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Conserved domains on  [gi|15226412|ref|NP_179682|]
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lipoic acid synthase 1 [Arabidopsis thaliana]

Protein Classification

lipoyl synthase( domain architecture ID 11476763)

lipoyl synthase catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives; belongs to the radical SAM superfamily

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02428 PLN02428
lipoic acid synthase
23-372 0e+00

lipoic acid synthase


:

Pssm-ID: 215236 [Multi-domain]  Cd Length: 349  Bit Score: 658.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412   23 SAVTPVTVTQSPKSLEALRARLANESPSLTDFIHGDTYSVEVGTKKKPLPKPKWMKESIPGGERYVQIKKKLRDLKLHTV 102
Cdd:PLN02428   1 VTSTSTTAPQTPQTLAALRARLASESPSLGDFVSLGPYTLGSYGRDKPLPKPKWLRQRAPGGEKYTEIKEKLRELKLNTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412  103 CEEAKCPNLGECWSGGETGTATATIMILGDTCTRGCRFCNVKTSRTPPPPDPNEPNNVAEAIASWGVDYVVITSVDRDDL 182
Cdd:PLN02428  81 CEEAQCPNIGECWNGGGTGTATATIMILGDTCTRGCRFCAVKTSRTPPPPDPDEPENVAEAIASWGVDYVVLTSVDRDDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412  183 PDQGSGHFAETVQRLKFLKPEMLIEALVPDFRGDGGCVEKVSKSGLDVLAHNIETVEELQSFVRDHRANFKQSLDVLRMA 262
Cdd:PLN02428 161 PDGGSGHFAETVRRLKQLKPEILVEALVPDFRGDLGAVETVATSGLDVFAHNIETVERLQRIVRDPRAGYKQSLDVLKHA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412  263 KEYAPaGTLTKTSVMLGCGETPDQVVKTMEKVRAAGVDVMTFGQYMRPSKRHMPVAEYVTPDAFERYRLLGMEMGFRYVA 342
Cdd:PLN02428 241 KESKP-GLLTKTSIMLGLGETDEEVVQTMEDLRAAGVDVVTFGQYLRPTKRHLPVKEYVTPEKFEFWREYGEEMGFRYVA 319
                        330       340       350
                 ....*....|....*....|....*....|
gi 15226412  343 SGPMVRSSYKAGEYYIKSMIEADRVASPST 372
Cdd:PLN02428 320 SGPLVRSSYKAGEFFIKSMIREDRAKAAAA 349
 
Name Accession Description Interval E-value
PLN02428 PLN02428
lipoic acid synthase
23-372 0e+00

lipoic acid synthase


Pssm-ID: 215236 [Multi-domain]  Cd Length: 349  Bit Score: 658.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412   23 SAVTPVTVTQSPKSLEALRARLANESPSLTDFIHGDTYSVEVGTKKKPLPKPKWMKESIPGGERYVQIKKKLRDLKLHTV 102
Cdd:PLN02428   1 VTSTSTTAPQTPQTLAALRARLASESPSLGDFVSLGPYTLGSYGRDKPLPKPKWLRQRAPGGEKYTEIKEKLRELKLNTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412  103 CEEAKCPNLGECWSGGETGTATATIMILGDTCTRGCRFCNVKTSRTPPPPDPNEPNNVAEAIASWGVDYVVITSVDRDDL 182
Cdd:PLN02428  81 CEEAQCPNIGECWNGGGTGTATATIMILGDTCTRGCRFCAVKTSRTPPPPDPDEPENVAEAIASWGVDYVVLTSVDRDDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412  183 PDQGSGHFAETVQRLKFLKPEMLIEALVPDFRGDGGCVEKVSKSGLDVLAHNIETVEELQSFVRDHRANFKQSLDVLRMA 262
Cdd:PLN02428 161 PDGGSGHFAETVRRLKQLKPEILVEALVPDFRGDLGAVETVATSGLDVFAHNIETVERLQRIVRDPRAGYKQSLDVLKHA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412  263 KEYAPaGTLTKTSVMLGCGETPDQVVKTMEKVRAAGVDVMTFGQYMRPSKRHMPVAEYVTPDAFERYRLLGMEMGFRYVA 342
Cdd:PLN02428 241 KESKP-GLLTKTSIMLGLGETDEEVVQTMEDLRAAGVDVVTFGQYLRPTKRHLPVKEYVTPEKFEFWREYGEEMGFRYVA 319
                        330       340       350
                 ....*....|....*....|....*....|
gi 15226412  343 SGPMVRSSYKAGEYYIKSMIEADRVASPST 372
Cdd:PLN02428 320 SGPLVRSSYKAGEFFIKSMIREDRAKAAAA 349
LipA COG0320
Lipoate synthase [Coenzyme transport and metabolism]; Lipoate synthase is part of the Pathway ...
76-361 2.88e-154

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: 436.46  E-value: 2.88e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412  76 WMKESIPGGERYVQIKKKLRDLKLHTVCEEAKCPNLGECWSGGetgtaTATIMILGDTCTRGCRFCNVKTSRTPPPPDPN 155
Cdd:COG0320  25 WLRVKLPTGPEYAEVKKLLREHKLHTVCEEARCPNIGECWSRG-----TATFMILGDICTRRCRFCDVATGRPLPLDPDE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412 156 EPNnVAEAIASWGVDYVVITSVDRDDLPDQGSGHFAETVQRLKFLKPEMLIEALVPDFRGDGGCVEKVSKSGLDVLAHNI 235
Cdd:COG0320 100 PER-VAEAVAEMGLKYVVITSVDRDDLPDGGAGHFAETIRAIRELNPGTTIEVLIPDFRGREEALDIVVDARPDVFNHNL 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412 236 ETVEELQSFVRdHRANFKQSLDVLRMAKEYAPaGTLTKTSVMLGCGETPDQVVKTMEKVRAAGVDVMTFGQYMRPSKRHM 315
Cdd:COG0320 179 ETVPRLYKRVR-PGADYERSLELLKRAKELDP-GIPTKSGLMLGLGETDEEVLEVMRDLRAAGVDILTIGQYLQPSKKHL 256
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15226412 316 PVAEYVTPDAFERYRLLGMEMGFRYVASGPMVRSSYKAGEYYIKSM 361
Cdd:COG0320 257 PVDRYVTPEEFEELKEIALELGFLHVASGPLVRSSYHADEQAAKAR 302
lipA TIGR00510
lipoate synthase; This enzyme is an iron-sulfur protein. It is localized to mitochondria in ...
76-361 6.41e-123

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: 6.41e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412    76 WMKESIPGGERYVQIKKKLRDLKLHTVCEEAKCPNLGECWSGGetgtaTATIMILGDTCTRGCRFCNVKTSRTPPPPDPN 155
Cdd:TIGR00510  20 WLKIKLPLGTVIAQIKNTMKNKGLHTVCEEASCPNLTECWNHG-----TATFMILGDICTRRCPFCDVAHGRNPLPPDPE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412   156 EPNNVAEAIASWGVDYVVITSVDRDDLPDQGSGHFAETVQRLKFLKPEMLIEALVPDFRGDGGCVEKVSKSGLDVLAHNI 235
Cdd:TIGR00510  95 EPAKLAETIKDMGLKYVVITSVDRDDLEDGGASHLAECIEAIREKLPNIKIETLVPDFRGNIAALDILLDAPPDVYNHNL 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412   236 ETVEELQSFVRdHRANFKQSLDVLRMAKEYAPAgTLTKTSVMLGCGETPDQVVKTMEKVRAAGVDVMTFGQYMRPSKRHM 315
Cdd:TIGR00510 175 ETVERLTPFVR-PGATYRWSLKLLERAKEYLPN-LPTKSGIMVGLGETNEEIKQTLKDLRDHGVTMVTLGQYLRPSRRHL 252
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 15226412   316 PVAEYVTPDAFERYRLLGMEMGFRYVASGPMVRSSYKAGEYYIKSM 361
Cdd:TIGR00510 253 PVKRYVSPEEFDYYRSVALEMGFLHAACGPFVRSSYHADSLFAAGR 298
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
130-290 2.68e-15

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: 72.56  E-value: 2.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412   130 LGDTCTRGCRFCNVKTSRTPPPPDPNEPNNV---AEAIASWGVDYVVITSVDRDDLPDQGSGHFAEtvqRLKFLKPEMLI 206
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKGRELSPEEIleeAKELKRLGVEVVILGGGEPLLLPDLVELLERL---LKLELAEGIRI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412   207 EALVPDFRGDGGCVEKVSKSGLDVLAHNIETVEELQSFVRDHRANFKQSLDVLRMAKEYapAGTLTKTSVMLGCGETPDQ 286
Cdd:pfam04055  78 TLETNGTLLDEELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREA--GIPVVTDNIVGLPGETDED 155

                  ....
gi 15226412   287 VVKT 290
Cdd:pfam04055 156 LEET 159
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
124-332 2.42e-14

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: 71.28  E-value: 2.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412    124 TATIMILGDTCTRGCRFCNVKTSRTPPPPDPNEP-NNVAEAIASWGVDYVVITSV-----DRDDLPDQGSGHFAETVQRL 197
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSFPSLRGKLRSRYLEAlVREIELLAEKGEKEGLVGTVfigggTPTLLSPEQLEELLEAIREI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412    198 K--FLKPEMLIEALVPDFRGDggCVEKVSKSGLDVLAHNIETVEE--LQSFVRDHraNFKQSLDVLRMAKEYAPAGtlTK 273
Cdd:smart00729  81 LglAKDVEITIETRPDTLTEE--LLEALKEAGVNRVSLGVQSGDDevLKAINRGH--TVEDVLEAVELLREAGPIK--VS 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226412    274 TSVMLG-CGETPDQVVKTMEKVRAAGVDVMTFGQYMrPsKRHMPVAE----YVTPDAFERYRLL 332
Cdd:smart00729 155 TDLIVGlPGETEEDFEETLKLLKELGPDRVSIFPLS-P-RPGTPLAKmykrLKPPTKEERAELL 216
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
128-330 3.17e-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: 53.49  E-value: 3.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412 128 MILGDTCTRGCRFCNVKTS---RTPPPPDPNEPNNVAEAIASWGVDYVVITSVDRDDLPdqgsgHFAETVQRLKFLKPEM 204
Cdd:cd01335   1 LELTRGCNLNCGFCSNPASkgrGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYP-----ELAELLRRLKKELPGF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412 205 LIEALVPDFRGDGGCVEKVSKSGLDVLAHNIETVEELQSfvRDHRANFKQSLDVLRMAKEYAPAGTLTKTSVMLG-CGET 283
Cdd:cd01335  76 EISIETNGTLLTEELLKELKELGLDGVGVSLDSGDEEVA--DKIRGSGESFKERLEALKELREAGLGLSTTLLVGlGDED 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15226412 284 PDQVVKTMEKVRAA-GVDVMTFGQYMrPSKRhMPVAEYVTPDAFERYR 330
Cdd:cd01335 154 EEDDLEELELLAEFrSPDRVSLFRLL-PEEG-TPLELAAPVVPAEKLL 199
 
Name Accession Description Interval E-value
PLN02428 PLN02428
lipoic acid synthase
23-372 0e+00

lipoic acid synthase


Pssm-ID: 215236 [Multi-domain]  Cd Length: 349  Bit Score: 658.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412   23 SAVTPVTVTQSPKSLEALRARLANESPSLTDFIHGDTYSVEVGTKKKPLPKPKWMKESIPGGERYVQIKKKLRDLKLHTV 102
Cdd:PLN02428   1 VTSTSTTAPQTPQTLAALRARLASESPSLGDFVSLGPYTLGSYGRDKPLPKPKWLRQRAPGGEKYTEIKEKLRELKLNTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412  103 CEEAKCPNLGECWSGGETGTATATIMILGDTCTRGCRFCNVKTSRTPPPPDPNEPNNVAEAIASWGVDYVVITSVDRDDL 182
Cdd:PLN02428  81 CEEAQCPNIGECWNGGGTGTATATIMILGDTCTRGCRFCAVKTSRTPPPPDPDEPENVAEAIASWGVDYVVLTSVDRDDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412  183 PDQGSGHFAETVQRLKFLKPEMLIEALVPDFRGDGGCVEKVSKSGLDVLAHNIETVEELQSFVRDHRANFKQSLDVLRMA 262
Cdd:PLN02428 161 PDGGSGHFAETVRRLKQLKPEILVEALVPDFRGDLGAVETVATSGLDVFAHNIETVERLQRIVRDPRAGYKQSLDVLKHA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412  263 KEYAPaGTLTKTSVMLGCGETPDQVVKTMEKVRAAGVDVMTFGQYMRPSKRHMPVAEYVTPDAFERYRLLGMEMGFRYVA 342
Cdd:PLN02428 241 KESKP-GLLTKTSIMLGLGETDEEVVQTMEDLRAAGVDVVTFGQYLRPTKRHLPVKEYVTPEKFEFWREYGEEMGFRYVA 319
                        330       340       350
                 ....*....|....*....|....*....|
gi 15226412  343 SGPMVRSSYKAGEYYIKSMIEADRVASPST 372
Cdd:PLN02428 320 SGPLVRSSYKAGEFFIKSMIREDRAKAAAA 349
LipA COG0320
Lipoate synthase [Coenzyme transport and metabolism]; Lipoate synthase is part of the Pathway ...
76-361 2.88e-154

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: 436.46  E-value: 2.88e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412  76 WMKESIPGGERYVQIKKKLRDLKLHTVCEEAKCPNLGECWSGGetgtaTATIMILGDTCTRGCRFCNVKTSRTPPPPDPN 155
Cdd:COG0320  25 WLRVKLPTGPEYAEVKKLLREHKLHTVCEEARCPNIGECWSRG-----TATFMILGDICTRRCRFCDVATGRPLPLDPDE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412 156 EPNnVAEAIASWGVDYVVITSVDRDDLPDQGSGHFAETVQRLKFLKPEMLIEALVPDFRGDGGCVEKVSKSGLDVLAHNI 235
Cdd:COG0320 100 PER-VAEAVAEMGLKYVVITSVDRDDLPDGGAGHFAETIRAIRELNPGTTIEVLIPDFRGREEALDIVVDARPDVFNHNL 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412 236 ETVEELQSFVRdHRANFKQSLDVLRMAKEYAPaGTLTKTSVMLGCGETPDQVVKTMEKVRAAGVDVMTFGQYMRPSKRHM 315
Cdd:COG0320 179 ETVPRLYKRVR-PGADYERSLELLKRAKELDP-GIPTKSGLMLGLGETDEEVLEVMRDLRAAGVDILTIGQYLQPSKKHL 256
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15226412 316 PVAEYVTPDAFERYRLLGMEMGFRYVASGPMVRSSYKAGEYYIKSM 361
Cdd:COG0320 257 PVDRYVTPEEFEELKEIALELGFLHVASGPLVRSSYHADEQAAKAR 302
PRK05481 PRK05481
lipoyl synthase; Provisional
76-357 2.10e-151

lipoyl synthase; Provisional


Pssm-ID: 235493 [Multi-domain]  Cd Length: 289  Bit Score: 428.35  E-value: 2.10e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412   76 WMKESIPGGERYVQIKKKLRDLKLHTVCEEAKCPNLGECWSGGetgtaTATIMILGDTCTRGCRFCNVKTSRTPPPPDPN 155
Cdd:PRK05481  10 WLRVKLPTGEEYTEIKKLLRELGLHTVCEEASCPNIGECWSRG-----TATFMILGDICTRRCPFCDVATGRPLPLDPDE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412  156 EPNnVAEAIASWGVDYVVITSVDRDDLPDQGSGHFAETVQRLKFLKPEMLIEALVPDFRGDGGCVEKVSKSGLDVLAHNI 235
Cdd:PRK05481  85 PER-VAEAVARMGLKYVVITSVDRDDLPDGGAQHFAETIRAIRELNPGTTIEVLIPDFRGRMDALLTVLDARPDVFNHNL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412  236 ETVEELQSFVRdHRANFKQSLDVLRMAKEYAPaGTLTKTSVMLGCGETPDQVVKTMEKVRAAGVDVMTFGQYMRPSKRHM 315
Cdd:PRK05481 164 ETVPRLYKRVR-PGADYERSLELLKRAKELHP-GIPTKSGLMVGLGETDEEVLEVMDDLRAAGVDILTIGQYLQPSRKHL 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 15226412  316 PVAEYVTPDAFERYRLLGMEMGFRYVASGPMVRSSYKAGEYY 357
Cdd:PRK05481 242 PVERYVTPEEFDEYKEIALELGFLHVASGPLVRSSYHADEQA 283
PTZ00413 PTZ00413
lipoate synthase; Provisional
76-368 2.05e-148

lipoate synthase; Provisional


Pssm-ID: 240408 [Multi-domain]  Cd Length: 398  Bit Score: 425.01  E-value: 2.05e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412   76 WMKESIPGG----ERYVQIKKKLRDLKLHTVCEEAKCPNLGECWSGG-ETGTATATIMILGDTCTRGCRFCNVKTSRTPP 150
Cdd:PTZ00413  96 WFKVKVPKGasrrPRFNRIRRSMREKKLHTVCEEAKCPNIGECWGGGdEEGTATATIMVMGDHCTRGCRFCSVKTSRKPP 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412  151 PPDPNEPNNVAEAIASWGVDYVVITSVDRDDLPDQGSGHFAETVQRLKFLKPEMLIEALVPDFRGDGGCVEKVSKSGLDV 230
Cdd:PTZ00413 176 PLDPNEPEKVAKAVAEMGVDYIVMTMVDRDDLPDGGASHVARCVELIKESNPELLLEALVGDFHGDLKSVEKLANSPLSV 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412  231 LAHNIETVEELQSFVRDHRANFKQSLDVLRMAKEYAPAGTLTKTSVMLGCGETPDQVVKTMEKVRAAGVDVMTFGQYMRP 310
Cdd:PTZ00413 256 YAHNIECVERITPYVRDRRASYRQSLKVLEHVKEFTNGAMLTKSSIMLGLGETEEEVRQTLRDLRTAGVSAVTLGQYLQP 335
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15226412  311 SKRHMPVAEYVTPDAFERYRLLGMEMGFRYVASGPMVRSSYKAGEYYIKSMIEADRVA 368
Cdd:PTZ00413 336 TKTRLKVSRYAHPKEFEMWEEEAMKMGFLYCASGPLVRSSYRAGEYYIKNLVKQRRKA 393
lipA TIGR00510
lipoate synthase; This enzyme is an iron-sulfur protein. It is localized to mitochondria in ...
76-361 6.41e-123

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: 6.41e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412    76 WMKESIPGGERYVQIKKKLRDLKLHTVCEEAKCPNLGECWSGGetgtaTATIMILGDTCTRGCRFCNVKTSRTPPPPDPN 155
Cdd:TIGR00510  20 WLKIKLPLGTVIAQIKNTMKNKGLHTVCEEASCPNLTECWNHG-----TATFMILGDICTRRCPFCDVAHGRNPLPPDPE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412   156 EPNNVAEAIASWGVDYVVITSVDRDDLPDQGSGHFAETVQRLKFLKPEMLIEALVPDFRGDGGCVEKVSKSGLDVLAHNI 235
Cdd:TIGR00510  95 EPAKLAETIKDMGLKYVVITSVDRDDLEDGGASHLAECIEAIREKLPNIKIETLVPDFRGNIAALDILLDAPPDVYNHNL 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412   236 ETVEELQSFVRdHRANFKQSLDVLRMAKEYAPAgTLTKTSVMLGCGETPDQVVKTMEKVRAAGVDVMTFGQYMRPSKRHM 315
Cdd:TIGR00510 175 ETVERLTPFVR-PGATYRWSLKLLERAKEYLPN-LPTKSGIMVGLGETNEEIKQTLKDLRDHGVTMVTLGQYLRPSRRHL 252
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 15226412   316 PVAEYVTPDAFERYRLLGMEMGFRYVASGPMVRSSYKAGEYYIKSM 361
Cdd:TIGR00510 253 PVKRYVSPEEFDYYRSVALEMGFLHAACGPFVRSSYHADSLFAAGR 298
PRK12928 PRK12928
lipoyl synthase; Provisional
76-355 2.65e-122

lipoyl synthase; Provisional


Pssm-ID: 237261  Cd Length: 290  Bit Score: 354.61  E-value: 2.65e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412   76 WMKESIPGGERYVQIKKKLRDLKLHTVCEEAKCPNLGECWSGGetgtaTATIMILGDTCTRGCRFCNVKTSRtPPPPDPN 155
Cdd:PRK12928  17 WLRAPIGKASELETVQRLVKQRRLHTICEEARCPNRGECYAQG-----TATFLIMGSICTRRCAFCQVDKGR-PMPLDPD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412  156 EPNNVAEAIASWGVDYVVITSVDRDDLPDQGSGHFAETVQRLKFLKPEMLIEALVPDFRG-DGGCVEKVSKSGLDVLAHN 234
Cdd:PRK12928  91 EPERVAEAVAALGLRYVVLTSVARDDLPDGGAAHFVATIAAIRARNPGTGIEVLTPDFWGgQRERLATVLAAKPDVFNHN 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412  235 IETVEELQSFVRdHRANFKQSLDVLRMAKEYAPaGTLTKTSVMLGCGETPDQVVKTMEKVRAAGVDVMTFGQYMRPSKRH 314
Cdd:PRK12928 171 LETVPRLQKAVR-RGADYQRSLDLLARAKELAP-DIPTKSGLMLGLGETEDEVIETLRDLRAVGCDRLTIGQYLRPSLAH 248
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 15226412  315 MPVAEYVTPDAFERYRLLGMEMGFRYVASGPMVRSSYKAGE 355
Cdd:PRK12928 249 LPVQRYWTPEEFEALGQIARELGFSHVRSGPLVRSSYHAGE 289
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
130-290 2.68e-15

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: 72.56  E-value: 2.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412   130 LGDTCTRGCRFCNVKTSRTPPPPDPNEPNNV---AEAIASWGVDYVVITSVDRDDLPDQGSGHFAEtvqRLKFLKPEMLI 206
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKGRELSPEEIleeAKELKRLGVEVVILGGGEPLLLPDLVELLERL---LKLELAEGIRI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412   207 EALVPDFRGDGGCVEKVSKSGLDVLAHNIETVEELQSFVRDHRANFKQSLDVLRMAKEYapAGTLTKTSVMLGCGETPDQ 286
Cdd:pfam04055  78 TLETNGTLLDEELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREA--GIPVVTDNIVGLPGETDED 155

                  ....
gi 15226412   287 VVKT 290
Cdd:pfam04055 156 LEET 159
LIAS_N pfam16881
N-terminal domain of lipoyl synthase of Radical_SAM family; LIAS_N is found as the N-terminal ...
17-108 7.58e-15

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: 69.47  E-value: 7.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412    17 RCFSSSSAVTPVTVTQSPkslEALRARLANeSPSLTDFIHGD-----TYSVEVGTKKKPLPKPK----WMKESIPGGERY 87
Cdd:pfam16881   1 RVFGSHLCSPASTSSSLP---DEKREFLQN-GPDLQDFVSGDlsdksTWAEYKGNLKRPKGERLrlppWLKTKIPLGKNY 76
                          90       100
                  ....*....|....*....|.
gi 15226412    88 VQIKKKLRDLKLHTVCEEAKC 108
Cdd:pfam16881  77 NKIKNTLRNLNLHTVCEEARC 97
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
124-332 2.42e-14

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: 71.28  E-value: 2.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412    124 TATIMILGDTCTRGCRFCNVKTSRTPPPPDPNEP-NNVAEAIASWGVDYVVITSV-----DRDDLPDQGSGHFAETVQRL 197
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSFPSLRGKLRSRYLEAlVREIELLAEKGEKEGLVGTVfigggTPTLLSPEQLEELLEAIREI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412    198 K--FLKPEMLIEALVPDFRGDggCVEKVSKSGLDVLAHNIETVEE--LQSFVRDHraNFKQSLDVLRMAKEYAPAGtlTK 273
Cdd:smart00729  81 LglAKDVEITIETRPDTLTEE--LLEALKEAGVNRVSLGVQSGDDevLKAINRGH--TVEDVLEAVELLREAGPIK--VS 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226412    274 TSVMLG-CGETPDQVVKTMEKVRAAGVDVMTFGQYMrPsKRHMPVAE----YVTPDAFERYRLL 332
Cdd:smart00729 155 TDLIVGlPGETEEDFEETLKLLKELGPDRVSIFPLS-P-RPGTPLAKmykrLKPPTKEERAELL 216
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
128-330 3.17e-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: 53.49  E-value: 3.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412 128 MILGDTCTRGCRFCNVKTS---RTPPPPDPNEPNNVAEAIASWGVDYVVITSVDRDDLPdqgsgHFAETVQRLKFLKPEM 204
Cdd:cd01335   1 LELTRGCNLNCGFCSNPASkgrGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYP-----ELAELLRRLKKELPGF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412 205 LIEALVPDFRGDGGCVEKVSKSGLDVLAHNIETVEELQSfvRDHRANFKQSLDVLRMAKEYAPAGTLTKTSVMLG-CGET 283
Cdd:cd01335  76 EISIETNGTLLTEELLKELKELGLDGVGVSLDSGDEEVA--DKIRGSGESFKERLEALKELREAGLGLSTTLLVGlGDED 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15226412 284 PDQVVKTMEKVRAA-GVDVMTFGQYMrPSKRhMPVAEYVTPDAFERYR 330
Cdd:cd01335 154 EEDDLEELELLAEFrSPDRVSLFRLL-PEEG-TPLELAAPVVPAEKLL 199
YgiQ COG1032
Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];
134-308 4.49e-03

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


Pssm-ID: 440655 [Multi-domain]  Cd Length: 394  Bit Score: 38.77  E-value: 4.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412 134 CTRGCRFCNVKTSRTPPPPDPNEPNNVAEA---IASWGVDYVVITsvdrDDLPDQGSGHFAETVQRLK------FLKPEM 204
Cdd:COG1032 184 CPFGCSFCSISALYGRKVRYRSPESVVEEIeelVKRYGIREIFFV----DDNFNVDKKRLKELLEELIerglnvSFPSEV 259
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226412 205 LIEALVPDFrgdggcVEKVSKSGLDVLAHNIETVEELqsfVRDH---RANFKQSLDVLRMAKEyapAGTLTKTSVMLGC- 280
Cdd:COG1032 260 RVDLLDEEL------LELLKKAGCRGLFIGIESGSQR---VLKAmnkGITVEDILEAVRLLKK---AGIRVKLYFIIGLp 327
                       170       180
                ....*....|....*....|....*...
gi 15226412 281 GETPDQVVKTMEKVRAAGVDVMTFGQYM 308
Cdd:COG1032 328 GETEEDIEETIEFIKELGPDQAQVSIFT 355
 
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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