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Conserved domains on  [gi|90111156|ref|NP_415163|]
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lipoyl(octanoyl) transferase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

lipoyl(octanoyl) transferase LipB( domain architecture ID 10014639)

lipoyl(octanoyl) transferase LipB catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes

EC:  2.3.1.181
Gene Symbol:  lipB
Gene Ontology:  GO:0033819|GO:0009249
PubMed:  16342964|15642479

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK14342 PRK14342
lipoyl(octanoyl) transferase LipB;
1-212 7.17e-158

lipoyl(octanoyl) transferase LipB;


:

Pssm-ID: 237681  Cd Length: 213  Bit Score: 434.69  E-value: 7.17e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156    1 MYQDKILVRQLGLQPYEPISQAMHEFTDTRDDSTLDEIWLVEHYPVFTQGQAGKAEHILMPGDIPVIQSDRGGQVTYHGP 80
Cdd:PRK14342   1 MMQNKLIVRQLGLQPYEPVWQAMQEFTDTRDEETPDEIWLVEHPPVFTQGQAGKPEHILNPGDIPVVQSDRGGQVTYHGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156   81 GQQVMYVLLNLKRRKLGVRELVTLLEQTVVNTLAELGIEAHPRADAPGVYVGEKKICSLGLRIRRGCSFHGLALNVNMDL 160
Cdd:PRK14342  81 GQLVMYVLLDLKRLKLGVRQLVTAIEQTVINTLAEYGIEAHAKPDAPGVYVDGKKIASLGLRIRRGCSFHGLALNVNMDL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 90111156  161 SPFLRINPCGYAGMEMAKISQWKPEATTNNIAPRLLENILALLNNPDFEYIT 212
Cdd:PRK14342 161 SPFLRINPCGYAGLEMTQLSDLGGPATVDEVAPRLLAELLALLGYNDQETIT 212
 
Name Accession Description Interval E-value
PRK14342 PRK14342
lipoyl(octanoyl) transferase LipB;
1-212 7.17e-158

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237681  Cd Length: 213  Bit Score: 434.69  E-value: 7.17e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156    1 MYQDKILVRQLGLQPYEPISQAMHEFTDTRDDSTLDEIWLVEHYPVFTQGQAGKAEHILMPGDIPVIQSDRGGQVTYHGP 80
Cdd:PRK14342   1 MMQNKLIVRQLGLQPYEPVWQAMQEFTDTRDEETPDEIWLVEHPPVFTQGQAGKPEHILNPGDIPVVQSDRGGQVTYHGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156   81 GQQVMYVLLNLKRRKLGVRELVTLLEQTVVNTLAELGIEAHPRADAPGVYVGEKKICSLGLRIRRGCSFHGLALNVNMDL 160
Cdd:PRK14342  81 GQLVMYVLLDLKRLKLGVRQLVTAIEQTVINTLAEYGIEAHAKPDAPGVYVDGKKIASLGLRIRRGCSFHGLALNVNMDL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 90111156  161 SPFLRINPCGYAGMEMAKISQWKPEATTNNIAPRLLENILALLNNPDFEYIT 212
Cdd:PRK14342 161 SPFLRINPCGYAGLEMTQLSDLGGPATVDEVAPRLLAELLALLGYNDQETIT 212
LipB COG0321
Lipoate-protein ligase B [Coenzyme transport and metabolism]; Lipoate-protein ligase B is part ...
 4-204 6.14e-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: 336.31  E-value: 6.14e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156   4 DKILVRQLGLQPYEPISQAMHEFTDTR-DDSTLDEIWLVEHYPVFTQGQAGKAEHILMPGDIPVIQSDRGGQVTYHGPGQ 82
Cdd:COG0321   2 RPLIIRDLGLVDYEEAWAAQRRLTAARvAGDTPDELWLLEHPPVYTLGRSGKPEHLLAPGGIPVVQTDRGGQITYHGPGQ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156  83 QVMYVLLNLKRRKLGVRELVTLLEQTVVNTLAELGIEAHPRADAPGVYVGEKKICSLGLRIRRGCSFHGLALNVNMDLSP 162
Cdd:COG0321  82 LVGYPILDLRRRGLDVRAYVRRLEEAVIDTLAEYGIEAERRPGAPGVWVDGRKIAAIGLRVRRGVTYHGFALNVNPDLSP 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 90111156 163 FLRINPCGYAGMEMAKISQW-KPEATTNNIAPRLLENILALLN 204
Cdd:COG0321 162 FSRIVPCGIADLGVTSLSDElGRPVTMEEVAEALIRHFAEVFG 204
LipB cd16444
lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein] ...
 7-203 1.33e-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: 1.33e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156   7 LVRQLGLQPYEPISQAMHEFTDTRD-DSTLDEIWLVEHYPVFTQGQAGKAEHILMPGDIPVIQSDRGGQVTYHGPGQQVM 85
Cdd:cd16444   1 IVRDLGLIPYEEAWELQKRLVAERIaGETPDTLWLLEHPPVYTLGRRGKPENLLNNGGIPVVRTDRGGQVTYHGPGQLVG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156  86 YVLLNLKRRKLGVRELVTLLEQTVVNTLAELGIEAHPRADAPGVYVGEKKICSLGLRIRRGCSFHGLALNVNMDLSPFLR 165
Cdd:cd16444  81 YPILDLRRRGLDVRRYVRALEEAVIRTLAEYGIEAGRRPGAPGVWVGDRKIASIGIRVRRGVTYHGLALNVNTDLSPFNR 160

