NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|13277380|ref|NP_077791|]
View 

lipoyl synthase, mitochondrial isoform 1 precursor [Mus musculus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLN02428 PLN02428
lipoic acid synthase
41-373 0e+00

lipoic acid synthase


:

Pssm-ID: 215236 [Multi-domain]  Cd Length: 349  Bit Score: 589.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380   41 GPDLQDFVSGDladksTWDEYKGNLKRQkgerLRLPPWLKTKIPMGKNYNKLKNTLRNLSLHTVCEEARCPNIGECWGGG 120
Cdd:PLN02428  26 SPSLGDFVSLG-----PYTLGSYGRDKP----LPKPKWLRQRAPGGEKYTEIKEKLRELKLNTVCEEAQCPNIGECWNGG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380  121 EYATATATIMLMGDTCTRGCRFCSVKTARNPPPLDANEPDNTAKAIAEWGLDYVVLTSVDRDDVADGGAEHIAKTVSCLK 200
Cdd:PLN02428  97 GTGTATATIMILGDTCTRGCRFCAVKTSRTPPPPDPDEPENVAEAIASWGVDYVVLTSVDRDDLPDGGSGHFAETVRRLK 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380  201 ERNPKILVECLTPDFRGDLRAVEKVALSGLDVYAHNVETVPELQRKVRDPRANFDQSLRVLRHAKEVQPDVVSKTSIMLG 280
Cdd:PLN02428 177 QLKPEILVEALVPDFRGDLGAVETVATSGLDVFAHNIETVERLQRIVRDPRAGYKQSLDVLKHAKESKPGLLTKTSIMLG 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380  281 LGETDEQVYATLKALRAADVDCLTLGQYMQPTKRHLKVEEYVTPEKFKYWEKVGNELGFLYTASGPLVRSSYKAGEFFLK 360
Cdd:PLN02428 257 LGETDEEVVQTMEDLRAAGVDVVTFGQYLRPTKRHLPVKEYVTPEKFEFWREYGEEMGFRYVASGPLVRSSYKAGEFFIK 336
                        330
                 ....*....|...
gi 13277380  361 NLVARRKTKASKV 373
Cdd:PLN02428 337 SMIREDRAKAAAA 349
 
Name Accession Description Interval E-value
PLN02428 PLN02428
lipoic acid synthase
41-373 0e+00

lipoic acid synthase


Pssm-ID: 215236 [Multi-domain]  Cd Length: 349  Bit Score: 589.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380   41 GPDLQDFVSGDladksTWDEYKGNLKRQkgerLRLPPWLKTKIPMGKNYNKLKNTLRNLSLHTVCEEARCPNIGECWGGG 120
Cdd:PLN02428  26 SPSLGDFVSLG-----PYTLGSYGRDKP----LPKPKWLRQRAPGGEKYTEIKEKLRELKLNTVCEEAQCPNIGECWNGG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380  121 EYATATATIMLMGDTCTRGCRFCSVKTARNPPPLDANEPDNTAKAIAEWGLDYVVLTSVDRDDVADGGAEHIAKTVSCLK 200
Cdd:PLN02428  97 GTGTATATIMILGDTCTRGCRFCAVKTSRTPPPPDPDEPENVAEAIASWGVDYVVLTSVDRDDLPDGGSGHFAETVRRLK 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380  201 ERNPKILVECLTPDFRGDLRAVEKVALSGLDVYAHNVETVPELQRKVRDPRANFDQSLRVLRHAKEVQPDVVSKTSIMLG 280
Cdd:PLN02428 177 QLKPEILVEALVPDFRGDLGAVETVATSGLDVFAHNIETVERLQRIVRDPRAGYKQSLDVLKHAKESKPGLLTKTSIMLG 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380  281 LGETDEQVYATLKALRAADVDCLTLGQYMQPTKRHLKVEEYVTPEKFKYWEKVGNELGFLYTASGPLVRSSYKAGEFFLK 360
Cdd:PLN02428 257 LGETDEEVVQTMEDLRAAGVDVVTFGQYLRPTKRHLPVKEYVTPEKFEFWREYGEEMGFRYVASGPLVRSSYKAGEFFIK 336
                        330
                 ....*....|...
gi 13277380  361 NLVARRKTKASKV 373
Cdd:PLN02428 337 SMIREDRAKAAAA 349
LipA COG0320
Lipoate synthase [Coenzyme transport and metabolism]; Lipoate synthase is part of the Pathway ...
66-366 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: 505.41  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380  66 KRQKGERLRLPPWLKTKIPMGKNYNKLKNTLRNLSLHTVCEEARCPNIGECWGGGeyataTATIMLMGDTCTRGCRFCSV 145
Cdd:COG0320  13 RNPETPILRKPDWLRVKLPTGPEYAEVKKLLREHKLHTVCEEARCPNIGECWSRG-----TATFMILGDICTRRCRFCDV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380 146 KTARnPPPLDANEPDNTAKAIAEWGLDYVVLTSVDRDDVADGGAEHIAKTVSCLKERNPKILVECLTPDFRGDLRAVEKV 225
Cdd:COG0320  88 ATGR-PLPLDPDEPERVAEAVAEMGLKYVVITSVDRDDLPDGGAGHFAETIRAIRELNPGTTIEVLIPDFRGREEALDIV 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380 226 ALSGLDVYAHNVETVPELQRKVRdPRANFDQSLRVLRHAKEVQPDVVSKTSIMLGLGETDEQVYATLKALRAADVDCLTL 305
Cdd:COG0320 167 VDARPDVFNHNLETVPRLYKRVR-PGADYERSLELLKRAKELDPGIPTKSGLMLGLGETDEEVLEVMRDLRAAGVDILTI 245
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13277380 306 GQYMQPTKRHLKVEEYVTPEKFKYWEKVGNELGFLYTASGPLVRSSYKAGEFFLKNLVARR 366
Cdd:COG0320 246 GQYLQPSKKHLPVDRYVTPEEFEELKEIALELGFLHVASGPLVRSSYHADEQAAKARAARG 306
lipA TIGR00510
lipoate synthase; This enzyme is an iron-sulfur protein. It is localized to mitochondria in ...
64-366 8.40e-146

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: 414.62  E-value: 8.40e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380    64 NLKRQKGERLRLPPWLKTKIPMGKNYNKLKNTLRNLSLHTVCEEARCPNIGECWGGGeyataTATIMLMGDTCTRGCRFC 143
Cdd:TIGR00510   6 NPIPNKEILLRKPEWLKIKLPLGTVIAQIKNTMKNKGLHTVCEEASCPNLTECWNHG-----TATFMILGDICTRRCPFC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380   144 SVKTARNPPPLDANEPDNTAKAIAEWGLDYVVLTSVDRDDVADGGAEHIAKTVSCLKERNPKILVECLTPDFRGDLRAVE 223
Cdd:TIGR00510  81 DVAHGRNPLPPDPEEPAKLAETIKDMGLKYVVITSVDRDDLEDGGASHLAECIEAIREKLPNIKIETLVPDFRGNIAALD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380   224 KVALSGLDVYAHNVETVPELQRKVRdPRANFDQSLRVLRHAKEVQPDVVSKTSIMLGLGETDEQVYATLKALRAADVDCL 303
Cdd:TIGR00510 161 ILLDAPPDVYNHNLETVERLTPFVR-PGATYRWSLKLLERAKEYLPNLPTKSGIMVGLGETNEEIKQTLKDLRDHGVTMV 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13277380   304 TLGQYMQPTKRHLKVEEYVTPEKFKYWEKVGNELGFLYTASGPLVRSSYKAGEFFLKNLVARR 366
Cdd:TIGR00510 240 TLGQYLRPSRRHLPVKRYVSPEEFDYYRSVALEMGFLHAACGPFVRSSYHADSLFAAGRLVKT 302
LIAS_N pfam16881
N-terminal domain of lipoyl synthase of Radical_SAM family; LIAS_N is found as the N-terminal ...
15-110 1.47e-59

