|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08330 |
PRK08330 |
biotin--protein ligase; Provisional |
9-235 |
1.14e-133 |
|
biotin--protein ligase; Provisional
Pssm-ID: 169384 [Multi-domain] Cd Length: 236 Bit Score: 375.62 E-value: 1.14e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 9 IGRRVIYFQEITSTNEFAK--TSYLEEGTVIVADKQTMGHGRLNRKWESPEGGLWLSIVLSPKVPQKDLPKIVFLGAVGV 86
Cdd:PRK08330 1 IGRNIIYFDEVDSTNEYAKriAPDEEEGTVIVADRQTAGHGRKGRAWASPEGGLWMSVILKPKVSPEHLPKLVFLGALAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 87 VETLKEFSIDGRIKWPNDVLVNYKAIAGVLVEGKGDKIVLGIGLNVNNKVPNG----ATSMKLELGSEVPLLSVFRSLIT 162
Cdd:PRK08330 81 VDTLREFGIEGKIKWPNDVLVNYKKIAGVLVEGKGDFVVLGIGLNVNNEIPDElretATSMKEVLGREVPLIEVFKRLVE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2DJZ_A 163 NLDRLYLNFLKNPMDIL-NLVRDNMILGVRVKILGDGSF--EGIAEDIDDFGRLIIRLDSGEVKKVIYGDVSLRFL 235
Cdd:PRK08330 161 NLDRWYKLFLEGPGEILeEVKGRSMILGKRVKIIGDGEIlvEGIAEDIDEFGALILRLDDGTVKKVLYGDVSLRFL 236
|
|
| BirA2 |
COG0340 |
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ... |
12-233 |
3.01e-76 |
|
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA carboxylase) ligase is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 440109 [Multi-domain] Cd Length: 241 Bit Score: 230.06 E-value: 3.01e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 12 RVIYFQEITSTNEFAK---TSYLEEGTVIVADKQTMGHGRLNRKWESPEG-GLWLSIVLSPKVPQKDLPKIVFLGAVGVV 87
Cdd:COG0340 1 RIEVFDEVDSTNDEAKelaREGAPEGTVVVAEEQTAGRGRRGRSWVSPPGkGLYFSLLLRPDLPPARLPLLSLAAGLAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 88 ETLKEFS-IDGRIKWPNDVLVNYKAIAGVLVEGKGDK-----IVLGIGLNVNNK------VPNGATSMKLELGSEVPLLS 155
Cdd:COG0340 81 EALRELTgVDVGLKWPNDILLNGKKLAGILIEASGEGdgidwVVIGIGINVNQPpfdpeeLDQPATSLKEETGKEVDREE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 156 VFRSLITNLDRLYLNFLKNPMD-ILNLVRDN-MILGVRVKI-LGDGSFEGIAEDIDDFGRLIIRLDSGEVKKVIYGDVSL 232
Cdd:COG0340 161 LLAALLEELEELYDRFLEEGFApILEEWRARlATLGRRVRVeTGGETLEGIAVGIDEDGALLLETADGEIRAVAAGEVSL 240
|
.
2DJZ_A 233 R 233
Cdd:COG0340 241 R 241
|
|
| BPL |
cd16442 |
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ... |
12-171 |
4.25e-57 |
|
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an activated form of biotin, biotinyl-5'-AMP, from substrates biotin and ATP followed by biotinylation of the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase. 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.
Pssm-ID: 319741 [Multi-domain] Cd Length: 173 Bit Score: 179.00 E-value: 4.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 12 RVIYFQEITSTNEFAKT---SYLEEGTVIVADKQTMGHGRLNRKWESPEG-GLWLSIVLSPKVPQKDLPKIVFLGAVGVV 87
Cdd:cd16442 1 KLIVLDEIDSTNDEAKElarSGAPEGTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPPAEAPLLTLLAAVAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 88 ETLKEFSI-DGRIKWPNDVLVNYKAIAGVLVEGKGDK-----IVLGIGLNVNNKVPNG---ATSMKLELGSEVPLLSVFR 158
Cdd:cd16442 81 EALEKLGGiPVQIKWPNDILVNGKKLAGILTEASAEGegvaaVVIGIGINVNNTPPPEplpDTSLATSLGKEVDRNELLE 160
|
170
....*....|...