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 90111156 166 INPCGYAGMEMAKISQW-KPEATTNNIAPRLLENILALL 203
Cdd:cd16444 161 INPCGIKGKGVTSLSDLgGREVDMEEVKQKLVEEFAKIF 199
lipB TIGR00214
lipoate-protein ligase B; Involved in lipoate biosynthesis as the main determinant of the ...
 26-204 1.64e-111

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: 316.74  E-value: 1.64e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156    26 FTDT--RDDSTLDEIWLVEHYPVFTQGQAGKAEHILMPGDIP---VIQSDRGGQVTYHGPGQQVMYVLLNLKRRKLGVRE 100
Cdd:TIGR00214   1 FTDTkqRDRQTLDEIMLVEHYPVYTQGQAGKTEHLLFDPDIPpaeVVQSERGGQVTYHGPGQQVMYVILDLKRFQLDVRW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156   101 LVTLLEQTVVNTLAELGIEAHPRADAPGVYVGEKKICSLGLRIRRGCSFHGLALNVNMDLSPFLRINPCGYAGMEMAKIS 180
Cdd:TIGR00214  81 LVTQLEQTVIITLAELGIEGEPIADATGVWVEGKKVASLGIRVRRGCTFHGLALNINMDLSPFSHINPCGYAGREMGSLN 160

                         170       180
                  ....*....|....*....|....
gi 90111156   181 QWKPEATTNNIAPRLLENILALLN 204
Cdd:TIGR00214 161 QFLPGATVENVAPLLIKAFAELLG 184
 
Name Accession Description Interval E-value
PRK14342 PRK14342
lipoyl(octanoyl) transferase LipB;
1-212 7.17e-158

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237681  Cd Length: 213  Bit Score: 434.69  E-value: 7.17e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156    1 MYQDKILVRQLGLQPYEPISQAMHEFTDTRDDSTLDEIWLVEHYPVFTQGQAGKAEHILMPGDIPVIQSDRGGQVTYHGP 80
Cdd:PRK14342   1 MMQNKLIVRQLGLQPYEPVWQAMQEFTDTRDEETPDEIWLVEHPPVFTQGQAGKPEHILNPGDIPVVQSDRGGQVTYHGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156   81 GQQVMYVLLNLKRRKLGVRELVTLLEQTVVNTLAELGIEAHPRADAPGVYVGEKKICSLGLRIRRGCSFHGLALNVNMDL 160
Cdd:PRK14342  81 GQLVMYVLLDLKRLKLGVRQLVTAIEQTVINTLAEYGIEAHAKPDAPGVYVDGKKIASLGLRIRRGCSFHGLALNVNMDL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 90111156  161 SPFLRINPCGYAGMEMAKISQWKPEATTNNIAPRLLENILALLNNPDFEYIT 212
Cdd:PRK14342 161 SPFLRINPCGYAGLEMTQLSDLGGPATVDEVAPRLLAELLALLGYNDQETIT 212
LipB COG0321
Lipoate-protein ligase B [Coenzyme transport and metabolism]; Lipoate-protein ligase B is part ...
 4-204 6.14e-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: 336.31  E-value: 6.14e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156   4 DKILVRQLGLQPYEPISQAMHEFTDTR-DDSTLDEIWLVEHYPVFTQGQAGKAEHILMPGDIPVIQSDRGGQVTYHGPGQ 82
Cdd:COG0321   2 RPLIIRDLGLVDYEEAWAAQRRLTAARvAGDTPDELWLLEHPPVYTLGRSGKPEHLLAPGGIPVVQTDRGGQITYHGPGQ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156  83 QVMYVLLNLKRRKLGVRELVTLLEQTVVNTLAELGIEAHPRADAPGVYVGEKKICSLGLRIRRGCSFHGLALNVNMDLSP 162
Cdd:COG0321  82 LVGYPILDLRRRGLDVRAYVRRLEEAVIDTLAEYGIEAERRPGAPGVWVDGRKIAAIGLRVRRGVTYHGFALNVNPDLSP 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 90111156 163 FLRINPCGYAGMEMAKISQW-KPEATTNNIAPRLLENILALLN 204
Cdd:COG0321 162 FSRIVPCGIADLGVTSLSDElGRPVTMEEVAEALIRHFAEVFG 204
LipB cd16444
lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein] ...
 7-203 1.33e-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: 1.33e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156   7 LVRQLGLQPYEPISQAMHEFTDTRD-DSTLDEIWLVEHYPVFTQGQAGKAEHILMPGDIPVIQSDRGGQVTYHGPGQQVM 85
Cdd:cd16444   1 IVRDLGLIPYEEAWELQKRLVAERIaGETPDTLWLLEHPPVYTLGRRGKPENLLNNGGIPVVRTDRGGQVTYHGPGQLVG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156  86 YVLLNLKRRKLGVRELVTLLEQTVVNTLAELGIEAHPRADAPGVYVGEKKICSLGLRIRRGCSFHGLALNVNMDLSPFLR 165
Cdd:cd16444  81 YPILDLRRRGLDVRRYVRALEEAVIRTLAEYGIEAGRRPGAPGVWVGDRKIASIGIRVRRGVTYHGLALNVNTDLSPFNR 160

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 90111156 166 INPCGYAGMEMAKISQW-KPEATTNNIAPRLLENILALL 203
Cdd:cd16444 161 INPCGIKGKGVTSLSDLgGREVDMEEVKQKLVEEFAKIF 199
lipB TIGR00214
lipoate-protein ligase B; Involved in lipoate biosynthesis as the main determinant of the ...
 26-204 1.64e-111

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: 316.74  E-value: 1.64e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156    26 FTDT--RDDSTLDEIWLVEHYPVFTQGQAGKAEHILMPGDIP---VIQSDRGGQVTYHGPGQQVMYVLLNLKRRKLGVRE 100
Cdd:TIGR00214   1 FTDTkqRDRQTLDEIMLVEHYPVYTQGQAGKTEHLLFDPDIPpaeVVQSERGGQVTYHGPGQQVMYVILDLKRFQLDVRW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156   101 LVTLLEQTVVNTLAELGIEAHPRADAPGVYVGEKKICSLGLRIRRGCSFHGLALNVNMDLSPFLRINPCGYAGMEMAKIS 180
Cdd:TIGR00214  81 LVTQLEQTVIITLAELGIEGEPIADATGVWVEGKKVASLGIRVRRGCTFHGLALNINMDLSPFSHINPCGYAGREMGSLN 160

                         170       180
                  ....*....|....*....|....
gi 90111156   181 QWKPEATTNNIAPRLLENILALLN 204
Cdd:TIGR00214 161 QFLPGATVENVAPLLIKAFAELLG 184
PRK14343 PRK14343
lipoyl(octanoyl) transferase LipB;
6-203 1.54e-95

