NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|502667345|ref|WP_012903257|]
View 

lipoyl(octanoyl) transferase LipB [Rothia mucilaginosa]

Protein Classification

lipoate-protein ligase B( domain architecture ID 10014643)

lipoyl/octanoyltransferase catalyzes the transfer of the lipoyl/octanoyl moiety of lipoyl/octanoyl-ACP onto lipoate-dependent enzymes like pyruvate dehydrogenase and the glycine cleavage system H protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK14345 PRK14345
lipoyl(octanoyl) transferase LipB;
1-223 1.81e-128

lipoyl(octanoyl) transferase LipB;


:

Pssm-ID: 184638  Cd Length: 234  Bit Score: 361.99  E-value: 1.81e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345   1 MSVTIERVGFapnyVNYVECLDEQYRIHDEVANRTRQNTILLLEHEAVITAGKRTEDHEYPADkSTPVVKIDRGGKLTWH 80
Cdd:PRK14345  10 MPIEVRRLGL----VDYQEAWDLQRELADARVAGEGPDTLLLLEHPAVYTAGKRTEPHERPTD-GTPVVDVDRGGKITWH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  81 GPGQLTGYPILRLPEPIDVVAYVRIIEEIIINVLAGLGIKGERVEGRSGVWILGDGVTQDKKIAALGMRVSRNTTMHGFA 160
Cdd:PRK14345  85 GPGQLVGYPIIKLAEPLDVVDYVRRLEEALIAVCADLGLNAGRVDGRSGVWVPADGGRPDRKIAAIGIRVSRGVTMHGFA 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502667345 161 INCCNDTAPFQQFIPCGISDAGVTTISEQLGRTVTPADILEPLEAELLKYQD-RLAESFEPVAA 223
Cdd:PRK14345 165 LNCDNDLAAFDAIVPCGISDAGVTTLSAELGRTVTVAEVVDPVAAALCDALDgRLPVRDHSPGS 228
 
Name Accession Description Interval E-value
PRK14345 PRK14345
lipoyl(octanoyl) transferase LipB;
1-223 1.81e-128

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 184638  Cd Length: 234  Bit Score: 361.99  E-value: 1.81e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345   1 MSVTIERVGFapnyVNYVECLDEQYRIHDEVANRTRQNTILLLEHEAVITAGKRTEDHEYPADkSTPVVKIDRGGKLTWH 80
Cdd:PRK14345  10 MPIEVRRLGL----VDYQEAWDLQRELADARVAGEGPDTLLLLEHPAVYTAGKRTEPHERPTD-GTPVVDVDRGGKITWH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  81 GPGQLTGYPILRLPEPIDVVAYVRIIEEIIINVLAGLGIKGERVEGRSGVWILGDGVTQDKKIAALGMRVSRNTTMHGFA 160
Cdd:PRK14345  85 GPGQLVGYPIIKLAEPLDVVDYVRRLEEALIAVCADLGLNAGRVDGRSGVWVPADGGRPDRKIAAIGIRVSRGVTMHGFA 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502667345 161 INCCNDTAPFQQFIPCGISDAGVTTISEQLGRTVTPADILEPLEAELLKYQD-RLAESFEPVAA 223
Cdd:PRK14345 165 LNCDNDLAAFDAIVPCGISDAGVTTLSAELGRTVTVAEVVDPVAAALCDALDgRLPVRDHSPGS 228
LipB COG0321
Lipoate-protein ligase B [Coenzyme transport and metabolism]; Lipoate-protein ligase B is part ...
1-209 2.65e-93

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: 271.98  E-value: 2.65e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345   1 MSVTIERVGFapnyVNYVECLDEQYRIHDEVANRTRQNTILLLEHEAVITAGKRTEDHEYPADKSTPVVKIDRGGKLTWH 80
Cdd:COG0321    2 RPLIIRDLGL----VDYEEAWAAQRRLTAARVAGDTPDELWLLEHPPVYTLGRSGKPEHLLAPGGIPVVQTDRGGQITYH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  81 GPGQLTGYPILRLP-EPIDVVAYVRIIEEIIINVLAGLGIKGERVEGRSGVWIlgdgvtQDKKIAALGMRVSRNTTMHGF 159
Cdd:COG0321   78 GPGQLVGYPILDLRrRGLDVRAYVRRLEEAVIDTLAEYGIEAERRPGAPGVWV------DGRKIAAIGLRVRRGVTYHGF 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 502667345 160 AINCCNDTAPFQQFIPCGISDAGVTTISEQLGRTVTPADILEPLEAELLK 209
Cdd:COG0321  152 ALNVNPDLSPFSRIVPCGIADLGVTSLSDELGRPVTMEEVAEALIRHFAE 201
LipB cd16444
lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein] ...
15-209 1.68e-89

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: 262.04  E-value: 1.68e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  15 VNYVECLDEQYRIHDEVANRTRQNTILLLEHEAVITAGKRTEDHEYPADKSTPVVKIDRGGKLTWHGPGQLTGYPILRLP 94
Cdd:cd16444    8 IPYEEAWELQKRLVAERIAGETPDTLWLLEHPPVYTLGRRGKPENLLNNGGIPVVRTDRGGQVTYHGPGQLVGYPILDLR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  95 EP-IDVVAYVRIIEEIIINVLAGLGIKGERVEGRSGVWIlgdgvtQDKKIAALGMRVSRNTTMHGFAINCCNDTAPFQQF 173
Cdd:cd16444   88 RRgLDVRRYVRALEEAVIRTLAEYGIEAGRRPGAPGVWV------GDRKIASIGIRVRRGVTYHGLALNVNTDLSPFNRI 161
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 502667345 174 IPCGISDAGVTTISEQLGRTVTPADILEPLEAELLK 209
Cdd:cd16444  162 NPCGIKGKGVTSLSDLGGREVDMEEVKQKLVEEFAK 197
lipB TIGR00214
lipoate-protein ligase B; Involved in lipoate biosynthesis as the main determinant of the ...
33-190 3.65e-41

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: 138.39  E-value: 3.65e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345   33 NRTRQNTILLLEHEAVITAGK--RTE----DHEYPADKstpVVKIDRGGKLTWHGPGQLTGYPILRLPE-PIDVVAYVRI 105
Cdd:TIGR00214   8 DRQTLDEIMLVEHYPVYTQGQagKTEhllfDPDIPPAE---VVQSERGGQVTYHGPGQQVMYVILDLKRfQLDVRWLVTQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  106 IEEIIINVLAGLGIKGERVEGRSGVWILGdgvtqdKKIAALGMRVSRNTTMHGFAINCCNDTAPFQQFIPCGISDAGVTT 185
Cdd:TIGR00214  85 LEQTVIITLAELGIEGEPIADATGVWVEG------KKVASLGIRVRRGCTFHGLALNINMDLSPFSHINPCGYAGREMGS 158

                  ....*
gi 502667345  186 ISEQL 190
Cdd:TIGR00214 159 LNQFL 163
 
Name Accession Description Interval E-value
PRK14345 PRK14345
lipoyl(octanoyl) transferase LipB;
1-223 1.81e-128

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 184638  Cd Length: 234  Bit Score: 361.99  E-value: 1.81e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345   1 MSVTIERVGFapnyVNYVECLDEQYRIHDEVANRTRQNTILLLEHEAVITAGKRTEDHEYPADkSTPVVKIDRGGKLTWH 80
Cdd:PRK14345  10 MPIEVRRLGL----VDYQEAWDLQRELADARVAGEGPDTLLLLEHPAVYTAGKRTEPHERPTD-GTPVVDVDRGGKITWH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  81 GPGQLTGYPILRLPEPIDVVAYVRIIEEIIINVLAGLGIKGERVEGRSGVWILGDGVTQDKKIAALGMRVSRNTTMHGFA 160
Cdd:PRK14345  85 GPGQLVGYPIIKLAEPLDVVDYVRRLEEALIAVCADLGLNAGRVDGRSGVWVPADGGRPDRKIAAIGIRVSRGVTMHGFA 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502667345 161 INCCNDTAPFQQFIPCGISDAGVTTISEQLGRTVTPADILEPLEAELLKYQD-RLAESFEPVAA 223
Cdd:PRK14345 165 LNCDNDLAAFDAIVPCGISDAGVTTLSAELGRTVTVAEVVDPVAAALCDALDgRLPVRDHSPGS 228
LipB COG0321
Lipoate-protein ligase B [Coenzyme transport and metabolism]; Lipoate-protein ligase B is part ...
1-209 2.65e-93

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: 271.98  E-value: 2.65e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345   1 MSVTIERVGFapnyVNYVECLDEQYRIHDEVANRTRQNTILLLEHEAVITAGKRTEDHEYPADKSTPVVKIDRGGKLTWH 80
Cdd:COG0321    2 RPLIIRDLGL----VDYEEAWAAQRRLTAARVAGDTPDELWLLEHPPVYTLGRSGKPEHLLAPGGIPVVQTDRGGQITYH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  81 GPGQLTGYPILRLP-EPIDVVAYVRIIEEIIINVLAGLGIKGERVEGRSGVWIlgdgvtQDKKIAALGMRVSRNTTMHGF 159
Cdd:COG0321   78 GPGQLVGYPILDLRrRGLDVRAYVRRLEEAVIDTLAEYGIEAERRPGAPGVWV------DGRKIAAIGLRVRRGVTYHGF 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 502667345 160 AINCCNDTAPFQQFIPCGISDAGVTTISEQLGRTVTPADILEPLEAELLK 209
Cdd:COG0321  152 ALNVNPDLSPFSRIVPCGIADLGVTSLSDELGRPVTMEEVAEALIRHFAE 201
LipB cd16444
lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein] ...
15-209 1.68e-89

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: 262.04  E-value: 1.68e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  15 VNYVECLDEQYRIHDEVANRTRQNTILLLEHEAVITAGKRTEDHEYPADKSTPVVKIDRGGKLTWHGPGQLTGYPILRLP 94
Cdd:cd16444    8 IPYEEAWELQKRLVAERIAGETPDTLWLLEHPPVYTLGRRGKPENLLNNGGIPVVRTDRGGQVTYHGPGQLVGYPILDLR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  95 EP-IDVVAYVRIIEEIIINVLAGLGIKGERVEGRSGVWIlgdgvtQDKKIAALGMRVSRNTTMHGFAINCCNDTAPFQQF 173
Cdd:cd16444   88 RRgLDVRRYVRALEEAVIRTLAEYGIEAGRRPGAPGVWV------GDRKIASIGIRVRRGVTYHGLALNVNTDLSPFNRI 161
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 502667345 174 IPCGISDAGVTTISEQLGRTVTPADILEPLEAELLK 209
Cdd:cd16444  162 NPCGIKGKGVTSLSDLGGREVDMEEVKQKLVEEFAK 197
BPL_LplA_LipB cd16435
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ...
15-207 1.06e-51

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: 165.79  E-value: 1.06e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  15 VNYVECLDEQYRIHDEVaNRTRQNTILLLEHEAVITAGKRTEDHEYPADKS-----TPVVKIDRGGKLTWHGPGQLTGYP 89
Cdd:cd16435    8 VDYESAWAAQEKSLREN-VSNQSSTLLLWEHPTTVTLGRLDRELPHLELAKkiergYELVVRNRGGRAVSHDPGQLVFSP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  90 ILRLPEPIDVVAYVRIIEEIIINVLAGLGIKGERVEGRSGVWIlgdgvtQDKKIAALGMRVSRNTTMHGFAINCCNDTAP 169
Cdd:cd16435   87 VIGPNVEFMISKFNLIIEEGIRDAIADFGQSAEVKWGRNDLWI------DNRKVCGIAVRVVKEAIFHGIALNLNQDLEN 160
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 502667345 170 FQQFIPCGISDAGVTTISEQLGRTVTPADILEPLEAEL 207
Cdd:cd16435  161 FTEIIPCGYKPERVTSLSLELGRKVTVEQVLERVLAAF 198
PRK14341 PRK14341
lipoyl(octanoyl) transferase LipB;
11-221 3.26e-48

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237680  Cd Length: 213  Bit Score: 157.38  E-value: 3.26e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  11 APNYVNYVECLDEQYRIHDEVANRTRQNTILLLEHEAVITAGKRTEDHEYPADKSTPVVKIDRGGKLTWHGPGQLTGYPI 90
Cdd:PRK14341   9 SDGLVPYPEALAFMEARVAAIAAGTADELVWLLEHPPLYTAGTSAKAEDLLDPDRFPVYETGRGGQYTYHGPGQRVAYVM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  91 LRLPEP-IDVVAYVRIIEEIIINVLAGLGIKGERVEGRSGVWIL--GDGVTQDKKIAALGMRVSRNTTMHGFAINCCNDT 167
Cdd:PRK14341  89 LDLKRRrRDVRAFVAALEEWIIATLAAFNIRGERREDRVGVWVRrpDKGSGAEDKIAAIGVRLRRWVSFHGISINVEPDL 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 502667345 168 APFQQFIPCGISDAGVTTIsEQLGRTVTPADilepleaellkYQDRLAESFEPV 221
Cdd:PRK14341 169 SHFSGIVPCGISEHGVTSL-VDLGLPVTMDD-----------VDAALKKAFEKV 210
lipB TIGR00214
lipoate-protein ligase B; Involved in lipoate biosynthesis as the main determinant of the ...
33-190 3.65e-41

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: 138.39  E-value: 3.65e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345   33 NRTRQNTILLLEHEAVITAGK--RTE----DHEYPADKstpVVKIDRGGKLTWHGPGQLTGYPILRLPE-PIDVVAYVRI 105
Cdd:TIGR00214   8 DRQTLDEIMLVEHYPVYTQGQagKTEhllfDPDIPPAE---VVQSERGGQVTYHGPGQQVMYVILDLKRfQLDVRWLVTQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  106 IEEIIINVLAGLGIKGERVEGRSGVWILGdgvtqdKKIAALGMRVSRNTTMHGFAINCCNDTAPFQQFIPCGISDAGVTT 185
Cdd:TIGR00214  85 LEQTVIITLAELGIEGEPIADATGVWVEG------KKVASLGIRVRRGCTFHGLALNINMDLSPFSHINPCGYAGREMGS 158

                  ....*
gi 502667345  186 ISEQL 190
Cdd:TIGR00214 159 LNQFL 163
PRK14348 PRK14348
lipoyl(octanoyl) transferase LipB;
13-209 8.98e-39

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 172824  Cd Length: 221  Bit Score: 133.61  E-value: 8.98e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  13 NYVNYVECLDEQYR-----IHDEVANRTRQNTILLLEHEAVITAGKRTE-------DHEYPADKSTpVVKIDRGGKLTWH 80
Cdd:PRK14348   9 ELIPYSEAWSRQTEwfdalVHAKQNGESYENRIIFCEHPHVYTLGRSGKennmllgEEQLKTIGAT-LYHIDRGGDITYH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  81 GPGQLTGYPILRLPE-PIDVVAYVRIIEEIIINVLAGLGIKGERVEGRSGVWILGDgVTQDKKIAALGMRVSRNTTMHGF 159
Cdd:PRK14348  88 GPGQLVCYPILNLEEfGLGLKEYVHLLEEAVIRVCASYGVVAGRLEKATGVWLEGD-TSRARKICAIGVRSSHYVTMHGL 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 502667345 160 AINCCNDTAPFQQFIPCGISDAGVTTISEQLGRTVTPADILEPLEAELLK 209
Cdd:PRK14348 167 ALNVNTDLRYFSYIHPCGFIDKGVTSLQQELGHSIDMAEVKERLGRELLA 216
PRK14342 PRK14342
lipoyl(octanoyl) transferase LipB;
28-209 5.87e-36

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237681  Cd Length: 213  Bit Score: 126.15  E-value: 5.87e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  28 HDEVANRTRQNT--ILLLEHEAVIT---AGKRtEDHEYPADksTPVVKIDRGGKLTWHGPGQLTGYPILRLPE-PIDVVA 101
Cdd:PRK14342  24 QEFTDTRDEETPdeIWLVEHPPVFTqgqAGKP-EHILNPGD--IPVVQSDRGGQVTYHGPGQLVMYVLLDLKRlKLGVRQ 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345 102 YVRIIEEIIINVLAGLGIKGERVEGRSGVWIlgDGvtqdKKIAALGMRVSRNTTMHGFAINCCNDTAPFQQFIPCGISDA 181
Cdd:PRK14342 101 LVTAIEQTVINTLAEYGIEAHAKPDAPGVYV--DG----KKIASLGLRIRRGCSFHGLALNVNMDLSPFLRINPCGYAGL 174
                        170       180
                 ....*....|....*....|....*...
gi 502667345 182 GVTTISeQLGRTVTPADILEPLEAELLK 209
Cdd:PRK14342 175 EMTQLS-DLGGPATVDEVAPRLLAELLA 201
PRK14344 PRK14344
lipoyl(octanoyl) transferase LipB;
40-188 8.59e-36

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237683  Cd Length: 223  Bit Score: 125.95  E-value: 8.59e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  40 ILLLEHEAVITAGK-RTEDHEY--PADKSTPVVKIDRGGKLTWHGPGQLTGYPILRLPE-PIDVVAYVRIIEEIIINVLA 115
Cdd:PRK14344  53 VWLLEHQLCYTLGRgASEDNLLfsLNNPPADVFRIDRGGEVTHHMPGQLVTYLVLDLRRfNKDLNWYLRQLEQVLIDVLA 132
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502667345 116 GLGIKGERVEGRSGVWIlgdgvtQDKKIAALGMRVSRNTTMHGFAINCCNDTAPFQQFIPCGISDAGVTTISE 188
Cdd:PRK14344 133 DLGIDGERLDGLTGVWI------GNKKVASIGIGCRRWITQHGFSLNVDCDLEGFNKIVPCGLEGCQVGRLSD 199
PRK14347 PRK14347
lipoyl(octanoyl) transferase LipB;
12-209 4.41e-35

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 172823  Cd Length: 209  Bit Score: 123.51  E-value: 4.41e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  12 PNYVNYVECLDEQYRIHDEVANRTRQNTILLLEHEAVITAGKRTEDHEYPADKSTPVVKIDRGGKLTWHGPGQLTGYPIL 91
Cdd:PRK14347   8 PDFADYQVTLKLMEDYVNKVISDHEPEIVYLVEHSEVYTAGTNYKQEELLNYGDIPVIYTGRGGKFTFHGPGQRVIYPIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  92 RLPEP---IDVVAYVRIIEEIIINVLAGLGIKGERVEGRSGVWIlgdGVTQDK--KIAALGMRVSRNTTMHGFAINCCND 166
Cdd:PRK14347  88 NLASPnrhKDLKLYIKMLEEWIINSLNYFGIKAYIIKDKVGIWV---KVRKDEfaKIAAIGVRVRKWVTYHGVAINISTD 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 502667345 167 TAPFQQFIPCGISDAGVTTISeQLGRTVTPADILEPLEAELLK 209
Cdd:PRK14347 165 LSKFSGIIPCGLENSLVTSLN-QLGIHVEMSEFDKIIQTEFNK 206
PRK14343 PRK14343
lipoyl(octanoyl) transferase LipB;
38-208 3.52e-34

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237682  Cd Length: 235  Bit Score: 122.21  E-value: 3.52e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  38 NTILLLEHEAVIT---AGKRTedHEYPADKSTPVVKIDRGGKLTWHGPGQLTGYPILRLP-EPIDVVAYVRIIEEIIINV 113
Cdd:PRK14343  45 DEIWLVEHPPVYTlgqAGDPA--HLLVADSGIPLVKVDRGGQITYHGPGQVVAYLLLDLRrRKLMVRELVTRIEQAVIDT 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345 114 LAGLGIKGERVEGRSGVWiLGDGVTQDKKIAALGMRVSRNTTMHGFAINCCNDTAPFQQFIPCGIsdAGVTTISEQ-LGR 192
Cdd:PRK14343 123 LAAYNLASERKAGAPGIY-VASGPHQGAKIAALGLKIRNGCSYHGLSLNVKMDLRPFLAINPCGY--AGLETVDMAsLGV 199
                        170
                 ....*....|....*.
gi 502667345 193 TVTPADILEPLEAELL 208
Cdd:PRK14343 200 AADWADVAQTLARRLI 215
PRK14346 PRK14346
lipoyl(octanoyl) transferase LipB;
42-210 2.15e-27

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237684  Cd Length: 230  Bit Score: 104.07  E-value: 2.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  42 LLEHEAVITAGKRTEDHEYPADKSTPVVKIDRGGKLTWHGPGQLTGYPILRLPEP-IDVVAYVRIIEEIIINVLAGLGIK 120
Cdd:PRK14346  37 ICEHPPVYTQGLAGKADHVLNPGDIPVVATNRGGQVTYHGPGQVVAYPLIDLRRAgYFVKEYVYRIEEAVIRTLAHFGVT 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345 121 GERVEGRSGVWIL-----------------GDGVTQDK-----KIAALGMRVSRNTTMHGFAINCCNDTAPFQQFIPCGI 178
Cdd:PRK14346 117 GHRVAGAPGIYVRlddpfshaalpqrpqkrGGGAPQPPfrglgKIAALGIKVSRHCTYHGVALNVAMDLEPFSRINPCGY 196
                        170       180       190
                 ....*....|....*....|....*....|...
gi 502667345 179 sdAGVTTIS-EQLGRTVTPADILEPLEAELLKY 210
Cdd:PRK14346 197 --AGLQTVDlSTIGVQTTWDEAASVLGQQLARY 227
PRK14349 PRK14349
lipoyl(octanoyl) transferase LipB;
40-220 1.91e-23

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 172825  Cd Length: 220  Bit Score: 93.50  E-value: 1.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  40 ILLLEHEAVITAGK--RTEDHEYPADksTPVVKIDRGGKLTWHGPGQLTGYPILRLPEP-IDVVAYVRIIEEIIINVLAG 116
Cdd:PRK14349  33 IWLCEHAPVYTLGQagRPEHLLNPGL--IPVVHCDRGGQVTYHGPGQVLAYTLFDLRRAgLYVREYVDMLEQATLATLRE 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345 117 LGIKG-ERVEGRSGVWILGDGVTQdKKIAALGMRVSRNTTMHGFAINCCNDTAPFQQFIPCGIsDAGVTTISEQLGRTVT 195
Cdd:PRK14349 111 LGLEQaCRKPGAPGIYVPQPGGEL-AKIAALGVKVRNGYAYHGLALNIDMDLSPFLGINPCGY-EGLRTVDLAACGVRTS 188
                        170       180       190
                 ....*....|....*....|....*....|
gi 502667345 196 PADILEPLEAELLK-----YQDRLAESFEP 220
Cdd:PRK14349 189 VERAGELLAAQLARahgqaVQQRAAALAGV 218
LplA COG0095
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part ...
29-217 5.19e-05

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: 42.91  E-value: 5.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  29 DEVANRTRQNTILLLEHEAVITAGK--RTE---DHEYPADKSTPVVKidR--GGKLTWHGPGQLTgYPILrLPE---PID 98
Cdd:COG0095   22 EEVAEGEDPPTLRLWRNPPTVVIGRfqNVLpevNLEYVEEHGIPVVR--RisGGGAVYHDPGNLN-YSLI-LPEddvPLS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  99 VVAYVRIIEEIIINVLAGLGIKGErVEGRSGVWIlgDGvtqdKKIAALGMRVSRNTTMHGFAINCCND--------TAPF 170
Cdd:COG0095   98 IEESYRKLLEPILEALRKLGVDAE-FSGRNDIVV--DG----RKISGNAQRRRKGAVLHHGTLLVDGDleklakvlRVPY 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 502667345 171 QQFIPCGISDA--GVTTISEQLGRTVTPADILEPLEAELLKYQDRLAES 217
Cdd:COG0095  171 EKLRDKGIKSVrsRVTNLSELLGTDITREEVKEALLEAFAEVLGVLEPG 219
LplA cd16443
lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide ...
67-207 1.23e-03

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: 38.78  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502667345  67 PVVKIDRGGKLTWHGPGQLTGYPILRLPEPIDVVAYvRIIEEIIINVLAGLGIKGERVEGrsgvwILGDGVTQDKKIAAL 146
Cdd:cd16443   65 PVVRRPSGGGAVFHDLGNLNYSLILPKEHPSIDESY-RALSQPVIKALRKLGVEAEFGGV-----GRNDLVVGGKKISGS 138
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502667345 147 GMRVSRNTTMHGFAINCCNDTAPFQQFIPCG----------ISDAGVTTISEQLGRTVTPADILEPLEAEL 207
Cdd:cd16443  139 AQRRTKGRILHHGTLLVDVDLEKLARVLNVPyeklkskgpkSVRSRVTNLSELLGRDITVEEVKNALLEAF 209
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH