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Conserved domains on  [gi|1805091844|gb|QHT56019|]
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lipoyl synthase [Cellulomonas sp. H30R-01]

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
19-305 0e+00

lipoyl synthase; Provisional


:

Pssm-ID: 235493 [Multi-domain]  Cd Length: 289  Bit Score: 543.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  19 ATPIEKKPEWIRTRATMGPEYSELKGLVKREGLHTVCEEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQIDTGKPADF 98
Cdd:PRK05481    1 AEKVARKPDWLRVKLPTGEEYTEIKKLLRELGLHTVCEEASCPNIGECWSRGTATFMILGDICTRRCPFCDVATGRPLPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  99 DADEPRRVAASVQAMGLKYATVTGVARDDLPDGGAWLYAETVRQIHAVNPGTGVELLIPDFNAVPELLDEVNESRPEVLA 178
Cdd:PRK05481   81 DPDEPERVAEAVARMGLKYVVITSVDRDDLPDGGAQHFAETIRAIRELNPGTTIEVLIPDFRGRMDALLTVLDARPDVFN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844 179 HNVETVPRIFKQIRPAFRYDRSLSVITRAREA--GLVTKSNLILGMGETTDEVKTALKDLVDAGCDIVTITQYLRPSLRH 256
Cdd:PRK05481  161 HNLETVPRLYKRVRPGADYERSLELLKRAKELhpGIPTKSGLMVGLGETDEEVLEVMDDLRAAGVDILTIGQYLQPSRKH 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1805091844 257 HPVDRWVRPEEFVELSDHAQELGFLGVMSGPLVRSSYRAGRLWGQAMRH 305
Cdd:PRK05481  241 LPVERYVTPEEFDEYKEIALELGFLHVASGPLVRSSYHADEQAAGAEVA 289
 
Name Accession Description Interval E-value
PRK05481 PRK05481
lipoyl synthase; Provisional
19-305 0e+00

lipoyl synthase; Provisional


Pssm-ID: 235493 [Multi-domain]  Cd Length: 289  Bit Score: 543.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  19 ATPIEKKPEWIRTRATMGPEYSELKGLVKREGLHTVCEEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQIDTGKPADF 98
Cdd:PRK05481    1 AEKVARKPDWLRVKLPTGEEYTEIKKLLRELGLHTVCEEASCPNIGECWSRGTATFMILGDICTRRCPFCDVATGRPLPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  99 DADEPRRVAASVQAMGLKYATVTGVARDDLPDGGAWLYAETVRQIHAVNPGTGVELLIPDFNAVPELLDEVNESRPEVLA 178
Cdd:PRK05481   81 DPDEPERVAEAVARMGLKYVVITSVDRDDLPDGGAQHFAETIRAIRELNPGTTIEVLIPDFRGRMDALLTVLDARPDVFN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844 179 HNVETVPRIFKQIRPAFRYDRSLSVITRAREA--GLVTKSNLILGMGETTDEVKTALKDLVDAGCDIVTITQYLRPSLRH 256
Cdd:PRK05481  161 HNLETVPRLYKRVRPGADYERSLELLKRAKELhpGIPTKSGLMVGLGETDEEVLEVMDDLRAAGVDILTIGQYLQPSRKH 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1805091844 257 HPVDRWVRPEEFVELSDHAQELGFLGVMSGPLVRSSYRAGRLWGQAMRH 305
Cdd:PRK05481  241 LPVERYVTPEEFDEYKEIALELGFLHVASGPLVRSSYHADEQAAGAEVA 289
LipA COG0320
Lipoate synthase [Coenzyme transport and metabolism]; Lipoate synthase is part of the Pathway ...
1-307 0e+00

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: 542.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844   1 MTIAPEGRRmlrVEARNAATPIEKKPEWIRTRATMGPEYSELKGLVKREGLHTVCEEAGCPNIFECWEDREATFLIGGDQ 80
Cdd:COG0320     1 MSTLPDIRR---PEARNPETPILRKPDWLRVKLPTGPEYAEVKKLLREHKLHTVCEEARCPNIGECWSRGTATFMILGDI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  81 CTRRCDFCQIDTGKPADFDADEPRRVAASVQAMGLKYATVTGVARDDLPDGGAWLYAETVRQIHAVNPGTGVELLIPDFN 160
Cdd:COG0320    78 CTRRCRFCDVATGRPLPLDPDEPERVAEAVAEMGLKYVVITSVDRDDLPDGGAGHFAETIRAIRELNPGTTIEVLIPDFR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844 161 AVPELLDEVNESRPEVLAHNVETVPRIFKQIRPAFRYDRSLSVITRAREA--GLVTKSNLILGMGETTDEVKTALKDLVD 238
Cdd:COG0320   158 GREEALDIVVDARPDVFNHNLETVPRLYKRVRPGADYERSLELLKRAKELdpGIPTKSGLMLGLGETDEEVLEVMRDLRA 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805091844 239 AGCDIVTITQYLRPSLRHHPVDRWVRPEEFVELSDHAQELGFLGVMSGPLVRSSYRAGRLWGQAMRHRG 307
Cdd:COG0320   238 AGVDILTIGQYLQPSKKHLPVDRYVTPEEFEELKEIALELGFLHVASGPLVRSSYHADEQAAKARAARG 306
lipA TIGR00510
lipoate synthase; This enzyme is an iron-sulfur protein. It is localized to mitochondria in ...
24-303 3.81e-109

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: 320.25  E-value: 3.81e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  24 KKPEWIRTRATMGPEYSELKGLVKREGLHTVCEEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQIDTG-KPADFDADE 102
Cdd:TIGR00510  16 RKPEWLKIKLPLGTVIAQIKNTMKNKGLHTVCEEASCPNLTECWNHGTATFMILGDICTRRCPFCDVAHGrNPLPPDPEE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844 103 PRRVAASVQAMGLKYATVTGVARDDLPDGGAWLYAETVRQIHAVNPGTGVELLIPDFNAVPELLDEVNESRPEVLAHNVE 182
Cdd:TIGR00510  96 PAKLAETIKDMGLKYVVITSVDRDDLEDGGASHLAECIEAIREKLPNIKIETLVPDFRGNIAALDILLDAPPDVYNHNLE 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844 183 TVPRIFKQIRPAFRYDRSLSVITRAREA--GLVTKSNLILGMGETTDEVKTALKDLVDAGCDIVTITQYLRPSLRHHPVD 260
Cdd:TIGR00510 176 TVERLTPFVRPGATYRWSLKLLERAKEYlpNLPTKSGIMVGLGETNEEIKQTLKDLRDHGVTMVTLGQYLRPSRRHLPVK 255
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1805091844 261 RWVRPEEFVELSDHAQELGFLGVMSGPLVRSSYRAGRLWGQAM 303
Cdd:TIGR00510 256 RYVSPEEFDYYRSVALEMGFLHAACGPFVRSSYHADSLFAAGR 298
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
81-228 1.94e-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: 1.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  81 CTRRCDFCQI----DTGKPADFDADEPRRVAASVQAMGLKYATVTGVARDDLPDGGAWLYAEtvrQIHAVNPGTGVELLI 156
Cdd:pfam04055   5 CNLRCTYCAFpsirARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERL---LKLELAEGIRITLET 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805091844 157 PDFNAVPELLDEVNESRPEVLAHNVETVPRIFKQ-IRPAFRYDRSLSVITRAREAGLVTKSNLILGMGETTDE 228
Cdd:pfam04055  82 NGTLLDEELLELLKEAGLDRVSIGLESGDDEVLKlINRGHTFEEVLEALELLREAGIPVVTDNIVGLPGETDE 154
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
74-249 1.74e-13

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: 68.58  E-value: 1.74e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844   74 FLIGGDQCTRRCDFCQI--DTGKPADFDADEPRRVAASVQAMGLK---YATVT--GVARDDLPDGGAWLYAETVRQIHAV 146
Cdd:smart00729   4 LYIITRGCPRRCTFCSFpsLRGKLRSRYLEALVREIELLAEKGEKeglVGTVFigGGTPTLLSPEQLEELLEAIREILGL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  147 NPGTGVELLIPDFNAVPELLDEVNESRPEVLAHNVETV-PRIFKQIRPAFRYDRSLSVITRAREAG-LVTKSNLILGM-G 223
Cdd:smart00729  84 AKDVEITIETRPDTLTEELLEALKEAGVNRVSLGVQSGdDEVLKAINRGHTVEDVLEAVELLREAGpIKVSTDLIVGLpG 163
                          170       180
                   ....*....|....*....|....*.
gi 1805091844  224 ETTDEVKTALKDLVDAGCDIVTITQY 249
Cdd:smart00729 164 ETEEDFEETLKLLKELGPDRVSIFPL 189
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
78-229 7.98e-09

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: 55.03  E-value: 7.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  78 GDQCTRRCDFCQIDTGKPADFD----ADEPRRVAASVQAMGLKYATVTGvaRDDLPDGGawlYAETVRQIHAVNPGTGVE 153
Cdd:cd01335     4 TRGCNLNCGFCSNPASKGRGPEsppeIEEILDIVLEAKERGVEVVILTG--GEPLLYPE---LAELLRRLKKELPGFEIS 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805091844 154 LLIPDFNAVPELLDEVNESRPEVLAHNVETVPRIF--KQIRPAFRYDRSLSVITRAREAGLVTKSNLILGMGETTDEV 229
Cdd:cd01335    79 IETNGTLLTEELLKELKELGLDGVGVSLDSGDEEVadKIRGSGESFKERLEALKELREAGLGLSTTLLVGLGDEDEED 156
 
Name Accession Description Interval E-value
PRK05481 PRK05481
lipoyl synthase; Provisional
19-305 0e+00

lipoyl synthase; Provisional


Pssm-ID: 235493 [Multi-domain]  Cd Length: 289  Bit Score: 543.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  19 ATPIEKKPEWIRTRATMGPEYSELKGLVKREGLHTVCEEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQIDTGKPADF 98
Cdd:PRK05481    1 AEKVARKPDWLRVKLPTGEEYTEIKKLLRELGLHTVCEEASCPNIGECWSRGTATFMILGDICTRRCPFCDVATGRPLPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  99 DADEPRRVAASVQAMGLKYATVTGVARDDLPDGGAWLYAETVRQIHAVNPGTGVELLIPDFNAVPELLDEVNESRPEVLA 178
Cdd:PRK05481   81 DPDEPERVAEAVARMGLKYVVITSVDRDDLPDGGAQHFAETIRAIRELNPGTTIEVLIPDFRGRMDALLTVLDARPDVFN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844 179 HNVETVPRIFKQIRPAFRYDRSLSVITRAREA--GLVTKSNLILGMGETTDEVKTALKDLVDAGCDIVTITQYLRPSLRH 256
Cdd:PRK05481  161 HNLETVPRLYKRVRPGADYERSLELLKRAKELhpGIPTKSGLMVGLGETDEEVLEVMDDLRAAGVDILTIGQYLQPSRKH 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1805091844 257 HPVDRWVRPEEFVELSDHAQELGFLGVMSGPLVRSSYRAGRLWGQAMRH 305
Cdd:PRK05481  241 LPVERYVTPEEFDEYKEIALELGFLHVASGPLVRSSYHADEQAAGAEVA 289
LipA COG0320
Lipoate synthase [Coenzyme transport and metabolism]; Lipoate synthase is part of the Pathway ...
1-307 0e+00

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: 542.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844   1 MTIAPEGRRmlrVEARNAATPIEKKPEWIRTRATMGPEYSELKGLVKREGLHTVCEEAGCPNIFECWEDREATFLIGGDQ 80
Cdd:COG0320     1 MSTLPDIRR---PEARNPETPILRKPDWLRVKLPTGPEYAEVKKLLREHKLHTVCEEARCPNIGECWSRGTATFMILGDI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  81 CTRRCDFCQIDTGKPADFDADEPRRVAASVQAMGLKYATVTGVARDDLPDGGAWLYAETVRQIHAVNPGTGVELLIPDFN 160
Cdd:COG0320    78 CTRRCRFCDVATGRPLPLDPDEPERVAEAVAEMGLKYVVITSVDRDDLPDGGAGHFAETIRAIRELNPGTTIEVLIPDFR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844 161 AVPELLDEVNESRPEVLAHNVETVPRIFKQIRPAFRYDRSLSVITRAREA--GLVTKSNLILGMGETTDEVKTALKDLVD 238
Cdd:COG0320   158 GREEALDIVVDARPDVFNHNLETVPRLYKRVRPGADYERSLELLKRAKELdpGIPTKSGLMLGLGETDEEVLEVMRDLRA 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805091844 239 AGCDIVTITQYLRPSLRHHPVDRWVRPEEFVELSDHAQELGFLGVMSGPLVRSSYRAGRLWGQAMRHRG 307
Cdd:COG0320   238 AGVDILTIGQYLQPSKKHLPVDRYVTPEEFEELKEIALELGFLHVASGPLVRSSYHADEQAAKARAARG 306
PRK12928 PRK12928
lipoyl synthase; Provisional
12-298 1.29e-167

lipoyl synthase; Provisional


Pssm-ID: 237261  Cd Length: 290  Bit Score: 467.86  E-value: 1.29e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  12 RVEARNAATPIEKKPEWIRTRATMGPEYSELKGLVKREGLHTVCEEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQID 91
Cdd:PRK12928    1 RSRDKSARIPVERLPEWLRAPIGKASELETVQRLVKQRRLHTICEEARCPNRGECYAQGTATFLIMGSICTRRCAFCQVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  92 TGKPADFDADEPRRVAASVQAMGLKYATVTGVARDDLPDGGAWLYAETVRQIHAVNPGTGVELLIPDFNA-VPELLDEVN 170
Cdd:PRK12928   81 KGRPMPLDPDEPERVAEAVAALGLRYVVLTSVARDDLPDGGAAHFVATIAAIRARNPGTGIEVLTPDFWGgQRERLATVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844 171 ESRPEVLAHNVETVPRIFKQIRPAFRYDRSLSVITRAREA--GLVTKSNLILGMGETTDEVKTALKDLVDAGCDIVTITQ 248
Cdd:PRK12928  161 AAKPDVFNHNLETVPRLQKAVRRGADYQRSLDLLARAKELapDIPTKSGLMLGLGETEDEVIETLRDLRAVGCDRLTIGQ 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1805091844 249 YLRPSLRHHPVDRWVRPEEFVELSDHAQELGFLGVMSGPLVRSSYRAGRL 298
Cdd:PRK12928  241 YLRPSLAHLPVQRYWTPEEFEALGQIARELGFSHVRSGPLVRSSYHAGEQ 290
lipA TIGR00510
lipoate synthase; This enzyme is an iron-sulfur protein. It is localized to mitochondria in ...
24-303 3.81e-109

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: 320.25  E-value: 3.81e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  24 KKPEWIRTRATMGPEYSELKGLVKREGLHTVCEEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQIDTG-KPADFDADE 102
Cdd:TIGR00510  16 RKPEWLKIKLPLGTVIAQIKNTMKNKGLHTVCEEASCPNLTECWNHGTATFMILGDICTRRCPFCDVAHGrNPLPPDPEE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844 103 PRRVAASVQAMGLKYATVTGVARDDLPDGGAWLYAETVRQIHAVNPGTGVELLIPDFNAVPELLDEVNESRPEVLAHNVE 182
Cdd:TIGR00510  96 PAKLAETIKDMGLKYVVITSVDRDDLEDGGASHLAECIEAIREKLPNIKIETLVPDFRGNIAALDILLDAPPDVYNHNLE 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844 183 TVPRIFKQIRPAFRYDRSLSVITRAREA--GLVTKSNLILGMGETTDEVKTALKDLVDAGCDIVTITQYLRPSLRHHPVD 260
Cdd:TIGR00510 176 TVERLTPFVRPGATYRWSLKLLERAKEYlpNLPTKSGIMVGLGETNEEIKQTLKDLRDHGVTMVTLGQYLRPSRRHLPVK 255
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1805091844 261 RWVRPEEFVELSDHAQELGFLGVMSGPLVRSSYRAGRLWGQAM 303
Cdd:TIGR00510 256 RYVSPEEFDYYRSVALEMGFLHAACGPFVRSSYHADSLFAAGR 298
PLN02428 PLN02428
lipoic acid synthase
21-303 2.64e-104

lipoic acid synthase


Pssm-ID: 215236 [Multi-domain]  Cd Length: 349  Bit Score: 309.37  E-value: 2.64e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  21 PIEKKPEWIRTRATMGPEYSELKGLVKREGLHTVCEEAGCPNIFECWEDRE-----ATFLIGGDQCTRRCDFCQIDTGK- 94
Cdd:PLN02428   47 KPLPKPKWLRQRAPGGEKYTEIKEKLRELKLNTVCEEAQCPNIGECWNGGGtgtatATIMILGDTCTRGCRFCAVKTSRt 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  95 PADFDADEPRRVAASVQAMGLKYATVTGVARDDLPDGGAWLYAETVRQIHAVNPGTGVELLIPDFNAVPELLDEVNESRP 174
Cdd:PLN02428  127 PPPPDPDEPENVAEAIASWGVDYVVLTSVDRDDLPDGGSGHFAETVRRLKQLKPEILVEALVPDFRGDLGAVETVATSGL 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844 175 EVLAHNVETVPRIFKQIR-PAFRYDRSLSVITRAREA--GLVTKSNLILGMGETTDEVKTALKDLVDAGCDIVTITQYLR 251
Cdd:PLN02428  207 DVFAHNIETVERLQRIVRdPRAGYKQSLDVLKHAKESkpGLLTKTSIMLGLGETDEEVVQTMEDLRAAGVDVVTFGQYLR 286
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1805091844 252 PSLRHHPVDRWVRPEEFVELSDHAQELGFLGVMSGPLVRSSYRAGRLWGQAM 303
Cdd:PLN02428  287 PTKRHLPVKEYVTPEKFEFWREYGEEMGFRYVASGPLVRSSYKAGEFFIKSM 338
PTZ00413 PTZ00413
lipoate synthase; Provisional
23-296 3.51e-85

lipoate synthase; Provisional


Pssm-ID: 240408 [Multi-domain]  Cd Length: 398  Bit Score: 262.46  E-value: 3.51e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  23 EKKPEWIRTRATMG----PEYSELKGLVKREGLHTVCEEAGCPNIFECW------EDREATFLIGGDQCTRRCDFCQIDT 92
Cdd:PTZ00413   91 EPLPPWFKVKVPKGasrrPRFNRIRRSMREKKLHTVCEEAKCPNIGECWgggdeeGTATATIMVMGDHCTRGCRFCSVKT 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  93 G-KPADFDADEPRRVAASVQAMGLKYATVTGVARDDLPDGGAWLYAETVRQIHAVNPGTGVELLIPDFNAVPELLDEVNE 171
Cdd:PTZ00413  171 SrKPPPLDPNEPEKVAKAVAEMGVDYIVMTMVDRDDLPDGGASHVARCVELIKESNPELLLEALVGDFHGDLKSVEKLAN 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844 172 SRPEVLAHNVETVPRIFKQIRPA-FRYDRSLSVITRARE---AGLVTKSNLILGMGETTDEVKTALKDLVDAGCDIVTIT 247
Cdd:PTZ00413  251 SPLSVYAHNIECVERITPYVRDRrASYRQSLKVLEHVKEftnGAMLTKSSIMLGLGETEEEVRQTLRDLRTAGVSAVTLG 330
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1805091844 248 QYLRPSLRHHPVDRWVRPEEFVELSDHAQELGFLGVMSGPLVRSSYRAG 296
Cdd:PTZ00413  331 QYLQPTKTRLKVSRYAHPKEFEMWEEEAMKMGFLYCASGPLVRSSYRAG 379
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
81-228 1.94e-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: 1.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  81 CTRRCDFCQI----DTGKPADFDADEPRRVAASVQAMGLKYATVTGVARDDLPDGGAWLYAEtvrQIHAVNPGTGVELLI 156
Cdd:pfam04055   5 CNLRCTYCAFpsirARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERL---LKLELAEGIRITLET 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805091844 157 PDFNAVPELLDEVNESRPEVLAHNVETVPRIFKQ-IRPAFRYDRSLSVITRAREAGLVTKSNLILGMGETTDE 228
Cdd:pfam04055  82 NGTLLDEELLELLKEAGLDRVSIGLESGDDEVLKlINRGHTFEEVLEALELLREAGIPVVTDNIVGLPGETDE 154
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
74-249 1.74e-13

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: 68.58  E-value: 1.74e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844   74 FLIGGDQCTRRCDFCQI--DTGKPADFDADEPRRVAASVQAMGLK---YATVT--GVARDDLPDGGAWLYAETVRQIHAV 146
Cdd:smart00729   4 LYIITRGCPRRCTFCSFpsLRGKLRSRYLEALVREIELLAEKGEKeglVGTVFigGGTPTLLSPEQLEELLEAIREILGL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  147 NPGTGVELLIPDFNAVPELLDEVNESRPEVLAHNVETV-PRIFKQIRPAFRYDRSLSVITRAREAG-LVTKSNLILGM-G 223
Cdd:smart00729  84 AKDVEITIETRPDTLTEELLEALKEAGVNRVSLGVQSGdDEVLKAINRGHTVEDVLEAVELLREAGpIKVSTDLIVGLpG 163
                          170       180
                   ....*....|....*....|....*.
gi 1805091844  224 ETTDEVKTALKDLVDAGCDIVTITQY 249
Cdd:smart00729 164 ETEEDFEETLKLLKELGPDRVSIFPL 189
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
78-229 7.98e-09

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: 55.03  E-value: 7.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  78 GDQCTRRCDFCQIDTGKPADFD----ADEPRRVAASVQAMGLKYATVTGvaRDDLPDGGawlYAETVRQIHAVNPGTGVE 153
Cdd:cd01335     4 TRGCNLNCGFCSNPASKGRGPEsppeIEEILDIVLEAKERGVEVVILTG--GEPLLYPE---LAELLRRLKKELPGFEIS 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805091844 154 LLIPDFNAVPELLDEVNESRPEVLAHNVETVPRIF--KQIRPAFRYDRSLSVITRAREAGLVTKSNLILGMGETTDEV 229
Cdd:cd01335    79 IETNGTLLTEELLKELKELGLDGVGVSLDSGDEEVadKIRGSGESFKERLEALKELREAGLGLSTTLLVGLGDEDEED 156
LIAS_N pfam16881
N-terminal domain of lipoyl synthase of Radical_SAM family; LIAS_N is found as the N-terminal ...
26-60 1.40e-06

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: 45.97  E-value: 1.40e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1805091844  26 PEWIRTRATMGPEYSELKGLVKREGLHTVCEEAGC 60
Cdd:pfam16881  63 PPWLKTKIPLGKNYNKIKNTLRNLNLHTVCEEARC 97
BioB COG0502
Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or ...
179-238 1.88e-05

Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 440268 [Multi-domain]  Cd Length: 308  Bit Score: 45.81  E-value: 1.88e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844 179 HNVETVPRIFKQIRPAFRYDRSLSVITRAREAGLVTKSNLILGMGETtdevktaLKDLVD 238
Cdd:COG0502   150 HNLETSPELYPKICTTHTYEDRLDTLKNAREAGLEVCSGGIVGMGET-------LEDRAD 202
YgiQ COG1032
Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];
81-252 9.61e-04

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


Pssm-ID: 440655 [Multi-domain]  Cd Length: 394  Bit Score: 40.70  E-value: 9.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844  81 CTRRCDFCQIDT---GKPADFDADeprRVAASVQAM--GLKYATVTGVARDDLPDGGAWLyaETVRQIHAVNPGT--GVE 153
Cdd:COG1032   184 CPFGCSFCSISAlygRKVRYRSPE---SVVEEIEELvkRYGIREIFFVDDNFNVDKKRLK--ELLEELIERGLNVsfPSE 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805091844 154 LLIPDFNavPELLDEVNESRPEVLAHNVETV-PRIFKQIRPAFRYDRSLSVITRAREAGLVTKSNLILGM-GETTDEVKT 231
Cdd:COG1032   259 VRVDLLD--EELLELLKKAGCRGLFIGIESGsQRVLKAMNKGITVEDILEAVRLLKKAGIRVKLYFIIGLpGETEEDIEE 336
                         170       180
                  ....*....|....*....|.
gi 1805091844 232 ALKDLVDAGCDIVTItQYLRP 252
Cdd:COG1032   337 TIEFIKELGPDQAQV-SIFTP 356
 
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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