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Conserved domains on  [gi|489927955|ref|WP_003831286|]
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MULTISPECIES: lipoyl(octanoyl) transferase LipB [Citrobacter]

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;
1-213 1.07e-155

lipoyl(octanoyl) transferase LipB;


:

Pssm-ID: 237681  Cd Length: 213  Bit Score: 429.30  E-value: 1.07e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955   1 MYQDKILVRQLGLQPYEPVSLAMHEFTDTRDENSYDEIWLVEHYPVFTQGQAGKAEHVLMPGDIPVIQSDRGGQVTYHGP 80
Cdd:PRK14342   1 MMQNKLIVRQLGLQPYEPVWQAMQEFTDTRDEETPDEIWLVEHPPVFTQGQAGKPEHILNPGDIPVVQSDRGGQVTYHGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955  81 GQQVMYVLLNLKRRKLGVRELVTLLEQTVVNTLAEIGIDAHPRADAPGVYVGEKKICSLGLRIRKGCSFHGLALNVDMDL 160
Cdd:PRK14342  81 GQLVMYVLLDLKRLKLGVRQLVTAIEQTVINTLAEYGIEAHAKPDAPGVYVDGKKIASLGLRIRRGCSFHGLALNVNMDL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489927955 161 SPFLRINPCGYAGMEMAKVSQWDSTATTESIRPRLLANILALLGNPPHEYIAD 213
Cdd:PRK14342 161 SPFLRINPCGYAGLEMTQLSDLGGPATVDEVAPRLLAELLALLGYNDQETITG 213
 
Name Accession Description Interval E-value
PRK14342 PRK14342
lipoyl(octanoyl) transferase LipB;
1-213 1.07e-155

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237681  Cd Length: 213  Bit Score: 429.30  E-value: 1.07e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955   1 MYQDKILVRQLGLQPYEPVSLAMHEFTDTRDENSYDEIWLVEHYPVFTQGQAGKAEHVLMPGDIPVIQSDRGGQVTYHGP 80
Cdd:PRK14342   1 MMQNKLIVRQLGLQPYEPVWQAMQEFTDTRDEETPDEIWLVEHPPVFTQGQAGKPEHILNPGDIPVVQSDRGGQVTYHGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955  81 GQQVMYVLLNLKRRKLGVRELVTLLEQTVVNTLAEIGIDAHPRADAPGVYVGEKKICSLGLRIRKGCSFHGLALNVDMDL 160
Cdd:PRK14342  81 GQLVMYVLLDLKRLKLGVRQLVTAIEQTVINTLAEYGIEAHAKPDAPGVYVDGKKIASLGLRIRRGCSFHGLALNVNMDL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489927955 161 SPFLRINPCGYAGMEMAKVSQWDSTATTESIRPRLLANILALLGNPPHEYIAD 213
Cdd:PRK14342 161 SPFLRINPCGYAGLEMTQLSDLGGPATVDEVAPRLLAELLALLGYNDQETITG 213
LipB COG0321
Lipoate-protein ligase B [Coenzyme transport and metabolism]; Lipoate-protein ligase B is part ...
 4-209 5.42e-115

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: 326.29  E-value: 5.42e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955   4 DKILVRQLGLQPYEPVSLAMHEFTDTR-DENSYDEIWLVEHYPVFTQGQAGKAEHVLMPGDIPVIQSDRGGQVTYHGPGQ 82
Cdd:COG0321    2 RPLIIRDLGLVDYEEAWAAQRRLTAARvAGDTPDELWLLEHPPVYTLGRSGKPEHLLAPGGIPVVQTDRGGQITYHGPGQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955  83 QVMYVLLNLKRRKLGVRELVTLLEQTVVNTLAEIGIDAHPRADAPGVYVGEKKICSLGLRIRKGCSFHGLALNVDMDLSP 162
Cdd:COG0321   82 LVGYPILDLRRRGLDVRAYVRRLEEAVIDTLAEYGIEAERRPGAPGVWVDGRKIAAIGLRVRRGVTYHGFALNVNPDLSP 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 489927955 163 FLRINPCGYAGMEMAKVSQW-DSTATTESIRPRLLANILALLGNPPHE 209
Cdd:COG0321  162 FSRIVPCGIADLGVTSLSDElGRPVTMEEVAEALIRHFAEVFGYELVE 209
LipB cd16444
lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein] ...
 7-203 9.21e-110

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: 312.50  E-value: 9.21e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955   7 LVRQLGLQPYEPVSLAMHEFTDTRDE-NSYDEIWLVEHYPVFTQGQAGKAEHVLMPGDIPVIQSDRGGQVTYHGPGQQVM 85
Cdd:cd16444    1 IVRDLGLIPYEEAWELQKRLVAERIAgETPDTLWLLEHPPVYTLGRRGKPENLLNNGGIPVVRTDRGGQVTYHGPGQLVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955  86 YVLLNLKRRKLGVRELVTLLEQTVVNTLAEIGIDAHPRADAPGVYVGEKKICSLGLRIRKGCSFHGLALNVDMDLSPFLR 165
Cdd:cd16444   81 YPILDLRRRGLDVRRYVRALEEAVIRTLAEYGIEAGRRPGAPGVWVGDRKIASIGIRVRRGVTYHGLALNVNTDLSPFNR 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 489927955 166 INPCGYAGMEMAKVSQW-DSTATTESIRPRLLANILALL 203
Cdd:cd16444  161 INPCGIKGKGVTSLSDLgGREVDMEEVKQKLVEEFAKIF 199
lipB TIGR00214
lipoate-protein ligase B; Involved in lipoate biosynthesis as the main determinant of the ...
 26-204 1.46e-101

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: 291.31  E-value: 1.46e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955   26 FTDT--RDENSYDEIWLVEHYPVFTQGQAGKAEHVLMPGDIP---VIQSDRGGQVTYHGPGQQVMYVLLNLKRRKLGVRE 100
Cdd:TIGR00214   1 FTDTkqRDRQTLDEIMLVEHYPVYTQGQAGKTEHLLFDPDIPpaeVVQSERGGQVTYHGPGQQVMYVILDLKRFQLDVRW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955  101 LVTLLEQTVVNTLAEIGIDAHPRADAPGVYVGEKKICSLGLRIRKGCSFHGLALNVDMDLSPFLRINPCGYAGMEMAKVS 180
Cdd:TIGR00214  81 LVTQLEQTVIITLAELGIEGEPIADATGVWVEGKKVASLGIRVRRGCTFHGLALNINMDLSPFSHINPCGYAGREMGSLN 160

                         170       180
                  ....*....|....*....|....
gi 489927955  181 QWDSTATTESIRPRLLANILALLG 204
Cdd:TIGR00214 161 QFLPGATVENVAPLLIKAFAELLG 184
 
Name Accession Description Interval E-value
PRK14342 PRK14342
lipoyl(octanoyl) transferase LipB;
1-213 1.07e-155

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237681  Cd Length: 213  Bit Score: 429.30  E-value: 1.07e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955   1 MYQDKILVRQLGLQPYEPVSLAMHEFTDTRDENSYDEIWLVEHYPVFTQGQAGKAEHVLMPGDIPVIQSDRGGQVTYHGP 80
Cdd:PRK14342   1 MMQNKLIVRQLGLQPYEPVWQAMQEFTDTRDEETPDEIWLVEHPPVFTQGQAGKPEHILNPGDIPVVQSDRGGQVTYHGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955  81 GQQVMYVLLNLKRRKLGVRELVTLLEQTVVNTLAEIGIDAHPRADAPGVYVGEKKICSLGLRIRKGCSFHGLALNVDMDL 160
Cdd:PRK14342  81 GQLVMYVLLDLKRLKLGVRQLVTAIEQTVINTLAEYGIEAHAKPDAPGVYVDGKKIASLGLRIRRGCSFHGLALNVNMDL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489927955 161 SPFLRINPCGYAGMEMAKVSQWDSTATTESIRPRLLANILALLGNPPHEYIAD 213
Cdd:PRK14342 161 SPFLRINPCGYAGLEMTQLSDLGGPATVDEVAPRLLAELLALLGYNDQETITG 213
LipB COG0321
Lipoate-protein ligase B [Coenzyme transport and metabolism]; Lipoate-protein ligase B is part ...
 4-209 5.42e-115

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: 326.29  E-value: 5.42e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955   4 DKILVRQLGLQPYEPVSLAMHEFTDTR-DENSYDEIWLVEHYPVFTQGQAGKAEHVLMPGDIPVIQSDRGGQVTYHGPGQ 82
Cdd:COG0321    2 RPLIIRDLGLVDYEEAWAAQRRLTAARvAGDTPDELWLLEHPPVYTLGRSGKPEHLLAPGGIPVVQTDRGGQITYHGPGQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955  83 QVMYVLLNLKRRKLGVRELVTLLEQTVVNTLAEIGIDAHPRADAPGVYVGEKKICSLGLRIRKGCSFHGLALNVDMDLSP 162
Cdd:COG0321   82 LVGYPILDLRRRGLDVRAYVRRLEEAVIDTLAEYGIEAERRPGAPGVWVDGRKIAAIGLRVRRGVTYHGFALNVNPDLSP 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 489927955 163 FLRINPCGYAGMEMAKVSQW-DSTATTESIRPRLLANILALLGNPPHE 209
Cdd:COG0321  162 FSRIVPCGIADLGVTSLSDElGRPVTMEEVAEALIRHFAEVFGYELVE 209
LipB cd16444
lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein] ...
 7-203 9.21e-110

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: 312.50  E-value: 9.21e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955   7 LVRQLGLQPYEPVSLAMHEFTDTRDE-NSYDEIWLVEHYPVFTQGQAGKAEHVLMPGDIPVIQSDRGGQVTYHGPGQQVM 85
Cdd:cd16444    1 IVRDLGLIPYEEAWELQKRLVAERIAgETPDTLWLLEHPPVYTLGRRGKPENLLNNGGIPVVRTDRGGQVTYHGPGQLVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955  86 YVLLNLKRRKLGVRELVTLLEQTVVNTLAEIGIDAHPRADAPGVYVGEKKICSLGLRIRKGCSFHGLALNVDMDLSPFLR 165
Cdd:cd16444   81 YPILDLRRRGLDVRRYVRALEEAVIRTLAEYGIEAGRRPGAPGVWVGDRKIASIGIRVRRGVTYHGLALNVNTDLSPFNR 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 489927955 166 INPCGYAGMEMAKVSQW-DSTATTESIRPRLLANILALL 203
Cdd:cd16444  161 INPCGIKGKGVTSLSDLgGREVDMEEVKQKLVEEFAKIF 199
lipB TIGR00214
lipoate-protein ligase B; Involved in lipoate biosynthesis as the main determinant of the ...
 26-204 1.46e-101

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: 291.31  E-value: 1.46e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955   26 FTDT--RDENSYDEIWLVEHYPVFTQGQAGKAEHVLMPGDIP---VIQSDRGGQVTYHGPGQQVMYVLLNLKRRKLGVRE 100
Cdd:TIGR00214   1 FTDTkqRDRQTLDEIMLVEHYPVYTQGQAGKTEHLLFDPDIPpaeVVQSERGGQVTYHGPGQQVMYVILDLKRFQLDVRW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955  101 LVTLLEQTVVNTLAEIGIDAHPRADAPGVYVGEKKICSLGLRIRKGCSFHGLALNVDMDLSPFLRINPCGYAGMEMAKVS 180
Cdd:TIGR00214  81 LVTQLEQTVIITLAELGIEGEPIADATGVWVEGKKVASLGIRVRRGCTFHGLALNINMDLSPFSHINPCGYAGREMGSLN 160

                         170       180
                  ....*....|....*....|....
gi 489927955  181 QWDSTATTESIRPRLLANILALLG 204
Cdd:TIGR00214 161 QFLPGATVENVAPLLIKAFAELLG 184
PRK14343 PRK14343
lipoyl(octanoyl) transferase LipB;
6-203 2.60e-93

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237682  Cd Length: 235  Bit Score: 272.43  E-value: 2.60e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955   6 ILVRQLGLQPYEPVSLAMHEFTDTRDENSYDEIWLVEHYPVFTQGQAGKAEHVLMPGD-IPVIQSDRGGQVTYHGPGQQV 84
Cdd:PRK14343  15 VTVRWRGREPYEACFDAMRAFTDARTADTPDEIWLVEHPPVYTLGQAGDPAHLLVADSgIPLVKVDRGGQITYHGPGQVV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955  85 MYVLLNLKRRKLGVRELVTLLEQTVVNTLAEIGIDAHPRADAPGVYVGE-----KKICSLGLRIRKGCSFHGLALNVDMD 159
Cdd:PRK14343  95 AYLLLDLRRRKLMVRELVTRIEQAVIDTLAAYNLASERKAGAPGIYVASgphqgAKIAALGLKIRNGCSYHGLSLNVKMD 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 489927955 160 LSPFLRINPCGYAGMEMAKVSQWDSTATTESIRPRLLANILALL 203
Cdd:PRK14343 175 LRPFLAINPCGYAGLETVDMASLGVAADWADVAQTLARRLIANL 218
PRK14346 PRK14346
lipoyl(octanoyl) transferase LipB;
6-186 6.87e-74

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237684  Cd Length: 230  Bit Score: 223.09  E-value: 6.87e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955   6 ILVRQLGLQPYEPVSLAMHEFTDTRDENSYDEIWLVEHYPVFTQGQAGKAEHVLMPGDIPVIQSDRGGQVTYHGPGQQVM 85
Cdd:PRK14346   3 MDRRMLGRVDYLATVQAMQAFTAERTPETPDELWICEHPPVYTQGLAGKADHVLNPGDIPVVATNRGGQVTYHGPGQVVA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955  86 YVLLNLKRRKLGVRELVTLLEQTVVNTLAEIGIDAHPRADAPGVYV----------------------------GEKKIC 137
Cdd:PRK14346  83 YPLIDLRRAGYFVKEYVYRIEEAVIRTLAHFGVTGHRVAGAPGIYVrlddpfshaalpqrpqkrgggapqppfrGLGKIA 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489927955 138 SLGLRIRKGCSFHGLALNVDMDLSPFLRINPCGYAGMEMAKVS------QWDSTA 186
Cdd:PRK14346 163 ALGIKVSRHCTYHGVALNVAMDLEPFSRINPCGYAGLQTVDLStigvqtTWDEAA 217
PRK14349 PRK14349
lipoyl(octanoyl) transferase LipB;
16-212 8.90e-72

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 172825  Cd Length: 220  Bit Score: 217.53  E-value: 8.90e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955  16 YEPVSLAMHEFTDTRDENSYDEIWLVEHYPVFTQGQAGKAEHVLMPGDIPVIQSDRGGQVTYHGPGQQVMYVLLNLKRRK 95
Cdd:PRK14349  11 YASVWDAMKAFTAARGPGTADEIWLCEHAPVYTLGQAGRPEHLLNPGLIPVVHCDRGGQVTYHGPGQVLAYTLFDLRRAG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955  96 LGVRELVTLLEQTVVNTLAEIGI-DAHPRADAPGVYV----GE-KKICSLGLRIRKGCSFHGLALNVDMDLSPFLRINPC 169
Cdd:PRK14349  91 LYVREYVDMLEQATLATLRELGLeQACRKPGAPGIYVpqpgGElAKIAALGVKVRNGYAYHGLALNIDMDLSPFLGINPC 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489927955 170 GYAGMEMAKVSQWDSTATTESIRPRLLANILALLGNPPHEYIA 212
Cdd:PRK14349 171 GYEGLRTVDLAACGVRTSVERAGELLAAQLARAHGQAVQQRAA 213
PRK14341 PRK14341
lipoyl(octanoyl) transferase LipB;
12-170 2.67e-52

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237680  Cd Length: 213  Bit Score: 167.39  E-value: 2.67e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955  12 GLQPYEPVSLAM-HEFTDTRDENSYDEIWLVEHYPVFTQGQAGKAEHVLMPGDIPVIQSDRGGQVTYHGPGQQVMYVLLN 90
Cdd:PRK14341  11 GLVPYPEALAFMeARVAAIAAGTADELVWLLEHPPLYTAGTSAKAEDLLDPDRFPVYETGRGGQYTYHGPGQRVAYVMLD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955  91 LKRRKLGVRELVTLLEQTVVNTLAEIGIDAHPRADAPGVYV--------GEKKICSLGLRIRKGCSFHGLALNVDMDLSP 162
Cdd:PRK14341  91 LKRRRRDVRAFVAALEEWIIATLAAFNIRGERREDRVGVWVrrpdkgsgAEDKIAAIGVRLRRWVSFHGISINVEPDLSH 170


                 ....*...
gi 489927955 163 FLRINPCG 170
Cdd:PRK14341 171 FSGIVPCG 178
PRK14344 PRK14344
lipoyl(octanoyl) transferase LipB;
31-201 4.17e-38

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237683  Cd Length: 223  Bit Score: 131.34  E-value: 4.17e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955  31 DENSYDEIWLVEHYPVFTQGQAGKAEHVLMPGD---IPVIQSDRGGQVTYHGPGQQVMYVLLNLKRRKLGVRELVTLLEQ 107
Cdd:PRK14344  46 DPSNPQAVWLLEHQLCYTLGRGASEDNLLFSLNnppADVFRIDRGGEVTHHMPGQLVTYLVLDLRRFNKDLNWYLRQLEQ 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955 108 TVVNTLAEIGIDAHPRADAPGVYVGEKKICSLGLRIRKGCSFHGLALNVDMDLSPFLRINPCGYAGMEMAKVSQWDSTAT 187
Cdd:PRK14344 126 VLIDVLADLGIDGERLDGLTGVWIGNKKVASIGIGCRRWITQHGFSLNVDCDLEGFNKIVPCGLEGCQVGRLSDWIPGLN 205

                        170
                 ....*....|....
gi 489927955 188 TESIRPrLLANILA 201
Cdd:PRK14344 206 IKEVKP-LLKKSLQ 218
PRK14347 PRK14347
lipoyl(octanoyl) transferase LipB;
31-170 2.78e-33

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 172823  Cd Length: 209  Bit Score: 118.50  E-value: 2.78e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955  31 DENSYDEIWLVEHYPVFTQGQAGKAEHVLMPGDIPVIQSDRGGQVTYHGPGQQVMYVLLNLK--RRKLGVRELVTLLEQT 108
Cdd:PRK14347  29 SDHEPEIVYLVEHSEVYTAGTNYKQEELLNYGDIPVIYTGRGGKFTFHGPGQRVIYPILNLAspNRHKDLKLYIKMLEEW 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489927955 109 VVNTLAEIGIDAHPRADAPGVYVGEK-----KICSLGLRIRKGCSFHGLALNVDMDLSPFLRINPCG 170
Cdd:PRK14347 109 IINSLNYFGIKAYIIKDKVGIWVKVRkdefaKIAAIGVRVRKWVTYHGVAINISTDLSKFSGIIPCG 175
PRK14345 PRK14345
lipoyl(octanoyl) transferase LipB;
6-203 6.14e-33

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 184638  Cd Length: 234  Bit Score: 118.55  E-value: 6.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955   6 ILVRQLGLQPYEPVSLAMHEFTDTRDENSY-DEIWLVEHYPVFTqgqAGK-AEHVLMPGD-IPVIQSDRGGQVTYHGPGQ 82
Cdd:PRK14345  12 IEVRRLGLVDYQEAWDLQRELADARVAGEGpDTLLLLEHPAVYT---AGKrTEPHERPTDgTPVVDVDRGGKITWHGPGQ 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955  83 QVMYVLLNLKRRkLGVRELVTLLEQTVVNTLAEIGIDAHPRADAPGVYV------GEKKICSLGLRIRKGCSFHGLALNV 156
Cdd:PRK14345  89 LVGYPIIKLAEP-LDVVDYVRRLEEALIAVCADLGLNAGRVDGRSGVWVpadggrPDRKIAAIGIRVSRGVTMHGFALNC 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489927955 157 DMDLSPFLRINPCGY--AGM-----EMAKvsqwdsTATTESIRPRLLANILALL 203
Cdd:PRK14345 168 DNDLAAFDAIVPCGIsdAGVttlsaELGR------TVTVAEVVDPVAAALCDAL 215
PRK14348 PRK14348
lipoyl(octanoyl) transferase LipB;
5-203 2.92e-31

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 172824  Cd Length: 221  Bit Score: 113.58  E-value: 2.92e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955   5 KILVRQLGLQPYEPVSLAMHEFTDT------RDENSYDEIWLVEHYPVFTQGQAGKAEHVLMPGD-IPVIQS-----DRG 72
Cdd:PRK14348   2 KTITTDWELIPYSEAWSRQTEWFDAlvhakqNGESYENRIIFCEHPHVYTLGRSGKENNMLLGEEqLKTIGAtlyhiDRG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955  73 GQVTYHGPGQQVMYVLLNLKRRKLGVRELVTLLEQTVVNTLAEIGIDAHPRADAPGVYVG-----EKKICSLGLRIRKGC 147
Cdd:PRK14348  82 GDITYHGPGQLVCYPILNLEEFGLGLKEYVHLLEEAVIRVCASYGVVAGRLEKATGVWLEgdtsrARKICAIGVRSSHYV 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489927955 148 SFHGLALNVDMDLSPFLRINPCGYAGMEMAKVSQ-WDSTATTESIRPRLLANILALL 203
Cdd:PRK14348 162 TMHGLALNVNTDLRYFSYIHPCGFIDKGVTSLQQeLGHSIDMAEVKERLGRELLAAL 218
BPL_LplA_LipB cd16435
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ...
 7-199 4.20e-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: 97.22  E-value: 4.20e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955   7 LVRQLGLQPYEPVSLAMHEFTDTRDENSYDEIWLVEHYPVFTQGQAGKAEHVLMPGD-----IPVIQSDRGGQVTYHGPG 81
Cdd:cd16435    1 FVEVLDSVDYESAWAAQEKSLRENVSNQSSTLLLWEHPTTVTLGRLDRELPHLELAKkiergYELVVRNRGGRAVSHDPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955  82 QQVMYVLLNlKRRKLGVRELVTLLEQTVVNTLAEIGIDAHPRADAPGVYVGEKKICSLGLRIRKGCSFHGLALNVDMDLS 161
Cdd:cd16435   81 QLVFSPVIG-PNVEFMISKFNLIIEEGIRDAIADFGQSAEVKWGRNDLWIDNRKVCGIAVRVVKEAIFHGIALNLNQDLE 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 489927955 162 PFLRINPCGYAGMEMAKVS-QWDSTATTESIRPRLLANI 199
Cdd:cd16435  160 NFTEIIPCGYKPERVTSLSlELGRKVTVEQVLERVLAAF 198
LplA COG0095
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part ...
 72-207 1.69e-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: 50.23  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955  72 GGQVtYHGPGQqVMY-VLLNLKRRKLGVRELVTLLEQTVVNTLAEIGIDAH--PRADapgVYVGEKKICSLGLRIRKGCS 148
Cdd:COG0095   73 GGAV-YHDPGN-LNYsLILPEDDVPLSIEESYRKLLEPILEALRKLGVDAEfsGRND---IVVDGRKISGNAQRRRKGAV 147

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489927955 149 F-HG-LALNVDMD-LSPFLRINPcgyagmemAKVSQWdstaTTESIRPRlLANILALLGNPP 207
Cdd:COG0095  148 LhHGtLLVDGDLEkLAKVLRVPY--------EKLRDK----GIKSVRSR-VTNLSELLGTDI 196
LplA cd16443
lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide ...
 63-166 3.46e-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: 48.79  E-value: 3.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489927955  63 DIPVIQSDRGGQVTYHGPGQqVMYVLLnLKRRKLGVRELVTLLEQTVVNTLAEIGIDAHPRAdaPGVY---VGEKKICSL 139
Cdd:cd16443   63 GIPVVRRPSGGGAVFHDLGN-LNYSLI-LPKEHPSIDESYRALSQPVIKALRKLGVEAEFGG--VGRNdlvVGGKKISGS 138

                         90       100
                 ....*....|....*....|....*..
gi 489927955 140 GLRIRKGCSFHGLALNVDMDLSPFLRI 166
Cdd:cd16443  139 AQRRTKGRILHHGTLLVDVDLEKLARV 165
 
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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