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Conserved domains on  [gi|123661322|sp|Q4L9F3|]
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RecName: Full=Adenosine 5'-phosphosulfate reductase; Short=APS reductase; AltName: Full=5'-adenylylsulfate reductase; AltName: Full=Thioredoxin-dependent 5'-adenylylsulfate reductase

Protein Classification

adenine nucleotide alpha hydrolase family protein( domain architecture ID 188)

AANH (adenine nucleotide alpha hydrolase) family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AANH_superfamily super family cl00292
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ...
 29-238 4.81e-108

Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase (AANH) superfamily includes N-type ATP PPases, ATP sulfurylases, universal stress response proteins (USPs), and electron transfer flavoproteins (ETFs). The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


The actual alignment was detected with superfamily member TIGR00434:

Pssm-ID: 469708  Cd Length: 212  Bit Score: 310.18  E-value: 4.81e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322   29 AYEILEWAYRTYGDSIVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFPkLRIEMKKPDLTLE 108
Cdd:TIGR00434   1 AQEIIAWAYVTFGGHLVYSTSFGIQGAVLLDLVSKISPDIPVIFLDTGYHFPETYELIDELTERYP-LNIKVYKPDLSLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322  109 EQADKYNPALWKNNPNQCCYIRKIKPLEEVLGG--AVAWVSGLRRDQSPTRANTNFINKDERFKSVKVCPLIYWTEDEVW 186
Cdd:TIGR00434  80 EQAAKYGDKLWEQDPNKYDYLRKVEPMHRALKElhASAWFTGLRRDQGPSRANLSILNIDEKFGILKVLPLIDWTWKDVY 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 123661322  187 DYIKKHDLPYNALHDQHYPSIGCIPCTAPVFDSEDSRAGRWSNFDKTECGLH 238
Cdd:TIGR00434 160 QYIDAHNLPYNPLHDQGYPSIGDYHSTRPVKEGEDERAGRWKGKAKTECGLH 211
 
Name Accession Description Interval E-value
cysH TIGR00434
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ...
 29-238 4.81e-108

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: 310.18  E-value: 4.81e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322   29 AYEILEWAYRTYGDSIVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFPkLRIEMKKPDLTLE 108
Cdd:TIGR00434   1 AQEIIAWAYVTFGGHLVYSTSFGIQGAVLLDLVSKISPDIPVIFLDTGYHFPETYELIDELTERYP-LNIKVYKPDLSLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322  109 EQADKYNPALWKNNPNQCCYIRKIKPLEEVLGG--AVAWVSGLRRDQSPTRANTNFINKDERFKSVKVCPLIYWTEDEVW 186
Cdd:TIGR00434  80 EQAAKYGDKLWEQDPNKYDYLRKVEPMHRALKElhASAWFTGLRRDQGPSRANLSILNIDEKFGILKVLPLIDWTWKDVY 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 123661322  187 DYIKKHDLPYNALHDQHYPSIGCIPCTAPVFDSEDSRAGRWSNFDKTECGLH 238
Cdd:TIGR00434 160 QYIDAHNLPYNPLHDQGYPSIGDYHSTRPVKEGEDERAGRWKGKAKTECGLH 211
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 29-237 2.35e-103

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: 299.07  E-value: 2.35e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322  29 AYEILEWAYRTYGDSIVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFpKLRIEMKKPDLTLE 108
Cdd:COG0175   21 AIEILREAAAEFGGRVVVSSSGGKDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDRLAERL-GLDLIVVRPEDAFA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 109 EQADKYNPALWKNNPNQCCYIRKIKPLEEVLGG--AVAWVSGLRRDQSPTRANTNFINKDERFKSVKVCPLIYWTEDEVW 186
Cdd:COG0175  100 EQLAEFGPPLFYRDPRWCCKIRKVEPLKRALAGydFDAWITGLRRDESPTRAKEPVVEWDPVGGLIKVNPLADWTELDVW 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 123661322 187 DYIKKHDLPYNALHDQHYPSIGCIPCTAPVFDSEDSRAGRWSNFDK--TECGL 237
Cdd:COG0175  180 AYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWWDEEKerKECGL 232
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
25-243 5.40e-100

