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Conserved domains on  [gi|37577164|ref|NP_919433|]
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lipoyl synthase, mitochondrial isoform 2 precursor [Homo sapiens]

Protein Classification

lipoyl synthase( domain architecture ID 1003513)

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 super family cl33489
lipoic acid synthase
22-319 8.31e-177

lipoic acid synthase


The actual alignment was detected with superfamily member PLN02428:

Pssm-ID: 215236 [Multi-domain]  Cd Length: 349  Bit Score: 493.11  E-value: 8.31e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164   22 CSPVRPLSSLPDKKKELLQNGPDLQDFVSGDladrsTWDEYKGNLKRQkgerLRLPPWLKTEIPMGKNYNKLKNTLRNLN 101
Cdd:PLN02428   6 TTAPQTPQTLAALRARLASESPSLGDFVSLG-----PYTLGSYGRDKP----LPKPKWLRQRAPGGEKYTEIKEKLRELK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164  102 LHTVCEEARCPNIGECWGGGEYATATATIMLMGDTCTRGCRFCSVKTARNPPPLDASEPYNTAKAIAEWGLDYVVLTSVD 181
Cdd:PLN02428  77 LNTVCEEAQCPNIGECWNGGGTGTATATIMILGDTCTRGCRFCAVKTSRTPPPPDPDEPENVAEAIASWGVDYVVLTSVD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164  182 RDDMPDGGAEHIAKTVSYLKERNPKILVECLTPDFRGDLKAIEKVALSGLDVYAHNVETVPELQSKVRDPRANFDQSLRV 261
Cdd:PLN02428 157 RDDLPDGGSGHFAETVRRLKQLKPEILVEALVPDFRGDLGAVETVATSGLDVFAHNIETVERLQRIVRDPRAGYKQSLDV 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 37577164  262 LKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCLTLGQYMQPTRRHLKV 319
Cdd:PLN02428 237 LKHAKESKPGLLTKTSIMLGLGETDEEVVQTMEDLRAAGVDVVTFGQYLRPTKRHLPV 294
 
Name Accession Description Interval E-value
PLN02428 PLN02428
lipoic acid synthase
22-319 8.31e-177

lipoic acid synthase


Pssm-ID: 215236 [Multi-domain]  Cd Length: 349  Bit Score: 493.11  E-value: 8.31e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164   22 CSPVRPLSSLPDKKKELLQNGPDLQDFVSGDladrsTWDEYKGNLKRQkgerLRLPPWLKTEIPMGKNYNKLKNTLRNLN 101
Cdd:PLN02428   6 TTAPQTPQTLAALRARLASESPSLGDFVSLG-----PYTLGSYGRDKP----LPKPKWLRQRAPGGEKYTEIKEKLRELK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164  102 LHTVCEEARCPNIGECWGGGEYATATATIMLMGDTCTRGCRFCSVKTARNPPPLDASEPYNTAKAIAEWGLDYVVLTSVD 181
Cdd:PLN02428  77 LNTVCEEAQCPNIGECWNGGGTGTATATIMILGDTCTRGCRFCAVKTSRTPPPPDPDEPENVAEAIASWGVDYVVLTSVD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164  182 RDDMPDGGAEHIAKTVSYLKERNPKILVECLTPDFRGDLKAIEKVALSGLDVYAHNVETVPELQSKVRDPRANFDQSLRV 261
Cdd:PLN02428 157 RDDLPDGGSGHFAETVRRLKQLKPEILVEALVPDFRGDLGAVETVATSGLDVFAHNIETVERLQRIVRDPRAGYKQSLDV 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 37577164  262 LKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCLTLGQYMQPTRRHLKV 319
Cdd:PLN02428 237 LKHAKESKPGLLTKTSIMLGLGETDEEVVQTMEDLRAAGVDVVTFGQYLRPTKRHLPV 294
LipA COG0320
Lipoate synthase [Coenzyme transport and metabolism]; Lipoate synthase is part of the Pathway ...
67-319 4.17e-150

