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Conserved domains on  [gi|489507433|ref|WP_003412303|]
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MULTISPECIES: phosphoadenylyl-sulfate reductase [Mycobacterium]

Protein Classification

phosphoadenosine phosphosulfate reductase family protein( domain architecture ID 10797699)

phosphoadenosine phosphosulfate reductase family protein is involved in the assimilation of sulfate and it catalyzes the reduction of 3'-phospho-adenylylsulfate (PAPS) or 5'-adenylyl sulfate to sulfite and phospho-adenosine-phosphate (PAP) or AMP using thioredoxin as the electron donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
APS_reductase TIGR02055
thioredoxin-dependent adenylylsulfate APS reductase; This model describes recently identified ...
 65-251 7.06e-111

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: 317.09  E-value: 7.06e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433   65 SNMADAVLVDLAAKVRPGVPVIFLDTGYHFVETIGTRDAIESVYDV-RVLNVTPEHTVAEQDELLGKDLFARN-PHECCR 142
Cdd:TIGR02055   1 LGAEDVVLVDLAAKVRPDVKVFFLDTGRLFKETYETIDQVRERYDIlIDVLSPPPLTVEEQVKEYGLNLFYRSvPHECCG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433  143 LRKVVPLGKTLRGYSAWVTGLRRVDAPTRANAPLVSFDETFKLVKVNPLAAWTDQDVQEYIADNDVLVNPLVREGYPSIG 222
Cdd:TIGR02055  81 IRKVEPLKRALAGVSAWITGLRRDQSPTRAQAPFLEIDEAFGLVKINPLADWTSEDVWEYIADNELPYNPLHDRGYPSIG 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 489507433  223 CAPCTAKPAEGADPRSGRWQGL--AKTECGL 251
Cdd:TIGR02055 161 CEPCTRPVAPGEDPRAGRWWWEeaAKKECGL 191
 
Name Accession Description Interval E-value
APS_reductase TIGR02055
thioredoxin-dependent adenylylsulfate APS reductase; This model describes recently identified ...
 65-251 7.06e-111

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: 317.09  E-value: 7.06e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433   65 SNMADAVLVDLAAKVRPGVPVIFLDTGYHFVETIGTRDAIESVYDV-RVLNVTPEHTVAEQDELLGKDLFARN-PHECCR 142
Cdd:TIGR02055   1 LGAEDVVLVDLAAKVRPDVKVFFLDTGRLFKETYETIDQVRERYDIlIDVLSPPPLTVEEQVKEYGLNLFYRSvPHECCG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433  143 LRKVVPLGKTLRGYSAWVTGLRRVDAPTRANAPLVSFDETFKLVKVNPLAAWTDQDVQEYIADNDVLVNPLVREGYPSIG 222
Cdd:TIGR02055  81 IRKVEPLKRALAGVSAWITGLRRDQSPTRAQAPFLEIDEAFGLVKINPLADWTSEDVWEYIADNELPYNPLHDRGYPSIG 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 489507433  223 CAPCTAKPAEGADPRSGRWQGL--AKTECGL 251
Cdd:TIGR02055 161 CEPCTRPVAPGEDPRAGRWWWEeaAKKECGL 191
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
4-254 1.47e-109

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 315.62  E-value: 1.47e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433   4 ETTRLTEPQLRELAARGAAELDGATATDMLRWTDETFGDIggagggvsghrgwttCNYVVASNMADAVLVDLAAKVRPGV 83
Cdd:PRK02090   3 ALNALPKADLALDLAELNAELEGASAQERLAWALENFGGR---------------LALVSSFGAEDAVLLHLVAQVDPDI 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433  84 PVIFLDTGYHFVETIGTRDAIESVYDVRVLNVTPEHTVAEQDELLGKDLFA--RNPHECCRLRKVVPLGKTLRGYSAWVT 161
Cdd:PRK02090  68 PVIFLDTGYLFPETYRFIDELTERLLLNLKVYRPDASAAEQEARYGGLWEQsvEDRDECCRIRKVEPLNRALAGLDAWIT 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433 162 GLRRVDAPTRANAPLVSFDEtfKLVKVNPLAAWTDQDVQEYIADNDVLVNPLVREGYPSIGCAPCTAKPAEGADPRSGRW 241
Cdd:PRK02090 148 GLRREQSGTRANLPVLEIDG--GRFKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGRW 225

