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Conserved domains on  [gi|506391080|ref|WP_015910799|]
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lipoyl synthase [Halorubrum lacusprofundi]

Protein Classification

lipoyl synthase( domain architecture ID 11481046)

lipoyl synthase is a radical SAM protein that catalyzes the formation of the lipoyl cofactor by catalyzing the insertion of sulfur atoms into the 6 and 8 positions of protein-bound derivatives of octanoic acid

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK05481 PRK05481
lipoyl synthase; Provisional
1-291 2.26e-178

lipoyl synthase; Provisional


:

Pssm-ID: 235493 [Multi-domain]  Cd Length: 289  Bit Score: 493.84  E-value: 2.26e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080   1 MQRGRRKPDWLKSRPPSGSRFTEIKERLRERDLHTVCEEANCPNMGECWSGrdgpGTATFMLMGDRCSRGCNFCDVETGG 80
Cdd:PRK05481   1 AEKVARKPDWLRVKLPTGEEYTEIKKLLRELGLHTVCEEASCPNIGECWSR----GTATFMILGDICTRRCPFCDVATGR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080  81 MKSLDSDEPENVADAVAEIGLDYVVLTSVDRDDLADGGSEHFAETIREIQRRDPEILVETLIPDFQGDPEAIDRIIDAGP 160
Cdd:PRK05481  77 PLPLDPDEPERVAEAVARMGLKYVVITSVDRDDLPDGGAQHFAETIRAIRELNPGTTIEVLIPDFRGRMDALLTVLDARP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080 161 DVIAHNVETVERLQWPVRdRRADYEQSLAVLDRVGRES-DIHTKTSLMLGVGEYDHEVYRTLGDLSEVGVDVVTFGQYLQ 239
Cdd:PRK05481 157 DVFNHNLETVPRLYKRVR-PGADYERSLELLKRAKELHpGIPTKSGLMVGLGETDEEVLEVMDDLRAAGVDILTIGQYLQ 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 506391080 240 PSRSHLDVFEYVHPDVFETWRAVAErEFDFLYCASGPMVRSSYKAGELFVEA 291
Cdd:PRK05481 236 PSRKHLPVERYVTPEEFDEYKEIAL-ELGFLHVASGPLVRSSYHADEQAAGA 286
 
Name Accession Description Interval E-value
PRK05481 PRK05481
lipoyl synthase; Provisional
1-291 2.26e-178

lipoyl synthase; Provisional


Pssm-ID: 235493 [Multi-domain]  Cd Length: 289  Bit Score: 493.84  E-value: 2.26e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080   1 MQRGRRKPDWLKSRPPSGSRFTEIKERLRERDLHTVCEEANCPNMGECWSGrdgpGTATFMLMGDRCSRGCNFCDVETGG 80
Cdd:PRK05481   1 AEKVARKPDWLRVKLPTGEEYTEIKKLLRELGLHTVCEEASCPNIGECWSR----GTATFMILGDICTRRCPFCDVATGR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080  81 MKSLDSDEPENVADAVAEIGLDYVVLTSVDRDDLADGGSEHFAETIREIQRRDPEILVETLIPDFQGDPEAIDRIIDAGP 160
Cdd:PRK05481  77 PLPLDPDEPERVAEAVARMGLKYVVITSVDRDDLPDGGAQHFAETIRAIRELNPGTTIEVLIPDFRGRMDALLTVLDARP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080 161 DVIAHNVETVERLQWPVRdRRADYEQSLAVLDRVGRES-DIHTKTSLMLGVGEYDHEVYRTLGDLSEVGVDVVTFGQYLQ 239
Cdd:PRK05481 157 DVFNHNLETVPRLYKRVR-PGADYERSLELLKRAKELHpGIPTKSGLMVGLGETDEEVLEVMDDLRAAGVDILTIGQYLQ 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 506391080 240 PSRSHLDVFEYVHPDVFETWRAVAErEFDFLYCASGPMVRSSYKAGELFVEA 291
Cdd:PRK05481 236 PSRKHLPVERYVTPEEFDEYKEIAL-ELGFLHVASGPLVRSSYHADEQAAGA 286
LipA COG0320
Lipoate synthase [Coenzyme transport and metabolism]; Lipoate synthase is part of the Pathway ...
5-296 2.63e-178

Lipoate synthase [Coenzyme transport and metabolism]; Lipoate synthase is part of the Pathway/BioSystem: Lipoate biosynthesis


Pssm-ID: 440089 [Multi-domain]  Cd Length: 306  Bit Score: 494.62  E-value: 2.63e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080   5 RRKPDWLKSRPPSGSRFTEIKERLRERDLHTVCEEANCPNMGECWSGrdgpGTATFMLMGDRCSRGCNFCDVETGGMKSL 84
Cdd:COG0320   20 LRKPDWLRVKLPTGPEYAEVKKLLREHKLHTVCEEARCPNIGECWSR----GTATFMILGDICTRRCRFCDVATGRPLPL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080  85 DSDEPENVADAVAEIGLDYVVLTSVDRDDLADGGSEHFAETIREIQRRDPEILVETLIPDFQGDPEAIDRIIDAGPDVIA 164
Cdd:COG0320   96 DPDEPERVAEAVAEMGLKYVVITSVDRDDLPDGGAGHFAETIRAIRELNPGTTIEVLIPDFRGREEALDIVVDARPDVFN 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080 165 HNVETVERLQWPVRdRRADYEQSLAVLDRVGRES-DIHTKTSLMLGVGEYDHEVYRTLGDLSEVGVDVVTFGQYLQPSRS 243
Cdd:COG0320  176 HNLETVPRLYKRVR-PGADYERSLELLKRAKELDpGIPTKSGLMLGLGETDEEVLEVMRDLRAAGVDILTIGQYLQPSKK 254
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 506391080 244 HLDVFEYVHPDVFETWRAVAeREFDFLYCASGPMVRSSYKAGELFVEALLREG 296
Cdd:COG0320  255 HLPVDRYVTPEEFEELKEIA-LELGFLHVASGPLVRSSYHADEQAAKARAARG 306
lipA TIGR00510
lipoate synthase; This enzyme is an iron-sulfur protein. It is localized to mitochondria in ...
6-295 6.67e-124

lipoate synthase; This enzyme is an iron-sulfur protein. It is localized to mitochondria in yeast and Arabidopsis. It generates lipoic acid, a thiol antioxidant that is linked to a specific Lys as prosthetic group for the pyruvate and alpha-ketoglutarate dehydrogenase complexes and the glycine-cleavage system. The family shows strong sequence conservation. [Biosynthesis of cofactors, prosthetic groups, and carriers, Lipoate]


Pssm-ID: 273111  Cd Length: 302  Bit Score: 356.84  E-value: 6.67e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080    6 RKPDWLKSRPPSGSRFTEIKERLRERDLHTVCEEANCPNMGECWsgrdGPGTATFMLMGDRCSRGCNFCDVETGGMKSL- 84
Cdd:TIGR00510  16 RKPEWLKIKLPLGTVIAQIKNTMKNKGLHTVCEEASCPNLTECW----NHGTATFMILGDICTRRCPFCDVAHGRNPLPp 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080   85 DSDEPENVADAVAEIGLDYVVLTSVDRDDLADGGSEHFAETIREIQRRDPEILVETLIPDFQGDPEAIDRIIDAGPDVIA 164
Cdd:TIGR00510  92 DPEEPAKLAETIKDMGLKYVVITSVDRDDLEDGGASHLAECIEAIREKLPNIKIETLVPDFRGNIAALDILLDAPPDVYN 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080  165 HNVETVERLQWPVRDrRADYEQSLAVLDRVGRE-SDIHTKTSLMLGVGEYDHEVYRTLGDLSEVGVDVVTFGQYLQPSRS 243
Cdd:TIGR00510 172 HNLETVERLTPFVRP-GATYRWSLKLLERAKEYlPNLPTKSGIMVGLGETNEEIKQTLKDLRDHGVTMVTLGQYLRPSRR 250
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 506391080  244 HLDVFEYVHPDVFETWRAVAErEFDFLYCASGPMVRSSYKAGELFVEALLRE 295
Cdd:TIGR00510 251 HLPVKRYVSPEEFDYYRSVAL-EMGFLHAACGPFVRSSYHADSLFAAGRLVK 301
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
63-220 2.77e-20

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 85.66  E-value: 2.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080   63 MGDRCSRGCNFCDV----ETGGMKSLDSDEPENVADAVAEIGLDYVVLTSVDRDDLADGGSEHFAETIREIqrrDPEILV 138
Cdd:pfam04055   1 ITRGCNLRCTYCAFpsirARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLEL---AEGIRI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080  139 ETLIPDFQGDPEAIDRIIDAGPDVIAHNVETVERLQWPVRDRRADYEQSLAVLDRVgRESDIHTKTSLMLGV-GEYDHEV 217
Cdd:pfam04055  78 TLETNGTLLDEELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELL-REAGIPVVTDNIVGLpGETDEDL 156

                  ...
gi 506391080  218 YRT 220
Cdd:pfam04055 157 EET 159
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
57-237 1.33e-15

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 74.36  E-value: 1.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080    57 TATFMLMGDRCSRGCNFCDV--ETGGMKSLDSDEPENVADAVAEIGLDYVVLTSV-----DRDDLADGGSEHFAETIREI 129
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSFpsLRGKLRSRYLEALVREIELLAEKGEKEGLVGTVfigggTPTLLSPEQLEELLEAIREI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080   130 Q--RRDPEILVETLIPDFqgDPEAIDRIIDAGPDVIAHNVETVERLQWPVRDRRADYEQSLAVLDRVGRESDIHTKTSLM 207
Cdd:smart00729  81 LglAKDVEITIETRPDTL--TEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAGPIKVSTDLI 158
                          170       180       190
                   ....*....|....*....|....*....|.
gi 506391080   208 LGV-GEYDHEVYRTLGDLSEVGVDVVTFGQY 237
Cdd:smart00729 159 VGLpGETEEDFEETLKLLKELGPDRVSIFPL 189
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
64-238 1.49e-08

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 53.88  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080  64 GDRCSRGCNFCDVETGGMKSLDSDEPENVADAVAE--IGLDYVVLTSVDRDDLADggsEHFAETIREIQRRDP--EILVE 139
Cdd:cd01335    4 TRGCNLNCGFCSNPASKGRGPESPPEIEEILDIVLeaKERGVEVVILTGGEPLLY---PELAELLRRLKKELPgfEISIE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080 140 TLIPDFqgDPEAIDRIIDAGPDVIAHNVETV-ERLQWPVRDRRADYEQSLAVLDRVgRESDIHTKTSLMLGVGEYDHEVY 218
Cdd:cd01335   81 TNGTLL--TEELLKELKELGLDGVGVSLDSGdEEVADKIRGSGESFKERLEALKEL-REAGLGLSTTLLVGLGDEDEEDD 157
                        170       180
                 ....*....|....*....|..
gi 506391080 219 R--TLGDLSEVGVDVVTFGQYL 238
Cdd:cd01335  158 LeeLELLAEFRSPDRVSLFRLL 179
 
Name Accession Description Interval E-value
PRK05481 PRK05481
lipoyl synthase; Provisional
1-291 2.26e-178

lipoyl synthase; Provisional


Pssm-ID: 235493 [Multi-domain]  Cd Length: 289  Bit Score: 493.84  E-value: 2.26e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080   1 MQRGRRKPDWLKSRPPSGSRFTEIKERLRERDLHTVCEEANCPNMGECWSGrdgpGTATFMLMGDRCSRGCNFCDVETGG 80
Cdd:PRK05481   1 AEKVARKPDWLRVKLPTGEEYTEIKKLLRELGLHTVCEEASCPNIGECWSR----GTATFMILGDICTRRCPFCDVATGR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080  81 MKSLDSDEPENVADAVAEIGLDYVVLTSVDRDDLADGGSEHFAETIREIQRRDPEILVETLIPDFQGDPEAIDRIIDAGP 160
Cdd:PRK05481  77 PLPLDPDEPERVAEAVARMGLKYVVITSVDRDDLPDGGAQHFAETIRAIRELNPGTTIEVLIPDFRGRMDALLTVLDARP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080 161 DVIAHNVETVERLQWPVRdRRADYEQSLAVLDRVGRES-DIHTKTSLMLGVGEYDHEVYRTLGDLSEVGVDVVTFGQYLQ 239
Cdd:PRK05481 157 DVFNHNLETVPRLYKRVR-PGADYERSLELLKRAKELHpGIPTKSGLMVGLGETDEEVLEVMDDLRAAGVDILTIGQYLQ 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 506391080 240 PSRSHLDVFEYVHPDVFETWRAVAErEFDFLYCASGPMVRSSYKAGELFVEA 291
Cdd:PRK05481 236 PSRKHLPVERYVTPEEFDEYKEIAL-ELGFLHVASGPLVRSSYHADEQAAGA 286
LipA COG0320
Lipoate synthase [Coenzyme transport and metabolism]; Lipoate synthase is part of the Pathway ...
5-296 2.63e-178

Lipoate synthase [Coenzyme transport and metabolism]; Lipoate synthase is part of the Pathway/BioSystem: Lipoate biosynthesis


Pssm-ID: 440089 [Multi-domain]  Cd Length: 306  Bit Score: 494.62  E-value: 2.63e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080   5 RRKPDWLKSRPPSGSRFTEIKERLRERDLHTVCEEANCPNMGECWSGrdgpGTATFMLMGDRCSRGCNFCDVETGGMKSL 84
Cdd:COG0320   20 LRKPDWLRVKLPTGPEYAEVKKLLREHKLHTVCEEARCPNIGECWSR----GTATFMILGDICTRRCRFCDVATGRPLPL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080  85 DSDEPENVADAVAEIGLDYVVLTSVDRDDLADGGSEHFAETIREIQRRDPEILVETLIPDFQGDPEAIDRIIDAGPDVIA 164
Cdd:COG0320   96 DPDEPERVAEAVAEMGLKYVVITSVDRDDLPDGGAGHFAETIRAIRELNPGTTIEVLIPDFRGREEALDIVVDARPDVFN 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080 165 HNVETVERLQWPVRdRRADYEQSLAVLDRVGRES-DIHTKTSLMLGVGEYDHEVYRTLGDLSEVGVDVVTFGQYLQPSRS 243
Cdd:COG0320  176 HNLETVPRLYKRVR-PGADYERSLELLKRAKELDpGIPTKSGLMLGLGETDEEVLEVMRDLRAAGVDILTIGQYLQPSKK 254
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 506391080 244 HLDVFEYVHPDVFETWRAVAeREFDFLYCASGPMVRSSYKAGELFVEALLREG 296
Cdd:COG0320  255 HLPVDRYVTPEEFEELKEIA-LELGFLHVASGPLVRSSYHADEQAAKARAARG 306
PLN02428 PLN02428
lipoic acid synthase
2-298 7.89e-162

lipoic acid synthase


Pssm-ID: 215236 [Multi-domain]  Cd Length: 349  Bit Score: 454.59  E-value: 7.89e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080   2 QRGRRKPDWLKSRPPSGSRFTEIKERLRERDLHTVCEEANCPNMGECWSG-RDGPGTATFMLMGDRCSRGCNFCDVETGG 80
Cdd:PLN02428  46 DKPLPKPKWLRQRAPGGEKYTEIKEKLRELKLNTVCEEAQCPNIGECWNGgGTGTATATIMILGDTCTRGCRFCAVKTSR 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080  81 MKS-LDSDEPENVADAVAEIGLDYVVLTSVDRDDLADGGSEHFAETIREIQRRDPEILVETLIPDFQGDPEAIDRIIDAG 159
Cdd:PLN02428 126 TPPpPDPDEPENVAEAIASWGVDYVVLTSVDRDDLPDGGSGHFAETVRRLKQLKPEILVEALVPDFRGDLGAVETVATSG 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080 160 PDVIAHNVETVERLQWPVRDRRADYEQSLAVLDRVGR-ESDIHTKTSLMLGVGEYDHEVYRTLGDLSEVGVDVVTFGQYL 238
Cdd:PLN02428 206 LDVFAHNIETVERLQRIVRDPRAGYKQSLDVLKHAKEsKPGLLTKTSIMLGLGETDEEVVQTMEDLRAAGVDVVTFGQYL 285
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080 239 QPSRSHLDVFEYVHPDVFETWRAVAErEFDFLYCASGPMVRSSYKAGELFVEALLREGRS 298
Cdd:PLN02428 286 RPTKRHLPVKEYVTPEKFEFWREYGE-EMGFRYVASGPLVRSSYKAGEFFIKSMIREDRA 344
PTZ00413 PTZ00413
lipoate synthase; Provisional
7-300 7.32e-136

lipoate synthase; Provisional


Pssm-ID: 240408 [Multi-domain]  Cd Length: 398  Bit Score: 390.73  E-value: 7.32e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080   7 KPDWLKSRPPSG----SRFTEIKERLRERDLHTVCEEANCPNMGECWSGRD--GPGTATFMLMGDRCSRGCNFCDVETGG 80
Cdd:PTZ00413  93 LPPWFKVKVPKGasrrPRFNRIRRSMREKKLHTVCEEAKCPNIGECWGGGDeeGTATATIMVMGDHCTRGCRFCSVKTSR 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080  81 MK-SLDSDEPENVADAVAEIGLDYVVLTSVDRDDLADGGSEHFAETIREIQRRDPEILVETLIPDFQGDPEAIDRIIDAG 159
Cdd:PTZ00413 173 KPpPLDPNEPEKVAKAVAEMGVDYIVMTMVDRDDLPDGGASHVARCVELIKESNPELLLEALVGDFHGDLKSVEKLANSP 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080 160 PDVIAHNVETVERLQWPVRDRRADYEQSLAVLDRVGRESD--IHTKTSLMLGVGEYDHEVYRTLGDLSEVGVDVVTFGQY 237
Cdd:PTZ00413 253 LSVYAHNIECVERITPYVRDRRASYRQSLKVLEHVKEFTNgaMLTKSSIMLGLGETEEEVRQTLRDLRTAGVSAVTLGQY 332
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506391080 238 LQPSRSHLDVFEYVHPDVFETWRAVAErEFDFLYCASGPMVRSSYKAGELFVEALLREGRSPE 300
Cdd:PTZ00413 333 LQPTKTRLKVSRYAHPKEFEMWEEEAM-KMGFLYCASGPLVRSSYRAGEYYIKNLVKQRRKAK 394
PRK12928 PRK12928
lipoyl synthase; Provisional
5-287 1.25e-134

lipoyl synthase; Provisional


Pssm-ID: 237261  Cd Length: 290  Bit Score: 383.50  E-value: 1.25e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080   5 RRKPDWLKSRPPSGSRFTEIKERLRERDLHTVCEEANCPNMGECWSGrdgpGTATFMLMGDRCSRGCNFCDVETGGMKSL 84
Cdd:PRK12928  12 ERLPEWLRAPIGKASELETVQRLVKQRRLHTICEEARCPNRGECYAQ----GTATFLIMGSICTRRCAFCQVDKGRPMPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080  85 DSDEPENVADAVAEIGLDYVVLTSVDRDDLADGGSEHFAETIREIQRRDPEILVETLIPDFQG-DPEAIDRIIDAGPDVI 163
Cdd:PRK12928  88 DPDEPERVAEAVAALGLRYVVLTSVARDDLPDGGAAHFVATIAAIRARNPGTGIEVLTPDFWGgQRERLATVLAAKPDVF 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080 164 AHNVETVERLQWPVRdRRADYEQSLAVLDRVgRE--SDIHTKTSLMLGVGEYDHEVYRTLGDLSEVGVDVVTFGQYLQPS 241
Cdd:PRK12928 168 NHNLETVPRLQKAVR-RGADYQRSLDLLARA-KElaPDIPTKSGLMLGLGETEDEVIETLRDLRAVGCDRLTIGQYLRPS 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 506391080 242 RSHLDVFEYVHPDVFETWRAVAeREFDFLYCASGPMVRSSYKAGEL 287
Cdd:PRK12928 246 LAHLPVQRYWTPEEFEALGQIA-RELGFSHVRSGPLVRSSYHAGEQ 290
lipA TIGR00510
lipoate synthase; This enzyme is an iron-sulfur protein. It is localized to mitochondria in ...
6-295 6.67e-124

lipoate synthase; This enzyme is an iron-sulfur protein. It is localized to mitochondria in yeast and Arabidopsis. It generates lipoic acid, a thiol antioxidant that is linked to a specific Lys as prosthetic group for the pyruvate and alpha-ketoglutarate dehydrogenase complexes and the glycine-cleavage system. The family shows strong sequence conservation. [Biosynthesis of cofactors, prosthetic groups, and carriers, Lipoate]


Pssm-ID: 273111  Cd Length: 302  Bit Score: 356.84  E-value: 6.67e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080    6 RKPDWLKSRPPSGSRFTEIKERLRERDLHTVCEEANCPNMGECWsgrdGPGTATFMLMGDRCSRGCNFCDVETGGMKSL- 84
Cdd:TIGR00510  16 RKPEWLKIKLPLGTVIAQIKNTMKNKGLHTVCEEASCPNLTECW----NHGTATFMILGDICTRRCPFCDVAHGRNPLPp 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080   85 DSDEPENVADAVAEIGLDYVVLTSVDRDDLADGGSEHFAETIREIQRRDPEILVETLIPDFQGDPEAIDRIIDAGPDVIA 164
Cdd:TIGR00510  92 DPEEPAKLAETIKDMGLKYVVITSVDRDDLEDGGASHLAECIEAIREKLPNIKIETLVPDFRGNIAALDILLDAPPDVYN 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080  165 HNVETVERLQWPVRDrRADYEQSLAVLDRVGRE-SDIHTKTSLMLGVGEYDHEVYRTLGDLSEVGVDVVTFGQYLQPSRS 243
Cdd:TIGR00510 172 HNLETVERLTPFVRP-GATYRWSLKLLERAKEYlPNLPTKSGIMVGLGETNEEIKQTLKDLRDHGVTMVTLGQYLRPSRR 250
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 506391080  244 HLDVFEYVHPDVFETWRAVAErEFDFLYCASGPMVRSSYKAGELFVEALLRE 295
Cdd:TIGR00510 251 HLPVKRYVSPEEFDYYRSVAL-EMGFLHAACGPFVRSSYHADSLFAAGRLVK 301
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
63-220 2.77e-20

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 85.66  E-value: 2.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080   63 MGDRCSRGCNFCDV----ETGGMKSLDSDEPENVADAVAEIGLDYVVLTSVDRDDLADGGSEHFAETIREIqrrDPEILV 138
Cdd:pfam04055   1 ITRGCNLRCTYCAFpsirARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLEL---AEGIRI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080  139 ETLIPDFQGDPEAIDRIIDAGPDVIAHNVETVERLQWPVRDRRADYEQSLAVLDRVgRESDIHTKTSLMLGV-GEYDHEV 217
Cdd:pfam04055  78 TLETNGTLLDEELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELL-REAGIPVVTDNIVGLpGETDEDL 156

                  ...
gi 506391080  218 YRT 220
Cdd:pfam04055 157 EET 159
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
57-237 1.33e-15

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 74.36  E-value: 1.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080    57 TATFMLMGDRCSRGCNFCDV--ETGGMKSLDSDEPENVADAVAEIGLDYVVLTSV-----DRDDLADGGSEHFAETIREI 129
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSFpsLRGKLRSRYLEALVREIELLAEKGEKEGLVGTVfigggTPTLLSPEQLEELLEAIREI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080   130 Q--RRDPEILVETLIPDFqgDPEAIDRIIDAGPDVIAHNVETVERLQWPVRDRRADYEQSLAVLDRVGRESDIHTKTSLM 207
Cdd:smart00729  81 LglAKDVEITIETRPDTL--TEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAGPIKVSTDLI 158
                          170       180       190
                   ....*....|....*....|....*....|.
gi 506391080   208 LGV-GEYDHEVYRTLGDLSEVGVDVVTFGQY 237
Cdd:smart00729 159 VGLpGETEEDFEETLKLLKELGPDRVSIFPL 189
LIAS_N pfam16881
N-terminal domain of lipoyl synthase of Radical_SAM family; LIAS_N is found as the N-terminal ...
6-42 1.53e-10

N-terminal domain of lipoyl synthase of Radical_SAM family; LIAS_N is found as the N-terminal domain of the Radical_SAM family in the members that are lipoyl synthase enzymes, particularly the mitochondrial ones in metazoa but also those in bacteria.


Pssm-ID: 465296 [Multi-domain]  Cd Length: 97  Bit Score: 57.14  E-value: 1.53e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 506391080    6 RKPDWLKSRPPSGSRFTEIKERLRERDLHTVCEEANC 42
Cdd:pfam16881  61 RLPPWLKTKIPLGKNYNKIKNTLRNLNLHTVCEEARC 97
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
64-238 1.49e-08

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 53.88  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080  64 GDRCSRGCNFCDVETGGMKSLDSDEPENVADAVAE--IGLDYVVLTSVDRDDLADggsEHFAETIREIQRRDP--EILVE 139
Cdd:cd01335    4 TRGCNLNCGFCSNPASKGRGPESPPEIEEILDIVLeaKERGVEVVILTGGEPLLY---PELAELLRRLKKELPgfEISIE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080 140 TLIPDFqgDPEAIDRIIDAGPDVIAHNVETV-ERLQWPVRDRRADYEQSLAVLDRVgRESDIHTKTSLMLGVGEYDHEVY 218
Cdd:cd01335   81 TNGTLL--TEELLKELKELGLDGVGVSLDSGdEEVADKIRGSGESFKERLEALKEL-REAGLGLSTTLLVGLGDEDEEDD 157
                        170       180
                 ....*....|....*....|..
gi 506391080 219 R--TLGDLSEVGVDVVTFGQYL 238
Cdd:cd01335  158 LeeLELLAEFRSPDRVSLFRLL 179
YgiQ COG1032
Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];
67-240 2.19e-05

Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];


Pssm-ID: 440655 [Multi-domain]  Cd Length: 394  Bit Score: 45.71  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080  67 CSRGCNFCDV---ETGGMKSLDsdePENVADAVAEI----GLDYVVLTsvdrDDLADGGSEHFAETIREIQRRDPEILVE 139
Cdd:COG1032  184 CPFGCSFCSIsalYGRKVRYRS---PESVVEEIEELvkryGIREIFFV----DDNFNVDKKRLKELLEELIERGLNVSFP 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080 140 TLI-PDFqGDPEAIDRIIDAGPDVI-----AHNVETVERLqwpvrDRRADYEQSLAVLDRVgRESDIHTKTSLMLGV-GE 212
Cdd:COG1032  257 SEVrVDL-LDEELLELLKKAGCRGLfigieSGSQRVLKAM-----NKGITVEDILEAVRLL-KKAGIRVKLYFIIGLpGE 329
                        170       180
                 ....*....|....*....|....*...
gi 506391080 213 YDHEVYRTLGDLSEVGVDVVTFgQYLQP 240
Cdd:COG1032  330 TEEDIEETIEFIKELGPDQAQV-SIFTP 356
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
93-163 6.22e-04

IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.


Pssm-ID: 238223 [Multi-domain]  Cd Length: 325  Bit Score: 40.96  E-value: 6.22e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506391080  93 ADAVAEIGLDYVVLtsvdrdDLADGGSEHFAETIREIQRRDPEIlveTLIPDFQGDPEAIDRIIDAGPDVI 163
Cdd:cd00381   99 AEALVEAGVDVIVI------DSAHGHSVYVIEMIKFIKKKYPNV---DVIAGNVVTAEAARDLIDAGADGV 160
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
67-200 5.27e-03

Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic radical activating enzyme NrdG/QueE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440367 [Multi-domain]  Cd Length: 205  Bit Score: 37.42  E-value: 5.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506391080  67 CSRGCNFCDVE-----TGGmKSLDSDEpenVADAVAEIGLDYVVLTsvdrddladGGsE-----HFAETIREIQRRDPEI 136
Cdd:COG0602   30 CNLRCSWCDTKyawdgEGG-KRMSAEE---ILEEVAALGARHVVIT---------GG-EpllqdDLAELLEALKDAGYEV 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506391080 137 LVETlipdfQG---DPEAIDRII-------DAGPDVIAHNVETVERLQW---PVrDRRADYEQSLAVLDRVGRESDI 200
Cdd:COG0602   96 ALET-----NGtlpIPAGIDWVTvspklpsSGEEEDNRENLEVLRRADElkfVV-ADETDLEEAEELLARLDFRCPV 166
 
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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