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: 423.74  E-value: 4.17e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164  67 KRQKGERLRLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGeyataTATIMLMGDTCTRGCRFCSV 146
Cdd:COG0320  13 RNPETPILRKPDWLRVKLPTGPEYAEVKKLLREHKLHTVCEEARCPNIGECWSRG-----TATFMILGDICTRRCRFCDV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164 147 KTARnPPPLDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTVSYLKERNPKILVECLTPDFRGDLKAIEKV 226
Cdd:COG0320  88 ATGR-PLPLDPDEPERVAEAVAEMGLKYVVITSVDRDDLPDGGAGHFAETIRAIRELNPGTTIEVLIPDFRGREEALDIV 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164 227 ALSGLDVYAHNVETVPELQSKVRdPRANFDQSLRVLKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCLTL 306
Cdd:COG0320 167 VDARPDVFNHNLETVPRLYKRVR-PGADYERSLELLKRAKELDPGIPTKSGLMLGLGETDEEVLEVMRDLRAAGVDILTI 245
                       250
                ....*....|...
gi 37577164 307 GQYMQPTRRHLKV 319
Cdd:COG0320 246 GQYLQPSKKHLPV 258
lipA TIGR00510
lipoate synthase; This enzyme is an iron-sulfur protein. It is localized to mitochondria in ...
65-319 2.17e-118

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: 342.97  E-value: 2.17e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164    65 NLKRQKGERLRLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGeyataTATIMLMGDTCTRGCRFC 144
Cdd:TIGR00510   6 NPIPNKEILLRKPEWLKIKLPLGTVIAQIKNTMKNKGLHTVCEEASCPNLTECWNHG-----TATFMILGDICTRRCPFC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164   145 SVKTARNPPPLDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTVSYLKERNPKILVECLTPDFRGDLKAIE 224
Cdd:TIGR00510  81 DVAHGRNPLPPDPEEPAKLAETIKDMGLKYVVITSVDRDDLEDGGASHLAECIEAIREKLPNIKIETLVPDFRGNIAALD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164   225 KVALSGLDVYAHNVETVPELQSKVRdPRANFDQSLRVLKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCL 304
Cdd:TIGR00510 161 ILLDAPPDVYNHNLETVERLTPFVR-PGATYRWSLKLLERAKEYLPNLPTKSGIMVGLGETNEEIKQTLKDLRDHGVTMV 239
                         250
                  ....*....|....*
gi 37577164   305 TLGQYMQPTRRHLKV 319
Cdd:TIGR00510 240 TLGQYLRPSRRHLPV 254
LIAS_N pfam16881
N-terminal domain of lipoyl synthase of Radical_SAM family; LIAS_N is found as the N-terminal ...
15-111 2.22e-66

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: 203.13  E-value: 2.22e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164    15 RVFGRYFCSPVRPLSSLPDKKKELLQNGPDLQDFVSGDLADRSTWDEYKGNLKRQKGERLRLPPWLKTEIPMGKNYNKLK 94
Cdd:pfam16881   1 RVFGSHLCSPASTSSSLPDEKREFLQNGPDLQDFVSGDLSDKSTWAEYKGNLKRPKGERLRLPPWLKTKIPLGKNYNKIK 80
                          90
                  ....*....|....*..
gi 37577164    95 NTLRNLNLHTVCEEARC 111
Cdd:pfam16881  81 NTLRNLNLHTVCEEARC 97
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
127-310 4.24e-19