                        250
                 ....*....|...
gi 489507433 242 QGLAKTECGLHAS 254
Cdd:PRK02090 226 WGGLKKECGLHEG 238
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 9-251 1.95e-89

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: 264.02  E-value: 1.95e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433   9 TEPQLRELAARGAAELDgATATDMLRWTDETFGDiggagggvsghrgwttcNYVVASNM--ADAVLVDLAAKVRPGVPVI 86
Cdd:COG0175    2 LPATLDDLLEELNAELE-AEAIEILREAAAEFGG-----------------RVVVSSSGgkDSTVLLHLAAKFKPPIPVL 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433  87 FLDTGYHFVETIGTRDAIESVYDVRVLNVTPEHTVAEQDELLGKDLFARNPHECCRLRKVVPLGKTLRGYS--AWVTGLR 164
Cdd:COG0175   64 FLDTGYEFPETYEFRDRLAERLGLDLIVVRPEDAFAEQLAEFGPPLFYRDPRWCCKIRKVEPLKRALAGYDfdAWITGLR 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433 165 RVDAPTRANAPLVSFDETFKLVKVNPLAAWTDQDVQEYIADNDVLVNPLVREGYPSIGCAPCTAKPAEGADPRSGRWQGL 244
Cdd:COG0175  144 RDESPTRAKEPVVEWDPVGGLIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWWDE 223


                 ....*....
gi 489507433 245 AK--TECGL 251
Cdd:COG0175  224 EKerKECGL 232
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 61-222 4.25e-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: 218.24  E-value: 4.25e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433  61 YVVASNMADAVLVDLAAKVRPGVPVIFLDTGYHFVETIGTRDAIESVYDVRVLNVTPEHTVAEQDELLGK----DLFARN 136
Cdd:cd23945   18 FATSFGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYGLNIEVYFPEGTEAEEEALEGGlnefYLEDEE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433 137 PHECCRLRKVVPLGKTLRGYSAWVTGLRRVDAPTRANAPLVSFDETFKLVKVNPLAAWTDQDVQEYIADNDVLVNPLVRE 216
Cdd:cd23945   98 RYDCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIVEVDEEGGLVKINPLADWTWEDVWAYIREHDLPYNPLHDQ 177


                 ....*.
gi 489507433 217 GYPSIG 222
Cdd:cd23945  178 GYPSIG 183
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 58-229 3.23e-67

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: 205.61  E-value: 3.23e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433   58 TCNYVVASNMADAVLVDLAAKVRPGVPVIFLDTGYHFVETIGTRDAIESVYDVRVLNVTPEHTVAEQDELLGKDLFARNp 137
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSSLYR- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433  138 hECCRLRKVVPLGKTLR--GYSAWVTGLRRVDAPTRANAPLVSFDETF-KLVKVNPLAAWTDQDVQEYIADNDVLVNPLV 214
Cdd:pfam01507  80 -RCCRLRKVEPLKRALKelGFDAWFTGLRRDESPSRAKLPIVSIDGDFpKVIKVFPLLNWTETDVWQYILANNVPYNPLY 158

                         170
                  ....*....|....*
gi 489507433  215 REGYPSIGCAPCTAK 229
Cdd:pfam01507 159 DQGYRSIGCYPCTGP 173
 
Name Accession Description Interval E-value
APS_reductase TIGR02055
thioredoxin-dependent adenylylsulfate APS reductase; This model describes recently identified ...
 65-251 7.06e-111

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: 317.09  E-value: 7.06e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433   65 SNMADAVLVDLAAKVRPGVPVIFLDTGYHFVETIGTRDAIESVYDV-RVLNVTPEHTVAEQDELLGKDLFARN-PHECCR 142
Cdd:TIGR02055   1 LGAEDVVLVDLAAKVRPDVKVFFLDTGRLFKETYETIDQVRERYDIlIDVLSPPPLTVEEQVKEYGLNLFYRSvPHECCG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433  143 LRKVVPLGKTLRGYSAWVTGLRRVDAPTRANAPLVSFDETFKLVKVNPLAAWTDQDVQEYIADNDVLVNPLVREGYPSIG 222
Cdd:TIGR02055  81 IRKVEPLKRALAGVSAWITGLRRDQSPTRAQAPFLEIDEAFGLVKINPLADWTSEDVWEYIADNELPYNPLHDRGYPSIG 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 489507433  223 CAPCTAKPAEGADPRSGRWQGL--AKTECGL 251
Cdd:TIGR02055 161 CEPCTRPVAPGEDPRAGRWWWEeaAKKECGL 191
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
4-254 1.47e-109

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 315.62  E-value: 1.47e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433   4 ETTRLTEPQLRELAARGAAELDGATATDMLRWTDETFGDIggagggvsghrgwttCNYVVASNMADAVLVDLAAKVRPGV 83
Cdd:PRK02090   3 ALNALPKADLALDLAELNAELEGASAQERLAWALENFGGR---------------LALVSSFGAEDAVLLHLVAQVDPDI 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433  84 PVIFLDTGYHFVETIGTRDAIESVYDVRVLNVTPEHTVAEQDELLGKDLFA--RNPHECCRLRKVVPLGKTLRGYSAWVT 161
Cdd:PRK02090  68 PVIFLDTGYLFPETYRFIDELTERLLLNLKVYRPDASAAEQEARYGGLWEQsvEDRDECCRIRKVEPLNRALAGLDAWIT 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433 162 GLRRVDAPTRANAPLVSFDEtfKLVKVNPLAAWTDQDVQEYIADNDVLVNPLVREGYPSIGCAPCTAKPAEGADPRSGRW 241
Cdd:PRK02090 148 GLRREQSGTRANLPVLEIDG--GRFKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGRW 225

                        250
                 ....*....|...
gi 489507433 242 QGLAKTECGLHAS 254
Cdd:PRK02090 226 WGGLKKECGLHEG 238
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 9-251 1.95e-89

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: 264.02  E-value: 1.95e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433   9 TEPQLRELAARGAAELDgATATDMLRWTDETFGDiggagggvsghrgwttcNYVVASNM--ADAVLVDLAAKVRPGVPVI 86
Cdd:COG0175    2 LPATLDDLLEELNAELE-AEAIEILREAAAEFGG-----------------RVVVSSSGgkDSTVLLHLAAKFKPPIPVL 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433  87 FLDTGYHFVETIGTRDAIESVYDVRVLNVTPEHTVAEQDELLGKDLFARNPHECCRLRKVVPLGKTLRGYS--AWVTGLR 164
Cdd:COG0175   64 FLDTGYEFPETYEFRDRLAERLGLDLIVVRPEDAFAEQLAEFGPPLFYRDPRWCCKIRKVEPLKRALAGYDfdAWITGLR 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433 165 RVDAPTRANAPLVSFDETFKLVKVNPLAAWTDQDVQEYIADNDVLVNPLVREGYPSIGCAPCTAKPAEGADPRSGRWQGL 244
Cdd:COG0175  144 RDESPTRAKEPVVEWDPVGGLIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWWDE 223


                 ....*....
gi 489507433 245 AK--TECGL 251
Cdd:COG0175  224 EKerKECGL 232
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 61-222 4.25e-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: 218.24  E-value: 4.25e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433  61 YVVASNMADAVLVDLAAKVRPGVPVIFLDTGYHFVETIGTRDAIESVYDVRVLNVTPEHTVAEQDELLGK----DLFARN 136
Cdd:cd23945   18 FATSFGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYGLNIEVYFPEGTEAEEEALEGGlnefYLEDEE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433 137 PHECCRLRKVVPLGKTLRGYSAWVTGLRRVDAPTRANAPLVSFDETFKLVKVNPLAAWTDQDVQEYIADNDVLVNPLVRE 216
Cdd:cd23945   98 RYDCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIVEVDEEGGLVKINPLADWTWEDVWAYIREHDLPYNPLHDQ 177


                 ....*.
gi 489507433 217 GYPSIG 222
Cdd:cd23945  178 GYPSIG 183
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 58-229 3.23e-67

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: 205.61  E-value: 3.23e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433   58 TCNYVVASNMADAVLVDLAAKVRPGVPVIFLDTGYHFVETIGTRDAIESVYDVRVLNVTPEHTVAEQDELLGKDLFARNp 137
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSSLYR- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433  138 hECCRLRKVVPLGKTLR--GYSAWVTGLRRVDAPTRANAPLVSFDETF-KLVKVNPLAAWTDQDVQEYIADNDVLVNPLV 214
Cdd:pfam01507  80 -RCCRLRKVEPLKRALKelGFDAWFTGLRRDESPSRAKLPIVSIDGDFpKVIKVFPLLNWTETDVWQYILANNVPYNPLY 158