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: 187.72  E-value: 1.47e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380    15 RIFGRYAFT-VRALSSLPDKKKEFLHNGPDLQDFVSGDLADKSTWDEYKGNLKRQKGERLRLPPWLKTKIPMGKNYNKLK 93
Cdd:pfam16881   1 RVFGSHLCSpASTSSSLPDEKREFLQNGPDLQDFVSGDLSDKSTWAEYKGNLKRPKGERLRLPPWLKTKIPLGKNYNKIK 80
                          90
                  ....*....|....*..
gi 13277380    94 NTLRNLSLHTVCEEARC 110
Cdd:pfam16881  81 NTLRNLNLHTVCEEARC 97
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
126-331 4.04e-20

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: 87.84  E-value: 4.04e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380    126 TATIMLMGDTCTRGCRFCSVKTAR-NPPPLDANEPDNTAKAIAEWGLDYVVltsVDRDDVADG-----GAEHIAKTVSCL 199
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSFPSLRgKLRSRYLEALVREIELLAEKGEKEGL---VGTVFIGGGtptllSPEQLEELLEAI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380    200 KERNPK-----ILVECLTPDFRGDLraVEKVALSGLDVYAHNVETVPELQRKVRDPRANFDQSLRVLRHAKEVQPDVVSk 274
Cdd:smart00729  78 REILGLakdveITIETRPDTLTEEL--LEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAGPIKVS- 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380    275 TSIMLGL-GETDEQVYATLKALRAADVDCLTLGQYM-QP-TKRHLKVEEYVTPEKFKYWE 331
Cdd:smart00729 155 TDLIVGLpGETEEDFEETLKLLKELGPDRVSIFPLSpRPgTPLAKMYKRLKPPTKEERAE 214
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
133-329 7.61e-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: 7.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380 133 GDTCTRGCRFCSV---KTARNPPPLDANEPDNTAKAIAEWGLDYVVLTsvdrddvadGGA----EHIAKTVSCLKERNPK 205
Cdd:cd01335   4 TRGCNLNCGFCSNpasKGRGPESPPEIEEILDIVLEAKERGVEVVILT---------GGEpllyPELAELLRRLKKELPG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380 206 ILVECLTPDFRGDLRAVEKVALSGLDVYAHNVETV-PELQRKVRDPRANFDQSLRVLRHAKEVqpDVVSKTSIMLGLGET 284
Cdd:cd01335  75 FEISIETNGTLLTEELLKELKELGLDGVGVSLDSGdEEVADKIRGSGESFKERLEALKELREA--GLGLSTTLLVGLGDE 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 13277380 285 DEQVYA-TLKALRAAD-VDCLTLGQYMqPTKRHLKVEEYVTPEKFKY 329
Cdd:cd01335 153 DEEDDLeELELLAEFRsPDRVSLFRLL-PEEGTPLELAAPVVPAEKL 198
 
Name Accession Description Interval E-value
PLN02428 PLN02428
lipoic acid synthase
41-373 0e+00

lipoic acid synthase


Pssm-ID: 215236 [Multi-domain]  Cd Length: 349  Bit Score: 589.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380   41 GPDLQDFVSGDladksTWDEYKGNLKRQkgerLRLPPWLKTKIPMGKNYNKLKNTLRNLSLHTVCEEARCPNIGECWGGG 120
Cdd:PLN02428  26 SPSLGDFVSLG-----PYTLGSYGRDKP----LPKPKWLRQRAPGGEKYTEIKEKLRELKLNTVCEEAQCPNIGECWNGG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380  121 EYATATATIMLMGDTCTRGCRFCSVKTARNPPPLDANEPDNTAKAIAEWGLDYVVLTSVDRDDVADGGAEHIAKTVSCLK 200
Cdd:PLN02428  97 GTGTATATIMILGDTCTRGCRFCAVKTSRTPPPPDPDEPENVAEAIASWGVDYVVLTSVDRDDLPDGGSGHFAETVRRLK 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380  201 ERNPKILVECLTPDFRGDLRAVEKVALSGLDVYAHNVETVPELQRKVRDPRANFDQSLRVLRHAKEVQPDVVSKTSIMLG 280
Cdd:PLN02428 177 QLKPEILVEALVPDFRGDLGAVETVATSGLDVFAHNIETVERLQRIVRDPRAGYKQSLDVLKHAKESKPGLLTKTSIMLG 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380  281 LGETDEQVYATLKALRAADVDCLTLGQYMQPTKRHLKVEEYVTPEKFKYWEKVGNELGFLYTASGPLVRSSYKAGEFFLK 360
Cdd:PLN02428 257 LGETDEEVVQTMEDLRAAGVDVVTFGQYLRPTKRHLPVKEYVTPEKFEFWREYGEEMGFRYVASGPLVRSSYKAGEFFIK 336
                        330
                 ....*....|...
gi 13277380  361 NLVARRKTKASKV 373
Cdd:PLN02428 337 SMIREDRAKAAAA 349
LipA COG0320
Lipoate synthase [Coenzyme transport and metabolism]; Lipoate synthase is part of the Pathway ...
66-366 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: 505.41  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380  66 KRQKGERLRLPPWLKTKIPMGKNYNKLKNTLRNLSLHTVCEEARCPNIGECWGGGeyataTATIMLMGDTCTRGCRFCSV 145
Cdd:COG0320  13 RNPETPILRKPDWLRVKLPTGPEYAEVKKLLREHKLHTVCEEARCPNIGECWSRG-----TATFMILGDICTRRCRFCDV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380 146 KTARnPPPLDANEPDNTAKAIAEWGLDYVVLTSVDRDDVADGGAEHIAKTVSCLKERNPKILVECLTPDFRGDLRAVEKV 225
Cdd:COG0320  88 ATGR-PLPLDPDEPERVAEAVAEMGLKYVVITSVDRDDLPDGGAGHFAETIRAIRELNPGTTIEVLIPDFRGREEALDIV 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380 226 ALSGLDVYAHNVETVPELQRKVRdPRANFDQSLRVLRHAKEVQPDVVSKTSIMLGLGETDEQVYATLKALRAADVDCLTL 305
Cdd:COG0320 167 VDARPDVFNHNLETVPRLYKRVR-PGADYERSLELLKRAKELDPGIPTKSGLMLGLGETDEEVLEVMRDLRAAGVDILTI 245
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13277380 306 GQYMQPTKRHLKVEEYVTPEKFKYWEKVGNELGFLYTASGPLVRSSYKAGEFFLKNLVARR 366
Cdd:COG0320 246 GQYLQPSKKHLPVDRYVTPEEFEELKEIALELGFLHVASGPLVRSSYHADEQAAKARAARG 306
PRK05481 PRK05481
lipoyl synthase; Provisional
74-364 8.29e-177

lipoyl synthase; Provisional


Pssm-ID: 235493 [Multi-domain]  Cd Length: 289  Bit Score: 492.68  E-value: 8.29e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380   74 RLPPWLKTKIPMGKNYNKLKNTLRNLSLHTVCEEARCPNIGECWGGGeyataTATIMLMGDTCTRGCRFCSVKTARnPPP 153
Cdd:PRK05481   6 RKPDWLRVKLPTGEEYTEIKKLLRELGLHTVCEEASCPNIGECWSRG-----TATFMILGDICTRRCPFCDVATGR-PLP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380  154 LDANEPDNTAKAIAEWGLDYVVLTSVDRDDVADGGAEHIAKTVSCLKERNPKILVECLTPDFRGDLRAVEKVALSGLDVY 233
Cdd:PRK05481  80 LDPDEPERVAEAVARMGLKYVVITSVDRDDLPDGGAQHFAETIRAIRELNPGTTIEVLIPDFRGRMDALLTVLDARPDVF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380  234 AHNVETVPELQRKVRdPRANFDQSLRVLRHAKEVQPDVVSKTSIMLGLGETDEQVYATLKALRAADVDCLTLGQYMQPTK 313
Cdd:PRK05481 160 NHNLETVPRLYKRVR-PGADYERSLELLKRAKELHPGIPTKSGLMVGLGETDEEVLEVMDDLRAAGVDILTIGQYLQPSR 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 13277380  314 RHLKVEEYVTPEKFKYWEKVGNELGFLYTASGPLVRSSYKAGEFFLKNLVA 364
Cdd:PRK05481 239 KHLPVERYVTPEEFDEYKEIALELGFLHVASGPLVRSSYHADEQAAGAEVA 289
PTZ00413 PTZ00413
lipoate synthase; Provisional
69-372 5.35e-172

lipoate synthase; Provisional


Pssm-ID: 240408 [Multi-domain]  Cd Length: 398  Bit Score: 484.72  E-value: 5.35e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380   69 KGERLRLPPWLKTKIPMGKN----YNKLKNTLRNLSLHTVCEEARCPNIGECWGGG-EYATATATIMLMGDTCTRGCRFC 143
Cdd:PTZ00413  87 KRGEEPLPPWFKVKVPKGASrrprFNRIRRSMREKKLHTVCEEAKCPNIGECWGGGdEEGTATATIMVMGDHCTRGCRFC 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380  144 SVKTARNPPPLDANEPDNTAKAIAEWGLDYVVLTSVDRDDVADGGAEHIAKTVSCLKERNPKILVECLTPDFRGDLRAVE 223
Cdd:PTZ00413 167 SVKTSRKPPPLDPNEPEKVAKAVAEMGVDYIVMTMVDRDDLPDGGASHVARCVELIKESNPELLLEALVGDFHGDLKSVE 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380  224 KVALSGLDVYAHNVETVPELQRKVRDPRANFDQSLRVLRHAKEV-QPDVVSKTSIMLGLGETDEQVYATLKALRAADVDC 302
Cdd:PTZ00413 247 KLANSPLSVYAHNIECVERITPYVRDRRASYRQSLKVLEHVKEFtNGAMLTKSSIMLGLGETEEEVRQTLRDLRTAGVSA 326
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380  303 LTLGQYMQPTKRHLKVEEYVTPEKFKYWEKVGNELGFLYTASGPLVRSSYKAGEFFLKNLVARRKTKASK 372
Cdd:PTZ00413 327 VTLGQYLQPTKTRLKVSRYAHPKEFEMWEEEAMKMGFLYCASGPLVRSSYRAGEYYIKNLVKQRRKAKTH 396
lipA TIGR00510
lipoate synthase; This enzyme is an iron-sulfur protein. It is localized to mitochondria in ...
64-366 8.40e-146

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: 414.62  E-value: 8.40e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380    64 NLKRQKGERLRLPPWLKTKIPMGKNYNKLKNTLRNLSLHTVCEEARCPNIGECWGGGeyataTATIMLMGDTCTRGCRFC 143
Cdd:TIGR00510   6 NPIPNKEILLRKPEWLKIKLPLGTVIAQIKNTMKNKGLHTVCEEASCPNLTECWNHG-----TATFMILGDICTRRCPFC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380   144 SVKTARNPPPLDANEPDNTAKAIAEWGLDYVVLTSVDRDDVADGGAEHIAKTVSCLKERNPKILVECLTPDFRGDLRAVE 223
Cdd:TIGR00510  81 DVAHGRNPLPPDPEEPAKLAETIKDMGLKYVVITSVDRDDLEDGGASHLAECIEAIREKLPNIKIETLVPDFRGNIAALD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380   224 KVALSGLDVYAHNVETVPELQRKVRdPRANFDQSLRVLRHAKEVQPDVVSKTSIMLGLGETDEQVYATLKALRAADVDCL 303
Cdd:TIGR00510 161 ILLDAPPDVYNHNLETVERLTPFVR-PGATYRWSLKLLERAKEYLPNLPTKSGIMVGLGETNEEIKQTLKDLRDHGVTMV 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13277380   304 TLGQYMQPTKRHLKVEEYVTPEKFKYWEKVGNELGFLYTASGPLVRSSYKAGEFFLKNLVARR 366
Cdd:TIGR00510 240 TLGQYLRPSRRHLPVKRYVSPEEFDYYRSVALEMGFLHAACGPFVRSSYHADSLFAAGRLVKT 302
PRK12928 PRK12928
lipoyl synthase; Provisional
71-356 6.03e-142

lipoyl synthase; Provisional


Pssm-ID: 237261  Cd Length: 290  Bit Score: 404.31  E-value: 6.03e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380   71 ERLRLPPWLKTKIPMGKNYNKLKNTLRNLSLHTVCEEARCPNIGECWGGGeyataTATIMLMGDTCTRGCRFCSVKTARn 150
Cdd:PRK12928  10 PVERLPEWLRAPIGKASELETVQRLVKQRRLHTICEEARCPNRGECYAQG-----TATFLIMGSICTRRCAFCQVDKGR- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380  151 PPPLDANEPDNTAKAIAEWGLDYVVLTSVDRDDVADGGAEHIAKTVSCLKERNPKILVECLTPDFRG-DLRAVEKVALSG 229
Cdd:PRK12928  84 PMPLDPDEPERVAEAVAALGLRYVVLTSVARDDLPDGGAAHFVATIAAIRARNPGTGIEVLTPDFWGgQRERLATVLAAK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380  230 LDVYAHNVETVPELQRKVRdPRANFDQSLRVLRHAKEVQPDVVSKTSIMLGLGETDEQVYATLKALRAADVDCLTLGQYM 309
Cdd:PRK12928 164 PDVFNHNLETVPRLQKAVR-RGADYQRSLDLLARAKELAPDIPTKSGLMLGLGETEDEVIETLRDLRAVGCDRLTIGQYL 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 13277380  310 QPTKRHLKVEEYVTPEKFKYWEKVGNELGFLYTASGPLVRSSYKAGE 356
Cdd:PRK12928 243 RPSLAHLPVQRYWTPEEFEALGQIARELGFSHVRSGPLVRSSYHAGE 289
LIAS_N pfam16881
N-terminal domain of lipoyl synthase of Radical_SAM family; LIAS_N is found as the N-terminal ...
15-110 1.47e-59

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: 187.72  E-value: 1.47e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380    15 RIFGRYAFT-VRALSSLPDKKKEFLHNGPDLQDFVSGDLADKSTWDEYKGNLKRQKGERLRLPPWLKTKIPMGKNYNKLK 93
Cdd:pfam16881   1 RVFGSHLCSpASTSSSLPDEKREFLQNGPDLQDFVSGDLSDKSTWAEYKGNLKRPKGERLRLPPWLKTKIPLGKNYNKIK 80
                          90
                  ....*....|....*..
gi 13277380    94 NTLRNLSLHTVCEEARC 110
Cdd:pfam16881  81 NTLRNLNLHTVCEEARC 97
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
132-291 1.58e-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: 95.29  E-value: 1.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380   132 MGDTCTRGCRFCSVKTARNPPP---LDANEPDNTAKAIAEWGLDYVVLTSVDRDDVADGGAEHIAKtvsCLKERNPKILV 208
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKgreLSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERL---LKLELAEGIRI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380   209 ECLTPDFRGDLRAVEKVALSGLDVYAHNVETVPELQRKVRDPRANFDQSLRVLRHAKEVQPDVVsKTSIMLGLGETDEQV 288
Cdd:pfam04055  78 TLETNGTLLDEELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIPVV-TDNIVGLPGETDEDL 156

                  ...
gi 13277380   289 YAT 291
Cdd:pfam04055 157 EET 159
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
126-331 4.04e-20

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: 87.84  E-value: 4.04e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380    126 TATIMLMGDTCTRGCRFCSVKTAR-NPPPLDANEPDNTAKAIAEWGLDYVVltsVDRDDVADG-----GAEHIAKTVSCL 199
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSFPSLRgKLRSRYLEALVREIELLAEKGEKEGL---VGTVFIGGGtptllSPEQLEELLEAI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380    200 KERNPK-----ILVECLTPDFRGDLraVEKVALSGLDVYAHNVETVPELQRKVRDPRANFDQSLRVLRHAKEVQPDVVSk 274
Cdd:smart00729  78 REILGLakdveITIETRPDTLTEEL--LEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAGPIKVS- 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380    275 TSIMLGL-GETDEQVYATLKALRAADVDCLTLGQYM-QP-TKRHLKVEEYVTPEKFKYWE 331
Cdd:smart00729 155 TDLIVGLpGETEEDFEETLKLLKELGPDRVSIFPLSpRPgTPLAKMYKRLKPPTKEERAE 214
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
133-329 7.61e-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: 7.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380 133 GDTCTRGCRFCSV---KTARNPPPLDANEPDNTAKAIAEWGLDYVVLTsvdrddvadGGA----EHIAKTVSCLKERNPK 205
Cdd:cd01335   4 TRGCNLNCGFCSNpasKGRGPESPPEIEEILDIVLEAKERGVEVVILT---------GGEpllyPELAELLRRLKKELPG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380 206 ILVECLTPDFRGDLRAVEKVALSGLDVYAHNVETV-PELQRKVRDPRANFDQSLRVLRHAKEVqpDVVSKTSIMLGLGET 284
Cdd:cd01335  75 FEISIETNGTLLTEELLKELKELGLDGVGVSLDSGdEEVADKIRGSGESFKERLEALKELREA--GLGLSTTLLVGLGDE 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 13277380 285 DEQVYA-TLKALRAAD-VDCLTLGQYMqPTKRHLKVEEYVTPEKFKY 329
Cdd:cd01335 153 DEEDDLeELELLAEFRsPDRVSLFRLL-PEEGTPLELAAPVVPAEKL 198
BioB COG0502
Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or ...
136-301 5.18e-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: 53.90  E-value: 5.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380 136 CTRGCRFCSvKTARNPPPLDA---NEPD---NTAKAIAEWGLD-YVVLTSV----DRDDvadggaEHIAKTVSCLKERNP 204
Cdd:COG0502  50 CPEDCKYCG-QSAHNKTGIERyrlLSVEeilEAARAAKEAGARrFCLVASGrdpsDRDF------EKVLEIVRAIKEELG 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380 205 kilVE-CLTPDFRGDLRAvEKVALSGLDVYAHNVETVPELQRKVRDPRaNFDQSLRVLRHAKEVQPDVVSktSIMLGLGE 283
Cdd:COG0502 123 ---LEvCASLGELSEEQA-KRLKEAGVDRYNHNLETSPELYPKICTTH-TYEDRLDTLKNAREAGLEVCS--GGIVGMGE 195
                       170
                ....*....|....*...
gi 13277380 284 TDEQVYATLKALRAADVD 301
Cdd:COG0502 196 TLEDRADLLLTLAELDPD 213
YgiQ COG1032
Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];
136-309 1.24e-07