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 290.97  E-value: 5.40e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322  25 ATKGAYEILEWAYRTYGDSIVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFpKLRIEMKKPD 104
Cdd:PRK02090  24 EGASAQERLAWALENFGGRLALVSSFGAEDAVLLHLVAQVDPDIPVIFLDTGYLFPETYRFIDELTERL-LLNLKVYRPD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 105 LTLEEQADKYNPaLWKN---NPNQCCYIRKIKPLEEVLGGAVAWVSGLRRDQSPTRANTNFINKDErfKSVKVCPLIYWT 181
Cdd:PRK02090 103 ASAAEQEARYGG-LWEQsveDRDECCRIRKVEPLNRALAGLDAWITGLRREQSGTRANLPVLEIDG--GRFKINPLADWT 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123661322 182 EDEVWDYIKKHDLPYNALHDQHYPSIGCIPCTAPVFDSEDSRAGRWSNFDKTECGLHVADKP 243
Cdd:PRK02090 180 NEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGRWWGGLKKECGLHEGNLP 241
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 31-208 2.04e-76

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


Pssm-ID: 467510 [Multi-domain]  Cd Length: 183  Bit Score: 229.02  E-value: 2.04e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322  31 EILEWAYRTYGDSIVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFPkLRIEMKKPDLTLEEQ 110
Cdd:cd23945    3 EILLWAAEEFGPKLVFATSFGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYG-LNIEVYFPEGTEAEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 111 --ADKYNPALWK--NNPNQCCYIRKIKPLEEVLGGAVAWVSGLRRDQSPTRANTNFINKDERFKSVKVCPLIYWTEDEVW 186
Cdd:cd23945   82 eaLEGGLNEFYLedEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIVEVDEEGGLVKINPLADWTWEDVW 161

                        170       180
                 ....*....|....*....|..
gi 123661322 187 DYIKKHDLPYNALHDQHYPSIG 208
Cdd:cd23945  162 AYIREHDLPYNPLHDQGYPSIG 183
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 44-215 2.37e-66

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: 202.91  E-value: 2.37e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322   44 IVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFPkLRIEMKKPDLTLEEQADKYNPALWKNNp 123
Cdd:pfam01507   2 LVVSFSGGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYG-LNLKVYLPEDSFAEGINPEGIPSSLYR- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322  124 nQCCYIRKIKPLEEVLG--GAVAWVSGLRRDQSPTRANTNFINKDERF-KSVKVCPLIYWTEDEVWDYIKKHDLPYNALH 200
Cdd:pfam01507  80 -RCCRLRKVEPLKRALKelGFDAWFTGLRRDESPSRAKLPIVSIDGDFpKVIKVFPLLNWTETDVWQYILANNVPYNPLY 158

                         170
                  ....*....|....*
gi 123661322  201 DQHYPSIGCIPCTAP 215
Cdd:pfam01507 159 DQGYRSIGCYPCTGP 173
 
Name Accession Description Interval E-value
cysH TIGR00434
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ...
 29-238 4.81e-108

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: 310.18  E-value: 4.81e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322   29 AYEILEWAYRTYGDSIVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFPkLRIEMKKPDLTLE 108
Cdd:TIGR00434   1 AQEIIAWAYVTFGGHLVYSTSFGIQGAVLLDLVSKISPDIPVIFLDTGYHFPETYELIDELTERYP-LNIKVYKPDLSLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322  109 EQADKYNPALWKNNPNQCCYIRKIKPLEEVLGG--AVAWVSGLRRDQSPTRANTNFINKDERFKSVKVCPLIYWTEDEVW 186
Cdd:TIGR00434  80 EQAAKYGDKLWEQDPNKYDYLRKVEPMHRALKElhASAWFTGLRRDQGPSRANLSILNIDEKFGILKVLPLIDWTWKDVY 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 123661322  187 DYIKKHDLPYNALHDQHYPSIGCIPCTAPVFDSEDSRAGRWSNFDKTECGLH 238
Cdd:TIGR00434 160 QYIDAHNLPYNPLHDQGYPSIGDYHSTRPVKEGEDERAGRWKGKAKTECGLH 211
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 29-237 2.35e-103