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237682  Cd Length: 235  Bit Score: 278.21  E-value: 1.54e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156    6 ILVRQLGLQPYEPISQAMHEFTDTRDDSTLDEIWLVEHYPVFTQGQAGKAEHILMPGD-IPVIQSDRGGQVTYHGPGQQV 84
Cdd:PRK14343  15 VTVRWRGREPYEACFDAMRAFTDARTADTPDEIWLVEHPPVYTLGQAGDPAHLLVADSgIPLVKVDRGGQITYHGPGQVV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156   85 MYVLLNLKRRKLGVRELVTLLEQTVVNTLAELGIEAHPRADAPGVYVGE-----KKICSLGLRIRRGCSFHGLALNVNMD 159
Cdd:PRK14343  95 AYLLLDLRRRKLMVRELVTRIEQAVIDTLAAYNLASERKAGAPGIYVASgphqgAKIAALGLKIRNGCSYHGLSLNVKMD 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 90111156  160 LSPFLRINPCGYAGMEMAKISQWKPEATTNNIAPRLLENILALL 203
Cdd:PRK14343 175 LRPFLAINPCGYAGLETVDMASLGVAADWADVAQTLARRLIANL 218
PRK14346 PRK14346
lipoyl(octanoyl) transferase LipB;
6-180 2.16e-76

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237684  Cd Length: 230  Bit Score: 229.26  E-value: 2.16e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156    6 ILVRQLGLQPYEPISQAMHEFTDTRDDSTLDEIWLVEHYPVFTQGQAGKAEHILMPGDIPVIQSDRGGQVTYHGPGQQVM 85
Cdd:PRK14346   3 MDRRMLGRVDYLATVQAMQAFTAERTPETPDELWICEHPPVYTQGLAGKADHVLNPGDIPVVATNRGGQVTYHGPGQVVA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156   86 YVLLNLKRRKLGVRELVTLLEQTVVNTLAELGIEAHPRADAPGVYV----------------------------GEKKIC 137
Cdd:PRK14346  83 YPLIDLRRAGYFVKEYVYRIEEAVIRTLAHFGVTGHRVAGAPGIYVrlddpfshaalpqrpqkrgggapqppfrGLGKIA 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 90111156  138 SLGLRIRRGCSFHGLALNVNMDLSPFLRINPCGYAGMEMAKIS 180
Cdd:PRK14346 163 ALGIKVSRHCTYHGVALNVAMDLEPFSRINPCGYAGLQTVDLS 205
PRK14349 PRK14349
lipoyl(octanoyl) transferase LipB;
16-174 1.25e-73

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 172825  Cd Length: 220  Bit Score: 222.15  E-value: 1.25e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156   16 YEPISQAMHEFTDTRDDSTLDEIWLVEHYPVFTQGQAGKAEHILMPGDIPVIQSDRGGQVTYHGPGQQVMYVLLNLKRRK 95
Cdd:PRK14349  11 YASVWDAMKAFTAARGPGTADEIWLCEHAPVYTLGQAGRPEHLLNPGLIPVVHCDRGGQVTYHGPGQVLAYTLFDLRRAG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156   96 LGVRELVTLLEQTVVNTLAELGIE-AHPRADAPGVYV----GE-KKICSLGLRIRRGCSFHGLALNVNMDLSPFLRINPC 169
Cdd:PRK14349  91 LYVREYVDMLEQATLATLRELGLEqACRKPGAPGIYVpqpgGElAKIAALGVKVRNGYAYHGLALNIDMDLSPFLGINPC 170


                 ....*
gi 90111156  170 GYAGM 174
Cdd:PRK14349 171 GYEGL 175
PRK14341 PRK14341
lipoyl(octanoyl) transferase LipB;
12-170 1.77e-53

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237680  Cd Length: 213  Bit Score: 170.48  E-value: 1.77e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156   12 GLQPYEPISQAMHEFTDTRDDSTLDE-IWLVEHYPVFTQGQAGKAEHILMPGDIPVIQSDRGGQVTYHGPGQQVMYVLLN 90
Cdd:PRK14341  11 GLVPYPEALAFMEARVAAIAAGTADElVWLLEHPPLYTAGTSAKAEDLLDPDRFPVYETGRGGQYTYHGPGQRVAYVMLD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156   91 LKRRKLGVRELVTLLEQTVVNTLAELGIEAHPRADAPGVYV--------GEKKICSLGLRIRRGCSFHGLALNVNMDLSP 162
Cdd:PRK14341  91 LKRRRRDVRAFVAALEEWIIATLAAFNIRGERREDRVGVWVrrpdkgsgAEDKIAAIGVRLRRWVSFHGISINVEPDLSH 170


                 ....*...
gi 90111156  163 FLRINPCG 170
Cdd:PRK14341 171 FSGIVPCG 178
PRK14344 PRK14344
lipoyl(octanoyl) transferase LipB;
31-201 4.70e-41

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237683  Cd Length: 223  Bit Score: 139.05  E-value: 4.70e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156   31 DDSTLDEIWLVEHYPVFTQGQAGKAEHILMPGD---IPVIQSDRGGQVTYHGPGQQVMYVLLNLKRRKLGVRELVTLLEQ 107
Cdd:PRK14344  46 DPSNPQAVWLLEHQLCYTLGRGASEDNLLFSLNnppADVFRIDRGGEVTHHMPGQLVTYLVLDLRRFNKDLNWYLRQLEQ 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156  108 TVVNTLAELGIEAHPRADAPGVYVGEKKICSLGLRIRRGCSFHGLALNVNMDLSPFLRINPCGYAGMEMAKISQWKPEAT 187
Cdd:PRK14344 126 VLIDVLADLGIDGERLDGLTGVWIGNKKVASIGIGCRRWITQHGFSLNVDCDLEGFNKIVPCGLEGCQVGRLSDWIPGLN 205

                        170
                 ....*....|....
gi 90111156  188 TNNIAPrLLENILA 201
Cdd:PRK14344 206 IKEVKP-LLKKSLQ 218
PRK14345 PRK14345
lipoyl(octanoyl) transferase LipB;
6-204 1.04e-35

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 184638  Cd Length: 234  Bit Score: 125.48  E-value: 1.04e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156    6 ILVRQLGLQPYEPISQAMHEFTDTR-DDSTLDEIWLVEHYPVFTqgqAGK-AEHILMPGD-IPVIQSDRGGQVTYHGPGQ 82
Cdd:PRK14345  12 IEVRRLGLVDYQEAWDLQRELADARvAGEGPDTLLLLEHPAVYT---AGKrTEPHERPTDgTPVVDVDRGGKITWHGPGQ 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156   83 QVMYVLLNLKRRkLGVRELVTLLEQTVVNTLAELGIEAHPRADAPGVYV------GEKKICSLGLRIRRGCSFHGLALNV 156
Cdd:PRK14345  89 LVGYPIIKLAEP-LDVVDYVRRLEEALIAVCADLGLNAGRVDGRSGVWVpadggrPDRKIAAIGIRVSRGVTMHGFALNC 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 90111156  157 NMDLSPFLRINPCGYAGMEMAKIS-QWKPEATTNNIAPRLLENILALLN 204
Cdd:PRK14345 168 DNDLAAFDAIVPCGISDAGVTTLSaELGRTVTVAEVVDPVAAALCDALD 216
PRK14348 PRK14348
lipoyl(octanoyl) transferase LipB;
5-205 1.28e-34

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 172824  Cd Length: 221  Bit Score: 122.44  E-value: 1.28e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156    5 KILVRQLGLQPYEPISQAMHEFTDT------RDDSTLDEIWLVEHYPVFTQGQAGKAEHILMPGD-IPVIQS-----DRG 72
Cdd:PRK14348   2 KTITTDWELIPYSEAWSRQTEWFDAlvhakqNGESYENRIIFCEHPHVYTLGRSGKENNMLLGEEqLKTIGAtlyhiDRG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156   73 GQVTYHGPGQQVMYVLLNLKRRKLGVRELVTLLEQTVVNTLAELGIEAHPRADAPGVYVG-----EKKICSLGLRIRRGC 147
Cdd:PRK14348  82 GDITYHGPGQLVCYPILNLEEFGLGLKEYVHLLEEAVIRVCASYGVVAGRLEKATGVWLEgdtsrARKICAIGVRSSHYV 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 90111156  148 SFHGLALNVNMDLSPFLRINPCGYAGMEMAKISQ-WKPEATTNNIAPRLLENILALLNN 205
Cdd:PRK14348 162 TMHGLALNVNTDLRYFSYIHPCGFIDKGVTSLQQeLGHSIDMAEVKERLGRELLAALLS 220
PRK14347 PRK14347
lipoyl(octanoyl) transferase LipB;
31-170 2.72e-33