2DJZ_A 159 SLITNLDRLYLNF 171
Cdd:cd16442 161 ELLAALENRLELF 173
|
|
| birA_ligase |
TIGR00121 |
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ... |
13-233 |
4.41e-50 |
|
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the biotin--acetyl-CoA-carboxylase ligase region of biotin--acetyl-CoA-carboxylase ligase. In Escherichia coli and some other species, this enzyme is part of a bifunction protein BirA that includes a small, N-terminal biotin operon repressor domain. Proteins identified by this model should not be called bifunctional unless they are also identified by birA_repr_reg (TIGR00122). The protein name suggests that this enzyme transfers biotin only to acetyl-CoA-carboxylase but it also transfers the biotin moiety to other proteins. The apparent orthologs among the eukaryotes are larger proteins that contain a single copy of this domain. [Protein fate, Protein modification and repair]
Pssm-ID: 272917 [Multi-domain] Cd Length: 237 Bit Score: 163.34 E-value: 4.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 13 VIYFQEITSTNEFAKTSYLE---EGTVIVADKQTMGHGRLNRKWESPEGGLWLSIVLSPKVPQKDLPKIVFLGAVGVVET 89
Cdd:TIGR00121 2 VIVLDVIDSTNQYALELAKEgklKGDLVVAEYQTAGRGRRGRKWLSPEGGLYFSLILRPDLPKSPAPGLTLVAGIAIAEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 90 LKEFSIDGRIKWPNDVLVNYKAIAGVLVEGKG-----DKIVLGIGLNVNNKVP-----NGATSMKLELGSEVPLLSVFRS 159
Cdd:TIGR00121 82 LKELGDQVQVKWPNDILLKDKKLGGILTELTGkenraDYVVIGIGINVQNRKPaeslrEQAISLSEEAGIDLDRGELIEG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2DJZ_A 160 LITNLDRLYLNFLKNPMD-ILNLVRD-NMILGVRVKIL-GDGSFEGIAEDIDDFGRLIIrLDSGEVKKVIYGDVSLR 233
Cdd:TIGR00121 162 FLRNFEENLEWFEQEGIDeILSKWEKlSAHIGREVSLTtGNGEIEGIARGIDKDGALLL-EDGGGIKKIISGEISLR 237
|
|
| BPL_LplA_LipB |
pfam03099 |
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ... |
13-133 |
1.37e-19 |
|
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: 81.33 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 13 VIYFQEITSTNEFA-KTSYLEEGTVIVADKQTMGHGRLNRKWESPEGGLWLSIVLS---PKVPQKDLPKIVFLGAVGVVE 88
Cdd:pfam03099 1 LGERIKSTNTYLEElNSSELESGGVVVVRRQTGGRGRGGNVWHSPKGCLTYSLLLSkehPNVDPSVLEFYVLELVLAVLE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
2DJZ_A 89 TLKEF-----SIDGRIKWPNDVLVNYKAIAGVLVEGKGDKIVLG--IGLNVN 133
Cdd:pfam03099 81 ALGLYkpgisGIPCFVKWPNDLYVNGRKLAGILQRSTRGGTLHHgvIGLGVN 132
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08330 |
PRK08330 |
biotin--protein ligase; Provisional |
9-235 |
1.14e-133 |
|
biotin--protein ligase; Provisional
Pssm-ID: 169384 [Multi-domain] Cd Length: 236 Bit Score: 375.62 E-value: 1.14e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 9 IGRRVIYFQEITSTNEFAK--TSYLEEGTVIVADKQTMGHGRLNRKWESPEGGLWLSIVLSPKVPQKDLPKIVFLGAVGV 86
Cdd:PRK08330 1 IGRNIIYFDEVDSTNEYAKriAPDEEEGTVIVADRQTAGHGRKGRAWASPEGGLWMSVILKPKVSPEHLPKLVFLGALAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 87 VETLKEFSIDGRIKWPNDVLVNYKAIAGVLVEGKGDKIVLGIGLNVNNKVPNG----ATSMKLELGSEVPLLSVFRSLIT 162
Cdd:PRK08330 81 VDTLREFGIEGKIKWPNDVLVNYKKIAGVLVEGKGDFVVLGIGLNVNNEIPDElretATSMKEVLGREVPLIEVFKRLVE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2DJZ_A 163 NLDRLYLNFLKNPMDIL-NLVRDNMILGVRVKILGDGSF--EGIAEDIDDFGRLIIRLDSGEVKKVIYGDVSLRFL 235
Cdd:PRK08330 161 NLDRWYKLFLEGPGEILeEVKGRSMILGKRVKIIGDGEIlvEGIAEDIDEFGALILRLDDGTVKKVLYGDVSLRFL 236
|
|
| BirA2 |
COG0340 |
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ... |
12-233 |
3.01e-76 |
|
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA carboxylase) ligase is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 440109 [Multi-domain] Cd Length: 241 Bit Score: 230.06 E-value: 3.01e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 12 RVIYFQEITSTNEFAK---TSYLEEGTVIVADKQTMGHGRLNRKWESPEG-GLWLSIVLSPKVPQKDLPKIVFLGAVGVV 87
Cdd:COG0340 1 RIEVFDEVDSTNDEAKelaREGAPEGTVVVAEEQTAGRGRRGRSWVSPPGkGLYFSLLLRPDLPPARLPLLSLAAGLAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 88 ETLKEFS-IDGRIKWPNDVLVNYKAIAGVLVEGKGDK-----IVLGIGLNVNNK------VPNGATSMKLELGSEVPLLS 155
Cdd:COG0340 81 EALRELTgVDVGLKWPNDILLNGKKLAGILIEASGEGdgidwVVIGIGINVNQPpfdpeeLDQPATSLKEETGKEVDREE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 156 VFRSLITNLDRLYLNFLKNPMD-ILNLVRDN-MILGVRVKI-LGDGSFEGIAEDIDDFGRLIIRLDSGEVKKVIYGDVSL 232
Cdd:COG0340 161 LLAALLEELEELYDRFLEEGFApILEEWRARlATLGRRVRVeTGGETLEGIAVGIDEDGALLLETADGEIRAVAAGEVSL 240
|
.
2DJZ_A 233 R 233
Cdd:COG0340 241 R 241
|
|
| BPL |
cd16442 |
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ... |
12-171 |
4.25e-57 |
|
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an activated form of biotin, biotinyl-5'-AMP, from substrates biotin and ATP followed by biotinylation of the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase. 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.
Pssm-ID: 319741 [Multi-domain] Cd Length: 173 Bit Score: 179.00 E-value: 4.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 12 RVIYFQEITSTNEFAKT---SYLEEGTVIVADKQTMGHGRLNRKWESPEG-GLWLSIVLSPKVPQKDLPKIVFLGAVGVV 87
Cdd:cd16442 1 KLIVLDEIDSTNDEAKElarSGAPEGTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPPAEAPLLTLLAAVAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 88 ETLKEFSI-DGRIKWPNDVLVNYKAIAGVLVEGKGDK-----IVLGIGLNVNNKVPNG---ATSMKLELGSEVPLLSVFR 158
Cdd:cd16442 81 EALEKLGGiPVQIKWPNDILVNGKKLAGILTEASAEGegvaaVVIGIGINVNNTPPPEplpDTSLATSLGKEVDRNELLE 160
|
170
....*....|...
2DJZ_A 159 SLITNLDRLYLNF 171
Cdd:cd16442 161 ELLAALENRLELF 173
|
|
| birA_ligase |
TIGR00121 |
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ... |
13-233 |
4.41e-50 |
|
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the biotin--acetyl-CoA-carboxylase ligase region of biotin--acetyl-CoA-carboxylase ligase. In Escherichia coli and some other species, this enzyme is part of a bifunction protein BirA that includes a small, N-terminal biotin operon repressor domain. Proteins identified by this model should not be called bifunctional unless they are also identified by birA_repr_reg (TIGR00122). The protein name suggests that this enzyme transfers biotin only to acetyl-CoA-carboxylase but it also transfers the biotin moiety to other proteins. The apparent orthologs among the eukaryotes are larger proteins that contain a single copy of this domain. [Protein fate, Protein modification and repair]
Pssm-ID: 272917 [Multi-domain] Cd Length: 237 Bit Score: 163.34 E-value: 4.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 13 VIYFQEITSTNEFAKTSYLE---EGTVIVADKQTMGHGRLNRKWESPEGGLWLSIVLSPKVPQKDLPKIVFLGAVGVVET 89
Cdd:TIGR00121 2 VIVLDVIDSTNQYALELAKEgklKGDLVVAEYQTAGRGRRGRKWLSPEGGLYFSLILRPDLPKSPAPGLTLVAGIAIAEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 90 LKEFSIDGRIKWPNDVLVNYKAIAGVLVEGKG-----DKIVLGIGLNVNNKVP-----NGATSMKLELGSEVPLLSVFRS 159
Cdd:TIGR00121 82 LKELGDQVQVKWPNDILLKDKKLGGILTELTGkenraDYVVIGIGINVQNRKPaeslrEQAISLSEEAGIDLDRGELIEG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2DJZ_A 160 LITNLDRLYLNFLKNPMD-ILNLVRD-NMILGVRVKIL-GDGSFEGIAEDIDDFGRLIIrLDSGEVKKVIYGDVSLR 233
Cdd:TIGR00121 162 FLRNFEENLEWFEQEGIDeILSKWEKlSAHIGREVSLTtGNGEIEGIARGIDKDGALLL-EDGGGIKKIISGEISLR 237
|
|
| PRK11886 |
PRK11886 |
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA; |