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: 299.07  E-value: 2.35e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322  29 AYEILEWAYRTYGDSIVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFpKLRIEMKKPDLTLE 108
Cdd:COG0175   21 AIEILREAAAEFGGRVVVSSSGGKDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDRLAERL-GLDLIVVRPEDAFA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 109 EQADKYNPALWKNNPNQCCYIRKIKPLEEVLGG--AVAWVSGLRRDQSPTRANTNFINKDERFKSVKVCPLIYWTEDEVW 186
Cdd:COG0175  100 EQLAEFGPPLFYRDPRWCCKIRKVEPLKRALAGydFDAWITGLRRDESPTRAKEPVVEWDPVGGLIKVNPLADWTELDVW 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 123661322 187 DYIKKHDLPYNALHDQHYPSIGCIPCTAPVFDSEDSRAGRWSNFDK--TECGL 237
Cdd:COG0175  180 AYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWWDEEKerKECGL 232
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
25-243 5.40e-100

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 290.97  E-value: 5.40e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322  25 ATKGAYEILEWAYRTYGDSIVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFpKLRIEMKKPD 104
Cdd:PRK02090  24 EGASAQERLAWALENFGGRLALVSSFGAEDAVLLHLVAQVDPDIPVIFLDTGYLFPETYRFIDELTERL-LLNLKVYRPD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 105 LTLEEQADKYNPaLWKN---NPNQCCYIRKIKPLEEVLGGAVAWVSGLRRDQSPTRANTNFINKDErfKSVKVCPLIYWT 181
Cdd:PRK02090 103 ASAAEQEARYGG-LWEQsveDRDECCRIRKVEPLNRALAGLDAWITGLRREQSGTRANLPVLEIDG--GRFKINPLADWT 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123661322 182 EDEVWDYIKKHDLPYNALHDQHYPSIGCIPCTAPVFDSEDSRAGRWSNFDKTECGLHVADKP 243
Cdd:PRK02090 180 NEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGRWWGGLKKECGLHEGNLP 241
APS_reductase TIGR02055
thioredoxin-dependent adenylylsulfate APS reductase; This model describes recently identified ...
 50-237 2.08e-97

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: 282.42  E-value: 2.08e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322   50 FGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFPKLRIEMKKPDLTLEEQADKYNPALW-KNNPNQCCY 128
Cdd:TIGR02055   1 LGAEDVVLVDLAAKVRPDVKVFFLDTGRLFKETYETIDQVRERYDILIDVLSPPPLTVEEQVKEYGLNLFyRSVPHECCG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322  129 IRKIKPLEEVLGGAVAWVSGLRRDQSPTRANTNFINKDERFKSVKVCPLIYWTEDEVWDYIKKHDLPYNALHDQHYPSIG 208
Cdd:TIGR02055  81 IRKVEPLKRALAGVSAWITGLRRDQSPTRAQAPFLEIDEAFGLVKINPLADWTSEDVWEYIADNELPYNPLHDRGYPSIG 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 123661322  209 CIPCTAPVFDSEDSRAGRW--SNFDKTECGL 237
Cdd:TIGR02055 161 CEPCTRPVAPGEDPRAGRWwwEEAAKKECGL 191
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 31-208 2.04e-76

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


Pssm-ID: 467510 [Multi-domain]  Cd Length: 183  Bit Score: 229.02  E-value: 2.04e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322  31 EILEWAYRTYGDSIVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFPkLRIEMKKPDLTLEEQ 110
Cdd:cd23945    3 EILLWAAEEFGPKLVFATSFGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYG-LNIEVYFPEGTEAEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 111 --ADKYNPALWK--NNPNQCCYIRKIKPLEEVLGGAVAWVSGLRRDQSPTRANTNFINKDERFKSVKVCPLIYWTEDEVW 186
Cdd:cd23945   82 eaLEGGLNEFYLedEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIVEVDEEGGLVKINPLADWTWEDVW 161

                        170       180
                 ....*....|....*....|..
gi 123661322 187 DYIKKHDLPYNALHDQHYPSIG 208
Cdd:cd23945  162 AYIREHDLPYNPLHDQGYPSIG 183
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 44-215 2.37e-66