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 172823  Cd Length: 209  Bit Score: 118.50  E-value: 2.72e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156   31 DDSTLDEIWLVEHYPVFTQGQAGKAEHILMPGDIPVIQSDRGGQVTYHGPGQQVMYVLLNLK--RRKLGVRELVTLLEQT 108
Cdd:PRK14347  29 SDHEPEIVYLVEHSEVYTAGTNYKQEELLNYGDIPVIYTGRGGKFTFHGPGQRVIYPILNLAspNRHKDLKLYIKMLEEW 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111156  109 VVNTLAELGIEAHPRADAPGVYVGEK-----KICSLGLRIRRGCSFHGLALNVNMDLSPFLRINPCG 170
Cdd:PRK14347 109 IINSLNYFGIKAYIIKDKVGIWVKVRkdefaKIAAIGVRVRKWVTYHGVAINISTDLSKFSGIIPCG 175
BPL_LplA_LipB cd16435
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ...
 7-199 5.41e-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: 96.84  E-value: 5.41e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156   7 LVRQLGLQPYEPISQAMHEFTDTRDDSTLDEIWLVEHYPVFTQGQAGKAEHILMPGD-----IPVIQSDRGGQVTYHGPG 81
Cdd:cd16435   1 FVEVLDSVDYESAWAAQEKSLRENVSNQSSTLLLWEHPTTVTLGRLDRELPHLELAKkiergYELVVRNRGGRAVSHDPG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156  82 QQVMYVLLNlKRRKLGVRELVTLLEQTVVNTLAELGIEAHPRADAPGVYVGEKKICSLGLRIRRGCSFHGLALNVNMDLS 161
Cdd:cd16435  81 QLVFSPVIG-PNVEFMISKFNLIIEEGIRDAIADFGQSAEVKWGRNDLWIDNRKVCGIAVRVVKEAIFHGIALNLNQDLE 159

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 90111156 162 PFLRINPCGYAGMEMAKIS-QWKPEATTNNIAPRLLENI 199
Cdd:cd16435 160 NFTEIIPCGYKPERVTSLSlELGRKVTVEQVLERVLAAF 198
LplA cd16443
lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide ...
 63-166 1.50e-07

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: 49.95  E-value: 1.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156  63 DIPVIQSDRGGQVTYHGPGQqVMYVLLnLKRRKLGVRELVTLLEQTVVNTLAELGIEAHPRAdaPGVY---VGEKKICSL 139
Cdd:cd16443  63 GIPVVRRPSGGGAVFHDLGN-LNYSLI-LPKEHPSIDESYRALSQPVIKALRKLGVEAEFGG--VGRNdlvVGGKKISGS 138

                        90       100
                ....*....|....*....|....*..
gi 90111156 140 GLRIRRGCSFHGLALNVNMDLSPFLRI 166
Cdd:cd16443 139 AQRRTKGRILHHGTLLVDVDLEKLARV 165
LplA COG0095
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part ...
 72-168 7.63e-06

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: 45.23  E-value: 7.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111156  72 GGQVtYHGPGQqVMY-VLLNLKRRKLGVRELVTLLEQTVVNTLAELGIEAH--PRADapgVYVGEKKICSLGLRIRRGCS 148
Cdd:COG0095  73 GGAV-YHDPGN-LNYsLILPEDDVPLSIEESYRKLLEPILEALRKLGVDAEfsGRND---IVVDGRKISGNAQRRRKGAV 147

                        90       100
                ....*....|....*....|...
gi 90111156 149 F-HG-LALNVNMD-LSPFLRINP 168
Cdd:COG0095 148 LhHGtLLVDGDLEkLAKVLRVPY 170
 
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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