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Conserved domains on  [gi|259586100|sp|C5D5A7|]
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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 ...
 24-233 3.00e-109

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: 312.88  E-value: 3.00e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100   24 ALDVLTWAFRQYKDDIVYACSFGVEGIVLIDLISQVKPDAEIVFLDTGLHFRETYKTIEKVKEKYPsLRIVMKKPSLSLE 103
Cdd:TIGR00434   1 AQEIIAWAYVTFGGHLVYSTSFGIQGAVLLDLVSKISPDIPVIFLDTGYHFPETYELIDELTERYP-LNIKVYKPDLSLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100  104 EQAQQLGDELWKHNPNKCCELRKVIPLREALTGIT--AWISGLRREQSPTRSHVEYINKDDKFKSIKICPLIHWTWKDVW 181
Cdd:TIGR00434  80 EQAAKYGDKLWEQDPNKYDYLRKVEPMHRALKELHasAWFTGLRRDQGPSRANLSILNIDEKFGILKVLPLIDWTWKDVY 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 259586100  182 NYVYKRRLPYNVLHDRGYPSIGCEPCTSPALDPNDLRSGRWVGHGKTECGLH 233
Cdd:TIGR00434 160 QYIDAHNLPYNPLHDQGYPSIGDYHSTRPVKEGEDERAGRWKGKAKTECGLH 211
 
Name Accession Description Interval E-value
cysH TIGR00434
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ...
 24-233 3.00e-109

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: 312.88  E-value: 3.00e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100   24 ALDVLTWAFRQYKDDIVYACSFGVEGIVLIDLISQVKPDAEIVFLDTGLHFRETYKTIEKVKEKYPsLRIVMKKPSLSLE 103
Cdd:TIGR00434   1 AQEIIAWAYVTFGGHLVYSTSFGIQGAVLLDLVSKISPDIPVIFLDTGYHFPETYELIDELTERYP-LNIKVYKPDLSLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100  104 EQAQQLGDELWKHNPNKCCELRKVIPLREALTGIT--AWISGLRREQSPTRSHVEYINKDDKFKSIKICPLIHWTWKDVW 181
Cdd:TIGR00434  80 EQAAKYGDKLWEQDPNKYDYLRKVEPMHRALKELHasAWFTGLRRDQGPSRANLSILNIDEKFGILKVLPLIDWTWKDVY 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 259586100  182 NYVYKRRLPYNVLHDRGYPSIGCEPCTSPALDPNDLRSGRWVGHGKTECGLH 233
Cdd:TIGR00434 160 QYIDAHNLPYNPLHDQGYPSIGDYHSTRPVKEGEDERAGRWKGKAKTECGLH 211
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 24-232 1.26e-95

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: 279.04  E-value: 1.26e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100  24 ALDVLTWAFRQYKDDIVYACSFGVEGIVLIDLISQVKPDAEIVFLDTGLHFRETYKTIEKVKEKYPsLRIVMKKPSLSLE 103
Cdd:COG0175   21 AIEILREAAAEFGGRVVVSSSGGKDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDRLAERLG-LDLIVVRPEDAFA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100 104 EQAQQLGDELWKHNPNKCCELRKVIPLREALTG--ITAWISGLRREQSPTRSHVEYINKDDKFKSIKICPLIHWTWKDVW 181
Cdd:COG0175  100 EQLAEFGPPLFYRDPRWCCKIRKVEPLKRALAGydFDAWITGLRRDESPTRAKEPVVEWDPVGGLIKVNPLADWTELDVW 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 259586100 182 NYVYKRRLPYNVLHDRGYPSIGCEPCTSPALDPNDLRSGRWVGHGK--TECGL 232
Cdd:COG0175  180 AYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWWDEEKerKECGL 232
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
20-235 6.67e-91

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 267.47  E-value: 6.67e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100  20 ETKGALDVLTWAFRQYKDDIVYACSFGVEGIVLIDLISQVKPDAEIVFLDTGLHFRETYKTIEKVKEKYpSLRIVMKKPS 99
Cdd:PRK02090  24 EGASAQERLAWALENFGGRLALVSSFGAEDAVLLHLVAQVDPDIPVIFLDTGYLFPETYRFIDELTERL-LLNLKVYRPD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100 100 LSLEEQAQQLGDeLWKH---NPNKCCELRKVIPLREALTGITAWISGLRREQSPTRSHVEYINKDDKFksIKICPLIHWT 176
Cdd:PRK02090 103 ASAAEQEARYGG-LWEQsveDRDECCRIRKVEPLNRALAGLDAWITGLRREQSGTRANLPVLEIDGGR--FKINPLADWT 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 259586100 177 WKDVWNYVYKRRLPYNVLHDRGYPSIGCEPCTSPALDPNDLRSGRWVGHGKTECGLHIS 235
Cdd:PRK02090 180 NEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGRWWGGLKKECGLHEG 238
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 24-203 7.05e-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: 224.78  E-value: 7.05e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100  24 ALDVLTWAFRQYKDDIVYACSFGVEGIVLIDLISQVKPDAEIVFLDTGLHFRETYKTIEKVKEKYPsLRIVMKKPSLSLE 103
Cdd:cd23945    1 PLEILLWAAEEFGPKLVFATSFGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYG-LNIEVYFPEGTEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100 104 EQAQQLG--DELWKHNPNK--CCELRKVIPLREALTGITAWISGLRREQSPTRSHVEYINKDDKFKSIKICPLIHWTWKD 179
Cdd:cd23945   80 EEEALEGglNEFYLEDEERydCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIVEVDEEGGLVKINPLADWTWED 159

                        170       180
                 ....*....|....*....|....
gi 259586100 180 VWNYVYKRRLPYNVLHDRGYPSIG 203
Cdd:cd23945  160 VWAYIREHDLPYNPLHDQGYPSIG 183
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 39-210 3.11e-65

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: 199.83  E-value: 3.11e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100   39 IVYACSFGVEGIVLIDLISQVKPDAEIVFLDTGLHFRETYKTIEKVKEKYPsLRIVMKKPSLSLEEQAQQLGDELWKHNp 118
Cdd:pfam01507   2 LVVSFSGGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYG-LNLKVYLPEDSFAEGINPEGIPSSLYR- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100  119 nKCCELRKVIPLREAL--TGITAWISGLRREQSPTRSHVEYINKDDKF-KSIKICPLIHWTWKDVWNYVYKRRLPYNVLH 195
Cdd:pfam01507  80 -RCCRLRKVEPLKRALkeLGFDAWFTGLRRDESPSRAKLPIVSIDGDFpKVIKVFPLLNWTETDVWQYILANNVPYNPLY 158

                         170
                  ....*....|....*
gi 259586100  196 DRGYPSIGCEPCTSP 210
Cdd:pfam01507 159 DQGYRSIGCYPCTGP 173
 
Name Accession Description Interval E-value
cysH TIGR00434
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ...
 24-233 3.00e-109

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: 312.88  E-value: 3.00e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100   24 ALDVLTWAFRQYKDDIVYACSFGVEGIVLIDLISQVKPDAEIVFLDTGLHFRETYKTIEKVKEKYPsLRIVMKKPSLSLE 103
Cdd:TIGR00434   1 AQEIIAWAYVTFGGHLVYSTSFGIQGAVLLDLVSKISPDIPVIFLDTGYHFPETYELIDELTERYP-LNIKVYKPDLSLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100  104 EQAQQLGDELWKHNPNKCCELRKVIPLREALTGIT--AWISGLRREQSPTRSHVEYINKDDKFKSIKICPLIHWTWKDVW 181
Cdd:TIGR00434  80 EQAAKYGDKLWEQDPNKYDYLRKVEPMHRALKELHasAWFTGLRRDQGPSRANLSILNIDEKFGILKVLPLIDWTWKDVY 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 259586100  182 NYVYKRRLPYNVLHDRGYPSIGCEPCTSPALDPNDLRSGRWVGHGKTECGLH 233
Cdd:TIGR00434 160 QYIDAHNLPYNPLHDQGYPSIGDYHSTRPVKEGEDERAGRWKGKAKTECGLH 211
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 24-232 1.26e-95

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: 279.04  E-value: 1.26e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100  24 ALDVLTWAFRQYKDDIVYACSFGVEGIVLIDLISQVKPDAEIVFLDTGLHFRETYKTIEKVKEKYPsLRIVMKKPSLSLE 103
Cdd:COG0175   21 AIEILREAAAEFGGRVVVSSSGGKDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDRLAERLG-LDLIVVRPEDAFA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100 104 EQAQQLGDELWKHNPNKCCELRKVIPLREALTG--ITAWISGLRREQSPTRSHVEYINKDDKFKSIKICPLIHWTWKDVW 181
Cdd:COG0175  100 EQLAEFGPPLFYRDPRWCCKIRKVEPLKRALAGydFDAWITGLRRDESPTRAKEPVVEWDPVGGLIKVNPLADWTELDVW 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 259586100 182 NYVYKRRLPYNVLHDRGYPSIGCEPCTSPALDPNDLRSGRWVGHGK--TECGL 232
Cdd:COG0175  180 AYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWWDEEKerKECGL 232
APS_reductase TIGR02055
thioredoxin-dependent adenylylsulfate APS reductase; This model describes recently identified ...
 45-232 9.52e-94

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: 272.79  E-value: 9.52e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100   45 FGVEGIVLIDLISQVKPDAEIVFLDTGLHFRETYKTIEKVKEKYPSLRIVMKKPSLSLEEQAQQLGDELW-KHNPNKCCE 123
Cdd:TIGR02055   1 LGAEDVVLVDLAAKVRPDVKVFFLDTGRLFKETYETIDQVRERYDILIDVLSPPPLTVEEQVKEYGLNLFyRSVPHECCG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100  124 LRKVIPLREALTGITAWISGLRREQSPTRSHVEYINKDDKFKSIKICPLIHWTWKDVWNYVYKRRLPYNVLHDRGYPSIG 203
Cdd:TIGR02055  81 IRKVEPLKRALAGVSAWITGLRRDQSPTRAQAPFLEIDEAFGLVKINPLADWTSEDVWEYIADNELPYNPLHDRGYPSIG 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 259586100  204 CEPCTSPALDPNDLRSGRWVG--HGKTECGL 232
Cdd:TIGR02055 161 CEPCTRPVAPGEDPRAGRWWWeeAAKKECGL 191
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
20-235 6.67e-91

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 267.47  E-value: 6.67e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100  20 ETKGALDVLTWAFRQYKDDIVYACSFGVEGIVLIDLISQVKPDAEIVFLDTGLHFRETYKTIEKVKEKYpSLRIVMKKPS 99
Cdd:PRK02090  24 EGASAQERLAWALENFGGRLALVSSFGAEDAVLLHLVAQVDPDIPVIFLDTGYLFPETYRFIDELTERL-LLNLKVYRPD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100 100 LSLEEQAQQLGDeLWKH---NPNKCCELRKVIPLREALTGITAWISGLRREQSPTRSHVEYINKDDKFksIKICPLIHWT 176
Cdd:PRK02090 103 ASAAEQEARYGG-LWEQsveDRDECCRIRKVEPLNRALAGLDAWITGLRREQSGTRANLPVLEIDGGR--FKINPLADWT 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 259586100 177 WKDVWNYVYKRRLPYNVLHDRGYPSIGCEPCTSPALDPNDLRSGRWVGHGKTECGLHIS 235
Cdd:PRK02090 180 NEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGRWWGGLKKECGLHEG 238
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 24-203 7.05e-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: 224.78  E-value: 7.05e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100  24 ALDVLTWAFRQYKDDIVYACSFGVEGIVLIDLISQVKPDAEIVFLDTGLHFRETYKTIEKVKEKYPsLRIVMKKPSLSLE 103
Cdd:cd23945    1 PLEILLWAAEEFGPKLVFATSFGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYG-LNIEVYFPEGTEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100 104 EQAQQLG--DELWKHNPNK--CCELRKVIPLREALTGITAWISGLRREQSPTRSHVEYINKDDKFKSIKICPLIHWTWKD 179
Cdd:cd23945   80 EEEALEGglNEFYLEDEERydCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIVEVDEEGGLVKINPLADWTWED 159

                        170       180
                 ....*....|....*....|....
gi 259586100 180 VWNYVYKRRLPYNVLHDRGYPSIG 203
Cdd:cd23945  160 VWAYIREHDLPYNPLHDQGYPSIG 183
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 39-210 3.11e-65

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: 199.83  E-value: 3.11e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100   39 IVYACSFGVEGIVLIDLISQVKPDAEIVFLDTGLHFRETYKTIEKVKEKYPsLRIVMKKPSLSLEEQAQQLGDELWKHNp 118
Cdd:pfam01507   2 LVVSFSGGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYG-LNLKVYLPEDSFAEGINPEGIPSSLYR- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100  119 nKCCELRKVIPLREAL--TGITAWISGLRREQSPTRSHVEYINKDDKF-KSIKICPLIHWTWKDVWNYVYKRRLPYNVLH 195
Cdd:pfam01507  80 -RCCRLRKVEPLKRALkeLGFDAWFTGLRRDESPSRAKLPIVSIDGDFpKVIKVFPLLNWTETDVWQYILANNVPYNPLY 158

                         170
                  ....*....|....*
gi 259586100  196 DRGYPSIGCEPCTSP 210
Cdd:pfam01507 159 DQGYRSIGCYPCTGP 173
PAPS_reductase TIGR02057
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ...
 20-233 4.79e-54

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: 173.10  E-value: 4.79e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100   20 ETKGALDVLTWAFRQYKDDIVYACSFGVEGIVLIDLISQ-VKPDAEIVFLDTGLHFRETYKTIEKVKEKYpSLRIVMKKP 98
Cdd:TIGR02057   9 EKLTPQEIIAWSIVTFPHGLVQTSAFGIQALVTLHLLSSiSEPMIPVIFIDTLYHFPQTLTLKDELTKKY-YQTLNLYKY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100   99 --SLSLEEQAQQLGDELWKHNPNKCCELRKVIPLREALT--GITAWISGLRREQSPTRSHVEYINKDDKFKSIKICPLIH 174
Cdd:TIGR02057  88 dgCESEADFEAKYGKLLWQKDIEKYDYIAKVEPMQRALKelNASAWFTGRRRDQGSARANLPVIEIDEQNGILKVNPLID 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 259586100  175 WTWKDVWNYVYKRRLPYNVLHDRGYPSIGCEPCTSPALDPNDLRSGRWVGHGKTECGLH 233
Cdd:TIGR02057 168 WTFEQVYQYLDAHNVPYNPLLDQGYRSIGDYHSTRKVKEGEDERAGRWKGKLKTECGIH 226
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 8-233 1.02e-39

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: 142.08  E-value: 1.02e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100    8 EAEEKPSFPHDNETKGALDVLTWAFRQYKDDIVYACSfGVEGIVLIDLISQVKPDAEIVFLDTGLHFRETYKTIEKVKEK 87
Cdd:TIGR00424  87 EVEDFEKLAKKLENASPLEIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRFFDAVEKQ 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100   88 YpSLRIVMKKPSlSLEEQAQQLGDEL---WKHNPNKCCELRKVIPLREALTGITAWISGLRREQSP-TRSHVEYINKDDK 163
Cdd:TIGR00424 166 Y-GIRIEYMFPD-AVEVQALVRSKGLfsfYEDGHQECCRVRKVRPLRRALKGLKAWITGQRKDQSPgTRSEIPVVQVDPV 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100  164 FKS--------IKICPLIHWTWKDVWNYVYKRRLPYNVLHDRGYPSIGCEPCTSPALDPNDLRSGRWVGHG--KTECGLH 233
Cdd:TIGR00424 244 FEGldggvgslVKWNPVANVEGKDVWNFLRTMDVPVNTLHAQGYVSIGCEPCTRPVLPGQHEREGRWWWEDakAKECGLH 323
PLN02309 PLN02309
5'-adenylylsulfate reductase
 20-233 1.63e-37

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 136.07  E-value: 1.63e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100  20 ETKGALDVLTWAFRQYKDDIVYACSfGVEGIVLIDLISQVKPDAEIVFLDTGLHFRETYKTIEKVkEKYPSLRI------ 93
Cdd:PLN02309  94 ENASPLEIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRLFDAV-EKHYGIRIeymfpd 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100  94 -------VMKKPSLSLEEQAQQlgdelwkhnpnKCCELRKVIPLREALTGITAWISGLRREQSP-TRSHVEYINKDDKFK 165
Cdd:PLN02309 172 avevqalVRNKGLFSFYEDGHQ-----------ECCRVRKVRPLRRALKGLRAWITGQRKDQSPgTRAEVPVVQVDPVFE 240

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 259586100 166 S--------IKICPLIHWTWKDVWNYVYKRRLPYNVLHDRGYPSIGCEPCTSPALDPNDLRSGRWV---GHGKtECGLH 233
Cdd:PLN02309 241 GldggpgslVKWNPLANVTGNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCTRPVLPGQHEREGRWWwedAKAK-ECGLH 318
PRK13794 PRK13794
hypothetical protein; Provisional
 64-213 6.43e-19

hypothetical protein; Provisional


Pssm-ID: 237509 [Multi-domain]  Cd Length: 479  Bit Score: 84.72  E-value: 6.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100  64 EIVFLDTGLHFRETYKTIEKVKEKYpSLRIVMKKPS---LSLEEQAQQLGDELWkhnpnkCCELRKVIPLREAL-----T 135
Cdd:PRK13794 276 PVLFNDTGLEFPETLENVEDVEKHY-GLEIIRTKSEefwEKLEEYGPPARDNRW------CSEVCKLEPLGKLIdekyeG 348

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 259586100 136 GITAWIsGLRREQSPTRSHVEYINKDDKF-KSIKICPLIHWTWKDVWNYVYKRRLPYNVLHDRGYPSIGCEPCtsPALD 213
Cdd:PRK13794 349 ECLSFV-GQRKYESFNRSKKPRIWRNPYIkKQILAAPILHWTAMHVWIYLFREKAPYNKLYEQGFDRIGCFMC--PAME 424
PRK08557 PRK08557
hypothetical protein; Provisional
 22-218 4.45e-18

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 82.11  E-value: 4.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100  22 KGALDVLTWAFRQYKD-DIVYACSF--GVEGIVLIDLISQVKPDAEIVFLDTGLHFRETYKTIEKVKEKYPSLRIVMKKP 98
Cdd:PRK08557 164 ENSLSILKDYIEKYKNkGYAINASFsgGKDSSVSTLLAKEVIPDLEVIFIDTGLEYPETINYVKDFAKKYDLNLDTLDGD 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100  99 SL--SLEEQAQQLGDELWkhnpnkCCELRKVIPLREALTGITAW-----ISGLRREQSPTRSHVEYINKDDKFK-SIKIC 170
Cdd:PRK08557 244 NFweNLEKEGIPTKDNRW------CNSACKLMPLKEYLKKKYGNkkvltIDGSRKYESFTRANLDYERKSGFIDfQTNVF 317

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 259586100 171 PLIHWTWKDVWNYVYKRRLPYNVLHDRGYPSIGCEPCTSpALDPNDLR 218
Cdd:PRK08557 318 PILDWNSLDIWSYIYLNDILYNPLYDKGFERIGCYLCPS-ALNSEFLR 364
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 53-207 5.79e-16

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: 73.58  E-value: 5.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100  53 IDLISQVKPDAEIVFLDTGLHFRETYKTIEKVKEKYpSLRIVMKKPSLSLE---EQAQQLGDELWKHNP-----NKCCEL 124
Cdd:cd23947   33 LEALRRLRKDVYVVFIDTGIEFPETIDFVEKLAETL-GLDVEAARPPLFLEwltSNFQPQWDPIWDNPPpprdyRWCCDE 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100 125 RKVIPLREAL-----TGITAWIsGLRREQSPTRSHVEYINKDDKFKS------IKICPLIHWTWKDVWNYVYKRRLPYNV 193
Cdd:cd23947  112 LKLEPFTKWLkekkpEGVLLLV-GIRADESLNRAKRPRVYRKYGWRNstlpgqIVAYPIKDWSVEDVWLYILRHGLPYNP 190

                        170
                 ....*....|....
gi 259586100 194 LHDRGYPSIGCEPC 207
Cdd:cd23947  191 LYDLGFDRGGCLVC 204
PRK13795 PRK13795
hypothetical protein; Provisional
 34-209 9.55e-16