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: 83.99  E-value: 4.24e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164    127 TATIMLMGDTCTRGCRFCSVKTARN---PPPLDASEpyNTAKAIAEWGLDYVVLTSV-----DRDDMPDGGAEHIAKTVS 198
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSFPSLRGklrSRYLEALV--REIELLAEKGEKEGLVGTVfigggTPTLLSPEQLEELLEAIR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164    199 YLKERNPKILVECLTPDFRGDLKAIEKVALSGLDVYAHNVETVPELQSKVRDPRANFDQSLRVLKHAKKVQPDVISkTSI 278
Cdd:smart00729  79 EILGLAKDVEITIETRPDTLTEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAGPIKVS-TDL 157
                          170       180       190
                   ....*....|....*....|....*....|...
gi 37577164    279 MLGL-GENDEQVYATMKALREADVDCLTLGQYM 310
Cdd:smart00729 158 IVGLpGETEEDFEETLKLLKELGPDRVSIFPLS 190
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
134-310 1.69e-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: 1.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164 134 GDTCTRGCRFCSV---KTARNPPPLDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPdggaeHIAKTVSYLKERNPKILVE 210
Cdd:cd01335   4 TRGCNLNCGFCSNpasKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYP-----ELAELLRRLKKELPGFEIS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164 211 CLTPDFRGDLKAIEKVALSGLDVYAHNVETV-PELQSKVRDPRANFDQSLRVLKHAKKVqpDVISKTSIMLGLGENDEQV 289
Cdd:cd01335  79 IETNGTLLTEELLKELKELGLDGVGVSLDSGdEEVADKIRGSGESFKERLEALKELREA--GLGLSTTLLVGLGDEDEED 156
                       170       180
                ....*....|....*....|...
gi 37577164 290 YA-TMKALREAD-VDCLTLGQYM 310
Cdd:cd01335 157 DLeELELLAEFRsPDRVSLFRLL 179
 
Name Accession Description Interval E-value
PLN02428 PLN02428
lipoic acid synthase
22-319 8.31e-177

lipoic acid synthase


Pssm-ID: 215236 [Multi-domain]  Cd Length: 349  Bit Score: 493.11  E-value: 8.31e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164   22 CSPVRPLSSLPDKKKELLQNGPDLQDFVSGDladrsTWDEYKGNLKRQkgerLRLPPWLKTEIPMGKNYNKLKNTLRNLN 101
Cdd:PLN02428   6 TTAPQTPQTLAALRARLASESPSLGDFVSLG-----PYTLGSYGRDKP----LPKPKWLRQRAPGGEKYTEIKEKLRELK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164  102 LHTVCEEARCPNIGECWGGGEYATATATIMLMGDTCTRGCRFCSVKTARNPPPLDASEPYNTAKAIAEWGLDYVVLTSVD 181
Cdd:PLN02428  77 LNTVCEEAQCPNIGECWNGGGTGTATATIMILGDTCTRGCRFCAVKTSRTPPPPDPDEPENVAEAIASWGVDYVVLTSVD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164  182 RDDMPDGGAEHIAKTVSYLKERNPKILVECLTPDFRGDLKAIEKVALSGLDVYAHNVETVPELQSKVRDPRANFDQSLRV 261
Cdd:PLN02428 157 RDDLPDGGSGHFAETVRRLKQLKPEILVEALVPDFRGDLGAVETVATSGLDVFAHNIETVERLQRIVRDPRAGYKQSLDV 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 37577164  262 LKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCLTLGQYMQPTRRHLKV 319
Cdd:PLN02428 237 LKHAKESKPGLLTKTSIMLGLGETDEEVVQTMEDLRAAGVDVVTFGQYLRPTKRHLPV 294
LipA COG0320
Lipoate synthase [Coenzyme transport and metabolism]; Lipoate synthase is part of the Pathway ...
67-319 4.17e-150

