPLHDQGYPSIG 183
Sulfate_adenylyltransferase_2 cd23946
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ...
 14-192 5.45e-27

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: 102.58  E-value: 5.45e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  14 ILKQAEKKYGlnDIALAWKGGKDTTTLMHIIL-CMYDGVIPYKVMFNDTTLEFPEMYKFIEKVAHQWNLNLLIERHS--- 89
Cdd:cd23946    12 IIREVAAEFS--NPVMLYSIGKDSSVMLHLARkAFYPGKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDLIVHVNPdgv 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  90 EEDLANYHKARGMVLKEeisrrAKINSLNRALEKYKLKGYMLGIRRDENPARANEKYFSPRP------------------ 151
Cdd:cd23946    90 EAGINPFTHGSAKHTDI-----MKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDsnhrwdpknqrpelwnqy 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1278577271 152 -------NHIRIHPLLDFTEEDVWNYIRLFNVPYSPLYDKGYRSIGEK 192
Cdd:cd23946   165 ngrvkkgESIRVFPLSNWTELDIWQYIYLENIPIVPLYFAAERPVIER 212
PRK12563 PRK12563
sulfate adenylyltransferase subunit CysD;
28-203 3.03e-20

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 237138  Cd Length: 312  Bit Score: 86.77  E-value: 3.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  28 ALAWKGGKDTTTLMHIIL-CMYDGVIPYKVMFNDTTLEFPEMYKFIEKVAHQWNLNLLIErHSEEDLANYHK--ARGMVL 104
Cdd:PRK12563   41 VMLYSIGKDSVVMLHLAMkAFRPTRPPFPLLHVDTTWKFREMIDFRDRRAKELGLDLVVH-HNPDGIARGIVpfRHGSAL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271 105 KEEIsrrAKINSLNRALEKYKLKGYMLGIRRDENPARANEKYFS------------PRPN-------------HIRIHPL 159
Cdd:PRK12563  120 HTDV---AKTQGLKQALDHHGFDAAIGGARRDEEKSRAKERIFSfrsafhrwdpkaQRPElwslynarlrrgeSLRVFPL 196

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1278577271 160 LDFTEEDVWNYIRLFNVPYSPLYDKGYRSIGEKPFTKKSSGDER 203
Cdd:PRK12563  197 SNWTELDVWQYIAREKIPLVPLYFAKRRPVVERDGLLIMVDDER 240
PRK13795 PRK13795
hypothetical protein; Provisional
 2-190 5.91e-19

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 84.66  E-value: 5.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271   2 QTLQEKIANTKKILKQAEKKYGLnDIALAWKGGKDTTTLMHIILCMYDGvipYKVMFNDTTLEFPEMYKFIEKVAHQWNL 81
Cdd:PRK13795  222 KHLEEKEKEAVNFIRGVAEKYNL-PVSVSFSGGKDSLVVLDLAREALKD---FKAFFNNTGLEFPETVENVKEVAEEYGI 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  82 NLLIERHSEedlaNYHKARGMVLKEEISRR-----AKINSLNRALEKYKLKGYM--LGIRRDENPARANekyfSPR---- 150
Cdd:PRK13795  298 ELIEADAGD----AFWRAVEKFGPPARDYRwcckvCKLGPITRAIKENFPKGCLtfVGQRKYESFSRAK----SPRvwrn 369

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1278577271 151 ---PNHIRIHPLLDFTEEDVWNYIRLFNVPYSPLYDKGYRSIG 190
Cdd:PRK13795  370 pwvPNQIGASPIQDWTALEVWLYIFWRKLPYNPLYERGFDRIG 412
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 2-206 1.85e-17

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: 80.06  E-value: 1.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271   2 QTLQEKIANTK--KILKQAEKKYGlNDIALAWKGGKDTTTLMHIILCMYdgviPYKVMFNDTTLEFPEMYKFIEKVAHQW 79
Cdd:TIGR00424  92 EKLAKKLENASplEIMDKALEKFG-NDIAIAFSGAEDVALIEYAHLTGR----PFRVFSLDTGRLNPETYRFFDAVEKQY 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  80 NLNLLIERHSEEDLANYHKARGMVL-----KEEISRRAKINSLNRALEKykLKGYMLGIRRDENPA-RANEKYFSPRP-- 151
Cdd:TIGR00424 167 GIRIEYMFPDAVEVQALVRSKGLFSfyedgHQECCRVRKVRPLRRALKG--LKAWITGQRKDQSPGtRSEIPVVQVDPvf 244

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278577271 152 --------NHIRIHPLLDFTEEDVWNYIRLFNVPYSPLYDKGYRSIGEKPFTKK--SSGDERSGR 206
Cdd:TIGR00424 245 egldggvgSLVKWNPVANVEGKDVWNFLRTMDVPVNTLHAQGYVSIGCEPCTRPvlPGQHEREGR 309
PRK08557 PRK08557
hypothetical protein; Provisional
 4-190 1.14e-16

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 77.87  E-value: 1.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271   4 LQEKIANTKKILKQAEKKYGLNDIAL--AWKGGKDT--TTLMHiilcmyDGVIP-YKVMFNDTTLEFPEMYKFIEKVAHQ 78
Cdd:PRK08557  159 IEKLEENSLSILKDYIEKYKNKGYAInaSFSGGKDSsvSTLLA------KEVIPdLEVIFIDTGLEYPETINYVKDFAKK 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  79 WNLNLLIERhsEEDLANYHKARGMVLKEE--ISRRAKINSLNRALEK---YKLKGYMLGIRRDENPARAN---EKYFSPR 150
Cdd:PRK08557  233 YDLNLDTLD--GDNFWENLEKEGIPTKDNrwCNSACKLMPLKEYLKKkygNKKVLTIDGSRKYESFTRANldyERKSGFI 310

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1278577271 151 PNHIRIHPLLDFTEEDVWNYIRLFNVPYSPLYDKGYRSIG 190
Cdd:PRK08557  311 DFQTNVFPILDWNSLDIWSYIYLNDILYNPLYDKGFERIG 350
PLN02309 PLN02309
5'-adenylylsulfate reductase
 14-212 1.69e-14

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 71.74  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  14 ILKQAEKKYGlNDIALAWKGGKDtttlmhIILCMYDGVI--PYKVMFNDTTLEFPEMYKFIEKVAHQWNLNLLIERHSEE 91
Cdd:PLN02309  101 IMDKALEKFG-NDIAIAFSGAED------VALIEYAHLTgrPFRVFSLDTGRLNPETYRLFDAVEKHYGIRIEYMFPDAV 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  92 DLANYHKARGMVL-----KEEISRRAKINSLNRALEKykLKGYMLGIRRDENPA-RANEKYFSPRP----------NHIR 155
Cdd:PLN02309  174 EVQALVRNKGLFSfyedgHQECCRVRKVRPLRRALKG--LRAWITGQRKDQSPGtRAEVPVVQVDPvfegldggpgSLVK 251

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278577271 156 IHPLLDFTEEDVWNYIRLFNVPYSPLYDKGYRSIGEKPFTKK--SSGDERSGR---EQNKEK 212
Cdd:PLN02309  252 WNPLANVTGNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCTRPvlPGQHEREGRwwwEDAKAK 313
PRK13794 PRK13794
hypothetical protein; Provisional
 9-190 5.86e-14

hypothetical protein; Provisional


Pssm-ID: 237509 [Multi-domain]  Cd Length: 479  Bit Score: 70.08  E-value: 5.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271   9 ANTKKILKQAEKKYGLnDIALAWKGGKDT-TTLmhiILCMYDGVIPYKVMFNDTTLEFPEMYKFIEKVAHQWNLNLLIER 87
Cdd:PRK13794  233 RNSIGFIRNTAEKINK-PVTVAYSGGKDSlATL---LLALKALGINFPVLFNDTGLEFPETLENVEDVEKHYGLEIIRTK 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  88 HSE--EDLANYH-KARGMVLKEEISrraKINSLNRALEKYKLKGYM--LGIRRDENPARANekyfSPR-------PNHIR 155
Cdd:PRK13794  309 SEEfwEKLEEYGpPARDNRWCSEVC---KLEPLGKLIDEKYEGECLsfVGQRKYESFNRSK----KPRiwrnpyiKKQIL 381

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1278577271 156 IHPLLDFTEEDVWNYIRLFNVPYSPLYDKGYRSIG 190
Cdd:PRK13794  382 AAPILHWTAMHVWIYLFREKAPYNKLYEQGFDRIG 416
PRK08576 PRK08576
hypothetical protein; Provisional
 6-190 1.68e-08

hypothetical protein; Provisional


Pssm-ID: 236300 [Multi-domain]  Cd Length: 438  Bit Score: 53.93  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271   6 EKIAntKKILKQaekkYGLNDIALAWKGGKDTTTLMHIILCMYDGVipyKVMFNDTTLEFPEMYKFIEKVAHQWNLNLLI 85
Cdd:PRK08576  222 EKAS--IKFLRK----FEEWTVIVPWSGGKDSTAALLLAKKAFGDV---TAVYVDTGYEMPLTDEYVEKVAEKLGVDLIR 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577271  86 erhSEEDLANYHKARGMVLKEeiSR---RAKINSLNRALEKYKLKGYMLGIRRDENPARanekyfSPRP----------N 152
Cdd:PRK08576  293 ---AGVDVPMPIEKYGMPTHS--NRwctKLKVEALEEAIRELEDGLLVVGDRDGESARR------RLRPpvverktnfgK 361

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1278577271 153 HIRIHPLLDFTEEDVWNYIRLFNVPYSPLYDKGYRSIG 190
Cdd:PRK08576  362 ILVVMPIKFWSGAMVQLYILMNGLELNPLYYKGFYRLG 399
 
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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