                         170
                  ....*....|....*
gi 489507433  215 REGYPSIGCAPCTAK 229
Cdd:pfam01507 159 DQGYRSIGCYPCTGP 173
cysH TIGR00434
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ...
 70-252 6.72e-66

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: 203.87  E-value: 6.72e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433   70 AVLVDLAAKVRPGVPVIFLDTGYHFVETIGTRDAIESVYDVRVLNVTPEHTVAEQDELLGKDLFARNPHECCRLRKVVPL 149
Cdd:TIGR00434  27 AVLLDLVSKISPDIPVIFLDTGYHFPETYELIDELTERYPLNIKVYKPDLSLAEQAAKYGDKLWEQDPNKYDYLRKVEPM 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433  150 GKTLRGY--SAWVTGLRRVDAPTRANAPLVSFDETFKLVKVNPLAAWTDQDVQEYIADNDVLVNPLVREGYPSIGCAPCT 227
Cdd:TIGR00434 107 HRALKELhaSAWFTGLRRDQGPSRANLSILNIDEKFGILKVLPLIDWTWKDVYQYIDAHNLPYNPLHDQGYPSIGDYHST 186

                         170       180
                  ....*....|....*....|....*
gi 489507433  228 AKPAEGADPRSGRWQGLAKTECGLH 252
Cdd:TIGR00434 187 RPVKEGEDERAGRWKGKAKTECGLH 211
PAPS_reductase TIGR02057
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ...
 22-252 1.70e-48

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: 159.61  E-value: 1.70e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433   22 AELDGATATDMLRWTDETFGDiggagggvsghrgwttcNYVVAS--NMADAVLVDLAAKVR-PGVPVIFLDTGYHFVETI 98
Cdd:TIGR02057   6 EQLEKLTPQEIIAWSIVTFPH-----------------GLVQTSafGIQALVTLHLLSSISePMIPVIFIDTLYHFPQTL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433   99 GTRDAIESVYDVRV-LNVTPE-HTVAEQDELLGKDLFARNPHECCRLRKVVPLGKTLR--GYSAWVTGLRRVDAPTRANA 174
Cdd:TIGR02057  69 TLKDELTKKYYQTLnLYKYDGcESEADFEAKYGKLLWQKDIEKYDYIAKVEPMQRALKelNASAWFTGRRRDQGSARANL 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489507433  175 PLVSFDETFKLVKVNPLAAWTDQDVQEYIADNDVLVNPLVREGYPSIGCAPCTAKPAEGADPRSGRWQGLAKTECGLH 252
Cdd:TIGR02057 149 PVIEIDEQNGILKVNPLIDWTFEQVYQYLDAHNVPYNPLLDQGYRSIGDYHSTRKVKEGEDERAGRWKGKLKTECGIH 226
PLN02309 PLN02309
5'-adenylylsulfate reductase
 69-252 2.79e-36

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 133.38  E-value: 2.79e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433  69 DAVLVDLAAKVRPGVPVIFLDTGYHFVETIGTRDAIESVYDVRVLNVTPEhTVAEQDELLGKDLFA--RNPH-ECCRLRK 145
Cdd:PLN02309 122 DVALIEYAHLTGRPFRVFSLDTGRLNPETYRLFDAVEKHYGIRIEYMFPD-AVEVQALVRNKGLFSfyEDGHqECCRVRK 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433 146 VVPLGKTLRGYSAWVTGLRRVDAP-TRANAPLVSFDETFK--------LVKVNPLAAWTDQDVQEYIADNDVLVNPLVRE 216
Cdd:PLN02309 201 VRPLRRALKGLRAWITGQRKDQSPgTRAEVPVVQVDPVFEgldggpgsLVKWNPLANVTGNEVWNFLRTMDVPVNSLHAQ 280

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 489507433 217 GYPSIGCAPCTAKPAEGADPRSGRW---QGLAKtECGLH 252
Cdd:PLN02309 281 GYVSIGCEPCTRPVLPGQHEREGRWwweDAKAK-ECGLH 318
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 65-252 2.63e-34

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: 128.21  E-value: 2.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433   65 SNMADAVLVDLAAKVRPGVPVIFLDTGYHFVETIGTRDAIESVYDVRVLNVTPEhTVAEQDELLGKDLFA--RNPH-ECC 141
Cdd:TIGR00424 123 SGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRFFDAVEKQYGIRIEYMFPD-AVEVQALVRSKGLFSfyEDGHqECC 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433  142 RLRKVVPLGKTLRGYSAWVTGLRRVDAP-TRANAPLVSFDETFK--------LVKVNPLAAWTDQDVQEYIADNDVLVNP 212
Cdd:TIGR00424 202 RVRKVRPLRRALKGLKAWITGQRKDQSPgTRSEIPVVQVDPVFEgldggvgsLVKWNPVANVEGKDVWNFLRTMDVPVNT 281

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 489507433  213 LVREGYPSIGCAPCTAKPAEGADPRSGR--WQGLAKTECGLH 252
Cdd:TIGR00424 282 LHAQGYVSIGCEPCTRPVLPGQHEREGRwwWEDAKAKECGLH 323
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 71-226 3.02e-14

uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to Escherichia coli YbdN; This subgroup contains Escherichia coli YbdN and other phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8)-like proteins. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP).


Pssm-ID: 467512 [Multi-domain]  Cd Length: 206  Bit Score: 69.34  E-value: 3.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433  71 VLVDLAAKV----RPGVPVIFLDTGYHFVETIgtrDAIESV---YDVRVLNVTPEHT--------VAEQDELLGKDLFAR 135
Cdd:cd23947   27 VLLHLALEAlrrlRKDVYVVFIDTGIEFPETI---DFVEKLaetLGLDVEAARPPLFlewltsnfQPQWDPIWDNPPPPR 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433 136 NPHECCRLRKVVPLGKTLR-----GYSAWVtGLRRVDAPTRANAPLVSF------DETFKLVKVNPLAAWTDQDVQEYIA 204
Cdd:cd23947  104 DYRWCCDELKLEPFTKWLKekkpeGVLLLV-GIRADESLNRAKRPRVYRkygwrnSTLPGQIVAYPIKDWSVEDVWLYIL 182

                        170       180
                 ....*....|....*....|..
gi 489507433 205 DNDVLVNPLVREGYPSIGCAPC 226
Cdd:cd23947  183 RHGLPYNPLYDLGFDRGGCLVC 204
PRK08557 PRK08557
hypothetical protein; Provisional
 70-228 4.46e-10

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 59.00  E-value: 4.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433  70 AVLVDLAAKVRPGVPVIFLDTGYHFVETIGTRDAIESVYDvrvLNVTPEHTVAEQDELLGKDLFARNPHECCRLRKVVPL 149
Cdd:PRK08557 195 SVSTLLAKEVIPDLEVIFIDTGLEYPETINYVKDFAKKYD---LNLDTLDGDNFWENLEKEGIPTKDNRWCNSACKLMPL 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433 150 GKTLR---GYSAWVT--GLRRVDAPTRANaplVSFDETFKLVK----VNPLAAWTDQDVQEYIADNDVLVNPLVREGYPS 220
Cdd:PRK08557 272 KEYLKkkyGNKKVLTidGSRKYESFTRAN---LDYERKSGFIDfqtnVFPILDWNSLDIWSYIYLNDILYNPLYDKGFER 348


                 ....*...
gi 489507433 221 IGCAPCTA 228
Cdd:PRK08557 349 IGCYLCPS 356
PRK13794 PRK13794
hypothetical protein; Provisional
 70-228 5.51e-10

hypothetical protein; Provisional


Pssm-ID: 237509 [Multi-domain]  Cd Length: 479  Bit Score: 58.91  E-value: 5.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433  70 AVLVdLAAKVRPG-VPVIFLDTGYHFVETIGTRDAIESVYDVRVLNVTPE---HTVAEQdellGKDlfARNPHECCRLRK 145
Cdd:PRK13794 262 ATLL-LALKALGInFPVLFNDTGLEFPETLENVEDVEKHYGLEIIRTKSEefwEKLEEY----GPP--ARDNRWCSEVCK 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433 146 VVPLGKTLRgySAWV------TGLRRVDAPTRANAPLVSFDETfklVKVNPLAA----WTDQDVQEYIADNDVLVNPLVR 215
Cdd:PRK13794 335 LEPLGKLID--EKYEgeclsfVGQRKYESFNRSKKPRIWRNPY---IKKQILAApilhWTAMHVWIYLFREKAPYNKLYE 409

                        170
                 ....*....|...
gi 489507433 216 EGYPSIGCAPCTA 228
Cdd:PRK13794 410 QGFDRIGCFMCPA 422
PRK05253 PRK05253
sulfate adenylyltransferase subunit CysD;
70-228 1.68e-07

