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Conserved domains on  [gi|1143467785|ref|NP_001335548|]
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Octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase LIPT2, mitochondrial [Caenorhabditis elegans]

Protein Classification

lipoyl(octanoyl) transferase( domain architecture ID 11612812)

lipoyl(octanoyl) transferase (LipB/LIPT2) catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LipB cd16444
lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein] ...
 16-226 5.67e-83

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: 246.25  E-value: 5.67e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  16 IDLGQISYGAALKEQQKYVDLVKANKSEthslNFILALEHTPVYTVGIRSKgytkeEETRLMRLGAEFHRTSRGGLITFH 95
Cdd:cd16444     3 RDLGLIPYEEAWELQKRLVAERIAGETP----DTLWLLEHPPVYTLGRRGK-----PENLLNNGGIPVVRTDRGGQVTYH 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  96 GPGQLVLYPICDVRRIsikQLGVRHFVDKLEQTIIDAATEgFGIKNVGRTANTGVWVsNERKLAAIGIAVSGGVSYHGIA 175
Cdd:cd16444    74 GPGQLVGYPILDLRRR---GLDVRRYVRALEEAVIRTLAE-YGIEAGRRPGAPGVWV-GDRKIASIGIRVRRGVTYHGLA 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1143467785 176 INCNTDLRWFDNIVGCGIEGVSTTSLSQETSRNVTVSDARPILLNAFANNF 226
Cdd:cd16444   149 LNVNTDLSPFNRINPCGIKGKGVTSLSDLGGREVDMEEVKQKLVEEFAKIF 199
 
Name Accession Description Interval E-value
LipB cd16444
lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein] ...
 16-226 5.67e-83

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: 246.25  E-value: 5.67e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  16 IDLGQISYGAALKEQQKYVDLVKANKSEthslNFILALEHTPVYTVGIRSKgytkeEETRLMRLGAEFHRTSRGGLITFH 95
Cdd:cd16444     3 RDLGLIPYEEAWELQKRLVAERIAGETP----DTLWLLEHPPVYTLGRRGK-----PENLLNNGGIPVVRTDRGGQVTYH 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  96 GPGQLVLYPICDVRRIsikQLGVRHFVDKLEQTIIDAATEgFGIKNVGRTANTGVWVsNERKLAAIGIAVSGGVSYHGIA 175
Cdd:cd16444    74 GPGQLVGYPILDLRRR---GLDVRRYVRALEEAVIRTLAE-YGIEAGRRPGAPGVWV-GDRKIASIGIRVRRGVTYHGLA 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1143467785 176 INCNTDLRWFDNIVGCGIEGVSTTSLSQETSRNVTVSDARPILLNAFANNF 226
Cdd:cd16444   149 LNVNTDLSPFNRINPCGIKGKGVTSLSDLGGREVDMEEVKQKLVEEFAKIF 199
LipB COG0321
Lipoate-protein ligase B [Coenzyme transport and metabolism]; Lipoate-protein ligase B is part ...
 10-233 1.05e-82

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: 246.17  E-value: 1.05e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  10 KSTVNAIDLGQISYGAALKEQQKYVDLVKANKSEthslNFILALEHTPVYTVGIRSKgytkeEETRLMRLGAEFHRTSRG 89
Cdd:COG0321     1 NRPLIIRDLGLVDYEEAWAAQRRLTAARVAGDTP----DELWLLEHPPVYTLGRSGK-----PEHLLAPGGIPVVQTDRG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  90 GLITFHGPGQLVLYPICDVRRisiKQLGVRHFVDKLEQTIIDAATEgFGIKNVGRTANTGVWVsNERKLAAIGIAVSGGV 169
Cdd:COG0321    72 GQITYHGPGQLVGYPILDLRR---RGLDVRAYVRRLEEAVIDTLAE-YGIEAERRPGAPGVWV-DGRKIAAIGLRVRRGV 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1143467785 170 SYHGIAINCNTDLRWFDNIVGCGIEGVSTTSLSQETSRNVTVSDARPILLNAFANNFECLLNEP 233
Cdd:COG0321   147 TYHGFALNVNPDLSPFSRIVPCGIADLGVTSLSDELGRPVTMEEVAEALIRHFAEVFGYELVEL 210
PRK14345 PRK14345
lipoyl(octanoyl) transferase LipB;
17-230 6.63e-52