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: 423.74  E-value: 4.17e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164  67 KRQKGERLRLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGeyataTATIMLMGDTCTRGCRFCSV 146
Cdd:COG0320  13 RNPETPILRKPDWLRVKLPTGPEYAEVKKLLREHKLHTVCEEARCPNIGECWSRG-----TATFMILGDICTRRCRFCDV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164 147 KTARnPPPLDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTVSYLKERNPKILVECLTPDFRGDLKAIEKV 226
Cdd:COG0320  88 ATGR-PLPLDPDEPERVAEAVAEMGLKYVVITSVDRDDLPDGGAGHFAETIRAIRELNPGTTIEVLIPDFRGREEALDIV 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164 227 ALSGLDVYAHNVETVPELQSKVRdPRANFDQSLRVLKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCLTL 306
Cdd:COG0320 167 VDARPDVFNHNLETVPRLYKRVR-PGADYERSLELLKRAKELDPGIPTKSGLMLGLGETDEEVLEVMRDLRAAGVDILTI 245
                       250
                ....*....|...
gi 37577164 307 GQYMQPTRRHLKV 319
Cdd:COG0320 246 GQYLQPSKKHLPV 258
PRK05481 PRK05481
lipoyl synthase; Provisional
75-319 4.79e-147

lipoyl synthase; Provisional


Pssm-ID: 235493 [Multi-domain]  Cd Length: 289  Bit Score: 415.26  E-value: 4.79e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164   75 RLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGeyataTATIMLMGDTCTRGCRFCSVKTARnPPP 154
Cdd:PRK05481   6 RKPDWLRVKLPTGEEYTEIKKLLRELGLHTVCEEASCPNIGECWSRG-----TATFMILGDICTRRCPFCDVATGR-PLP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164  155 LDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTVSYLKERNPKILVECLTPDFRGDLKAIEKVALSGLDVY 234
Cdd:PRK05481  80 LDPDEPERVAEAVARMGLKYVVITSVDRDDLPDGGAQHFAETIRAIRELNPGTTIEVLIPDFRGRMDALLTVLDARPDVF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164  235 AHNVETVPELQSKVRdPRANFDQSLRVLKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCLTLGQYMQPTR 314
Cdd:PRK05481 160 NHNLETVPRLYKRVR-PGADYERSLELLKRAKELHPGIPTKSGLMVGLGETDEEVLEVMDDLRAAGVDILTIGQYLQPSR 238

                 ....*
gi 37577164  315 RHLKV 319
Cdd:PRK05481 239 KHLPV 243
PTZ00413 PTZ00413
lipoate synthase; Provisional
70-319 3.99e-142

lipoate synthase; Provisional


Pssm-ID: 240408 [Multi-domain]  Cd Length: 398  Bit Score: 406.91  E-value: 3.99e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164   70 KGERLRLPPWLKTEIPMGKN----YNKLKNTLRNLNLHTVCEEARCPNIGECWGGG-EYATATATIMLMGDTCTRGCRFC 144
Cdd:PTZ00413  87 KRGEEPLPPWFKVKVPKGASrrprFNRIRRSMREKKLHTVCEEAKCPNIGECWGGGdEEGTATATIMVMGDHCTRGCRFC 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164  145 SVKTARNPPPLDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTVSYLKERNPKILVECLTPDFRGDLKAIE 224
Cdd:PTZ00413 167 SVKTSRKPPPLDPNEPEKVAKAVAEMGVDYIVMTMVDRDDLPDGGASHVARCVELIKESNPELLLEALVGDFHGDLKSVE 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164  225 KVALSGLDVYAHNVETVPELQSKVRDPRANFDQSLRVLKHAKKV-QPDVISKTSIMLGLGENDEQVYATMKALREADVDC 303
Cdd:PTZ00413 247 KLANSPLSVYAHNIECVERITPYVRDRRASYRQSLKVLEHVKEFtNGAMLTKSSIMLGLGETEEEVRQTLRDLRTAGVSA 326
                        250
                 ....*....|....*.
gi 37577164  304 LTLGQYMQPTRRHLKV 319
Cdd:PTZ00413 327 VTLGQYLQPTKTRLKV 342
lipA TIGR00510
lipoate synthase; This enzyme is an iron-sulfur protein. It is localized to mitochondria in ...
65-319 2.17e-118