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 235375  Cd Length: 301  Bit Score: 50.91  E-value: 1.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433  70 AVLVDLAAK-VRPG---VPVIFLDTGYHFVETIGTRDAIESVYDVRVLnvtpEHTVaeQDEL-LGKDLFARNPHECCRLR 144
Cdd:PRK05253  41 SVMLHLARKaFYPGklpFPLLHVDTGWKFPEMIEFRDRRAKELGLELI----VHSN--PEGIaRGINPFRHGSAKHTNAM 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433 145 KVVPLGKTLR--GYSAWVTGLRRVDAPTRANAPLVSF-------D------ETFKL----------VKVNPLAAWTDQDV 199
Cdd:PRK05253 115 KTEGLKQALEkyGFDAAFGGARRDEEKSRAKERIFSFrdefgqwDpknqrpELWNLyngrinkgehIRVFPLSNWTELDI 194

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489507433 200 QEYIA----------------------------------DNDVLVNPLVRegYPSIGCAPCTA 228
Cdd:PRK05253 195 WQYIErenipivplyfaherpvverdgmlimvddrmplrPGEVVEERMVR--FRTLGCYPCTG 255
PRK08576 PRK08576
hypothetical protein; Provisional
 75-228 4.70e-07

hypothetical protein; Provisional


Pssm-ID: 236300 [Multi-domain]  Cd Length: 438  Bit Score: 50.08  E-value: 4.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433  75 LAAKVRPGVPVIFLDTGYHFVETigtRDAIESVydVRVLNVtpEHTVAEQDELLGKDLFARNPHE--CCRLRKVVPLGKT 152
Cdd:PRK08576 253 LAKKAFGDVTAVYVDTGYEMPLT---DEYVEKV--AEKLGV--DLIRAGVDVPMPIEKYGMPTHSnrWCTKLKVEALEEA 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433 153 LRGYS--AWVTGLRRVDAPTRANAPLVSFDET--FKLVKVNPLAAWTDQDVQEYIADNDVLVNPLVREGYPSIGCAPCTA 228
Cdd:PRK08576 326 IRELEdgLLVVGDRDGESARRRLRPPVVERKTnfGKILVVMPIKFWSGAMVQLYILMNGLELNPLYYKGFYRLGCYICPS 405
Sulfate_adenylyltransferase_2 cd23946
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ...
 70-213 1.84e-06

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: 47.49  E-value: 1.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433  70 AVLVDLAAKV----RPGVPVIFLDTGYHFVETIGTRDAIESVYDVRVL-NVTPEHTVAeqdellGKDLFARNPHECCRLR 144
Cdd:cd23946   34 SVMLHLARKAfypgKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDLIvHVNPDGVEA------GINPFTHGSAKHTDIM 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433 145 KVVPLGKTLR--GYSAWVTGLRRVDAPTRANAPLVSFDETF-----------------------KLVKVNPLAAWTDQDV 199
Cdd:cd23946  108 KTEGLKQALDkyGFDAAFGGARRDEEKSRAKERVYSFRDSNhrwdpknqrpelwnqyngrvkkgESIRVFPLSNWTELDI 187

                        170
                 ....*....|....
gi 489507433 200 QEYIADNDVLVNPL 213
Cdd:cd23946  188 WQYIYLENIPIVPL 201
PRK13795 PRK13795
hypothetical protein; Provisional
 70-228 7.10e-05

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 43.44  E-value: 7.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433  70 AVLvDLAAKVRPGVPVIFLDTGYHFVETIGTRDAIESVYDVRVLNVTPEHTVAEQDELLGKDlfARNPHECCRLRKVVPL 149
Cdd:PRK13795 258 VVL-DLAREALKDFKAFFNNTGLEFPETVENVKEVAEEYGIELIEADAGDAFWRAVEKFGPP--ARDYRWCCKVCKLGPI 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507433 150 GKTLR-----GYSAWVtGLRRVDAPTRANAPLVsfdETFKLV----KVNPLAAWTDQDVQEYIADNDVLVNPLVREGYPS 220
Cdd:PRK13795 335 TRAIKenfpkGCLTFV-GQRKYESFSRAKSPRV---WRNPWVpnqiGASPIQDWTALEVWLYIFWRKLPYNPLYERGFDR 410


                 ....*...
gi 489507433 221 IGCAPCTA 228
Cdd:PRK13795 411 IGCWLCPS 418
 
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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