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 184638  Cd Length: 234  Bit Score: 168.62  E-value: 6.63e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  17 DLGQISYGAALKEQQKYVDLVKANKSEthslNFILALEHTPVYTVGIRSkgytkEEETRLMRlGAEFHRTSRGGLITFHG 96
Cdd:PRK14345   16 RLGLVDYQEAWDLQRELADARVAGEGP----DTLLLLEHPAVYTAGKRT-----EPHERPTD-GTPVVDVDRGGKITWHG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  97 PGQLVLYPIcdvrrISIKQ-LGVRHFVDKLEQTIIDAATEgFGIkNVGRTAN-TGVWVSN-----ERKLAAIGIAVSGGV 169
Cdd:PRK14345   86 PGQLVGYPI-----IKLAEpLDVVDYVRRLEEALIAVCAD-LGL-NAGRVDGrSGVWVPAdggrpDRKIAAIGIRVSRGV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1143467785 170 SYHGIAINCNTDLRWFDNIVGCGIEGVSTTSLSQETSRNVTVSDARPILLNAFANNFECLL 230
Cdd:PRK14345  159 TMHGFALNCDNDLAAFDAIVPCGISDAGVTTLSAELGRTVTVAEVVDPVAAALCDALDGRL 219
lipB TIGR00214
lipoate-protein ligase B; Involved in lipoate biosynthesis as the main determinant of the ...
 37-226 7.14e-43

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: 143.78  E-value: 7.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  37 VKANKSETHSLNFILALEHTPVYTVGIRSKGYTKEEETRLMRlgAEFHRTSRGGLITFHGPGQLVLYPICDVRRisiKQL 116
Cdd:TIGR00214   2 TDTKQRDRQTLDEIMLVEHYPVYTQGQAGKTEHLLFDPDIPP--AEVVQSERGGQVTYHGPGQQVMYVILDLKR---FQL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785 117 GVRHFVDKLEQTIIDAATEgFGIKNVGRTANTGVWVsNERKLAAIGIAVSGGVSYHGIAINCNTDLRWFDNIVGCGIEGV 196
Cdd:TIGR00214  77 DVRWLVTQLEQTVIITLAE-LGIEGEPIADATGVWV-EGKKVASLGIRVRRGCTFHGLALNINMDLSPFSHINPCGYAGR 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 1143467785 197 STTSLSQETSRnVTVSDARPILLNAFANNF 226
Cdd:TIGR00214 155 EMGSLNQFLPG-ATVENVAPLLIKAFAELL 183
 
Name Accession Description Interval E-value
LipB cd16444
lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein] ...
 16-226 5.67e-83

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: 246.25  E-value: 5.67e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  16 IDLGQISYGAALKEQQKYVDLVKANKSEthslNFILALEHTPVYTVGIRSKgytkeEETRLMRLGAEFHRTSRGGLITFH 95
Cdd:cd16444     3 RDLGLIPYEEAWELQKRLVAERIAGETP----DTLWLLEHPPVYTLGRRGK-----PENLLNNGGIPVVRTDRGGQVTYH 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  96 GPGQLVLYPICDVRRIsikQLGVRHFVDKLEQTIIDAATEgFGIKNVGRTANTGVWVsNERKLAAIGIAVSGGVSYHGIA 175
Cdd:cd16444    74 GPGQLVGYPILDLRRR---GLDVRRYVRALEEAVIRTLAE-YGIEAGRRPGAPGVWV-GDRKIASIGIRVRRGVTYHGLA 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1143467785 176 INCNTDLRWFDNIVGCGIEGVSTTSLSQETSRNVTVSDARPILLNAFANNF 226
Cdd:cd16444   149 LNVNTDLSPFNRINPCGIKGKGVTSLSDLGGREVDMEEVKQKLVEEFAKIF 199
LipB COG0321
Lipoate-protein ligase B [Coenzyme transport and metabolism]; Lipoate-protein ligase B is part ...
 10-233 1.05e-82