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 75.80  E-value: 9.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100  34 QYKDDIVYACSFGVEGIVLIDLISQVKPDAEIVFLDTGLHFRETYKTIEKVKEKYpSLRIVMKKPSLSLEEQAQQLG--- 110
Cdd:PRK13795 241 KYNLPVSVSFSGGKDSLVVLDLAREALKDFKAFFNNTGLEFPETVENVKEVAEEY-GIELIEADAGDAFWRAVEKFGppa 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100 111 -DELWkhnpnkCCELRKVIPLREALTG------ITawISGLRREQSPTRSHVEYINKDdKF--KSIKICPLIHWTWKDVW 181
Cdd:PRK13795 320 rDYRW------CCKVCKLGPITRAIKEnfpkgcLT--FVGQRKYESFSRAKSPRVWRN-PWvpNQIGASPIQDWTALEVW 390

                        170       180
                 ....*....|....*....|....*...
gi 259586100 182 NYVYKRRLPYNVLHDRGYPSIGCEPCTS 209
Cdd:PRK13795 391 LYIFWRKLPYNPLYERGFDRIGCWLCPS 418
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 169-203 2.03e-08

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: 52.14  E-value: 2.03e-08
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 259586100 169 ICPLIHWTWKDVWNYVYKRRLPYNVLHDRGYPSIG 203
Cdd:cd23948  136 VNPILDWSYHDVWEFLRTLNLPYCSLYDQGYTSLG 170
Sulfate_adenylyltransferase_2 cd23946
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ...
 60-190 2.52e-08

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: 52.50  E-value: 2.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100  60 KPDAEIVFLDTGLHFRETYKTIEKVKEKYPSLRIVMKKPslsleeQAQQLGDELWKHNPNKCCELRKVIPLREALT--GI 137
Cdd:cd23946   48 KPPFPLLHVDTTWKFREMIEFRDRVAKEYGLDLIVHVNP------DGVEAGINPFTHGSAKHTDIMKTEGLKQALDkyGF 121

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 259586100 138 TAWISGLRREQSPTRSHVE-----------------------YINKDDKFKSIKICPLIHWTWKDVWNYVYKRRLP 190
Cdd:cd23946  122 DAAFGGARRDEEKSRAKERvysfrdsnhrwdpknqrpelwnqYNGRVKKGESIRVFPLSNWTELDIWQYIYLENIP 197
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
 24-95 3.68e-05

Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 41.68  E-value: 3.68e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 259586100  24 ALDVLTWAFRQYKD-DIVYACSFGVEGIvliDLISQVKPDaeIVFLD------TGLHFretyktIEKVKEKYPSLRIVM 95
Cdd:COG4753   11 IREGLKRILEWEAGfEVVGEAENGEEAL---ELLEEHKPD--LVITDinmpgmDGLEL------LEAIRELDPDTKIII 78
PRK08576 PRK08576
hypothetical protein; Provisional
 33-212 6.78e-05

hypothetical protein; Provisional


Pssm-ID: 236300 [Multi-domain]  Cd Length: 438  Bit Score: 43.14  E-value: 6.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100  33 RQYKD-DIVYACSFGVEGIVLIDLISQVKPDAEIVFLDTGLHFRETYKTIEKVKEKypsLRIVMKKPSLSLEEQAQQLGd 111
Cdd:PRK08576 230 RKFEEwTVIVPWSGGKDSTAALLLAKKAFGDVTAVYVDTGYEMPLTDEYVEKVAEK---LGVDLIRAGVDVPMPIEKYG- 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259586100 112 eLWKHNpNKCCELRKVIPLREALTGIT--AWISGLRREQSPTRS--HVEYINKDDKFKSIKICPLIHWTWKDVWNYVYKR 187
Cdd:PRK08576 306 -MPTHS-NRWCTKLKVEALEEAIRELEdgLLVVGDRDGESARRRlrPPVVERKTNFGKILVVMPIKFWSGAMVQLYILMN 383

                        170       180
                 ....*....|....*....|....*
gi 259586100 188 RLPYNVLHDRGYPSIGCEPCtsPAL 212
Cdd:PRK08576 384 GLELNPLYYKGFYRLGCYIC--PSL 406
 
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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