|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14342 |
PRK14342 |
lipoyl(octanoyl) transferase LipB; |
1-211 |
7.76e-158 |
|
lipoyl(octanoyl) transferase LipB;
Pssm-ID: 237681 Cd Length: 213 Bit Score: 435.08 E-value: 7.76e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 1 MQNKLIVKKLGRQDYEPVWKAMHKFTDERTEEDVDQVWLVEHNPVFTQGQAGKAEHVLNAGDIPVIQSDRGGQVTYHGPG 80
Cdd:PRK14342 2 MQNKLIVRQLGLQPYEPVWQAMQEFTDTRDEETPDEIWLVEHPPVFTQGQAGKPEHILNPGDIPVVQSDRGGQVTYHGPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 81 QLVAYFLINIRRKKFGVRDLVTHIENLVINTLKAYNINSTARPDAPGVYVDGKKICSLGLRIRRGCSFHGLALNVDMDLS 160
Cdd:PRK14342 82 QLVMYVLLDLKRLKLGVRQLVTAIEQTVINTLAEYGIEAHAKPDAPGVYVDGKKIASLGLRIRRGCSFHGLALNVNMDLS 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515647337 161 PFLRINPCGYQGMEMAQVSQLGGPSELENVEQQLIQELVELLGYDQVDIQA 211
Cdd:PRK14342 162 PFLRINPCGYAGLEMTQLSDLGGPATVDEVAPRLLAELLALLGYNDQETIT 212
|
|
| LipB |
COG0321 |
Lipoate-protein ligase B [Coenzyme transport and metabolism]; Lipoate-protein ligase B is part ... |
3-210 |
4.97e-119 |
|
Lipoate-protein ligase B [Coenzyme transport and metabolism]; Lipoate-protein ligase B is part of the Pathway/BioSystem: Lipoate biosynthesis
Pssm-ID: 440090 Cd Length: 211 Bit Score: 336.69 E-value: 4.97e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 3 NKLIVKKLGRQDYEPVWKAMHKFTDERTEEDV-DQVWLVEHNPVFTQGQAGKAEHVLNAGDIPVIQSDRGGQVTYHGPGQ 81
Cdd:COG0321 2 RPLIIRDLGLVDYEEAWAAQRRLTAARVAGDTpDELWLLEHPPVYTLGRSGKPEHLLAPGGIPVVQTDRGGQITYHGPGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 82 LVAYFLINIRRKKFGVRDLVTHIENLVINTLKAYNINSTARPDAPGVYVDGKKICSLGLRIRRGCSFHGLALNVDMDLSP 161
Cdd:COG0321 82 LVGYPILDLRRRGLDVRAYVRRLEEAVIDTLAEYGIEAERRPGAPGVWVDGRKIAAIGLRVRRGVTYHGFALNVNPDLSP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515647337 162 FLRINPCGYQGMEMAQVSQ-LGGPSELENVEQQLIQELVELLGYDQVDIQ 210
Cdd:COG0321 162 FSRIVPCGIADLGVTSLSDeLGRPVTMEEVAEALIRHFAEVFGYELVELS 211
|
|
| LipB |
cd16444 |
lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein] ... |
6-202 |
1.57e-112 |
|
lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein]-protein acyltransferase the catalyzes the first step of lipoic acid synthesis. It transfers endogenous octanoic acid attached via a thioester bond to acyl carrier protein (ACP) onto lipoyl domains, which is later converted by lipoate synthase LipA into lipoylated derivatives.