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: 246.17  E-value: 1.05e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  10 KSTVNAIDLGQISYGAALKEQQKYVDLVKANKSEthslNFILALEHTPVYTVGIRSKgytkeEETRLMRLGAEFHRTSRG 89
Cdd:COG0321     1 NRPLIIRDLGLVDYEEAWAAQRRLTAARVAGDTP----DELWLLEHPPVYTLGRSGK-----PEHLLAPGGIPVVQTDRG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  90 GLITFHGPGQLVLYPICDVRRisiKQLGVRHFVDKLEQTIIDAATEgFGIKNVGRTANTGVWVsNERKLAAIGIAVSGGV 169
Cdd:COG0321    72 GQITYHGPGQLVGYPILDLRR---RGLDVRAYVRRLEEAVIDTLAE-YGIEAERRPGAPGVWV-DGRKIAAIGLRVRRGV 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1143467785 170 SYHGIAINCNTDLRWFDNIVGCGIEGVSTTSLSQETSRNVTVSDARPILLNAFANNFECLLNEP 233
Cdd:COG0321   147 TYHGFALNVNPDLSPFSRIVPCGIADLGVTSLSDELGRPVTMEEVAEALIRHFAEVFGYELVEL 210
PRK14345 PRK14345
lipoyl(octanoyl) transferase LipB;
17-230 6.63e-52

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 184638  Cd Length: 234  Bit Score: 168.62  E-value: 6.63e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  17 DLGQISYGAALKEQQKYVDLVKANKSEthslNFILALEHTPVYTVGIRSkgytkEEETRLMRlGAEFHRTSRGGLITFHG 96
Cdd:PRK14345   16 RLGLVDYQEAWDLQRELADARVAGEGP----DTLLLLEHPAVYTAGKRT-----EPHERPTD-GTPVVDVDRGGKITWHG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  97 PGQLVLYPIcdvrrISIKQ-LGVRHFVDKLEQTIIDAATEgFGIkNVGRTAN-TGVWVSN-----ERKLAAIGIAVSGGV 169
Cdd:PRK14345   86 PGQLVGYPI-----IKLAEpLDVVDYVRRLEEALIAVCAD-LGL-NAGRVDGrSGVWVPAdggrpDRKIAAIGIRVSRGV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1143467785 170 SYHGIAINCNTDLRWFDNIVGCGIEGVSTTSLSQETSRNVTVSDARPILLNAFANNFECLL 230
Cdd:PRK14345  159 TMHGFALNCDNDLAAFDAIVPCGISDAGVTTLSAELGRTVTVAEVVDPVAAALCDALDGRL 219
lipB TIGR00214
lipoate-protein ligase B; Involved in lipoate biosynthesis as the main determinant of the ...
 37-226 7.14e-43

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: 143.78  E-value: 7.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  37 VKANKSETHSLNFILALEHTPVYTVGIRSKGYTKEEETRLMRlgAEFHRTSRGGLITFHGPGQLVLYPICDVRRisiKQL 116
Cdd:TIGR00214   2 TDTKQRDRQTLDEIMLVEHYPVYTQGQAGKTEHLLFDPDIPP--AEVVQSERGGQVTYHGPGQQVMYVILDLKR---FQL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785 117 GVRHFVDKLEQTIIDAATEgFGIKNVGRTANTGVWVsNERKLAAIGIAVSGGVSYHGIAINCNTDLRWFDNIVGCGIEGV 196
Cdd:TIGR00214  77 DVRWLVTQLEQTVIITLAE-LGIEGEPIADATGVWV-EGKKVASLGIRVRRGCTFHGLALNINMDLSPFSHINPCGYAGR 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 1143467785 197 STTSLSQETSRnVTVSDARPILLNAFANNF 226
Cdd:TIGR00214 155 EMGSLNQFLPG-ATVENVAPLLIKAFAELL 183
PRK14341 PRK14341
lipoyl(octanoyl) transferase LipB;
19-226 1.41e-37

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237680  Cd Length: 213  Bit Score: 130.80  E-value: 1.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  19 GQISYGAALKEQQKYVDLVKANksETHSLNFILalEHTPVYTVGIRSKgytkeEETRLMRLGAEFHRTSRGGLITFHGPG 98
Cdd:PRK14341   11 GLVPYPEALAFMEARVAAIAAG--TADELVWLL--EHPPLYTAGTSAK-----AEDLLDPDRFPVYETGRGGQYTYHGPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  99 QLVLYPICDVRRisiKQLGVRHFVDKLEQTIIDAATEgFGIKNVGRTANTGVWVSN-------ERKLAAIGIAVSGGVSY 171
Cdd:PRK14341   82 QRVAYVMLDLKR---RRRDVRAFVAALEEWIIATLAA-FNIRGERREDRVGVWVRRpdkgsgaEDKIAAIGVRLRRWVSF 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1143467785 172 HGIAINCNTDLRWFDNIVGCGIEGVSTTSLsQETSRNVTVSDARPILLNAFANNF 226
Cdd:PRK14341  158 HGISINVEPDLSHFSGIVPCGISEHGVTSL-VDLGLPVTMDDVDAALKKAFEKVF 211
PRK14342 PRK14342
lipoyl(octanoyl) transferase LipB;
9-226 3.58e-37

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237681  Cd Length: 213  Bit Score: 130.00  E-value: 3.58e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785   9 QKSTVNAIDLGQISYGAALKEQQKYVDlvkaNKSEtHSLNFILALEHTPVYTVGIRSKgytkeEETRLMRLGAEFHRTSR 88
Cdd:PRK14342    2 MQNKLIVRQLGLQPYEPVWQAMQEFTD----TRDE-ETPDEIWLVEHPPVFTQGQAGK-----PEHILNPGDIPVVQSDR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  89 GGLITFHGPGQLVLYPICDVRRisiKQLGVRHFVDKLEQTIIDAATEgFGIKNVGRTANTGVWVsNERKLAAIGIAVSGG 168
Cdd:PRK14342   72 GGQVTYHGPGQLVMYVLLDLKR---LKLGVRQLVTAIEQTVINTLAE-YGIEAHAKPDAPGVYV-DGKKIASLGLRIRRG 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1143467785 169 VSYHGIAINCNTDLRWFDNIVGCGIEGVSTTSLSQETSRnVTVSDARPILLNAFANNF 226
Cdd:PRK14342  147 CSFHGLALNVNMDLSPFLRINPCGYAGLEMTQLSDLGGP-ATVDEVAPRLLAELLALL 203
PRK14344 PRK14344
lipoyl(octanoyl) transferase LipB;
21-226 1.93e-33

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237683  Cd Length: 223  Bit Score: 120.56  E-value: 1.93e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  21 ISYGAALKEQQKYVDLVKANKSethSLNFILALEHTPVYTVGirsKGYTkeEETRLMRLG---AEFHRTSRGGLITFHGP 97
Cdd:PRK14344   27 VPFEDAWKWQKEWQQALIEDPS---NPQAVWLLEHQLCYTLG---RGAS--EDNLLFSLNnppADVFRIDRGGEVTHHMP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  98 GQLVLYPICDVRRisiKQLGVRHFVDKLEQTIIDaATEGFGIKNVGRTANTGVWVsNERKLAAIGIAVSGGVSYHGIAIN 177
Cdd:PRK14344   99 GQLVTYLVLDLRR---FNKDLNWYLRQLEQVLID-VLADLGIDGERLDGLTGVWI-GNKKVASIGIGCRRWITQHGFSLN 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1143467785 178 CNTDLRWFDNIVGCGIEGVSTTSLSQeTSRNVTVSDARPILLNAFANNF 226
Cdd:PRK14344  174 VDCDLEGFNKIVPCGLEGCQVGRLSD-WIPGLNIKEVKPLLKKSLQERF 221
PRK14348 PRK14348
lipoyl(octanoyl) transferase LipB;
16-215 6.93e-33

