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Conserved domains on  [gi|16132203|ref|NP_418803|]
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lipoate--protein ligase A [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

lipoate--protein ligase A( domain architecture ID 11480058)

lipoate--protein ligase A catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes; also catalyzes very poorly the transfer of lipoyl and octanoyl moiety from their acyl carrier protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
lplA PRK03822
lipoate-protein ligase A; Provisional
1-338 0e+00

lipoate-protein ligase A; Provisional


:

Pssm-ID: 179655  Cd Length: 338  Bit Score: 799.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203    1 MSTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFH 80
Cdd:PRK03822   1 MSTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203   81 DLGNTCFTFMAGKPEYDKTISTSIVLNALNALGVSAEASGRNDLVVKTVEGDRKVSGSAYRETKDRGFHHGTLLLNADLS 160
Cdd:PRK03822  81 DLGNTCFTFMAGKPEYDKTISTSIVLNALNSLGVSAEASGRNDLVVKTAEGDRKVSGSAYRETKDRGFHHGTLLLNADLS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203  161 RLANYLNPDKKKLAAKGITSVRSRVTNLTELLPGITHEQVCEAITEAFFAHYGERVEAEIISPNKTPDLPNFAETFARQS 240
Cdd:PRK03822 161 RLANYLNPDKKKLQAKGITSVRSRVTNLTELLPGITHEQVCEAITEAFFAHYGERVEAEVISPDKTPDLPGFAETFARQS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203  241 SWEWNFGQAPAFSHLLDERFTWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVDFP 320
Cdd:PRK03822 241 SWEWNFGQAPAFSHLLDERFTWGGVELHFDVEKGHITRAQIFTDSLNPAPLEALAGRLQGCLYRADALQQECEALIVDFP 320
                        330
                 ....*....|....*...
gi 16132203  321 EQEKELRELSAWMAGAVR 338
Cdd:PRK03822 321 EQEKELRELSAWLAGAVR 338
 
Name Accession Description Interval E-value
lplA PRK03822
lipoate-protein ligase A; Provisional
1-338 0e+00

lipoate-protein ligase A; Provisional


Pssm-ID: 179655  Cd Length: 338  Bit Score: 799.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203    1 MSTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFH 80
Cdd:PRK03822   1 MSTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203   81 DLGNTCFTFMAGKPEYDKTISTSIVLNALNALGVSAEASGRNDLVVKTVEGDRKVSGSAYRETKDRGFHHGTLLLNADLS 160
Cdd:PRK03822  81 DLGNTCFTFMAGKPEYDKTISTSIVLNALNSLGVSAEASGRNDLVVKTAEGDRKVSGSAYRETKDRGFHHGTLLLNADLS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203  161 RLANYLNPDKKKLAAKGITSVRSRVTNLTELLPGITHEQVCEAITEAFFAHYGERVEAEIISPNKTPDLPNFAETFARQS 240
Cdd:PRK03822 161 RLANYLNPDKKKLQAKGITSVRSRVTNLTELLPGITHEQVCEAITEAFFAHYGERVEAEVISPDKTPDLPGFAETFARQS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203  241 SWEWNFGQAPAFSHLLDERFTWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVDFP 320
Cdd:PRK03822 241 SWEWNFGQAPAFSHLLDERFTWGGVELHFDVEKGHITRAQIFTDSLNPAPLEALAGRLQGCLYRADALQQECEALIVDFP 320
                        330
                 ....*....|....*...
gi 16132203  321 EQEKELRELSAWMAGAVR 338
Cdd:PRK03822 321 EQEKELRELSAWLAGAVR 338
lipoyltrans TIGR00545
lipoyltransferase and lipoate-protein ligase; One member of this group of proteins is bovine ...
4-330 0e+00