Pssm-ID: 319743 Cd Length: 199 Bit Score: 319.82 E-value: 1.57e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 6 IVKKLGRQDYEPVWKAMHKFTDERTEEDV-DQVWLVEHNPVFTQGQAGKAEHVLNAGDIPVIQSDRGGQVTYHGPGQLVA 84
Cdd:cd16444 1 IVRDLGLIPYEEAWELQKRLVAERIAGETpDTLWLLEHPPVYTLGRRGKPENLLNNGGIPVVRTDRGGQVTYHGPGQLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 85 YFLINIRRKKFGVRDLVTHIENLVINTLKAYNINSTARPDAPGVYVDGKKICSLGLRIRRGCSFHGLALNVDMDLSPFLR 164
Cdd:cd16444 81 YPILDLRRRGLDVRRYVRALEEAVIRTLAEYGIEAGRRPGAPGVWVGDRKIASIGIRVRRGVTYHGLALNVNTDLSPFNR 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 515647337 165 INPCGYQGMEMAQVSQLGGPS-ELENVEQQLIQELVELL 202
Cdd:cd16444 161 INPCGIKGKGVTSLSDLGGREvDMEEVKQKLVEEFAKIF 199
|
|
| lipB |
TIGR00214 |
lipoate-protein ligase B; Involved in lipoate biosynthesis as the main determinant of the ... |
26-203 |
1.52e-83 |
|
lipoate-protein ligase B; Involved in lipoate biosynthesis as the main determinant of the lipoyl-protein ligase activity required for lipoylation of enzymes such as alpha-ketoacid dehydrogenases. Involved in activation and re-activation (following denaturation) of lipoyl-protein ligases (calcium ion-dependant process). [Protein fate, Protein modification and repair]
Pssm-ID: 272964 Cd Length: 184 Bit Score: 246.25 E-value: 1.52e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 26 TDERTEEDVDQVWLVEHNPVFTQGQAGKAEHVLNAGDIP---VIQSDRGGQVTYHGPGQLVAYFLINIRRKKFGVRDLVT 102
Cdd:TIGR00214 4 TKQRDRQTLDEIMLVEHYPVYTQGQAGKTEHLLFDPDIPpaeVVQSERGGQVTYHGPGQQVMYVILDLKRFQLDVRWLVT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 103 HIENLVINTLKAYNINSTARPDAPGVYVDGKKICSLGLRIRRGCSFHGLALNVDMDLSPFLRINPCGYQGMEMAQVSQLG 182
Cdd:TIGR00214 84 QLEQTVIITLAELGIEGEPIADATGVWVEGKKVASLGIRVRRGCTFHGLALNINMDLSPFSHINPCGYAGREMGSLNQFL 163
|
170 180
....*....|....*....|.
gi 515647337 183 GPSELENVEQQLIQELVELLG 203
Cdd:TIGR00214 164 PGATVENVAPLLIKAFAELLG 184
|
|
| BPL_LplA_LipB |
pfam03099 |
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ... |
58-158 |
3.36e-03 |
|
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, lipoate-protein ligase A and B. Biotin is covalently attached at the active site of certain enzymes that transfer carbon dioxide from bicarbonate to organic acids to form cellular metabolites. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Each organizm probably has only one BPL. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine. Lipoate-protein ligase A (LPLA) catalyzes the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes. The unusual biosynthesis pathway of lipoic acid is mechanistically intertwined with attachment of the cofactor.
Pssm-ID: 427135 Cd Length: 132 Bit Score: 36.65 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 58 LNAGDIPVIQSDRGGQ----VTYHGPGQLVAY-FLINIRRKKFGVRDLVTHIENLVINTLKAYNINSTARPDAP------ 126
Cdd:pfam03099 20 LESGGVVVVRRQTGGRgrggNVWHSPKGCLTYsLLLSKEHPNVDPSVLEFYVLELVLAVLEALGLYKPGISGIPcfvkwp 99
