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Conserved domains on  [gi|359278121|dbj|BAL35638|]
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hypothetical protein SYNPCCP_1552 [Synechocystis sp. PCC 6803 substr. PCC-P]

Protein Classification

lipoate--protein ligase family protein( domain architecture ID 46944)

lipoate--protein ligase family protein, similar to Staphylococcus aureus lipoate--protein ligase 1 and Saccharomyces cerevisiae octanoyltransferase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BPL_LplA_LipB super family cl14057
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ...
 1-172 1.34e-30

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.


The actual alignment was detected with superfamily member cd16443:

Pssm-ID: 449326  Cd Length: 209  Bit Score: 111.96  E-value: 1.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359278121   1 MALDQWLLEDYFprtGRSVLRFYGWSRP-TISLGYLQKSWPDHWRQLtWQGQSLGLVTRPSGGRAVLH-QGGLTYAVVTG 78
Cdd:cd16443   15 LALDEALLRSVA---APPTLRLYLWQNPpTVVIGRFQNPLEEVNLEY-AEEDGIPVVRRPSGGGAVFHdLGNLNYSLILP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359278121  79 ATGGKRREIYQHICQFLIQGWDQLGLSLTYGRGGRGyihnascfstatmaDLVSPtGDKLIGSAQRQTSNALLQHGEMIW 158
Cdd:cd16443   91 KEHPSIDESYRALSQPVIKALRKLGVEAEFGGVGRN--------------DLVVG-GKKISGSAQRRTKGRILHHGTLLV 155

                        170
                 ....*....|....
gi 359278121 159 HGDRHLFELVFNQP 172
Cdd:cd16443  156 DVDLEKLARVLNVP 169
 
Name Accession Description Interval E-value
LplA cd16443
lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide ...
 1-172 1.34e-30

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: 111.96  E-value: 1.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359278121   1 MALDQWLLEDYFprtGRSVLRFYGWSRP-TISLGYLQKSWPDHWRQLtWQGQSLGLVTRPSGGRAVLH-QGGLTYAVVTG 78
Cdd:cd16443   15 LALDEALLRSVA---APPTLRLYLWQNPpTVVIGRFQNPLEEVNLEY-AEEDGIPVVRRPSGGGAVFHdLGNLNYSLILP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359278121  79 ATGGKRREIYQHICQFLIQGWDQLGLSLTYGRGGRGyihnascfstatmaDLVSPtGDKLIGSAQRQTSNALLQHGEMIW 158
Cdd:cd16443   91 KEHPSIDESYRALSQPVIKALRKLGVEAEFGGVGRN--------------DLVVG-GKKISGSAQRRTKGRILHHGTLLV 155

                        170
                 ....*....|....
gi 359278121 159 HGDRHLFELVFNQP 172
Cdd:cd16443  156 DVDLEKLARVLNVP 169
LplA COG0095
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part ...
 1-223 5.75e-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: 106.09  E-value: 5.75e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359278121   1 MALDQWLLEDYFPRTGRSVLRFYGwSRPTISLGYLQKSWPD-HWRQLtwQGQSLGLVTRPSGGRAVLHQGG-LTYAVVTG 78
Cdd:COG0095   14 LALDEALLEEVAEGEDPPTLRLWR-NPPTVVIGRFQNVLPEvNLEYV--EEHGIPVVRRISGGGAVYHDPGnLNYSLILP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359278121  79 ATGGKRR--EIYQHICQFLIQGWDQLGLSLTYGrgGRGyihnascfstatmaDLVSPtGDKLIGSAQRQTSNALLQHGEM 156
Cdd:COG0095   91 EDDVPLSieESYRKLLEPILEALRKLGVDAEFS--GRN--------------DIVVD-GRKISGNAQRRRKGAVLHHGTL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359278121 157 IWHGDRHLFELVFNQP---------APWQKTMA----ELTNDPSLPQVLKVLTTAAQQHFqSHLRWEPLTPQEWA----M 219
Cdd:COG0095  154 LVDGDLEKLAKVLRVPyeklrdkgiKSVRSRVTnlseLLGTDITREEVKEALLEAFAEVL-GVLEPGELTDEELEaaeeL 232


                 ....
gi 359278121 220 VKEK 223
Cdd:COG0095  233 AEEK 236
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 32-161 1.52e-20

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: 83.65  E-value: 1.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359278121   32 LGYLQKS---WPDHWRQLTWQGQSLGLVTRPSGGR----AVLHQ--GGLTYAVVTGATGGKR--REIYQHICQFLIQGWD 100
Cdd:pfam03099   1 LGERIKStntYLEELNSSELESGGVVVVRRQTGGRgrggNVWHSpkGCLTYSLLLSKEHPNVdpSVLEFYVLELVLAVLE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 359278121  101 QLGLSltygrggRGYIHNASCFStATMADLVSpTGDKLIGSAQRQTSNALLQHGEMIWHGD 161
Cdd:pfam03099  81 ALGLY-------KPGISGIPCFV-KWPNDLYV-NGRKLAGILQRSTRGGTLHHGVIGLGVN 132
lipoyltrans TIGR00545
lipoyltransferase and lipoate-protein ligase; One member of this group of proteins is bovine ...
 1-223 8.50e-07

lipoyltransferase and lipoate-protein ligase; One member of this group of proteins is bovine lipoyltransferase, which transfers the lipoyl group from lipoyl-AMP to the specific Lys of lipoate-dependent enzymes. However, it does not first activate lipoic acid with ATP to create lipoyl-AMP and pyrophosphate. Another member of this group, lipoate-protein ligase A from E. coli, catalyzes both the activation and the transfer of lipoate. Homology between the two is full-length, except for the bovine mitochondrial targeting signal, but is strongest toward the N-terminus. [Protein fate, Protein modification and repair]


Pssm-ID: 161920 [Multi-domain]  Cd Length: 324  Bit Score: 48.66  E-value: 8.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359278121    1 MALDQWLLEDyFPRTGRSVLRFYGWSRPTISLGYLQKSWPD-HWRQLtwQGQSLGLVTRPSGGRAVLHQ-GGLTYAVVTG 78
Cdd:TIGR00545  15 LALEEYLFKE-FPKTQRGKVLLFWQNANTIVIGRNQNTWAEvNLKEL--EEDNVNLFRRFSGGGAVFHDlGNICFSFITP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359278121   79 ATgGKRREIYQHICQFLIQGWDQLGLSLTYgrGGRGyihnascfstatmaDLVSpTGDKLIGSAQRQTSNALLQHGEMIW 158
Cdd:TIGR00545  92 KD-GKEFENAKIFTRNVIKALNSLGVEAEL--SGRN--------------DLVV-DGRKISGSAYYITKDRGFHHGTLLF 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359278121  159 HGDrhlFELVFNQPAPWQKTMA---------------ELTNDPSLPQVLKVLTtaaqQHFQS---HLRWEPLTPQEWAMV 220
Cdd:TIGR00545 154 DAD---LSKLAKYLNVDKTKIEskgitsvrsrvvnvkEYLPNITTEQFLEEMT----QAFFTyteRVETYILDENKTPDV 226


                  ...
gi 359278121  221 KEK 223
Cdd:TIGR00545 227 EKR 229
 
Name Accession Description Interval E-value
LplA cd16443
lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide ...
 1-172 1.34e-30

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: 111.96  E-value: 1.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359278121   1 MALDQWLLEDYFprtGRSVLRFYGWSRP-TISLGYLQKSWPDHWRQLtWQGQSLGLVTRPSGGRAVLH-QGGLTYAVVTG 78
Cdd:cd16443   15 LALDEALLRSVA---APPTLRLYLWQNPpTVVIGRFQNPLEEVNLEY-AEEDGIPVVRRPSGGGAVFHdLGNLNYSLILP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359278121  79 ATGGKRREIYQHICQFLIQGWDQLGLSLTYGRGGRGyihnascfstatmaDLVSPtGDKLIGSAQRQTSNALLQHGEMIW 158
Cdd:cd16443   91 KEHPSIDESYRALSQPVIKALRKLGVEAEFGGVGRN--------------DLVVG-GKKISGSAQRRTKGRILHHGTLLV 155

                        170
                 ....*....|....
gi 359278121 159 HGDRHLFELVFNQP 172
Cdd:cd16443  156 DVDLEKLARVLNVP 169
LplA COG0095
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part ...
 1-223 5.75e-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: 106.09  E-value: 5.75e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359278121   1 MALDQWLLEDYFPRTGRSVLRFYGwSRPTISLGYLQKSWPD-HWRQLtwQGQSLGLVTRPSGGRAVLHQGG-LTYAVVTG 78
Cdd:COG0095   14 LALDEALLEEVAEGEDPPTLRLWR-NPPTVVIGRFQNVLPEvNLEYV--EEHGIPVVRRISGGGAVYHDPGnLNYSLILP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359278121  79 ATGGKRR--EIYQHICQFLIQGWDQLGLSLTYGrgGRGyihnascfstatmaDLVSPtGDKLIGSAQRQTSNALLQHGEM 156
Cdd:COG0095   91 EDDVPLSieESYRKLLEPILEALRKLGVDAEFS--GRN--------------DIVVD-GRKISGNAQRRRKGAVLHHGTL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359278121 157 IWHGDRHLFELVFNQP---------APWQKTMA----ELTNDPSLPQVLKVLTTAAQQHFqSHLRWEPLTPQEWA----M 219
Cdd:COG0095  154 LVDGDLEKLAKVLRVPyeklrdkgiKSVRSRVTnlseLLGTDITREEVKEALLEAFAEVL-GVLEPGELTDEELEaaeeL 232


                 ....
gi 359278121 220 VKEK 223
Cdd:COG0095  233 AEEK 236
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 32-161 1.52e-20

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: 83.65  E-value: 1.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359278121   32 LGYLQKS---WPDHWRQLTWQGQSLGLVTRPSGGR----AVLHQ--GGLTYAVVTGATGGKR--REIYQHICQFLIQGWD 100
Cdd:pfam03099   1 LGERIKStntYLEELNSSELESGGVVVVRRQTGGRgrggNVWHSpkGCLTYSLLLSKEHPNVdpSVLEFYVLELVLAVLE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 359278121  101 QLGLSltygrggRGYIHNASCFStATMADLVSpTGDKLIGSAQRQTSNALLQHGEMIWHGD 161
Cdd:pfam03099  81 ALGLY-------KPGISGIPCFV-KWPNDLYV-NGRKLAGILQRSTRGGTLHHGVIGLGVN 132
lipoyltrans TIGR00545
lipoyltransferase and lipoate-protein ligase; One member of this group of proteins is bovine ...
 1-223 8.50e-07

lipoyltransferase and lipoate-protein ligase; One member of this group of proteins is bovine lipoyltransferase, which transfers the lipoyl group from lipoyl-AMP to the specific Lys of lipoate-dependent enzymes. However, it does not first activate lipoic acid with ATP to create lipoyl-AMP and pyrophosphate. Another member of this group, lipoate-protein ligase A from E. coli, catalyzes both the activation and the transfer of lipoate. Homology between the two is full-length, except for the bovine mitochondrial targeting signal, but is strongest toward the N-terminus. [Protein fate, Protein modification and repair]


Pssm-ID: 161920 [Multi-domain]  Cd Length: 324  Bit Score: 48.66  E-value: 8.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359278121    1 MALDQWLLEDyFPRTGRSVLRFYGWSRPTISLGYLQKSWPD-HWRQLtwQGQSLGLVTRPSGGRAVLHQ-GGLTYAVVTG 78
Cdd:TIGR00545  15 LALEEYLFKE-FPKTQRGKVLLFWQNANTIVIGRNQNTWAEvNLKEL--EEDNVNLFRRFSGGGAVFHDlGNICFSFITP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359278121   79 ATgGKRREIYQHICQFLIQGWDQLGLSLTYgrGGRGyihnascfstatmaDLVSpTGDKLIGSAQRQTSNALLQHGEMIW 158
Cdd:TIGR00545  92 KD-GKEFENAKIFTRNVIKALNSLGVEAEL--SGRN--------------DLVV-DGRKISGSAYYITKDRGFHHGTLLF 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359278121  159 HGDrhlFELVFNQPAPWQKTMA---------------ELTNDPSLPQVLKVLTtaaqQHFQS---HLRWEPLTPQEWAMV 220
Cdd:TIGR00545 154 DAD---LSKLAKYLNVDKTKIEskgitsvrsrvvnvkEYLPNITTEQFLEEMT----QAFFTyteRVETYILDENKTPDV 226


                  ...
gi 359278121  221 KEK 223
Cdd:TIGR00545 227 EKR 229
 
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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