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: 508.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203     4 LRLLISDSYDPWFNLAVEECIFRQMPATQR--VLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHD 81
Cdd:TIGR00545   1 TRILTSPSNDPYFNLALEEYLFKEFPKTQRgkVLLFWQNANTIVIGRNQNTWAEVNLKELEEDNVNLFRRFSGGGAVFHD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203    82 LGNTCFTFMAGK--PEYDK-TISTSIVLNALNALGVSAEASGRNDLVVKtvegDRKVSGSAYRETKDRGFHHGTLLLNAD 158
Cdd:TIGR00545  81 LGNICFSFITPKdgKEFENaKIFTRNVIKALNSLGVEAELSGRNDLVVD----GRKISGSAYYITKDRGFHHGTLLFDAD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203   159 LSRLANYLNPDKKKLAAKGITSVRSRVTNLTELLPGITHEQVCEAITEAFFAhYGERVEAEIISPNKTPDLPNFAEtfAR 238
Cdd:TIGR00545 157 LSKLAKYLNVDKTKIESKGITSVRSRVVNVKEYLPNITTEQFLEEMTQAFFT-YTERVETYILDENKTPDVEKRAK--ER 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203   239 QSSWEWNFGQAPAFSHLLDERFTWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVd 318
Cdd:TIGR00545 234 FQSWEWNFGKTPKFNFKNKKRFTAGGFELHVQVEKGKIVDCKFFGDFLSVADITPVTNRLIGQKYDYDTFAKELENLDV- 312
                         330
                  ....*....|..
gi 16132203   319 FPEQEKELRELS 330
Cdd:TIGR00545 313 FKEYFGELTPEQ 324
LplA COG0095
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part ...
5-248 1.90e-97

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: 288.29  E-value: 1.90e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203   5 RLLISDSYDPWFNLAVEECIFRQM--PATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDL 82
Cdd:COG0095   1 RLIDSGSTDPAFNLALDEALLEEVaeGEDPPTLRLWRNPPTVVIGRFQNVLPEVNLEYVEEHGIPVVRRISGGGAVYHDP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203  83 GNTCFTFMAGKPEYDKTIS------TSIVLNALNALGVSAEASGRNDLVVktveGDRKVSGSAYRETKDRGFHHGTLLLN 156
Cdd:COG0095  81 GNLNYSLILPEDDVPLSIEesyrklLEPILEALRKLGVDAEFSGRNDIVV----DGRKISGNAQRRRKGAVLHHGTLLVD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203 157 ADLSRLANYLNPDKKKLAAKGITSVRSRVTNLTELLP-GITHEQVCEAITEAFFAHYGERVEAEIispnkTPDLPNFAET 235
Cdd:COG0095 157 GDLEKLAKVLRVPYEKLRDKGIKSVRSRVTNLSELLGtDITREEVKEALLEAFAEVLGVLEPGEL-----TDEELEAAEE 231
                       250
                ....*....|....*
gi 16132203 236 FA--RQSSWEWNFGQ 248
Cdd:COG0095 232 LAeeKYSSWEWNYGR 246
BPL_LplA_LipB cd16435
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ...
5-208 7.56e-76

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: 231.66  E-value: 7.56e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203   5 RLLISDSYDPWFNLAVEECIFRQMPA-TQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLG 83
Cdd:cd16435   1 FVEVLDSVDYESAWAAQEKSLRENVSnQSSTLLLWEHPTTVTLGRLDRELPHLELAKKIERGYELVVRNRGGRAVSHDPG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203  84 NTCFTFMAGKP-----EYDKTISTSIVLNALNALGVSAEAS-GRNDLVVKtvegDRKVSGSAYRETKDRGFHHGTLLLNA 157
Cdd:cd16435  81 QLVFSPVIGPNvefmiSKFNLIIEEGIRDAIADFGQSAEVKwGRNDLWID----NRKVCGIAVRVVKEAIFHGIALNLNQ 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 16132203 158 DLSRLANYLNPDKKklaakgitsVRSRVTNLTELLPGITHEQVCEAITEAF 208
Cdd:cd16435 157 DLENFTEIIPCGYK---------PERVTSLSLELGRKVTVEQVLERVLAAF 198
Lip_prot_lig_C pfam10437
Bacterial lipoate protein ligase C-terminus; This is the C-terminal domain of a bacterial ...
249-333 2.91e-22

Bacterial lipoate protein ligase C-terminus; This is the C-terminal domain of a bacterial lipoate protein ligase. There is no conservation between this C-terminus and that of vertebrate lipoate protein ligase C-termini, but both are associated with the domain BPL_LipA_LipB pfam03099, further upstream. This domain is required for adenylation of lipoic acid by lipoate protein ligases. The domain is not required for transfer of lipoic acid from the adenylate to the lipoyl domain. Upon adenylation, this domain rotates 180 degrees away from the active site cleft. Therefore, the domain does not interact with the lipoyl domain during transfer.


Pssm-ID: 431286 [Multi-domain]  Cd Length: 85  Bit Score: 89.07  E-value: 2.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203   249 APAFSHLLDERFTWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVD--FPEQEKEl 326
Cdd:pfam10437   1 SPEFNYKRSKRFDWGTIEVRLNVEKGIIKDIKIYGDFFGPGDIEELEEALIGVRYEKEAIEKALEDIDLEeyFGNITLE- 79

                  ....*..
gi 16132203   327 rELSAWM 333
Cdd:pfam10437  80 -ELIELL 85
 
Name Accession Description Interval E-value
lplA PRK03822
lipoate-protein ligase A; Provisional
1-338 0e+00

lipoate-protein ligase A; Provisional


Pssm-ID: 179655  Cd Length: 338  Bit Score: 799.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203    1 MSTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFH 80
Cdd:PRK03822   1 MSTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203   81 DLGNTCFTFMAGKPEYDKTISTSIVLNALNALGVSAEASGRNDLVVKTVEGDRKVSGSAYRETKDRGFHHGTLLLNADLS 160
Cdd:PRK03822  81 DLGNTCFTFMAGKPEYDKTISTSIVLNALNSLGVSAEASGRNDLVVKTAEGDRKVSGSAYRETKDRGFHHGTLLLNADLS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203  161 RLANYLNPDKKKLAAKGITSVRSRVTNLTELLPGITHEQVCEAITEAFFAHYGERVEAEIISPNKTPDLPNFAETFARQS 240
Cdd:PRK03822 161 RLANYLNPDKKKLQAKGITSVRSRVTNLTELLPGITHEQVCEAITEAFFAHYGERVEAEVISPDKTPDLPGFAETFARQS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203  241 SWEWNFGQAPAFSHLLDERFTWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVDFP 320
Cdd:PRK03822 241 SWEWNFGQAPAFSHLLDERFTWGGVELHFDVEKGHITRAQIFTDSLNPAPLEALAGRLQGCLYRADALQQECEALIVDFP 320
                        330
                 ....*....|....*...
gi 16132203  321 EQEKELRELSAWMAGAVR 338
Cdd:PRK03822 321 EQEKELRELSAWLAGAVR 338
PRK14061 PRK14061
unknown domain/lipoate-protein ligase A fusion protein; Provisional
1-338 0e+00

unknown domain/lipoate-protein ligase A fusion protein; Provisional


Pssm-ID: 172552 [Multi-domain]  Cd Length: 562  Bit Score: 714.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203    1 MSTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFH 80
Cdd:PRK14061 225 MSTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFH 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203   81 DLGNTCFTFMAGKPEYDKTISTSIVLNALNALGVSAEASGRNDLVVKTVEGDRKVSGSAYRETKDRGFHHGTLLLNADLS 160
Cdd:PRK14061 305 DLGNTCFTFMAGKPEYDKTISTSIVLNALNALGVSAEASGRNDLVVKTAEGDRKVSGSAYRETKDRGFHHGTLLLNADLS 384
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203  161 RLANYLNPDKKKLAAKGITSVRSRVTNLTELLPGITHEQVCEAITEAFFAHYGERVEAEIISPNKTPDLPNFAETFARQS 240
Cdd:PRK14061 385 RLANYLNPDKKKLAAKGITSVRSRVTNLTELLPGIPHEQVCEAITEAFFAHYGERVEAEIISPDKTPDLPNFAETFARQS 464
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203  241 SWEWNFGQAPAFSHLLDERFTWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVDFP 320
Cdd:PRK14061 465 SWEWNFGQAPAFSHLLDERFSWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVDFP 544
                        330
                 ....*....|....*...
gi 16132203  321 EQEKELRELSAWMAGAVR 338
Cdd:PRK14061 545 DQEKELRELSTWIAGAVR 562
lipoyltrans TIGR00545
lipoyltransferase and lipoate-protein ligase; One member of this group of proteins is bovine ...
4-330 0e+00

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: 508.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203     4 LRLLISDSYDPWFNLAVEECIFRQMPATQR--VLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHD 81
Cdd:TIGR00545   1 TRILTSPSNDPYFNLALEEYLFKEFPKTQRgkVLLFWQNANTIVIGRNQNTWAEVNLKELEEDNVNLFRRFSGGGAVFHD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203    82 LGNTCFTFMAGK--PEYDK-TISTSIVLNALNALGVSAEASGRNDLVVKtvegDRKVSGSAYRETKDRGFHHGTLLLNAD 158
Cdd:TIGR00545  81 LGNICFSFITPKdgKEFENaKIFTRNVIKALNSLGVEAELSGRNDLVVD----GRKISGSAYYITKDRGFHHGTLLFDAD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203   159 LSRLANYLNPDKKKLAAKGITSVRSRVTNLTELLPGITHEQVCEAITEAFFAhYGERVEAEIISPNKTPDLPNFAEtfAR 238
Cdd:TIGR00545 157 LSKLAKYLNVDKTKIESKGITSVRSRVVNVKEYLPNITTEQFLEEMTQAFFT-YTERVETYILDENKTPDVEKRAK--ER 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203   239 QSSWEWNFGQAPAFSHLLDERFTWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVd 318
Cdd:TIGR00545 234 FQSWEWNFGKTPKFNFKNKKRFTAGGFELHVQVEKGKIVDCKFFGDFLSVADITPVTNRLIGQKYDYDTFAKELENLDV- 312
                         330
                  ....*....|..
gi 16132203   319 FPEQEKELRELS 330
Cdd:TIGR00545 313 FKEYFGELTPEQ 324
LplA COG0095
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part ...
5-248 1.90e-97

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: 288.29  E-value: 1.90e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203   5 RLLISDSYDPWFNLAVEECIFRQM--PATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDL 82
Cdd:COG0095   1 RLIDSGSTDPAFNLALDEALLEEVaeGEDPPTLRLWRNPPTVVIGRFQNVLPEVNLEYVEEHGIPVVRRISGGGAVYHDP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203  83 GNTCFTFMAGKPEYDKTIS------TSIVLNALNALGVSAEASGRNDLVVktveGDRKVSGSAYRETKDRGFHHGTLLLN 156
Cdd:COG0095  81 GNLNYSLILPEDDVPLSIEesyrklLEPILEALRKLGVDAEFSGRNDIVV----DGRKISGNAQRRRKGAVLHHGTLLVD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203 157 ADLSRLANYLNPDKKKLAAKGITSVRSRVTNLTELLP-GITHEQVCEAITEAFFAHYGERVEAEIispnkTPDLPNFAET 235
Cdd:COG0095 157 GDLEKLAKVLRVPYEKLRDKGIKSVRSRVTNLSELLGtDITREEVKEALLEAFAEVLGVLEPGEL-----TDEELEAAEE 231
                       250
                ....*....|....*
gi 16132203 236 FA--RQSSWEWNFGQ 248
Cdd:COG0095 232 LAeeKYSSWEWNYGR 246
BPL_LplA_LipB cd16435
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ...
5-208 7.56e-76

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: 231.66  E-value: 7.56e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203   5 RLLISDSYDPWFNLAVEECIFRQMPA-TQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLG 83
Cdd:cd16435   1 FVEVLDSVDYESAWAAQEKSLRENVSnQSSTLLLWEHPTTVTLGRLDRELPHLELAKKIERGYELVVRNRGGRAVSHDPG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203  84 NTCFTFMAGKP-----EYDKTISTSIVLNALNALGVSAEAS-GRNDLVVKtvegDRKVSGSAYRETKDRGFHHGTLLLNA 157
Cdd:cd16435  81 QLVFSPVIGPNvefmiSKFNLIIEEGIRDAIADFGQSAEVKwGRNDLWID----NRKVCGIAVRVVKEAIFHGIALNLNQ 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 16132203 158 DLSRLANYLNPDKKklaakgitsVRSRVTNLTELLPGITHEQVCEAITEAF 208
Cdd:cd16435 157 DLENFTEIIPCGYK---------PERVTSLSLELGRKVTVEQVLERVLAAF 198
LplA cd16443
lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide ...
5-208 2.38e-75

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: 230.60  E-value: 2.38e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203   5 RLLISDSYDPWFNLAVEECIFRQMPA-TQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLG 83
Cdd:cd16443   2 RLIDSSGDPPAENLALDEALLRSVAApPTLRLYLWQNPPTVVIGRFQNPLEEVNLEYAEEDGIPVVRRPSGGGAVFHDLG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203  84 NTCFTFMAGKP----EYDKTISTSIVLNALNALGVSAEAS--GRNDLVVktveGDRKVSGSAYRETKDRGFHHGTLLLNA 157
Cdd:cd16443  82 NLNYSLILPKEhpsiDESYRALSQPVIKALRKLGVEAEFGgvGRNDLVV----GGKKISGSAQRRTKGRILHHGTLLVDV 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 16132203 158 DLSRLANYLNPDKKKLAAKGITSVRSRVTNLTELLPG-ITHEQVCEAITEAF 208
Cdd:cd16443 158 DLEKLARVLNVPYEKLKSKGPKSVRSRVTNLSELLGRdITVEEVKNALLEAF 209
Lip_prot_lig_C pfam10437
Bacterial lipoate protein ligase C-terminus; This is the C-terminal domain of a bacterial ...
249-333 2.91e-22

Bacterial lipoate protein ligase C-terminus; This is the C-terminal domain of a bacterial lipoate protein ligase. There is no conservation between this C-terminus and that of vertebrate lipoate protein ligase C-termini, but both are associated with the domain BPL_LipA_LipB pfam03099, further upstream. This domain is required for adenylation of lipoic acid by lipoate protein ligases. The domain is not required for transfer of lipoic acid from the adenylate to the lipoyl domain. Upon adenylation, this domain rotates 180 degrees away from the active site cleft. Therefore, the domain does not interact with the lipoyl domain during transfer.


Pssm-ID: 431286 [Multi-domain]  Cd Length: 85  Bit Score: 89.07  E-value: 2.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203   249 APAFSHLLDERFTWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVD--FPEQEKEl 326
Cdd:pfam10437   1 SPEFNYKRSKRFDWGTIEVRLNVEKGIIKDIKIYGDFFGPGDIEELEEALIGVRYEKEAIEKALEDIDLEeyFGNITLE- 79

                  ....*..
gi 16132203   327 rELSAWM 333
Cdd:pfam10437  80 -ELIELL 85
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
62-158 4.94e-07

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: 48.21  E-value: 4.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132203    62 EEDNVRLARRSSGG----GAVFHDLG---NTCFTFMAGKPEYD----KTISTSIVLNALNALGVSA--------EASGRN 122
Cdd:pfam03099  21 ESGGVVVVRRQTGGrgrgGNVWHSPKgclTYSLLLSKEHPNVDpsvlEFYVLELVLAVLEALGLYKpgisgipcFVKWPN 100
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 16132203   123 DLVVKtvegDRKVSGSAYRETKDRGFHHGTLLLNAD 158
Cdd:pfam03099 101 DLYVN----GRKLAGILQRSTRGGTLHHGVIGLGVN 132
 
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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