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: 342.97  E-value: 2.17e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164    65 NLKRQKGERLRLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGeyataTATIMLMGDTCTRGCRFC 144
Cdd:TIGR00510   6 NPIPNKEILLRKPEWLKIKLPLGTVIAQIKNTMKNKGLHTVCEEASCPNLTECWNHG-----TATFMILGDICTRRCPFC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164   145 SVKTARNPPPLDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTVSYLKERNPKILVECLTPDFRGDLKAIE 224
Cdd:TIGR00510  81 DVAHGRNPLPPDPEEPAKLAETIKDMGLKYVVITSVDRDDLEDGGASHLAECIEAIREKLPNIKIETLVPDFRGNIAALD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164   225 KVALSGLDVYAHNVETVPELQSKVRdPRANFDQSLRVLKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCL 304
Cdd:TIGR00510 161 ILLDAPPDVYNHNLETVERLTPFVR-PGATYRWSLKLLERAKEYLPNLPTKSGIMVGLGETNEEIKQTLKDLRDHGVTMV 239
                         250
                  ....*....|....*
gi 37577164   305 TLGQYMQPTRRHLKV 319
Cdd:TIGR00510 240 TLGQYLRPSRRHLPV 254
PRK12928 PRK12928
lipoyl synthase; Provisional
72-319 1.68e-116

lipoyl synthase; Provisional


Pssm-ID: 237261  Cd Length: 290  Bit Score: 337.67  E-value: 1.68e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164   72 ERLRLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGeyataTATIMLMGDTCTRGCRFCSVKTARn 151
Cdd:PRK12928  10 PVERLPEWLRAPIGKASELETVQRLVKQRRLHTICEEARCPNRGECYAQG-----TATFLIMGSICTRRCAFCQVDKGR- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164  152 PPPLDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTVSYLKERNPKILVECLTPDFRGDLK-AIEKVALSG 230
Cdd:PRK12928  84 PMPLDPDEPERVAEAVAALGLRYVVLTSVARDDLPDGGAAHFVATIAAIRARNPGTGIEVLTPDFWGGQReRLATVLAAK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164  231 LDVYAHNVETVPELQSKVRdPRANFDQSLRVLKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCLTLGQYM 310
Cdd:PRK12928 164 PDVFNHNLETVPRLQKAVR-RGADYQRSLDLLARAKELAPDIPTKSGLMLGLGETEDEVIETLRDLRAVGCDRLTIGQYL 242

                 ....*....
gi 37577164  311 QPTRRHLKV 319
Cdd:PRK12928 243 RPSLAHLPV 251
LIAS_N pfam16881
N-terminal domain of lipoyl synthase of Radical_SAM family; LIAS_N is found as the N-terminal ...
15-111 2.22e-66

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: 203.13  E-value: 2.22e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164    15 RVFGRYFCSPVRPLSSLPDKKKELLQNGPDLQDFVSGDLADRSTWDEYKGNLKRQKGERLRLPPWLKTEIPMGKNYNKLK 94
Cdd:pfam16881   1 RVFGSHLCSPASTSSSLPDEKREFLQNGPDLQDFVSGDLSDKSTWAEYKGNLKRPKGERLRLPPWLKTKIPLGKNYNKIK 80
                          90
                  ....*....|....*..
gi 37577164    95 NTLRNLNLHTVCEEARC 111
Cdd:pfam16881  81 NTLRNLNLHTVCEEARC 97
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
133-292 3.13e-23

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: 93.74  E-value: 3.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164   133 MGDTCTRGCRFCSVKTARNPPP---LDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTvsyLKERNPKILV 209
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKgreLSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLL---KLELAEGIRI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164   210 ECLTPDFRGDLKAIEKVALSGLDVYAHNVETVPELQSKVRDPRANFDQSLRVLKHAKKVQPDViSKTSIMLGLGENDEQV 289
Cdd:pfam04055  78 TLETNGTLLDEELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIPV-VTDNIVGLPGETDEDL 156

                  ...
gi 37577164   290 YAT 292
Cdd:pfam04055 157 EET 159
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
127-310 4.24e-19

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: 83.99  E-value: 4.24e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164    127 TATIMLMGDTCTRGCRFCSVKTARN---PPPLDASEpyNTAKAIAEWGLDYVVLTSV-----DRDDMPDGGAEHIAKTVS 198
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSFPSLRGklrSRYLEALV--REIELLAEKGEKEGLVGTVfigggTPTLLSPEQLEELLEAIR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164    199 YLKERNPKILVECLTPDFRGDLKAIEKVALSGLDVYAHNVETVPELQSKVRDPRANFDQSLRVLKHAKKVQPDVISkTSI 278
Cdd:smart00729  79 EILGLAKDVEITIETRPDTLTEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAGPIKVS-TDL 157
                          170       180       190
                   ....*....|....*....|....*....|...
gi 37577164    279 MLGL-GENDEQVYATMKALREADVDCLTLGQYM 310
Cdd:smart00729 158 IVGLpGETEEDFEETLKLLKELGPDRVSIFPLS 190
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
134-310 1.69e-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: 1.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164 134 GDTCTRGCRFCSV---KTARNPPPLDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPdggaeHIAKTVSYLKERNPKILVE 210
Cdd:cd01335   4 TRGCNLNCGFCSNpasKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYP-----ELAELLRRLKKELPGFEIS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164 211 CLTPDFRGDLKAIEKVALSGLDVYAHNVETV-PELQSKVRDPRANFDQSLRVLKHAKKVqpDVISKTSIMLGLGENDEQV 289
Cdd:cd01335  79 IETNGTLLTEELLKELKELGLDGVGVSLDSGdEEVADKIRGSGESFKERLEALKELREA--GLGLSTTLLVGLGDEDEED 156
                       170       180
                ....*....|....*....|...
gi 37577164 290 YA-TMKALREAD-VDCLTLGQYM 310
Cdd:cd01335 157 DLeELELLAEFRsPDRVSLFRLL 179
BioB COG0502
Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or ...
137-302 6.10e-08

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: 53.13  E-value: 6.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164 137 CTRGCRFCSvKTARNPPP------LDASEPYNTAKAIAEWGLDYVVL----TSVDRDDMpdggaEHIAKTVSYLKERNPk 206
Cdd:COG0502  50 CPEDCKYCG-QSAHNKTGieryrlLSVEEILEAARAAKEAGARRFCLvasgRDPSDRDF-----EKVLEIVRAIKEELG- 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164 207 ilVE-CLTPDFRGDLKAiEKVALSGLDVYAHNVETVPELQSKVRDPRaNFDQSLRVLKHAKKVQPDVISktSIMLGLGEN 285
Cdd:COG0502 123 --LEvCASLGELSEEQA-KRLKEAGVDRYNHNLETSPELYPKICTTH-TYEDRLDTLKNAREAGLEVCS--GGIVGMGET 196
                       170
                ....*....|....*..
gi 37577164 286 DEQVYATMKALREADVD 302
Cdd:COG0502 197 LEDRADLLLTLAELDPD 213
YgiQ COG1032
Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];
137-310 1.22e-07

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


Pssm-ID: 440655 [Multi-domain]  Cd Length: 394  Bit Score: 52.64  E-value: 1.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164 137 CTRGCRFCSV-----KTARNPPP---LDASEpyntaKAIAEWGLDYVVLTsvdrDDMPDGGAEHIAKTVSYLKERNPKIL 208
Cdd:COG1032 184 CPFGCSFCSIsalygRKVRYRSPesvVEEIE-----ELVKRYGIREIFFV----DDNFNVDKKRLKELLEELIERGLNVS 254
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164 209 ------VECLTPDFrgdLKAIEKVALSGLDVyahNVETV-PELQSKVRDpRANFDQSLRVLKHAKKVQPDVisKTSIMLG 281
Cdd:COG1032 255 fpsevrVDLLDEEL---LELLKKAGCRGLFI---GIESGsQRVLKAMNK-GITVEDILEAVRLLKKAGIRV--KLYFIIG 325
                       170       180       190
                ....*....|....*....|....*....|
gi 37577164 282 L-GENDEQVYATMKALREADVDCLTLGQYM 310
Cdd:COG1032 326 LpGETEEDIEETIEFIKELGPDQAQVSIFT 355
COG2516 COG2516
Biotin synthase-related protein, radical SAM superfamily [General function prediction only];
132-298 1.97e-05

Biotin synthase-related protein, radical SAM superfamily [General function prediction only];


Pssm-ID: 442006 [Multi-domain]  Cd Length: 322  Bit Score: 45.73  E-value: 1.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164 132 LMGDTCTRGCRFCS--------------VKTarnpPPLDASEPYNTAKAIAE-WGLDYVVLTSVDrddmPDGGAEHIAKT 196
Cdd:COG2516  53 TVLQGCIRNCQFCGiarslaagrdrtirVKW----PTYDLEQLAEVAKAAVElDGVKRMCMTTGT----PPGSDRGAAES 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164 197 VSYLKER-NPKILVECLTPDFRGDLKAIEKVALSGLDVyaHnVETV-PELQSKVRD--PRANFDQSLRVLKHAKKV-QPD 271
Cdd:COG2516 125 ARAIKAAvDLPISVQCEPPDDDAWLERLKDAGADRLGI--H-LDAAtPEVFERIRGgkARVSWERYWEAIEEAVEVfGPG 201
                       170       180
                ....*....|....*....|....*..
gi 37577164 272 VISkTSIMLGLGENDEQVYATMKALRE 298
Cdd:COG2516 202 QVS-THLIVGLGETEEEIVELCQRLID 227
ThiH COG1060
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme ...
137-298 1.59e-04

2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme transport and metabolism]; 2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440680 [Multi-domain]  Cd Length: 351  Bit Score: 42.81  E-value: 1.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164 137 CTRGCRFCS-VKTARNPPP--LDASEPYNTAKAIAEWGLDYVVLTS-VDrddmPDGGAEHIAKTVSYLKERNPKILVECL 212
Cdd:COG1060  61 CVNGCKFCAfSRDNGDIDRytLSPEEILEEAEEAKALGATEILLVGgEH----PDLPLEYYLDLLRAIKERFPNIHIHAL 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164 213 TPDfrgDLKAIEKVA-LSGLDVYAHNVE----TVPE-----LQSKVRDPRA----NFDQSLRVLK--HAKKVqpdvisKT 276
Cdd:COG1060 137 SPE---EIAHLARASgLSVEEVLERLKEagldSLPGggaeiLDDEVRHPIGpgkiDYEEWLEVMEraHELGI------RT 207
                       170       180
                ....*....|....*....|....
gi 37577164 277 S--IMLGLGENDEQVYATMKALRE 298
Cdd:COG1060 208 TatMLYGHVETREERVDHLLHLRE 231
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
141-268 2.61e-04

Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, chromosome partitioning, Coenzyme transport and metabolism];


Pssm-ID: 440301 [Multi-domain]  Cd Length: 159  Bit Score: 40.66  E-value: 2.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577164 141 CRFCSVKTARNPPP-LDASEPYNTAKAIAEWGLDYVVLTsvdrddmpdGGA----EHIAKTVSYLKERNPKILVEC---- 211
Cdd:COG0535  14 CKHCYADAGPKRPGeLSTEEAKRILDELAELGVKVVGLT---------GGEpllrPDLFELVEYAKELGIRVNLSTngtl 84
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37577164 212 LTPDFRGDLKA--IEKVALS--GLDvyahnvetvPELQSKVRDPRANFDQSLRVLKHAKKV 268
Cdd:COG0535  85 LTEELAERLAEagLDHVTISldGVD---------PETHDKIRGVPGAFDKVLEAIKLLKEA 136
 
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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