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Conserved domains on  [gi|1563131591|gb|RXK11425|]
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ligase [Halarcobacter bivalviorum]

Protein Classification

biotin/lipoate A/B protein ligase family protein( domain architecture ID 10000572)

biotin/lipoate A/B protein ligase family protein is responsible for attaching biotin and lipoic acid to a specific lysine at the active site of biotin and lipoate-dependent enzymes, respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LplA COG0095
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part ...
 9-241 3.68e-42

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: 143.84  E-value: 3.68e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131591   9 RVINSSKASAKINMATDDALL-SCFEKNNLPILRVYYWDKSFTVGISQDVntysfKEEYNENFAK--------RITGGGV 79
Cdd:COG0095     1 RLIDSGSTDPAFNLALDEALLeEVAEGEDPPTLRLWRNPPTVVIGRFQNV-----LPEVNLEYVEehgipvvrRISGGGA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131591  80 LFHGHD-ISYSLVIPTTLlEGLNIKESYEFICRFIINFYRKLNLDARYAkdieeinlsksefcqvgfEAYDIIANGKKIG 158
Cdd:COG0095    76 VYHDPGnLNYSLILPEDD-VPLSIEESYRKLLEPILEALRKLGVDAEFS------------------GRNDIVVDGRKIS 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131591 159 GNAQRRTKKAIFQHGSIPLK-NLS--GKY----DEKIG-----------TTLKDF-NINLEYEKASVLLIEAFNETFNvE 219
Cdd:COG0095   137 GNAQRRRKGAVLHHGTLLVDgDLEklAKVlrvpYEKLRdkgiksvrsrvTNLSELlGTDITREEVKEALLEAFAEVLG-V 215

                         250       260
                  ....*....|....*....|..
gi 1563131591 220 LIQSELTEEENIKKNELLKDKY 241
Cdd:COG0095   216 LEPGELTDEELEAAEELAEEKY 237
 
Name Accession Description Interval E-value
LplA COG0095
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part ...
 9-241 3.68e-42

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: 143.84  E-value: 3.68e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131591   9 RVINSSKASAKINMATDDALL-SCFEKNNLPILRVYYWDKSFTVGISQDVntysfKEEYNENFAK--------RITGGGV 79
Cdd:COG0095     1 RLIDSGSTDPAFNLALDEALLeEVAEGEDPPTLRLWRNPPTVVIGRFQNV-----LPEVNLEYVEehgipvvrRISGGGA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131591  80 LFHGHD-ISYSLVIPTTLlEGLNIKESYEFICRFIINFYRKLNLDARYAkdieeinlsksefcqvgfEAYDIIANGKKIG 158
Cdd:COG0095    76 VYHDPGnLNYSLILPEDD-VPLSIEESYRKLLEPILEALRKLGVDAEFS------------------GRNDIVVDGRKIS 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131591 159 GNAQRRTKKAIFQHGSIPLK-NLS--GKY----DEKIG-----------TTLKDF-NINLEYEKASVLLIEAFNETFNvE 219
Cdd:COG0095   137 GNAQRRRKGAVLHHGTLLVDgDLEklAKVlrvpYEKLRdkgiksvrsrvTNLSELlGTDITREEVKEALLEAFAEVLG-V 215

                         250       260
                  ....*....|....*....|..
gi 1563131591 220 LIQSELTEEENIKKNELLKDKY 241
Cdd:COG0095   216 LEPGELTDEELEAAEELAEEKY 237
LplA cd16443
lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide ...
 9-177 6.38e-34

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: 121.21  E-value: 6.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131591   9 RVINSSKASAKINMATDDALLscFEKNNLPILRVYYW--DKSFTVGISQ----DVNTYSFKEEyNENFAKRITGGGVLFH 82
Cdd:cd16443     2 RLIDSSGDPPAENLALDEALL--RSVAAPPTLRLYLWqnPPTVVIGRFQnpleEVNLEYAEED-GIPVVRRPSGGGAVFH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131591  83 G-HDISYSLVIPttlLEGLNIKESYEFICRFIINFYRKLNLDARYAkdieeinlsksefcqvGFEAYDIIANGKKIGGNA 161
Cdd:cd16443    79 DlGNLNYSLILP---KEHPSIDESYRALSQPVIKALRKLGVEAEFG----------------GVGRNDLVVGGKKISGSA 139

                         170
                  ....*....|....*.
gi 1563131591 162 QRRTKKAIFQHGSIPL 177
Cdd:cd16443   140 QRRTKGRILHHGTLLV 155
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 60-175 9.12e-09

Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, lipoate-protein ligase A and B. Biotin is covalently attached at the active site of certain enzymes that transfer carbon dioxide from bicarbonate to organic acids to form cellular metabolites. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Each organizm probably has only one BPL. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine. Lipoate-protein ligase A (LPLA) catalyzes the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes. The unusual biosynthesis pathway of lipoic acid is mechanistically intertwined with attachment of the cofactor.


Pssm-ID: 427135  Cd Length: 132  Bit Score: 52.44  E-value: 9.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131591  60 YSFKEEYNENFAKRITGG----GVLFHGHD--ISYSLVIPTTLLEGLN-IKESYefICRFIINFYRKLNLDARYAKDIee 132
Cdd:pfam03099  17 SSELESGGVVVVRRQTGGrgrgGNVWHSPKgcLTYSLLLSKEHPNVDPsVLEFY--VLELVLAVLEALGLYKPGISGI-- 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1563131591 133 inlskseFCQVGFeAYDIIANGKKIGGNAQRRTKKAIFQHGSI 175
Cdd:pfam03099  93 -------PCFVKW-PNDLYVNGRKLAGILQRSTRGGTLHHGVI 127
 
Name Accession Description Interval E-value
LplA COG0095
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part ...
 9-241 3.68e-42

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: 143.84  E-value: 3.68e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131591   9 RVINSSKASAKINMATDDALL-SCFEKNNLPILRVYYWDKSFTVGISQDVntysfKEEYNENFAK--------RITGGGV 79
Cdd:COG0095     1 RLIDSGSTDPAFNLALDEALLeEVAEGEDPPTLRLWRNPPTVVIGRFQNV-----LPEVNLEYVEehgipvvrRISGGGA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131591  80 LFHGHD-ISYSLVIPTTLlEGLNIKESYEFICRFIINFYRKLNLDARYAkdieeinlsksefcqvgfEAYDIIANGKKIG 158
Cdd:COG0095    76 VYHDPGnLNYSLILPEDD-VPLSIEESYRKLLEPILEALRKLGVDAEFS------------------GRNDIVVDGRKIS 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131591 159 GNAQRRTKKAIFQHGSIPLK-NLS--GKY----DEKIG-----------TTLKDF-NINLEYEKASVLLIEAFNETFNvE 219
Cdd:COG0095   137 GNAQRRRKGAVLHHGTLLVDgDLEklAKVlrvpYEKLRdkgiksvrsrvTNLSELlGTDITREEVKEALLEAFAEVLG-V 215

                         250       260
                  ....*....|....*....|..
gi 1563131591 220 LIQSELTEEENIKKNELLKDKY 241
Cdd:COG0095   216 LEPGELTDEELEAAEELAEEKY 237
LplA cd16443
lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide ...
 9-177 6.38e-34

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: 121.21  E-value: 6.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131591   9 RVINSSKASAKINMATDDALLscFEKNNLPILRVYYW--DKSFTVGISQ----DVNTYSFKEEyNENFAKRITGGGVLFH 82
Cdd:cd16443     2 RLIDSSGDPPAENLALDEALL--RSVAAPPTLRLYLWqnPPTVVIGRFQnpleEVNLEYAEED-GIPVVRRPSGGGAVFH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131591  83 G-HDISYSLVIPttlLEGLNIKESYEFICRFIINFYRKLNLDARYAkdieeinlsksefcqvGFEAYDIIANGKKIGGNA 161
Cdd:cd16443    79 DlGNLNYSLILP---KEHPSIDESYRALSQPVIKALRKLGVEAEFG----------------GVGRNDLVVGGKKISGSA 139

                         170
                  ....*....|....*.
gi 1563131591 162 QRRTKKAIFQHGSIPL 177
Cdd:cd16443   140 QRRTKGRILHHGTLLV 155
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 60-175 9.12e-09

Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, lipoate-protein ligase A and B. Biotin is covalently attached at the active site of certain enzymes that transfer carbon dioxide from bicarbonate to organic acids to form cellular metabolites. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Each organizm probably has only one BPL. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine. Lipoate-protein ligase A (LPLA) catalyzes the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes. The unusual biosynthesis pathway of lipoic acid is mechanistically intertwined with attachment of the cofactor.


Pssm-ID: 427135  Cd Length: 132  Bit Score: 52.44  E-value: 9.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131591  60 YSFKEEYNENFAKRITGG----GVLFHGHD--ISYSLVIPTTLLEGLN-IKESYefICRFIINFYRKLNLDARYAKDIee 132
Cdd:pfam03099  17 SSELESGGVVVVRRQTGGrgrgGNVWHSPKgcLTYSLLLSKEHPNVDPsVLEFY--VLELVLAVLEALGLYKPGISGI-- 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1563131591 133 inlskseFCQVGFeAYDIIANGKKIGGNAQRRTKKAIFQHGSI 175
Cdd:pfam03099  93 -------PCFVKW-PNDLYVNGRKLAGILQRSTRGGTLHHGVI 127
BPL_LplA_LipB cd16435
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ...
 63-177 9.87e-03

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: 35.98  E-value: 9.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131591  63 KEEYNENFAKRITGGGVLFHGHDI-SYSLVIPttLLEGLNIKESYEFICRFIINFYRKLNLDArYAKDIEeinlsksefc 141
Cdd:cd16435    58 KIERGYELVVRNRGGRAVSHDPGQlVFSPVIG--PNVEFMISKFNLIIEEGIRDAIADFGQSA-EVKWGR---------- 124

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1563131591 142 qvgfeaYDIIANGKKIGGNAQRRTKKAIFQHGSIPL 177
Cdd:cd16435   125 ------NDLWIDNRKVCGIAVRVVKEAIFHGIALNL 154
 
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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