|
90 100 110
....*....|....*....|....*....|...
gi 515647337 127 -GVYVDGKKICSLGLRIRRGCSFHGLALNVDMD 158
Cdd:pfam03099 100 nDLYVNGRKLAGILQRSTRGGTLHHGVIGLGVN 132
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14342 |
PRK14342 |
lipoyl(octanoyl) transferase LipB; |
1-211 |
7.76e-158 |
|
lipoyl(octanoyl) transferase LipB;
Pssm-ID: 237681 Cd Length: 213 Bit Score: 435.08 E-value: 7.76e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 1 MQNKLIVKKLGRQDYEPVWKAMHKFTDERTEEDVDQVWLVEHNPVFTQGQAGKAEHVLNAGDIPVIQSDRGGQVTYHGPG 80
Cdd:PRK14342 2 MQNKLIVRQLGLQPYEPVWQAMQEFTDTRDEETPDEIWLVEHPPVFTQGQAGKPEHILNPGDIPVVQSDRGGQVTYHGPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 81 QLVAYFLINIRRKKFGVRDLVTHIENLVINTLKAYNINSTARPDAPGVYVDGKKICSLGLRIRRGCSFHGLALNVDMDLS 160
Cdd:PRK14342 82 QLVMYVLLDLKRLKLGVRQLVTAIEQTVINTLAEYGIEAHAKPDAPGVYVDGKKIASLGLRIRRGCSFHGLALNVNMDLS 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515647337 161 PFLRINPCGYQGMEMAQVSQLGGPSELENVEQQLIQELVELLGYDQVDIQA 211
Cdd:PRK14342 162 PFLRINPCGYAGLEMTQLSDLGGPATVDEVAPRLLAELLALLGYNDQETIT 212
|
|
| LipB |
COG0321 |
Lipoate-protein ligase B [Coenzyme transport and metabolism]; Lipoate-protein ligase B is part ... |
3-210 |
4.97e-119 |
|
Lipoate-protein ligase B [Coenzyme transport and metabolism]; Lipoate-protein ligase B is part of the Pathway/BioSystem: Lipoate biosynthesis
Pssm-ID: 440090 Cd Length: 211 Bit Score: 336.69 E-value: 4.97e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 3 NKLIVKKLGRQDYEPVWKAMHKFTDERTEEDV-DQVWLVEHNPVFTQGQAGKAEHVLNAGDIPVIQSDRGGQVTYHGPGQ 81
Cdd:COG0321 2 RPLIIRDLGLVDYEEAWAAQRRLTAARVAGDTpDELWLLEHPPVYTLGRSGKPEHLLAPGGIPVVQTDRGGQITYHGPGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 82 LVAYFLINIRRKKFGVRDLVTHIENLVINTLKAYNINSTARPDAPGVYVDGKKICSLGLRIRRGCSFHGLALNVDMDLSP 161
Cdd:COG0321 82 LVGYPILDLRRRGLDVRAYVRRLEEAVIDTLAEYGIEAERRPGAPGVWVDGRKIAAIGLRVRRGVTYHGFALNVNPDLSP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515647337 162 FLRINPCGYQGMEMAQVSQ-LGGPSELENVEQQLIQELVELLGYDQVDIQ 210
Cdd:COG0321 162 FSRIVPCGIADLGVTSLSDeLGRPVTMEEVAEALIRHFAEVFGYELVELS 211
|
|
| LipB |
cd16444 |
lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein] ... |
6-202 |
1.57e-112 |
|
lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein]-protein acyltransferase the catalyzes the first step of lipoic acid synthesis. It transfers endogenous octanoic acid attached via a thioester bond to acyl carrier protein (ACP) onto lipoyl domains, which is later converted by lipoate synthase LipA into lipoylated derivatives.
Pssm-ID: 319743 Cd Length: 199 Bit Score: 319.82 E-value: 1.57e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 6 IVKKLGRQDYEPVWKAMHKFTDERTEEDV-DQVWLVEHNPVFTQGQAGKAEHVLNAGDIPVIQSDRGGQVTYHGPGQLVA 84
Cdd:cd16444 1 IVRDLGLIPYEEAWELQKRLVAERIAGETpDTLWLLEHPPVYTLGRRGKPENLLNNGGIPVVRTDRGGQVTYHGPGQLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 85 YFLINIRRKKFGVRDLVTHIENLVINTLKAYNINSTARPDAPGVYVDGKKICSLGLRIRRGCSFHGLALNVDMDLSPFLR 164
Cdd:cd16444 81 YPILDLRRRGLDVRRYVRALEEAVIRTLAEYGIEAGRRPGAPGVWVGDRKIASIGIRVRRGVTYHGLALNVNTDLSPFNR 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 515647337 165 INPCGYQGMEMAQVSQLGGPS-ELENVEQQLIQELVELL 202
Cdd:cd16444 161 INPCGIKGKGVTSLSDLGGREvDMEEVKQKLVEEFAKIF 199
|
|
| PRK14343 |
PRK14343 |
lipoyl(octanoyl) transferase LipB; |
5-202 |
1.18e-99 |
|
lipoyl(octanoyl) transferase LipB;
Pssm-ID: 237682 Cd Length: 235 Bit Score: 289.00 E-value: 1.18e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 5 LIVKKLGRQDYEPVWKAMHKFTDERTEEDVDQVWLVEHNPVFTQGQAGKAEHVLNAGD-IPVIQSDRGGQVTYHGPGQLV 83
Cdd:PRK14343 15 VTVRWRGREPYEACFDAMRAFTDARTADTPDEIWLVEHPPVYTLGQAGDPAHLLVADSgIPLVKVDRGGQITYHGPGQVV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 84 AYFLINIRRKKFGVRDLVTHIENLVINTLKAYNINSTARPDAPGVYVD-----GKKICSLGLRIRRGCSFHGLALNVDMD 158
Cdd:PRK14343 95 AYLLLDLRRRKLMVRELVTRIEQAVIDTLAAYNLASERKAGAPGIYVAsgphqGAKIAALGLKIRNGCSYHGLSLNVKMD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515647337 159 LSPFLRINPCGYQGMEMAQVSQLGGPSELENVEQQLIQELVELL 202
Cdd:PRK14343 175 LRPFLAINPCGYAGLETVDMASLGVAADWADVAQTLARRLIANL 218
|
|
| lipB |
TIGR00214 |
lipoate-protein ligase B; Involved in lipoate biosynthesis as the main determinant of the ... |
26-203 |
1.52e-83 |
|
lipoate-protein ligase B; Involved in lipoate biosynthesis as the main determinant of the lipoyl-protein ligase activity required for lipoylation of enzymes such as alpha-ketoacid dehydrogenases. Involved in activation and re-activation (following denaturation) of lipoyl-protein ligases (calcium ion-dependant process). [Protein fate, Protein modification and repair]
Pssm-ID: 272964 Cd Length: 184 Bit Score: 246.25 E-value: 1.52e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 26 TDERTEEDVDQVWLVEHNPVFTQGQAGKAEHVLNAGDIP---VIQSDRGGQVTYHGPGQLVAYFLINIRRKKFGVRDLVT 102
Cdd:TIGR00214 4 TKQRDRQTLDEIMLVEHYPVYTQGQAGKTEHLLFDPDIPpaeVVQSERGGQVTYHGPGQQVMYVILDLKRFQLDVRWLVT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 103 HIENLVINTLKAYNINSTARPDAPGVYVDGKKICSLGLRIRRGCSFHGLALNVDMDLSPFLRINPCGYQGMEMAQVSQLG 182
Cdd:TIGR00214 84 QLEQTVIITLAELGIEGEPIADATGVWVEGKKVASLGIRVRRGCTFHGLALNINMDLSPFSHINPCGYAGREMGSLNQFL 163
|
170 180
....*....|....*....|.
gi 515647337 183 GPSELENVEQQLIQELVELLG 203
Cdd:TIGR00214 164 PGATVENVAPLLIKAFAELLG 184
|
|
| PRK14349 |
PRK14349 |
lipoyl(octanoyl) transferase LipB; |
7-203 |
7.31e-78 |
|
lipoyl(octanoyl) transferase LipB;
Pssm-ID: 172825 Cd Length: 220 Bit Score: 232.94 E-value: 7.31e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 7 VKKLGR-QDYEPVWKAMHKFTDERTEEDVDQVWLVEHNPVFTQGQAGKAEHVLNAGDIPVIQSDRGGQVTYHGPGQLVAY 85
Cdd:PRK14349 2 IKWLARpADYASVWDAMKAFTAARGPGTADEIWLCEHAPVYTLGQAGRPEHLLNPGLIPVVHCDRGGQVTYHGPGQVLAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 86 FLINIRRKKFGVRDLVTHIENLVINTLKAYNINSTAR-PDAPGVYVDG-----KKICSLGLRIRRGCSFHGLALNVDMDL 159
Cdd:PRK14349 82 TLFDLRRAGLYVREYVDMLEQATLATLRELGLEQACRkPGAPGIYVPQpggelAKIAALGVKVRNGYAYHGLALNIDMDL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515647337 160 SPFLRINPCGYQGMEMAQVSQLGGPSELENVEQQLIQELVELLG 203
Cdd:PRK14349 162 SPFLGINPCGYEGLRTVDLAACGVRTSVERAGELLAAQLARAHG 205
|
|
| PRK14346 |
PRK14346 |
lipoyl(octanoyl) transferase LipB; |
5-202 |
1.11e-77 |
|
lipoyl(octanoyl) transferase LipB;
Pssm-ID: 237684 Cd Length: 230 Bit Score: 232.72 E-value: 1.11e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 5 LIVKKLGRQDYEPVWKAMHKFTDERTEEDVDQVWLVEHNPVFTQGQAGKAEHVLNAGDIPVIQSDRGGQVTYHGPGQLVA 84
Cdd:PRK14346 3 MDRRMLGRVDYLATVQAMQAFTAERTPETPDELWICEHPPVYTQGLAGKADHVLNPGDIPVVATNRGGQVTYHGPGQVVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 85 YFLINIRRKKFGVRDLVTHIENLVINTLKAYNINSTARPDAPGVYV-------------------DGK---------KIC 136
Cdd:PRK14346 83 YPLIDLRRAGYFVKEYVYRIEEAVIRTLAHFGVTGHRVAGAPGIYVrlddpfshaalpqrpqkrgGGApqppfrglgKIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515647337 137 SLGLRIRRGCSFHGLALNVDMDLSPFLRINPCGYQGMEMAQVSQLGGPSELENVEQQLIQELVELL 202
Cdd:PRK14346 163 ALGIKVSRHCTYHGVALNVAMDLEPFSRINPCGYAGLQTVDLSTIGVQTTWDEAASVLGQQLARYL 228
|
|
| PRK14341 |
PRK14341 |
lipoyl(octanoyl) transferase LipB; |
36-203 |
2.09e-49 |
|
lipoyl(octanoyl) transferase LipB;
Pssm-ID: 237680 Cd Length: 213 Bit Score: 160.46 E-value: 2.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 36 QVWLVEHNPVFTQGQAGKAEHVLNAGDIPVIQSDRGGQVTYHGPGQLVAYFLINIRRKKFGVRDLVTHIENLVINTLKAY 115
Cdd:PRK14341 37 LVWLLEHPPLYTAGTSAKAEDLLDPDRFPVYETGRGGQYTYHGPGQRVAYVMLDLKRRRRDVRAFVAALEEWIIATLAAF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 116 NINSTARPDAPGVYVDG--------KKICSLGLRIRRGCSFHGLALNVDMDLSPFLRINPCGYQGMEMAQVSQLGGPSEL 187
Cdd:PRK14341 117 NIRGERREDRVGVWVRRpdkgsgaeDKIAAIGVRLRRWVSFHGISINVEPDLSHFSGIVPCGISEHGVTSLVDLGLPVTM 196
|
170
....*....|....*.
gi 515647337 188 ENVEQQLIQELVELLG 203
Cdd:PRK14341 197 DDVDAALKKAFEKVFG 212
|
|
| PRK14344 |
PRK14344 |
lipoyl(octanoyl) transferase LipB; |
14-180 |
1.29e-37 |
|
lipoyl(octanoyl) transferase LipB;
Pssm-ID: 237683 Cd Length: 223 Bit Score: 130.19 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 14 DYEPVWKAMHKFTDERTEE--DVDQVWLVEHNPVFTQGQAGKAEHVL---NAGDIPVIQSDRGGQVTYHGPGQLVAYFLI 88
Cdd:PRK14344 28 PFEDAWKWQKEWQQALIEDpsNPQAVWLLEHQLCYTLGRGASEDNLLfslNNPPADVFRIDRGGEVTHHMPGQLVTYLVL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 89 NIRRKKfgvRDL---VTHIENLVINTLKAYNINSTARPDAPGVYVDGKKICSLGLRIRRGCSFHGLALNVDMDLSPFLRI 165
Cdd:PRK14344 108 DLRRFN---KDLnwyLRQLEQVLIDVLADLGIDGERLDGLTGVWIGNKKVASIGIGCRRWITQHGFSLNVDCDLEGFNKI 184
|
170
....*....|....*
gi 515647337 166 NPCGYQGMEMAQVSQ 180
Cdd:PRK14344 185 VPCGLEGCQVGRLSD 199
|
|
| PRK14345 |
PRK14345 |
lipoyl(octanoyl) transferase LipB; |
7-205 |
5.91e-35 |
|
lipoyl(octanoyl) transferase LipB;
Pssm-ID: 184638 Cd Length: 234 Bit Score: 123.94 E-value: 5.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 7 VKKLGRQDYEPVWKAMHKFTDERTEEDV-DQVWLVEHNPVFTqgqAGK--AEHVLNAGDIPVIQSDRGGQVTYHGPGQLV 83
Cdd:PRK14345 14 VRRLGLVDYQEAWDLQRELADARVAGEGpDTLLLLEHPAVYT---AGKrtEPHERPTDGTPVVDVDRGGKITWHGPGQLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 84 AYFLINIrRKKFGVRDLVTHIENLVINTLKAYNINSTARPDAPGVYVDG------KKICSLGLRIRRGCSFHGLALNVDM 157
Cdd:PRK14345 91 GYPIIKL-AEPLDVVDYVRRLEEALIAVCADLGLNAGRVDGRSGVWVPAdggrpdRKIAAIGIRVSRGVTMHGFALNCDN 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515647337 158 DLSPFLRINPCGYQGMEMAQVS-QLGGPSELENVEQQLIQELVELLGYD 205
Cdd:PRK14345 170 DLAAFDAIVPCGISDAGVTTLSaELGRTVTVAEVVDPVAAALCDALDGR 218
|
|
| PRK14347 |
PRK14347 |
lipoyl(octanoyl) transferase LipB; |
14-202 |
3.34e-32 |
|
lipoyl(octanoyl) transferase LipB;
Pssm-ID: 172823 Cd Length: 209 Bit Score: 116.19 E-value: 3.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 14 DYEPVWKAMHKFTDER-TEEDVDQVWLVEHNPVFTQGQAGKAEHVLNAGDIPVIQSDRGGQVTYHGPGQLVAYFLINI-- 90
Cdd:PRK14347 12 DYQVTLKLMEDYVNKViSDHEPEIVYLVEHSEVYTAGTNYKQEELLNYGDIPVIYTGRGGKFTFHGPGQRVIYPILNLas 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 91 -RRKKfGVRDLVTHIENLVINTLKAYNINSTARPDAPGVYVDGK-----KICSLGLRIRRGCSFHGLALNVDMDLSPFLR 164
Cdd:PRK14347 92 pNRHK-DLKLYIKMLEEWIINSLNYFGIKAYIIKDKVGIWVKVRkdefaKIAAIGVRVRKWVTYHGVAINISTDLSKFSG 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 515647337 165 INPCGYQGMEMAQVSQLGGPSELENVEQQLIQELVELL 202
Cdd:PRK14347 171 IIPCGLENSLVTSLNQLGIHVEMSEFDKIIQTEFNKIF 208
|
|
| PRK14348 |
PRK14348 |
lipoyl(octanoyl) transferase LipB; |
35-202 |
7.52e-31 |
|
lipoyl(octanoyl) transferase LipB;
Pssm-ID: 172824 Cd Length: 221 Bit Score: 112.81 E-value: 7.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 35 DQVWLVEHNPVFTQGQAGKAEH-VLNAGDIPVIQS-----DRGGQVTYHGPGQLVAYFLINIRRKKFGVRDLVTHIENLV 108
Cdd:PRK14348 39 NRIIFCEHPHVYTLGRSGKENNmLLGEEQLKTIGAtlyhiDRGGDITYHGPGQLVCYPILNLEEFGLGLKEYVHLLEEAV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 109 INTLKAYNINSTARPDAPGVYVDG-----KKICSLGLRIRRGCSFHGLALNVDMDLSPFLRINPCGYQGMEMAQVSQ-LG 182
Cdd:PRK14348 119 IRVCASYGVVAGRLEKATGVWLEGdtsraRKICAIGVRSSHYVTMHGLALNVNTDLRYFSYIHPCGFIDKGVTSLQQeLG 198
|
170 180
....*....|....*....|
gi 515647337 183 GPSELENVEQQLIQELVELL 202
Cdd:PRK14348 199 HSIDMAEVKERLGRELLAAL 218
|
|
| BPL_LplA_LipB |
cd16435 |
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ... |
7-198 |
1.47e-25 |
|
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), lipoate-protein ligase A (LplA) and octanoyl-[acyl carrier protein]-protein acyltransferase (LipB). Biotin is covalently attached at the active site of certain enzymes that transfer carbon dioxide from bicarbonate to organic acids to form cellular metabolites. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine. Lipoate-protein ligase A (LplA) catalyses the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes.
Pssm-ID: 319740 Cd Length: 198 Bit Score: 98.38 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 7 VKKLGRQDYEPVWKAMHKFTDERTEEDVDQVWLVEHNPVFTQGQAGKAEHVLN-----AGDIPVIQSDRGGQVTYHGPGQ 81
Cdd:cd16435 2 VEVLDSVDYESAWAAQEKSLRENVSNQSSTLLLWEHPTTVTLGRLDRELPHLElakkiERGYELVVRNRGGRAVSHDPGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 82 LVAYFLINIRRKkFGVRDLVTHIENLVINTLKAYNINSTARPDAPGVYVDGKKICSLGLRIRRGCSFHGLALNVDMDLSP 161
Cdd:cd16435 82 LVFSPVIGPNVE-FMISKFNLIIEEGIRDAIADFGQSAEVKWGRNDLWIDNRKVCGIAVRVVKEAIFHGIALNLNQDLEN 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 515647337 162 FLRINPCGYQGMEMAQVS-QLGGPSELENVEQQLIQEL 198
Cdd:cd16435 161 FTEIIPCGYKPERVTSLSlELGRKVTVEQVLERVLAAF 198
|
|
| LplA |
COG0095 |
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part ... |
71-203 |
3.23e-07 |
|
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part of the Pathway/BioSystem: Lipoate biosynthesis
Pssm-ID: 439865 Cd Length: 246 Bit Score: 49.46 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 71 GGQVtYHGPGQLVAYFLINIRRKKFGVRDLVTHIENLVINTLKAYNINSTARP--DapgVYVDGKKICSLGLRIRRGCSF 148
Cdd:COG0095 73 GGAV-YHDPGNLNYSLILPEDDVPLSIEESYRKLLEPILEALRKLGVDAEFSGrnD---IVVDGRKISGNAQRRRKGAVL 148
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515647337 149 -HG-LALNVDMD-LSPFLRINP-----CGYQGMEmAQV----SQLGGPSELENVEQQLIQELVELLG 203
Cdd:COG0095 149 hHGtLLVDGDLEkLAKVLRVPYeklrdKGIKSVR-SRVtnlsELLGTDITREEVKEALLEAFAEVLG 214
|
|
| LplA |
cd16443 |
lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide ... |
29-202 |
1.69e-06 |
|
lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide linkage between free lipoic acid and a specific lysine residue of the lipoyl domain in lipoate dependent enzymes, similar to the biotinylation reaction mediated by biotinyl protein ligase (BPL). The two step reaction includes activation of exogenously supplied lipoic acid at the expense of ATP to lipoyl-AMP and then transfer to the epsilon-amino group of a specific lysine residue of the lipoyl domain of the target protein.
Pssm-ID: 319742 Cd Length: 209 Bit Score: 46.86 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 29 RTEEDVDQVWLVEHNpvftqgqagkaehvlnagdIPVIQSDRGGQVTYHGPGQLVAYFLINirRKKFGVRDLVTHIENLV 108
Cdd:cd16443 49 NPLEEVNLEYAEEDG-------------------IPVVRRPSGGGAVFHDLGNLNYSLILP--KEHPSIDESYRALSQPV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 109 INTLKAYNINstARPDAPGVY---VDGKKICSLGLRIRRGCSFHGLALNVDMDLSPFLRINPCGYQGME----------M 175
Cdd:cd16443 108 IKALRKLGVE--AEFGGVGRNdlvVGGKKISGSAQRRTKGRILHHGTLLVDVDLEKLARVLNVPYEKLKskgpksvrsrV 185
|
170 180
....*....|....*....|....*..
gi 515647337 176 AQVSQLGGpsELENVEqQLIQELVELL 202
Cdd:cd16443 186 TNLSELLG--RDITVE-EVKNALLEAF 209
|
|
| BPL_LplA_LipB |
pfam03099 |
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ... |
58-158 |
3.36e-03 |
|
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, lipoate-protein ligase A and B. Biotin is covalently attached at the active site of certain enzymes that transfer carbon dioxide from bicarbonate to organic acids to form cellular metabolites. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Each organizm probably has only one BPL. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine. Lipoate-protein ligase A (LPLA) catalyzes the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes. The unusual biosynthesis pathway of lipoic acid is mechanistically intertwined with attachment of the cofactor.
Pssm-ID: 427135 Cd Length: 132 Bit Score: 36.65 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515647337 58 LNAGDIPVIQSDRGGQ----VTYHGPGQLVAY-FLINIRRKKFGVRDLVTHIENLVINTLKAYNINSTARPDAP------ 126
Cdd:pfam03099 20 LESGGVVVVRRQTGGRgrggNVWHSPKGCLTYsLLLSKEHPNVDPSVLEFYVLELVLAVLEALGLYKPGISGIPcfvkwp 99
|
90 100 110
....*....|....*....|....*....|...
gi 515647337 127 -GVYVDGKKICSLGLRIRRGCSFHGLALNVDMD 158
Cdd:pfam03099 100 nDLYVNGRKLAGILQRSTRGGTLHHGVIGLGVN 132
|
|
| |