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: 202.91  E-value: 2.37e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322   44 IVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFPkLRIEMKKPDLTLEEQADKYNPALWKNNp 123
Cdd:pfam01507   2 LVVSFSGGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYG-LNLKVYLPEDSFAEGINPEGIPSSLYR- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322  124 nQCCYIRKIKPLEEVLG--GAVAWVSGLRRDQSPTRANTNFINKDERF-KSVKVCPLIYWTEDEVWDYIKKHDLPYNALH 200
Cdd:pfam01507  80 -RCCRLRKVEPLKRALKelGFDAWFTGLRRDESPSRAKLPIVSIDGDFpKVIKVFPLLNWTETDVWQYILANNVPYNPLY 158

                         170
                  ....*....|....*
gi 123661322  201 DQHYPSIGCIPCTAP 215
Cdd:pfam01507 159 DQGYRSIGCYPCTGP 173
PAPS_reductase TIGR02057
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ...
 29-238 1.65e-61

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: 192.74  E-value: 1.65e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322   29 AYEILEWAYRTYGDSIVYSCSFGAESMVLIDLIYQI-KPDAQIVFLDTDLHFQETYDLIDRVKEHFpKLRIEMKKPD--L 105
Cdd:TIGR02057  13 PQEIIAWSIVTFPHGLVQTSAFGIQALVTLHLLSSIsEPMIPVIFIDTLYHFPQTLTLKDELTKKY-YQTLNLYKYDgcE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322  106 TLEEQADKYNPALWKNNPNQCCYIRKIKPLEEVLG--GAVAWVSGLRRDQSPTRANTNFINKDERFKSVKVCPLIYWTED 183
Cdd:TIGR02057  92 SEADFEAKYGKLLWQKDIEKYDYIAKVEPMQRALKelNASAWFTGRRRDQGSARANLPVIEIDEQNGILKVNPLIDWTFE 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 123661322  184 EVWDYIKKHDLPYNALHDQHYPSIGCIPCTAPVFDSEDSRAGRWSNFDKTECGLH 238
Cdd:TIGR02057 172 QVYQYLDAHNVPYNPLLDQGYRSIGDYHSTRKVKEGEDERAGRWKGKLKTECGIH 226
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 31-238 1.97e-40

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: 144.39  E-value: 1.97e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322   31 EILEWAYRTYGDSIVYSCSfGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFpKLRIEMKKPDlTLEEQ 110
Cdd:TIGR00424 105 EIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRFFDAVEKQY-GIRIEYMFPD-AVEVQ 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322  111 ADKYNPAL---WKNNPNQCCYIRKIKPLEEVLGGAVAWVSGLRRDQSP-TRANTNFINKDERFKSVK--VCPLIYWTE-- 182
Cdd:TIGR00424 182 ALVRSKGLfsfYEDGHQECCRVRKVRPLRRALKGLKAWITGQRKDQSPgTRSEIPVVQVDPVFEGLDggVGSLVKWNPva 261

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123661322  183 ----DEVWDYIKKHDLPYNALHDQHYPSIGCIPCTAPVFDSEDSRAGR--WSNFDKTECGLH 238
Cdd:TIGR00424 262 nvegKDVWNFLRTMDVPVNTLHAQGYVSIGCEPCTRPVLPGQHEREGRwwWEDAKAKECGLH 323
PLN02309 PLN02309
5'-adenylylsulfate reductase
 31-238 3.39e-40

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 143.78  E-value: 3.39e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322  31 EILEWAYRTYGDSIVYSCSfGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFpKLRIEMKKPDlTLEEQ 110
Cdd:PLN02309 100 EIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRLFDAVEKHY-GIRIEYMFPD-AVEVQ 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 111 A---DKYNPALWKNNPNQCCYIRKIKPLEEVLGGAVAWVSGLRRDQSP-TRANTNFINKDERFKS--------VKVCPLI 178
Cdd:PLN02309 177 AlvrNKGLFSFYEDGHQECCRVRKVRPLRRALKGLRAWITGQRKDQSPgTRAEVPVVQVDPVFEGldggpgslVKWNPLA 256

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123661322 179 YWTEDEVWDYIKKHDLPYNALHDQHYPSIGCIPCTAPVFDSEDSRAGRWSNFDKT--ECGLH 238
Cdd:PLN02309 257 NVTGNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCTRPVLPGQHEREGRWWWEDAKakECGLH 318
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 29-212 1.31e-23

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: 94.38  E-value: 1.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322  29 AYEILEWAYRTyGDSIVYSCSFGAESMVLIDL----IYQIKPDAQIVFLDTDLHFQETYDLIDRVKEhFPKLRIEMKKPD 104
Cdd:cd23947    1 ALERIRKVFEE-FDPVIVSFSGGKDSLVLLHLaleaLRRLRKDVYVVFIDTGIEFPETIDFVEKLAE-TLGLDVEAARPP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 105 LTLE---EQADKYNPALWKNNP-----NQCCYIRKIKPLEEVL----GGAVAWVSGLRRDQSPTRANTNFINKDERFKS- 171
Cdd:cd23947   79 LFLEwltSNFQPQWDPIWDNPPpprdyRWCCDELKLEPFTKWLkekkPEGVLLLVGIRADESLNRAKRPRVYRKYGWRNs 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 123661322 172 -----VKVCPLIYWTEDEVWDYIKKHDLPYNALHDQHYPSIGCIPC 212
Cdd:cd23947  159 tlpgqIVAYPIKDWSVEDVWLYILRHGLPYNPLYDLGFDRGGCLVC 204
PRK13794 PRK13794
hypothetical protein; Provisional
 70-214 3.29e-14

hypothetical protein; Provisional


Pssm-ID: 237509 [Multi-domain]  Cd Length: 479  Bit Score: 71.24  E-value: 3.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322  70 IVFLDTDLHFQETYDLIDRVKEHF--PKLRIEMKKPDLTLEEQADKYNPALWknnpnqCCYIRKIKPLEEVL-----GGA 142
Cdd:PRK13794 277 VLFNDTGLEFPETLENVEDVEKHYglEIIRTKSEEFWEKLEEYGPPARDNRW------CSEVCKLEPLGKLIdekyeGEC 350

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123661322 143 VAWVsGLRRDQSPTRANTNFINKDERF-KSVKVCPLIYWTEDEVWDYIKKHDLPYNALHDQHYPSIGCIPCTA 214
Cdd:PRK13794 351 LSFV-GQRKYESFNRSKKPRIWRNPYIkKQILAAPILHWTAMHVWIYLFREKAPYNKLYEQGFDRIGCFMCPA 422
PRK13795 PRK13795
hypothetical protein; Provisional
 40-214 1.72e-12

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 66.17  E-value: 1.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322  40 YGDSIVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFpKLRIEMKKPDLTLEEQADKYNP--- 116
Cdd:PRK13795 242 YNLPVSVSFSGGKDSLVVLDLAREALKDFKAFFNNTGLEFPETVENVKEVAEEY-GIELIEADAGDAFWRAVEKFGPpar 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 117 -ALWknnpnqCCYIRKIKP----LEEVLGGAVAWVSGLRRDQSPTRANTNFINKDErF--KSVKVCPLIYWTEDEVWDYI 189
Cdd:PRK13795 321 dYRW------CCKVCKLGPitraIKENFPKGCLTFVGQRKYESFSRAKSPRVWRNP-WvpNQIGASPIQDWTALEVWLYI 393

                        170       180
                 ....*....|....*....|....*
gi 123661322 190 KKHDLPYNALHDQHYPSIGCIPCTA 214
Cdd:PRK13795 394 FWRKLPYNPLYERGFDRIGCWLCPS 418
PRK08557 PRK08557
hypothetical protein; Provisional
 27-214 9.18e-12

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 64.00  E-value: 9.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322  27 KGAYEILEWAYRTY---GDSIVYSCSFGAESMVLIDLIYQIKPDAQIVFLDTDLHFQETydlIDRVKEHfpklrieMKKP 103
Cdd:PRK08557 164 ENSLSILKDYIEKYknkGYAINASFSGGKDSSVSTLLAKEVIPDLEVIFIDTGLEYPET---INYVKDF-------AKKY 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 104 DLTLEE-QADKYNPALWKNN-PNQ----CCYIRKIKPLEEVL-----GGAVAWVSGLRRDQSPTRANTNFiNKDERF--K 170
Cdd:PRK08557 234 DLNLDTlDGDNFWENLEKEGiPTKdnrwCNSACKLMPLKEYLkkkygNKKVLTIDGSRKYESFTRANLDY-ERKSGFidF 312