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 172824  Cd Length: 221  Bit Score: 119.36  E-value: 6.93e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  16 IDLGQISYGAALKEQQKYVD-LVKANKSETHSLNFILALEHTPVYTVGiRSKgytKEE-----ETRLMRLGAEFHRTSRG 89
Cdd:PRK14348    6 TDWELIPYSEAWSRQTEWFDaLVHAKQNGESYENRIIFCEHPHVYTLG-RSG---KENnmllgEEQLKTIGATLYHIDRG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  90 GLITFHGPGQLVLYPICDVRRIsikQLGVRHFVDKLEQTIIDAATEgFGIKNVGRTANTGVWV----SNERKLAAIGIAV 165
Cdd:PRK14348   82 GDITYHGPGQLVCYPILNLEEF---GLGLKEYVHLLEEAVIRVCAS-YGVVAGRLEKATGVWLegdtSRARKICAIGVRS 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1143467785 166 SGGVSYHGIAINCNTDLRWFDNIVGCGIEGVSTTSLSQETSRNVTVSDAR 215
Cdd:PRK14348  158 SHYVTMHGLALNVNTDLRYFSYIHPCGFIDKGVTSLQQELGHSIDMAEVK 207
BPL_LplA_LipB cd16435
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ...
 17-222 9.73e-33

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: 118.02  E-value: 9.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  17 DLGQISYGAALKEQQKYVDLVKANKSEThslnFILaLEHTPVYTVGIRSKGYTKEEETRLMRLGAEFHRTSRGGLITFHG 96
Cdd:cd16435     4 VLDSVDYESAWAAQEKSLRENVSNQSST----LLL-WEHPTTVTLGRLDRELPHLELAKKIERGYELVVRNRGGRAVSHD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  97 PGQLVLYPICDVRRisikQLGVRHFVDKLEQTIIDAAtEGFGIKNVGRTANTGVWVsNERKLAAIGIAVSGGVSYHGIAI 176
Cdd:cd16435    79 PGQLVFSPVIGPNV----EFMISKFNLIIEEGIRDAI-ADFGQSAEVKWGRNDLWI-DNRKVCGIAVRVVKEAIFHGIAL 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1143467785 177 NCNTDLRWFDNIVGCGIEGVSTTSLSQETSRNVTVSDARPILLNAF 222
Cdd:cd16435   153 NLNQDLENFTEIIPCGYKPERVTSLSLELGRKVTVEQVLERVLAAF 198
PRK14343 PRK14343
lipoyl(octanoyl) transferase LipB;
16-198 2.61e-28

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237682  Cd Length: 235  Bit Score: 107.57  E-value: 2.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  16 IDLGQISYGAALKEQQKYVDLVKANKSEThslnfILALEHTPVYTVGIRSKgytkeeETRLMRLGAEFH--RTSRGGLIT 93
Cdd:PRK14343   18 RWRGREPYEACFDAMRAFTDARTADTPDE-----IWLVEHPPVYTLGQAGD------PAHLLVADSGIPlvKVDRGGQIT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  94 FHGPGQLVLYPICDVRRisiKQLGVRHFVDKLEQTIID--AAtegFGIKNVGRTANTGVWVSNER----KLAAIGIAVSG 167
Cdd:PRK14343   87 YHGPGQVVAYLLLDLRR---RKLMVRELVTRIEQAVIDtlAA---YNLASERKAGAPGIYVASGPhqgaKIAALGLKIRN 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1143467785 168 GVSYHGIAINCNTDLRWFDNIVGCGIEGVST 198
Cdd:PRK14343  161 GCSYHGLSLNVKMDLRPFLAINPCGYAGLET 191
PRK14347 PRK14347
lipoyl(octanoyl) transferase LipB;
21-203 1.26e-26

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 172823  Cd Length: 209  Bit Score: 102.32  E-value: 1.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  21 ISYGAALKEQQKYVDLVkankSETHSLNFILALEHTPVYTVGirsKGYTKEEETRLMRLGAEFhrTSRGGLITFHGPGQL 100
Cdd:PRK14347   11 ADYQVTLKLMEDYVNKV----ISDHEPEIVYLVEHSEVYTAG---TNYKQEELLNYGDIPVIY--TGRGGKFTFHGPGQR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785 101 VLYPICDVRRISiKQLGVRHFVDKLEQTIIDAATEgFGIKNVGRTANTGVWVSNER----KLAAIGIAVSGGVSYHGIAI 176
Cdd:PRK14347   82 VIYPILNLASPN-RHKDLKLYIKMLEEWIINSLNY-FGIKAYIIKDKVGIWVKVRKdefaKIAAIGVRVRKWVTYHGVAI 159

                         170       180
                  ....*....|....*....|....*..
gi 1143467785 177 NCNTDLRWFDNIVGCGIEGVSTTSLSQ 203
Cdd:PRK14347  160 NISTDLSKFSGIIPCGLENSLVTSLNQ 186
PRK14349 PRK14349
lipoyl(octanoyl) transferase LipB;
54-202 4.35e-25

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 172825  Cd Length: 220  Bit Score: 98.89  E-value: 4.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  54 EHTPVYTVGIRSKgytkeeETRLMRLGA-EFHRTSRGGLITFHGPGQLVLYPICDVRRISikqLGVRHFVDKLEQTIIdA 132
Cdd:PRK14349   37 EHAPVYTLGQAGR------PEHLLNPGLiPVVHCDRGGQVTYHGPGQVLAYTLFDLRRAG---LYVREYVDMLEQATL-A 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1143467785 133 ATEGFGIKNVGRTANT-GVWVSNE----RKLAAIGIAVSGGVSYHGIAINCNTDLRWFDNIVGCGIEGVSTTSLS 202
Cdd:PRK14349  107 TLRELGLEQACRKPGApGIYVPQPggelAKIAALGVKVRNGYAYHGLALNIDMDLSPFLGINPCGYEGLRTVDLA 181
PRK14346 PRK14346
lipoyl(octanoyl) transferase LipB;
18-202 7.06e-21

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237684  Cd Length: 230  Bit Score: 87.89  E-value: 7.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  18 LGQISYGAALKEQQKYVdlvKANKSETHSLNFILalEHTPVYTVGIRSKgytkeEETRLMRLGAEFHRTSRGGLITFHGP 97
Cdd:PRK14346    8 LGRVDYLATVQAMQAFT---AERTPETPDELWIC--EHPPVYTQGLAGK-----ADHVLNPGDIPVVATNRGGQVTYHGP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143467785  98 GQLVLYPICDVRRISIKqlgVRHFVDKLEQTIIdAATEGFGIKNVGRTANTGVWVSNER--------------------- 156
Cdd:PRK14346   78 GQVVAYPLIDLRRAGYF---VKEYVYRIEEAVI-RTLAHFGVTGHRVAGAPGIYVRLDDpfshaalpqrpqkrgggapqp 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1143467785 157 ------KLAAIGIAVSGGVSYHGIAINCNTDLRWFDNIVGCGIEGVSTTSLS 202
Cdd:PRK14346  154 pfrglgKIAALGIKVSRHCTYHGVALNVAMDLEPFSRINPCGYAGLQTVDLS 205
 
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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