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


Pssm-ID: 440655 [Multi-domain]  Cd Length: 394  Bit Score: 53.03  E-value: 1.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380 136 CTRGCRFCSV-----KTARnpppldANEPDNTAKAI----AEWGLDYVVLTsvdrDDVADGGAEHIAKTVSCLKERNPKI 206
Cdd:COG1032 184 CPFGCSFCSIsalygRKVR------YRSPESVVEEIeelvKRYGIREIFFV----DDNFNVDKKRLKELLEELIERGLNV 253
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380 207 L------VECLTPDFrgdLRAVEKVALSGLDVyahNVETV-PELQRKVRDpRANFDQSLRVLRHAKEVQPDVvsKTSIML 279
Cdd:COG1032 254 SfpsevrVDLLDEEL---LELLKKAGCRGLFI---GIESGsQRVLKAMNK-GITVEDILEAVRLLKKAGIRV--KLYFII 324
                       170       180       190
                ....*....|....*....|....*....|.
gi 13277380 280 GL-GETDEQVYATLKALRAADVDCLTLGQYM 309
Cdd:COG1032 325 GLpGETEEDIEETIEFIKELGPDQAQVSIFT 355
COG2516 COG2516
Biotin synthase-related protein, radical SAM superfamily [General function prediction only];
131-297 1.23e-05

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


Pssm-ID: 442006 [Multi-domain]  Cd Length: 322  Bit Score: 46.50  E-value: 1.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380 131 LMGDTCTRGCRFCS--------------VKTarnpPPLDANEPDNTAKAIAE-WGLDYVVLTSVDRDDVADGGAEHIAKt 195
Cdd:COG2516  53 TVLQGCIRNCQFCGiarslaagrdrtirVKW----PTYDLEQLAEVAKAAVElDGVKRMCMTTGTPPGSDRGAAESARA- 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380 196 vscLKER-NPKILVECLTPDFRGDLRAVEKVALSGLDVyaHnVETV-PELQRKVRD--PRANFDQSLRVLRHAKEV-QPD 270
Cdd:COG2516 128 ---IKAAvDLPISVQCEPPDDDAWLERLKDAGADRLGI--H-LDAAtPEVFERIRGgkARVSWERYWEAIEEAVEVfGPG 201
                       170       180
                ....*....|....*....|....*..
gi 13277380 271 VVSkTSIMLGLGETDEQVYATLKALRA 297
Cdd:COG2516 202 QVS-THLIVGLGETEEEIVELCQRLID 227
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
140-267 2.16e-03

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: 38.35  E-value: 2.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380 140 CRFCSVKTARNPPP-LDANEPDNTAKAIAEWGLDYVVLTsvdrddvadGGA----EHIAKTVSCLKERNPKILVEC---- 210
Cdd:COG0535  14 CKHCYADAGPKRPGeLSTEEAKRILDELAELGVKVVGLT---------GGEpllrPDLFELVEYAKELGIRVNLSTngtl 84
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13277380 211 LTPDFRGDLRA--VEKVALS--GLDvyahnvetvPELQRKVRDPRANFDQSLRVLRHAKEV 267
Cdd:COG0535  85 LTEELAERLAEagLDHVTISldGVD---------PETHDKIRGVPGAFDKVLEAIKLLKEA 136
ThiH COG1060
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme ...
136-296 3.07e-03

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: 39.34  E-value: 3.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380 136 CTRGCRFCS-VKTARNPPP--LDANEPDNTAKAIAEWGLDYVVLTS-VDRDDvadgGAEHIAKTVSCLKERNPKILVECL 211
Cdd:COG1060  61 CVNGCKFCAfSRDNGDIDRytLSPEEILEEAEEAKALGATEILLVGgEHPDL----PLEYYLDLLRAIKERFPNIHIHAL 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277380 212 TPDfrgDLRAVEKVA-LSGLDVYAHNVE----TVPE-----LQRKVRDPRA----NFDQSLRVLRHAKEVQPDVvskTS- 276
Cdd:COG1060 137 SPE---EIAHLARASgLSVEEVLERLKEagldSLPGggaeiLDDEVRHPIGpgkiDYEEWLEVMERAHELGIRT---TAt 210
                       170       180
                ....*....|....*....|
gi 13277380 277 IMLGLGETDEQVYATLKALR 296
Cdd:COG1060 211 MLYGHVETREERVDHLLHLR 230
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH