NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488145980|ref|WP_002217188|]
View 

phosphoadenylyl-sulfate reductase [Neisseria meningitidis]

Protein Classification

adenylyl/phosphoadenylyl-sulfate reductase( domain architecture ID 10792199)

adenylyl/phosphoadenylyl-sulfate reductase catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS)/phosphoadenosine 5'-phosphosulfate (PAPS) using thioredoxin as the electron donor

CATH:  3.40.50.620
EC:  1.8.4.-
Gene Ontology:  GO:0016671|GO:0070814|GO:0019379|GO:0006790
PubMed:  9261082|17352498|12012333
SCOP:  4003838

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
6-243 4.32e-104

phosphoadenylyl-sulfate reductase;


:

Pssm-ID: 234997  Cd Length: 241  Bit Score: 301.37  E-value: 4.32e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980   6 PALWKIPPIENGSETALAEKTETLKQRLHRIAGshrDARFASSLAAEDMVITDLIAGENLNIGIFTLDTGLLHAETLNLL 85
Cdd:PRK02090   9 KADLALDLAELNAELEGASAQERLAWALENFGG---RLALVSSFGAEDAVLLHLVAQVDPDIPVIFLDTGYLFPETYRFI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980  86 DRIERVYpHMQIKRFQPIREDALHYVESKGRFAfyDSVEARRECCRIRKTEPLDRAIAGADAWLTGQRREQSATRTELPF 165
Cdd:PRK02090  86 DELTERL-LLNLKVYRPDASAAEQEARYGGLWE--QSVEDRDECCRIRKVEPLNRALAGLDAWITGLRREQSGTRANLPV 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488145980 166 AEYDagRGIDKYNPIFDWSEHDVWAYILANNVPYNDLYRQGFPSIGCDPCTRPVKAGEDIRAGRWWWEDKnsKECGLH 243
Cdd:PRK02090 163 LEID--GGRFKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGRWWGGLK--KECGLH 236
 
Name Accession Description Interval E-value
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
6-243 4.32e-104

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 301.37  E-value: 4.32e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980   6 PALWKIPPIENGSETALAEKTETLKQRLHRIAGshrDARFASSLAAEDMVITDLIAGENLNIGIFTLDTGLLHAETLNLL 85
Cdd:PRK02090   9 KADLALDLAELNAELEGASAQERLAWALENFGG---RLALVSSFGAEDAVLLHLVAQVDPDIPVIFLDTGYLFPETYRFI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980  86 DRIERVYpHMQIKRFQPIREDALHYVESKGRFAfyDSVEARRECCRIRKTEPLDRAIAGADAWLTGQRREQSATRTELPF 165
Cdd:PRK02090  86 DELTERL-LLNLKVYRPDASAAEQEARYGGLWE--QSVEDRDECCRIRKVEPLNRALAGLDAWITGLRREQSGTRANLPV 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488145980 166 AEYDagRGIDKYNPIFDWSEHDVWAYILANNVPYNDLYRQGFPSIGCDPCTRPVKAGEDIRAGRWWWEDKnsKECGLH 243
Cdd:PRK02090 163 LEID--GGRFKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGRWWGGLK--KECGLH 236
APS_reductase TIGR02055
thioredoxin-dependent adenylylsulfate APS reductase; This model describes recently identified ...
 49-242 2.69e-91

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: 267.02  E-value: 2.69e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980   49 LAAEDMVITDLIAGENLNIGIFTLDTGLLHAETLNLLDRIERVYPhMQIKRFQPIREDALHYVESKGRFAFYDSVeaRRE 128
Cdd:TIGR02055   1 LGAEDVVLVDLAAKVRPDVKVFFLDTGRLFKETYETIDQVRERYD-ILIDVLSPPPLTVEEQVKEYGLNLFYRSV--PHE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980  129 CCRIRKTEPLDRAIAGADAWLTGQRREQSATRTELPFAEYDAGRGIDKYNPIFDWSEHDVWAYILANNVPYNDLYRQGFP 208
Cdd:TIGR02055  78 CCGIRKVEPLKRALAGVSAWITGLRRDQSPTRAQAPFLEIDEAFGLVKINPLADWTSEDVWEYIADNELPYNPLHDRGYP 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 488145980  209 SIGCDPCTRPVKAGEDIRAGRWWWEDKNSKECGL 242
Cdd:TIGR02055 158 SIGCEPCTRPVAPGEDPRAGRWWWEEAAKKECGL 191
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 45-242 1.57e-87

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: 259.01  E-value: 1.57e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980  45 FASSLAAEDMVITDLIAGENLNIGIFTLDTGLLHAETLNLLDRIERVYPhMQIKRFQPiREDALHYVESKGRFAFYdsvE 124
Cdd:COG0175   38 VSSSGGKDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDRLAERLG-LDLIVVRP-EDAFAEQLAEFGPPLFY---R 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980 125 ARRECCRIRKTEPLDRAIAG--ADAWLTGQRREQSATRTELPFAEYDAGRGIDKYNPIFDWSEHDVWAYILANNVPYNDL 202
Cdd:COG0175  113 DPRWCCKIRKVEPLKRALAGydFDAWITGLRRDESPTRAKEPVVEWDPVGGLIKVNPLADWTELDVWAYIRREDLPYNPL 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 488145980 203 YRQGFPSIGCDPCTRPVKAGEDIRAGRWWWEDKNSKECGL 242
Cdd:COG0175  193 YDQGYPSIGCAPCTRAVESGEDERAGRWWDEEKERKECGL 232
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 28-211 1.58e-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: 226.71  E-value: 1.58e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980  28 TLKQRLHRIAGSHRDARFASSLAAEDMVITDLIAGENLNIGIFTLDTGLLHAETLNLLDRIERVYPHMQIKRFQPIREDA 107
Cdd:cd23945    1 PLEILLWAAEEFGPKLVFATSFGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYGLNIEVYFPEGTEAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980 108 LhYVESKGRFAFYDSVEARRECCRIRKTEPLDRAIAGADAWLTGQRREQSATRTELPFAEYDAGRGIDKYNPIFDWSEHD 187
Cdd:cd23945   81 E-EALEGGLNEFYLEDEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIVEVDEEGGLVKINPLADWTWED 159

                        170       180
                 ....*....|....*....|....
gi 488145980 188 VWAYILANNVPYNDLYRQGFPSIG 211
Cdd:cd23945  160 VWAYIREHDLPYNPLHDQGYPSIG 183
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 45-218 3.76e-47

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: 153.99  E-value: 3.76e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980   45 FASSLAAEDMVITDLIAGENLNIGIFTLDTGLLHAETLNLLDRIERVYPhMQIKRFQPIREDALHYVESKGRFAFYdsve 124
Cdd:pfam01507   4 VSFSGGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYG-LNLKVYLPEDSFAEGINPEGIPSSLY---- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980  125 arRECCRIRKTEPLDRAIA--GADAWLTGQRREQSATRTELPFAEYDAGRG-IDKYNPIFDWSEHDVWAYILANNVPYND 201
Cdd:pfam01507  79 --RRCCRLRKVEPLKRALKelGFDAWFTGLRRDESPSRAKLPIVSIDGDFPkVIKVFPLLNWTETDVWQYILANNVPYNP 156

                         170
                  ....*....|....*..
gi 488145980  202 LYRQGFPSIGCDPCTRP 218
Cdd:pfam01507 157 LYDQGYRSIGCYPCTGP 173
 
Name Accession Description Interval E-value
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
6-243 4.32e-104

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 301.37  E-value: 4.32e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980   6 PALWKIPPIENGSETALAEKTETLKQRLHRIAGshrDARFASSLAAEDMVITDLIAGENLNIGIFTLDTGLLHAETLNLL 85
Cdd:PRK02090   9 KADLALDLAELNAELEGASAQERLAWALENFGG---RLALVSSFGAEDAVLLHLVAQVDPDIPVIFLDTGYLFPETYRFI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980  86 DRIERVYpHMQIKRFQPIREDALHYVESKGRFAfyDSVEARRECCRIRKTEPLDRAIAGADAWLTGQRREQSATRTELPF 165
Cdd:PRK02090  86 DELTERL-LLNLKVYRPDASAAEQEARYGGLWE--QSVEDRDECCRIRKVEPLNRALAGLDAWITGLRREQSGTRANLPV 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488145980 166 AEYDagRGIDKYNPIFDWSEHDVWAYILANNVPYNDLYRQGFPSIGCDPCTRPVKAGEDIRAGRWWWEDKnsKECGLH 243
Cdd:PRK02090 163 LEID--GGRFKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGRWWGGLK--KECGLH 236
APS_reductase TIGR02055
thioredoxin-dependent adenylylsulfate APS reductase; This model describes recently identified ...
 49-242 2.69e-91

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: 267.02  E-value: 2.69e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980   49 LAAEDMVITDLIAGENLNIGIFTLDTGLLHAETLNLLDRIERVYPhMQIKRFQPIREDALHYVESKGRFAFYDSVeaRRE 128
Cdd:TIGR02055   1 LGAEDVVLVDLAAKVRPDVKVFFLDTGRLFKETYETIDQVRERYD-ILIDVLSPPPLTVEEQVKEYGLNLFYRSV--PHE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980  129 CCRIRKTEPLDRAIAGADAWLTGQRREQSATRTELPFAEYDAGRGIDKYNPIFDWSEHDVWAYILANNVPYNDLYRQGFP 208
Cdd:TIGR02055  78 CCGIRKVEPLKRALAGVSAWITGLRRDQSPTRAQAPFLEIDEAFGLVKINPLADWTSEDVWEYIADNELPYNPLHDRGYP 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 488145980  209 SIGCDPCTRPVKAGEDIRAGRWWWEDKNSKECGL 242
Cdd:TIGR02055 158 SIGCEPCTRPVAPGEDPRAGRWWWEEAAKKECGL 191
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 45-242 1.57e-87

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: 259.01  E-value: 1.57e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980  45 FASSLAAEDMVITDLIAGENLNIGIFTLDTGLLHAETLNLLDRIERVYPhMQIKRFQPiREDALHYVESKGRFAFYdsvE 124
Cdd:COG0175   38 VSSSGGKDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDRLAERLG-LDLIVVRP-EDAFAEQLAEFGPPLFY---R 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980 125 ARRECCRIRKTEPLDRAIAG--ADAWLTGQRREQSATRTELPFAEYDAGRGIDKYNPIFDWSEHDVWAYILANNVPYNDL 202
Cdd:COG0175  113 DPRWCCKIRKVEPLKRALAGydFDAWITGLRRDESPTRAKEPVVEWDPVGGLIKVNPLADWTELDVWAYIRREDLPYNPL 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 488145980 203 YRQGFPSIGCDPCTRPVKAGEDIRAGRWWWEDKNSKECGL 242
Cdd:COG0175  193 YDQGYPSIGCAPCTRAVESGEDERAGRWWDEEKERKECGL 232
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 28-211 1.58e-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: 226.71  E-value: 1.58e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980  28 TLKQRLHRIAGSHRDARFASSLAAEDMVITDLIAGENLNIGIFTLDTGLLHAETLNLLDRIERVYPHMQIKRFQPIREDA 107
Cdd:cd23945    1 PLEILLWAAEEFGPKLVFATSFGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYGLNIEVYFPEGTEAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980 108 LhYVESKGRFAFYDSVEARRECCRIRKTEPLDRAIAGADAWLTGQRREQSATRTELPFAEYDAGRGIDKYNPIFDWSEHD 187
Cdd:cd23945   81 E-EALEGGLNEFYLEDEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIVEVDEEGGLVKINPLADWTWED 159

                        170       180
                 ....*....|....*....|....
gi 488145980 188 VWAYILANNVPYNDLYRQGFPSIG 211
Cdd:cd23945  160 VWAYIREHDLPYNPLHDQGYPSIG 183
PLN02309 PLN02309
5'-adenylylsulfate reductase
 69-244 4.21e-61

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 198.48  E-value: 4.21e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980  69 IFTLDTGLLHAETLNLLDRIERVYpHMQIKRFQPIREDALHYVESKGRFAFYDsvEARRECCRIRKTEPLDRAIAGADAW 148
Cdd:PLN02309 138 VFSLDTGRLNPETYRLFDAVEKHY-GIRIEYMFPDAVEVQALVRNKGLFSFYE--DGHQECCRVRKVRPLRRALKGLRAW 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980 149 LTGQRREQS-ATRTELPFAEYD-AGRGID-------KYNPIFDWSEHDVWAYILANNVPYNDLYRQGFPSIGCDPCTRPV 219
Cdd:PLN02309 215 ITGQRKDQSpGTRAEVPVVQVDpVFEGLDggpgslvKWNPLANVTGNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCTRPV 294

                        170       180
                 ....*....|....*....|....*
gi 488145980 220 KAGEDIRAGRWWWEDKNSKECGLHK 244
Cdd:PLN02309 295 LPGQHEREGRWWWEDAKAKECGLHK 319
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 43-244 2.12e-58

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: 191.77  E-value: 2.12e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980   43 ARFASSLA-----AEDMVITDLIAGENLNIGIFTLDTGLLHAETLNLLDRIERVYpHMQIKRFQPIREDALHYVESKGRF 117
Cdd:TIGR00424 112 EKFGNDIAiafsgAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRFFDAVEKQY-GIRIEYMFPDAVEVQALVRSKGLF 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980  118 AFYDsvEARRECCRIRKTEPLDRAIAGADAWLTGQRREQS-ATRTELP-------FAEYDAGRG-IDKYNPIFDWSEHDV 188
Cdd:TIGR00424 191 SFYE--DGHQECCRVRKVRPLRRALKGLKAWITGQRKDQSpGTRSEIPvvqvdpvFEGLDGGVGsLVKWNPVANVEGKDV 268

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 488145980  189 WAYILANNVPYNDLYRQGFPSIGCDPCTRPVKAGEDIRAGRWWWEDKNSKECGLHK 244
Cdd:TIGR00424 269 WNFLRTMDVPVNTLHAQGYVSIGCEPCTRPVLPGQHEREGRWWWEDAKAKECGLHK 324
cysH TIGR00434
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ...
 45-243 1.85e-52

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: 169.20  E-value: 1.85e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980   45 FASSLAAEDMVITDLIAGENLNIGIFTLDTGLLHAETLNLLDRIERVYPhMQIKRFQPirEDALHYVESK-GRFAFYDSV 123
Cdd:TIGR00434  18 YSTSFGIQGAVLLDLVSKISPDIPVIFLDTGYHFPETYELIDELTERYP-LNIKVYKP--DLSLAEQAAKyGDKLWEQDP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980  124 EarrECCRIRKTEPLDRAIAG--ADAWLTGQRREQSATRTELPFAEYDAGRGIDKYNPIFDWSEHDVWAYILANNVPYND 201
Cdd:TIGR00434  95 N---KYDYLRKVEPMHRALKElhASAWFTGLRRDQGPSRANLSILNIDEKFGILKVLPLIDWTWKDVYQYIDAHNLPYNP 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 488145980  202 LYRQGFPSIGCDPCTRPVKAGEDIRAGRWWWEDKnsKECGLH 243
Cdd:TIGR00434 172 LHDQGYPSIGDYHSTRPVKEGEDERAGRWKGKAK--TECGLH 211
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 45-218 3.76e-47

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: 153.99  E-value: 3.76e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980   45 FASSLAAEDMVITDLIAGENLNIGIFTLDTGLLHAETLNLLDRIERVYPhMQIKRFQPIREDALHYVESKGRFAFYdsve 124
Cdd:pfam01507   4 VSFSGGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYG-LNLKVYLPEDSFAEGINPEGIPSSLY---- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980  125 arRECCRIRKTEPLDRAIA--GADAWLTGQRREQSATRTELPFAEYDAGRG-IDKYNPIFDWSEHDVWAYILANNVPYND 201
Cdd:pfam01507  79 --RRCCRLRKVEPLKRALKelGFDAWFTGLRRDESPSRAKLPIVSIDGDFPkVIKVFPLLNWTETDVWQYILANNVPYNP 156

                         170
                  ....*....|....*..
gi 488145980  202 LYRQGFPSIGCDPCTRP 218
Cdd:pfam01507 157 LYDQGYRSIGCYPCTGP 173
PAPS_reductase TIGR02057
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ...
 47-243 1.52e-42

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: 144.21  E-value: 1.52e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980   47 SSLAAEDMVITDLIAGENL-NIGIFTLDTGLLHAETLNLLDRI-ERVYPHMQIKRFQPIREDAlhYVESK-GRFAFYDSV 123
Cdd:TIGR02057  32 SAFGIQALVTLHLLSSISEpMIPVIFIDTLYHFPQTLTLKDELtKKYYQTLNLYKYDGCESEA--DFEAKyGKLLWQKDI 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980  124 EARREccrIRKTEPLDRAIA--GADAWLTGQRREQSATRTELPFAEYDAGRGIDKYNPIFDWSEHDVWAYILANNVPYND 201
Cdd:TIGR02057 110 EKYDY---IAKVEPMQRALKelNASAWFTGRRRDQGSARANLPVIEIDEQNGILKVNPLIDWTFEQVYQYLDAHNVPYNP 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 488145980  202 LYRQGFPSIGCDPCTRPVKAGEDIRAGRwwWEDKNSKECGLH 243
Cdd:TIGR02057 187 LLDQGYRSIGDYHSTRKVKEGEDERAGR--WKGKLKTECGIH 226
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 64-217 2.37e-21

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: 88.22  E-value: 2.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980  64 NLNIGIFTLDTGLLHAETLNLLDRIERVYpHMQIKRFQPIREDALHYVESKGRFAFYDSVEA----RRECCRIRKTEPLD 139
Cdd:cd23947   40 RKDVYVVFIDTGIEFPETIDFVEKLAETL-GLDVEAARPPLFLEWLTSNFQPQWDPIWDNPPpprdYRWCCDELKLEPFT 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980 140 RAIA----GADAWLTGQRREQSATRTELP------FAEYDAGRGIDKYNPIFDWSEHDVWAYILANNVPYNDLYRQGFPS 209
Cdd:cd23947  119 KWLKekkpEGVLLLVGIRADESLNRAKRPrvyrkyGWRNSTLPGQIVAYPIKDWSVEDVWLYILRHGLPYNPLYDLGFDR 198


                 ....*...
gi 488145980 210 IGCDPCTR 217
Cdd:cd23947  199 GGCLVCPR 206
PRK13795 PRK13795
hypothetical protein; Provisional
 55-212 7.09e-14

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 70.41  E-value: 7.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980  55 VITDLIAGENLNIGIFTLDTGLLHAETLNLLDRIERvypHMQIKrfqpiredalhYVESKGRFAFYDSVE-----AR--R 127
Cdd:PRK13795 258 VVLDLAREALKDFKAFFNNTGLEFPETVENVKEVAE---EYGIE-----------LIEADAGDAFWRAVEkfgppARdyR 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980 128 ECCRIRKTEPLDRAI--AGADAWLT--GQRREQSATRTELPFAEYD---AGR-GIdkyNPIFDWSEHDVWAYILANNVPY 199
Cdd:PRK13795 324 WCCKVCKLGPITRAIkeNFPKGCLTfvGQRKYESFSRAKSPRVWRNpwvPNQiGA---SPIQDWTALEVWLYIFWRKLPY 400

                        170
                 ....*....|...
gi 488145980 200 NDLYRQGFPSIGC 212
Cdd:PRK13795 401 NPLYERGFDRIGC 413
PRK08557 PRK08557
hypothetical protein; Provisional
 46-215 2.74e-13

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 68.63  E-value: 2.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980  46 ASSLAAEDMVITDLIAGENL-NIGIFTLDTGLLHAETLNLldriervyphmqIKRFQPIREDALHYVESKGrfaFYDSVE 124
Cdd:PRK08557 186 ASFSGGKDSSVSTLLAKEVIpDLEVIFIDTGLEYPETINY------------VKDFAKKYDLNLDTLDGDN---FWENLE 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980 125 AR-------RECCRIRKTEPLDRAIAGADAW-----LTGQRREQSATRTELpfaEYDAGRG-IDKYN---PIFDWSEHDV 188
Cdd:PRK08557 251 KEgiptkdnRWCNSACKLMPLKEYLKKKYGNkkvltIDGSRKYESFTRANL---DYERKSGfIDFQTnvfPILDWNSLDI 327

                        170       180
                 ....*....|....*....|....*..
gi 488145980 189 WAYILANNVPYNDLYRQGFPSIGCDPC 215
Cdd:PRK08557 328 WSYIYLNDILYNPLYDKGFERIGCYLC 354
PRK13794 PRK13794
hypothetical protein; Provisional
 53-215 2.92e-13

hypothetical protein; Provisional


Pssm-ID: 237509 [Multi-domain]  Cd Length: 479  Bit Score: 68.54  E-value: 2.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980  53 DMVITDLIAGENLNIGIFTL--DTGLLHAETLNLLDRIERVYpHMQIKRFQPIredalhyveskgrfAFYDSVE-----A 125
Cdd:PRK13794 259 DSLATLLLALKALGINFPVLfnDTGLEFPETLENVEDVEKHY-GLEIIRTKSE--------------EFWEKLEeygppA 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980 126 R--RECCRIRKTEPLDRAI----AGADAWLTGQRREQSATRTELPFAEYDagRGIDKY---NPIFDWSEHDVWAYILANN 196
Cdd:PRK13794 324 RdnRWCSEVCKLEPLGKLIdekyEGECLSFVGQRKYESFNRSKKPRIWRN--PYIKKQilaAPILHWTAMHVWIYLFREK 401

                        170
                 ....*....|....*....
gi 488145980 197 VPYNDLYRQGFPSIGCDPC 215
Cdd:PRK13794 402 APYNKLYEQGFDRIGCFMC 420
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 130-211 9.76e-12

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: 61.77  E-value: 9.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980 130 CRIRKTEPLDRAIagadawLTGQRREQSATRTELPFAEYDAG-----RgidkYNPIFDWSEHDVWAYILANNVPYNDLYR 204
Cdd:cd23948   94 EELLKEHPIIKAV------FMGTRRTDPHGENLKPFSPTDPGwpqfmR----VNPILDWSYHDVWEFLRTLNLPYCSLYD 163


                 ....*..
gi 488145980 205 QGFPSIG 211
Cdd:cd23948  164 QGYTSLG 170
PRK08576 PRK08576
hypothetical protein; Provisional
 130-215 2.83e-07

hypothetical protein; Provisional


Pssm-ID: 236300 [Multi-domain]  Cd Length: 438  Bit Score: 50.46  E-value: 2.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980 130 CRIRKTEPLDRAIAG-ADAWL-TGQRREQSATRTELP--FAEYDAGRGIDKYNPIFDWSEHDVWAYILANNVPYNDLYRQ 205
Cdd:PRK08576 314 CTKLKVEALEEAIRElEDGLLvVGDRDGESARRRLRPpvVERKTNFGKILVVMPIKFWSGAMVQLYILMNGLELNPLYYK 393

                         90
                 ....*....|
gi 488145980 206 GFPSIGCDPC 215
Cdd:PRK08576 394 GFYRLGCYIC 403
PRK05253 PRK05253
sulfate adenylyltransferase subunit CysD;
127-219 1.26e-05

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 235375  Cd Length: 301  Bit Score: 45.13  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980 127 RECCRIRKTEPLDRAIA--GADAWLTGQRREQSATRT-ELPFAEYDAGRGID----------KYN------------PIF 181
Cdd:PRK05253 108 AKHTNAMKTEGLKQALEkyGFDAAFGGARRDEEKSRAkERIFSFRDEFGQWDpknqrpelwnLYNgrinkgehirvfPLS 187

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980 182 DWSEHDVWAYILANNVPYNDLY---------RQG-----------------------FPSIGCDPCTRPV 219
Cdd:PRK05253 188 NWTELDIWQYIERENIPIVPLYfaherpvveRDGmlimvddrmplrpgevveermvrFRTLGCYPCTGAV 257
Sulfate_adenylyltransferase_2 cd23946
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ...
 126-203 1.90e-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: 44.41  E-value: 1.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488145980 126 RRECCRIRKTEPLDRAIA--GADAWLTGQRREQSATRT-ELPFAEYDAGRGID----------KYN------------PI 180
Cdd:cd23946  100 SAKHTDIMKTEGLKQALDkyGFDAAFGGARRDEEKSRAkERVYSFRDSNHRWDpknqrpelwnQYNgrvkkgesirvfPL 179

                         90       100
                 ....*....|....*....|...
gi 488145980 181 FDWSEHDVWAYILANNVPYNDLY 203
Cdd:cd23946  180 SNWTELDIWQYIYLENIPIVPLY 202
DNA_S_dndC TIGR03183
putative sulfurtransferase DndC; Members of this protein family are the DndC protein from the ...
 151-204 9.42e-03

putative sulfurtransferase DndC; Members of this protein family are the DndC protein from the dnd (degradation during electrophoresis) operon. The dnd phenotype reflects a sulfur-containing modification to DNA. This operon is sparsely and sporadically distributed among bactera; among the first eight examples are members from the Actinobacteria, Firmicutes, Gammaproteobacteria, Cyanobacteria. DndC is suggested to be a sulfurtransferase. [DNA metabolism, Restriction/modification]


Pssm-ID: 163177  Cd Length: 447  Bit Score: 37.02  E-value: 9.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488145980  151 GQRREQSATRTELpFAEYDAGRGIDK------------YNPIFDWSEHDVWAYILANNVPY-------NDLYR 204
Cdd:TIGR03183 145 GTRKAESQARAAV-MEKHESGSLRDRlsrnsslpnswvYSPIEDWSNDDVWMYLLQVPNPWgidnkdlFGMYQ 216
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH