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Conserved domains on  [gi|392891368|ref|NP_001254234|]
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FAD synthase [Caenorhabditis elegans]

Protein Classification

FAD synthase( domain architecture ID 19233630)

FAD (Flavin adenine dinucleotide) synthase catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme

CATH:  3.40.50.620
EC:  2.7.7.2
Gene Ontology:  GO:0005524|GO:0003919|GO:0006747
PubMed:  19375431|12012333
SCOP:  3001593

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 161-339 3.91e-93

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: 275.94  E-value: 3.91e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368 161 KLNEAESIVEEIVEKYPLEQIALSFNGGKDCTVLLHLLRLKVDEKY-GPSTPIQGFHIMVEDQFPEATQFIIDAAKFYNI 239
Cdd:cd23948    1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYpSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368 240 QVLEFPGPLKTGLAALKKTRPSIIPVLMGSRATDPNGKYMKtPVEWTDSDWPQVLRVCPILNWTYTDVWHMLRGLCVPYC 319
Cdd:cd23948   81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLK-PFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYC 159

                        170       180
                 ....*....|....*....|
gi 392891368 320 KLYDQGYTSLGGRDNTVKHP 339
Cdd:cd23948  160 SLYDQGYTSLGSVDNTLPNP 179
 
Name Accession Description Interval E-value
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 161-339 3.91e-93

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: 275.94  E-value: 3.91e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368 161 KLNEAESIVEEIVEKYPLEQIALSFNGGKDCTVLLHLLRLKVDEKY-GPSTPIQGFHIMVEDQFPEATQFIIDAAKFYNI 239
Cdd:cd23948    1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYpSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368 240 QVLEFPGPLKTGLAALKKTRPSIIPVLMGSRATDPNGKYMKtPVEWTDSDWPQVLRVCPILNWTYTDVWHMLRGLCVPYC 319
Cdd:cd23948   81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLK-PFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYC 159

                        170       180
                 ....*....|....*....|
gi 392891368 320 KLYDQGYTSLGGRDNTVKHP 339
Cdd:cd23948  160 SLYDQGYTSLGSVDNTLPNP 179
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 180-337 2.61e-47

Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine phosphosulfate (PAPS) reductase enzymes or PAPS sulfotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). It is also found in NodP nodulation protein P from Rhizobium which has ATP sulfurylase activity (sulfate adenylate transferase).


Pssm-ID: 396201 [Multi-domain]  Cd Length: 173  Bit Score: 158.61  E-value: 2.61e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368  180 QIALSFNGGKDCTVLLHLLRLKVDekygpstPIQGFHIMVEDQFPEATQFIIDAAKFYNIqVLEFPGPLKTGLAA----- 254
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHLASKAFP-------PGPVIFIDTGYEFPETYEFVDELEEKYGL-NLKVYLPEDSFAEGinpeg 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368  255 -----------LKKTRPSIIP--------VLMGSRATDPNgKYMKTPVEWTDSDWPQVLRVCPILNWTYTDVWHMLRGLC 315
Cdd:pfam01507  73 ipsslyrrccrLRKVEPLKRAlkelgfdaWFTGLRRDESP-SRAKLPIVSIDGDFPKVIKVFPLLNWTETDVWQYILANN 151

                         170       180
                  ....*....|....*....|..
gi 392891368  316 VPYCKLYDQGYTSLGGRDNTVK 337
Cdd:pfam01507 152 VPYNPLYDQGYRSIGCYPCTGP 173
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 163-330 1.51e-19

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: 86.44  E-value: 1.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368 163 NEAESIVEEIVEKYPlEQIALSFNGGKDCTVLLHLLRlkvdeKYGPSTPIqgFHImveD---QFPEATQFIIDAAKFYNI 239
Cdd:COG0175   19 AEAIEILREAAAEFG-GRVVVSSSGGKDSTVLLHLAA-----KFKPPIPV--LFL---DtgyEFPETYEFRDRLAERLGL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368 240 QV------------LEFPGP-------------LKTG--LAALKKTRPSIipVLMGSRAtDPNGKYMKTPVEWTDSDwPQ 292
Cdd:COG0175   88 DLivvrpedafaeqLAEFGPplfyrdprwcckiRKVEplKRALAGYDFDA--WITGLRR-DESPTRAKEPVVEWDPV-GG 163