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 123661322 171 SVKVCPLIYWTEDEVWDYIKKHDLPYNALHDQHYPSIGCIPCTA 214
Cdd:PRK08557 313 QTNVFPILDWNSLDIWSYIYLNDILYNPLYDKGFERIGCYLCPS 356
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 174-208 1.98e-07

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


Pssm-ID: 467513 [Multi-domain]  Cd Length: 179  Bit Score: 49.44  E-value: 1.98e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 123661322 174 VCPLIYWTEDEVWDYIKKHDLPYNALHDQHYPSIG 208
Cdd:cd23948  136 VNPILDWSYHDVWEFLRTLNLPYCSLYDQGYTSLG 170
Sulfate_adenylyltransferase_2 cd23946
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ...
 32-200 4.41e-07

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: 49.03  E-value: 4.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322  32 ILEWAYRTYGDSIVYScSFGAESMVLIDL----IYQIKPDAQIVFLDTDLHFQETYDLIDRVKEHFPKLRIEMKKPDLTl 107
Cdd:cd23946   12 IIREVAAEFSNPVMLY-SIGKDSSVMLHLarkaFYPGKPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDLIVHVNPDGV- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 108 eeqADKYNPalWKNNPNQCCYIRKIKPLEEVLG--GAVAWVSGLRRDQSPTRANT---NFINKDERF------------- 169
Cdd:cd23946   90 ---EAGINP--FTHGSAKHTDIMKTEGLKQALDkyGFDAAFGGARRDEEKSRAKErvySFRDSNHRWdpknqrpelwnqy 164

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 123661322 170 -------KSVKVCPLIYWTEDEVWDYIKKHDLPYNALH 200
Cdd:cd23946  165 ngrvkkgESIRVFPLSNWTELDIWQYIYLENIPIVPLY 202
PRK12563 PRK12563
sulfate adenylyltransferase subunit CysD;
49-216 9.55e-05

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 237138  Cd Length: 312  Bit Score: 42.85  E-value: 9.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322  49 SFGAESMVLIDL----IYQIKPDAQIVFLDTDLHFQETYDLIDRVkehfpklrieMKKPDLTL------EEQADKYNP-- 116
Cdd:PRK12563  45 SIGKDSVVMLHLamkaFRPTRPPFPLLHVDTTWKFREMIDFRDRR----------AKELGLDLvvhhnpDGIARGIVPfr 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 117 ---ALWKNnpnqccyIRKIKPLEEVLG--GAVAWVSGLRRDQSPTRANTN-FINKDE----------------------R 168
Cdd:PRK12563 115 hgsALHTD-------VAKTQGLKQALDhhGFDAAIGGARRDEEKSRAKERiFSFRSAfhrwdpkaqrpelwslynarlrR 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 169 FKSVKVCPLIYWTEDEVWDYIKKHDLPYNALH------------------DQHYP---------------SIGCIPCTAP 215
Cdd:PRK12563 188 GESLRVFPLSNWTELDVWQYIAREKIPLVPLYfakrrpvverdgllimvdDERTPlrpgetpqqrkvrfrTLGCYPLTGA 267


                 .
gi 123661322 216 V 216
Cdd:PRK12563 268 V 268
PRK08576 PRK08576
hypothetical protein; Provisional
 67-214 2.99e-04

hypothetical protein; Provisional


Pssm-ID: 236300 [Multi-domain]  Cd Length: 438  Bit Score: 41.60  E-value: 2.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322  67 DAQIVFLDTDLHFQETYDLIDRVKEhfpKLRIEMKKPDLTLEEQADKYN-PalwkNNPNQCCYIRKIKPLEEVLG----G 141
Cdd:PRK08576 260 DVTAVYVDTGYEMPLTDEYVEKVAE---KLGVDLIRAGVDVPMPIEKYGmP----THSNRWCTKLKVEALEEAIReledG 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123661322 142 AVawVSGLRRDQSPTR--------ANTNFINKDErfksvkVCPLIYWTEDEVWDYIKKHDLPYNALHDQHYPSIGCIPCT 213
Cdd:PRK08576 333 LL--VVGDRDGESARRrlrppvveRKTNFGKILV------VMPIKFWSGAMVQLYILMNGLELNPLYYKGFYRLGCYICP 404


                 .
gi 123661322 214 A 214
Cdd:PRK08576 405 S 405
 
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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