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Conserved domains on  [gi|501683928|ref|WP_012615750|]
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ligase [Chloroflexus aggregans]

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 ...
 36-229 1.49e-28

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: 109.17  E-value: 1.49e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501683928  36 QPAIRWYAaaPQPALVIGSGQKVC-EVDQAALANAGITLHRRASGGTAVLFVPGFLMQDIVLPADHPLAhpDVSESYRWL 114
Cdd:COG0095   30 PPTLRLWR--NPPTVVIGRFQNVLpEVNLEYVEEHGIPVVRRISGGGAVYHDPGNLNYSLILPEDDVPL--SIEESYRKL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501683928 115 GEVWQATLAHFGVQADlitiaaaradrasldplvaracFGGWspYELLVAGRKLVGFAQIRRREGLLFQVGVYTHWPGAQ 194
Cdd:COG0095  106 LEPILEALRKLGVDAE----------------------FSGR--NDIVVDGRKISGNAQRRRKGAVLHHGTLLVDGDLEK 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 501683928 195 LADLLNIAASE-RQLLIDRLSARVTDLAAVCVKPPD 229
Cdd:COG0095  162 LAKVLRVPYEKlRDKGIKSVRSRVTNLSELLGTDIT 197
 
Name Accession Description Interval E-value
LplA COG0095
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part ...
 36-229 1.49e-28

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: 109.17  E-value: 1.49e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501683928  36 QPAIRWYAaaPQPALVIGSGQKVC-EVDQAALANAGITLHRRASGGTAVLFVPGFLMQDIVLPADHPLAhpDVSESYRWL 114
Cdd:COG0095   30 PPTLRLWR--NPPTVVIGRFQNVLpEVNLEYVEEHGIPVVRRISGGGAVYHDPGNLNYSLILPEDDVPL--SIEESYRKL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501683928 115 GEVWQATLAHFGVQADlitiaaaradrasldplvaracFGGWspYELLVAGRKLVGFAQIRRREGLLFQVGVYTHWPGAQ 194
Cdd:COG0095  106 LEPILEALRKLGVDAE----------------------FSGR--NDIVVDGRKISGNAQRRRKGAVLHHGTLLVDGDLEK 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 501683928 195 LADLLNIAASE-RQLLIDRLSARVTDLAAVCVKPPD 229
Cdd:COG0095  162 LAKVLRVPYEKlRDKGIKSVRSRVTNLSELLGTDIT 197
LplA cd16443
lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide ...
 36-221 1.90e-15

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: 73.06  E-value: 1.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501683928  36 QPAIRWYAAAPQPALVIGSGQKVC-EVDQAALANAGITLHRRASGGTAVLFVPGFLMQDIVLPADhplaHPDVSESYRWL 114
Cdd:cd16443   28 PPTLRLYLWQNPPTVVIGRFQNPLeEVNLEYAEEDGIPVVRRPSGGGAVFHDLGNLNYSLILPKE----HPSIDESYRAL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501683928 115 GEVWQATLAHFGVQADlitiaaaradrasldplvaracFGGWSPYELLVAGRKLVGFAQIRRREGLLFQVGVYTHWPGAQ 194
Cdd:cd16443  104 SQPVIKALRKLGVEAE----------------------FGGVGRNDLVVGGKKISGSAQRRTKGRILHHGTLLVDVDLEK 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 501683928 195 LADLLNIaaSERQLL---IDRLSARVTDLA 221
Cdd:cd16443  162 LARVLNV--PYEKLKskgPKSVRSRVTNLS 189
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 152-184 1.55e-03

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: 37.81  E-value: 1.55e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 501683928  152 CFGGWsPYELLVAGRKLVGFAQIRRREGLLFQV 184
Cdd:pfam03099  94 CFVKW-PNDLYVNGRKLAGILQRSTRGGTLHHG 125
 
Name Accession Description Interval E-value
LplA COG0095
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part ...
 36-229 1.49e-28

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: 109.17  E-value: 1.49e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501683928  36 QPAIRWYAaaPQPALVIGSGQKVC-EVDQAALANAGITLHRRASGGTAVLFVPGFLMQDIVLPADHPLAhpDVSESYRWL 114
Cdd:COG0095   30 PPTLRLWR--NPPTVVIGRFQNVLpEVNLEYVEEHGIPVVRRISGGGAVYHDPGNLNYSLILPEDDVPL--SIEESYRKL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501683928 115 GEVWQATLAHFGVQADlitiaaaradrasldplvaracFGGWspYELLVAGRKLVGFAQIRRREGLLFQVGVYTHWPGAQ 194
Cdd:COG0095  106 LEPILEALRKLGVDAE----------------------FSGR--NDIVVDGRKISGNAQRRRKGAVLHHGTLLVDGDLEK 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 501683928 195 LADLLNIAASE-RQLLIDRLSARVTDLAAVCVKPPD 229
Cdd:COG0095  162 LAKVLRVPYEKlRDKGIKSVRSRVTNLSELLGTDIT 197
LplA cd16443
lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide ...
 36-221 1.90e-15

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: 73.06  E-value: 1.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501683928  36 QPAIRWYAAAPQPALVIGSGQKVC-EVDQAALANAGITLHRRASGGTAVLFVPGFLMQDIVLPADhplaHPDVSESYRWL 114
Cdd:cd16443   28 PPTLRLYLWQNPPTVVIGRFQNPLeEVNLEYAEEDGIPVVRRPSGGGAVFHDLGNLNYSLILPKE----HPSIDESYRAL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501683928 115 GEVWQATLAHFGVQADlitiaaaradrasldplvaracFGGWSPYELLVAGRKLVGFAQIRRREGLLFQVGVYTHWPGAQ 194
Cdd:cd16443  104 SQPVIKALRKLGVEAE----------------------FGGVGRNDLVVGGKKISGSAQRRTKGRILHHGTLLVDVDLEK 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 501683928 195 LADLLNIaaSERQLL---IDRLSARVTDLA 221
Cdd:cd16443  162 LARVLNV--PYEKLKskgPKSVRSRVTNLS 189
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 152-184 1.55e-03

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: 37.81  E-value: 1.55e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 501683928  152 CFGGWsPYELLVAGRKLVGFAQIRRREGLLFQV 184
Cdd:pfam03099  94 CFVKW-PNDLYVNGRKLAGILQRSTRGGTLHHG 125
 
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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