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 392891368 293 VLRVCPILNWTYTDVWHMLRGLCVPYCKLYDQGYTSLG 330
Cdd:COG0175  164 LIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIG 201
PRK13795 PRK13795
hypothetical protein; Provisional
 150-330 6.72e-11

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 63.47  E-value: 6.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368 150 KASENQIEfiQKLNEAESIVEEIVEKYPLEqIALSFNGGKDCTVLLHLLRLKVDEkygpstpiqgFHIMVED---QFPEA 226
Cdd:PRK13795 218 EANRKHLE--EKEKEAVNFIRGVAEKYNLP-VSVSFSGGKDSLVVLDLAREALKD----------FKAFFNNtglEFPET 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368 227 TQFIIDAAKFYNIQVLE-------------FPGPLK--------TGLA----ALKKTRPSIIPVLMGSRatdpngKY--- 278
Cdd:PRK13795 285 VENVKEVAEEYGIELIEadagdafwravekFGPPARdyrwcckvCKLGpitrAIKENFPKGCLTFVGQR------KYesf 358

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 392891368 279 --MKTPVEWTdSDW-PQVLRVCPILNWTYTDVW---HMlRGLcvPYCKLYDQGYTSLG 330
Cdd:PRK13795 359 srAKSPRVWR-NPWvPNQIGASPIQDWTALEVWlyiFW-RKL--PYNPLYERGFDRIG 412
cysH TIGR00434
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ...
 293-330 1.90e-07

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: 51.33  E-value: 1.90e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 392891368  293 VLRVCPILNWTYTDVWHMLRGLCVPYCKLYDQGYTSLG 330
Cdd:TIGR00434 144 ILKVLPLIDWTWKDVYQYIDAHNLPYNPLHDQGYPSIG 181
 
Name Accession Description Interval E-value
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 161-339 3.91e-93

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: 275.94  E-value: 3.91e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368 161 KLNEAESIVEEIVEKYPLEQIALSFNGGKDCTVLLHLLRLKVDEKY-GPSTPIQGFHIMVEDQFPEATQFIIDAAKFYNI 239
Cdd:cd23948    1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYpSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368 240 QVLEFPGPLKTGLAALKKTRPSIIPVLMGSRATDPNGKYMKtPVEWTDSDWPQVLRVCPILNWTYTDVWHMLRGLCVPYC 319
Cdd:cd23948   81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLK-PFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYC 159

                        170       180
                 ....*....|....*....|
gi 392891368 320 KLYDQGYTSLGGRDNTVKHP 339
Cdd:cd23948  160 SLYDQGYTSLGSVDNTLPNP 179
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 180-337 2.61e-47

Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine phosphosulfate (PAPS) reductase enzymes or PAPS sulfotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). It is also found in NodP nodulation protein P from Rhizobium which has ATP sulfurylase activity (sulfate adenylate transferase).


Pssm-ID: 396201 [Multi-domain]  Cd Length: 173  Bit Score: 158.61  E-value: 2.61e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368  180 QIALSFNGGKDCTVLLHLLRLKVDekygpstPIQGFHIMVEDQFPEATQFIIDAAKFYNIqVLEFPGPLKTGLAA----- 254
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHLASKAFP-------PGPVIFIDTGYEFPETYEFVDELEEKYGL-NLKVYLPEDSFAEGinpeg 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368  255 -----------LKKTRPSIIP--------VLMGSRATDPNgKYMKTPVEWTDSDWPQVLRVCPILNWTYTDVWHMLRGLC 315
Cdd:pfam01507  73 ipsslyrrccrLRKVEPLKRAlkelgfdaWFTGLRRDESP-SRAKLPIVSIDGDFPKVIKVFPLLNWTETDVWQYILANN 151

                         170       180
                  ....*....|....*....|..
gi 392891368  316 VPYCKLYDQGYTSLGGRDNTVK 337
Cdd:pfam01507 152 VPYNPLYDQGYRSIGCYPCTGP 173
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 163-330 1.51e-19

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: 86.44  E-value: 1.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368 163 NEAESIVEEIVEKYPlEQIALSFNGGKDCTVLLHLLRlkvdeKYGPSTPIqgFHImveD---QFPEATQFIIDAAKFYNI 239
Cdd:COG0175   19 AEAIEILREAAAEFG-GRVVVSSSGGKDSTVLLHLAA-----KFKPPIPV--LFL---DtgyEFPETYEFRDRLAERLGL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368 240 QV------------LEFPGP-------------LKTG--LAALKKTRPSIipVLMGSRAtDPNGKYMKTPVEWTDSDwPQ 292
Cdd:COG0175   88 DLivvrpedafaeqLAEFGPplfyrdprwcckiRKVEplKRALAGYDFDA--WITGLRR-DESPTRAKEPVVEWDPV-GG 163

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 392891368 293 VLRVCPILNWTYTDVWHMLRGLCVPYCKLYDQGYTSLG 330
Cdd:COG0175  164 LIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIG 201
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 166-330 1.89e-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: 71.27  E-value: 1.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368 166 ESIVEEIVEKYPleqIALSFNGGKDCTVLLHLLrLKVDEKYGPSTPIqgFHIMVEDQFPEATQFIIDAAKFYNIQVL--- 242
Cdd:cd23947    3 ERIRKVFEEFDP---VIVSFSGGKDSLVLLHLA-LEALRRLRKDVYV--VFIDTGIEFPETIDFVEKLAETLGLDVEaar 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368 243 ----------------------EFPG--------PLKTGLAA--LKKTRPSIIPVLMGSRATDP----NGKYMKTPVEWT 286
Cdd:cd23947   77 pplflewltsnfqpqwdpiwdnPPPPrdyrwccdELKLEPFTkwLKEKKPEGVLLLVGIRADESlnraKRPRVYRKYGWR 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 392891368 287 DSDWPQVLRVCPILNWTYTDVWHMLRGLCVPYCKLYDQGYTSLG 330
Cdd:cd23947  157 NSTLPGQIVAYPIKDWSVEDVWLYILRHGLPYNPLYDLGFDRGG 200
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 165-330 3.67e-11

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: 61.46  E-value: 3.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368 165 AESIVEEIVEKYPlEQIALSFNGGKDCTVLLHLLRlkvdeKYGPSTPI----QGFHimvedqFPEATQFIIDAAKFYNIQ 240
Cdd:cd23945    1 PLEILLWAAEEFG-PKLVFATSFGAEDAVILDLLS-----KVRPDIPVvfldTGYL------FPETYDLIDEVEARYGLN 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368 241 VLEFPGPLK--------TGLAALKKTRP------SIIPVL--------------------MGSRATDPngkymktPVEWT 286
Cdd:cd23945   69 IEVYFPEGTeaeeealeGGLNEFYLEDEerydccRKRKPFplalallgvkawitgrrrdqSPTRANLP-------IVEVD 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 392891368 287 DSDwpQVLRVCPILNWTYTDVWHMLRGLCVPYCKLYDQGYTSLG 330
Cdd:cd23945  142 EEG--GLVKINPLADWTWEDVWAYIREHDLPYNPLHDQGYPSIG 183
PRK13795 PRK13795
hypothetical protein; Provisional
 150-330 6.72e-11

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 63.47  E-value: 6.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368 150 KASENQIEfiQKLNEAESIVEEIVEKYPLEqIALSFNGGKDCTVLLHLLRLKVDEkygpstpiqgFHIMVED---QFPEA 226
Cdd:PRK13795 218 EANRKHLE--EKEKEAVNFIRGVAEKYNLP-VSVSFSGGKDSLVVLDLAREALKD----------FKAFFNNtglEFPET 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368 227 TQFIIDAAKFYNIQVLE-------------FPGPLK--------TGLA----ALKKTRPSIIPVLMGSRatdpngKY--- 278
Cdd:PRK13795 285 VENVKEVAEEYGIELIEadagdafwravekFGPPARdyrwcckvCKLGpitrAIKENFPKGCLTFVGQR------KYesf 358

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 392891368 279 --MKTPVEWTdSDW-PQVLRVCPILNWTYTDVW---HMlRGLcvPYCKLYDQGYTSLG 330
Cdd:PRK13795 359 srAKSPRVWR-NPWvPNQIGASPIQDWTALEVWlyiFW-RKL--PYNPLYERGFDRIG 412
cysH TIGR00434
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ...
 293-330 1.90e-07

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: 51.33  E-value: 1.90e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 392891368  293 VLRVCPILNWTYTDVWHMLRGLCVPYCKLYDQGYTSLG 330
Cdd:TIGR00434 144 ILKVLPLIDWTWKDVYQYIDAHNLPYNPLHDQGYPSIG 181
PRK13794 PRK13794
hypothetical protein; Provisional
 164-330 3.37e-06

hypothetical protein; Provisional


Pssm-ID: 237509 [Multi-domain]  Cd Length: 479  Bit Score: 48.90  E-value: 3.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368 164 EAESI--VEEIVEKYPLeQIALSFNGGKDCTVLLhLLRLKVDEKygpstpiqGFHIMVED---QFPEATQFIIDAAKFYN 238
Cdd:PRK13794 232 ERNSIgfIRNTAEKINK-PVTVAYSGGKDSLATL-LLALKALGI--------NFPVLFNDtglEFPETLENVEDVEKHYG 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368 239 IQVL-----EF---------PG-------------PLKTglaALKKTRPSIIPVLMGSRatdpngKY-----MKTPVEWT 286
Cdd:PRK13794 302 LEIIrtkseEFwekleeygpPArdnrwcsevcklePLGK---LIDEKYEGECLSFVGQR------KYesfnrSKKPRIWR 372

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 392891368 287 DSDWPQVLRVCPILNWTYTDVWHMLRGLCVPYCKLYDQGYTSLG 330
Cdd:PRK13794 373 NPYIKKQILAAPILHWTAMHVWIYLFREKAPYNKLYEQGFDRIG 416
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
292-330 5.19e-06

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 47.14  E-value: 5.19e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 392891368 292 QVLRVCPILNWTYTDVWHMLRGLCVPYCKLYDQGYTSLG 330
Cdd:PRK02090 168 GRFKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIG 206
PAPS_reductase TIGR02057
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ...
 165-337 2.89e-05

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: 44.82  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368  165 AESIVEEIVEKYPLEqIALSFNGGKDCTVLLHLLRLKVDekygPSTPI----QGFHimvedqFPEATQFIIDAAKFYN-- 238
Cdd:TIGR02057  13 PQEIIAWSIVTFPHG-LVQTSAFGIQALVTLHLLSSISE----PMIPVifidTLYH------FPQTLTLKDELTKKYYqt 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368  239 IQVLEFPGPLK-----------------TGLAALKKTRP--------SIIPVLMGSRATDPNGKYMKTPVEWTDSDwpQV 293
Cdd:TIGR02057  82 LNLYKYDGCESeadfeakygkllwqkdiEKYDYIAKVEPmqralkelNASAWFTGRRRDQGSARANLPVIEIDEQN--GI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 392891368  294 LRVCPILNWTYTDVWHMLRGLCVPYCKLYDQGYTSLGGRDNTVK 337
Cdd:TIGR02057 160 LKVNPLIDWTFEQVYQYLDAHNVPYNPLLDQGYRSIGDYHSTRK 203
PRK08557 PRK08557
hypothetical protein; Provisional
 157-330 3.77e-04

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 42.05  E-value: 3.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368 157 EFIQKL-NEAESIVEEIVEKYPLEQIAL--SFNGGKDCTVLLHLLRLKVDEkygpstpIQGFHIMVEDQFPEATQFIIDA 233
Cdd:PRK08557 157 ERIEKLeENSLSILKDYIEKYKNKGYAInaSFSGGKDSSVSTLLAKEVIPD-------LEVIFIDTGLEYPETINYVKDF 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891368 234 AKFYNIQVLEFPG---------------------------PLKTGLAalKKTRPSIIPVLMGSRA----TDPNGKYmktp 282
Cdd:PRK08557 230 AKKYDLNLDTLDGdnfwenlekegiptkdnrwcnsacklmPLKEYLK--KKYGNKKVLTIDGSRKyesfTRANLDY---- 303

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 392891368 283 vEWTDSDWPQVLRVCPILNWTYTDVWHMLRGLCVPYCKLYDQGYTSLG 330
Cdd:PRK08557 304 -ERKSGFIDFQTNVFPILDWNSLDIWSYIYLNDILYNPLYDKGFERIG 350
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 181-235 2.00e-03

adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


Pssm-ID: 467490 [Multi-domain]  Cd Length: 74  Bit Score: 36.66  E-value: 2.00e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 392891368 181 IALSFNGGKDCTVLLHLLRlkvdeKYGPSTPIQGFHIMVEDQFPEATQFIIDAAK 235
Cdd:cd01986    1 VVVGYSGGKDSSVALHLAS-----RLGRKAEVAVVHIDHGIGFKEEAESVASIAR 50
 
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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