4-233 |
2.47e-36 |
|
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
Pssm-ID: 237010 [Multi-domain] Cd Length: 319 Bit Score: 130.29 E-value: 2.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 4 LKTSIIGRRVIYFQEITSTNEFAK--TSYLEEGTVIVADKQTMGHGRLNRKWESPEGG-LWLSIVLSPKVPQKDLPKIVF 80
Cdd:PRK11886 71 ISSQLPPGRVTVLPVIDSTNQYLLdrIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGnLYLSLYWRLNQGPAQAMGLSL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 81 LGAVGVVETLKEFSIDG-RIKWPNDVLVNYKAIAGVLVEGKGDK-----IVLGIGLNVNNKVPNGA------TSMKlELG 148
Cdd:PRK11886 151 VVGIAIAEALRRLGAIDvGLKWPNDIYLNDRKLAGILVELSGETgdaahVVIGIGINVAMPDFPEElidqpwSDLQ-EAG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 149 SEVP----LLSVFRSLITNLDRlylnFLKNPMDILNLV--RDNMILGVRVKIL-GDGSFEGIAEDIDDFGRLIIRLDsGE 221
Cdd:PRK11886 230 PTIDrnqlAAELIKQLRAALEL----FEQEGLAPFLERwkKLDLFLGREVKLIiGDKEISGIARGIDEQGALLLEDD-GV 304
|
250
....*....|..
2DJZ_A 222 VKKVIYGDVSLR 233
Cdd:PRK11886 305 EKPFNGGEISLR 316
|
|
| BirA |
COG1654 |
Biotin operon repressor [Transcription]; |
3-233 |
8.14e-20 |
|
Biotin operon repressor [Transcription];
Pssm-ID: 441260 [Multi-domain] Cd Length: 324 Bit Score: 86.19 E-value: 8.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 3 GLKTSIIGRRVIYFQEITSTNEFAKTSYLE---EGTVIVADKQTMGHGRLNRKWESPEGGLWLSIVLSPKVPQKDLPKIV 79
Cdd:COG1654 74 GLSTKRLGREILYVISSTSTNLLALELAAQggdAGTVVAAEQQRGGRGRRRRSWSSPGGGGLLYSLLLRPPIAPALLSLL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 80 FLGAVGVVETLKEFS--IDGRIKWPNDVLVNYKAIAGVLVEGKGD----KIVLGIGLNVNNKVPNG--------ATSMKL 145
Cdd:COG1654 154 LLAAAVAVAAALAEGggLVKWKKWPNDLLKKGKKILGILEEEGGDadgvVIVVGGGGNNNNSNPEEepqelaelATSLLL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 146 ELGSEVPLLSVFRSLITNLDRLYLNFLKN---PMDILNLVRDNMILGVRVKILGDGSFEGIAEDIDDFGRLIIRLDSGEV 222
Cdd:COG1654 234 ILRLRLLRLLLLLLLLLLELLELLGFLEFfflWERLDWELLRVLKLVVVVVEIGGGGGGGGALGGGLLGLLLLGGGGGGG 313
|
250
....*....|.
2DJZ_A 223 KKVIYGDVSLR 233
Cdd:COG1654 314 EGSLSAVVVLL 324
|
|
| BPL_LplA_LipB |
pfam03099 |
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ... |
13-133 |
1.37e-19 |
|
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: 81.33 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 13 VIYFQEITSTNEFA-KTSYLEEGTVIVADKQTMGHGRLNRKWESPEGGLWLSIVLS---PKVPQKDLPKIVFLGAVGVVE 88
Cdd:pfam03099 1 LGERIKSTNTYLEElNSSELESGGVVVVRRQTGGRGRGGNVWHSPKGCLTYSLLLSkehPNVDPSVLEFYVLELVLAVLE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
2DJZ_A 89 TLKEF-----SIDGRIKWPNDVLVNYKAIAGVLVEGKGDKIVLG--IGLNVN 133
Cdd:pfam03099 81 ALGLYkpgisGIPCFVKWPNDLYVNGRKLAGILQRSTRGGTLHHgvIGLGVN 132
|
|
| PRK05935 |
PRK05935 |
biotin--protein ligase; Provisional |
12-161 |
2.94e-19 |
|
biotin--protein ligase; Provisional
Pssm-ID: 235649 [Multi-domain] Cd Length: 190 Bit Score: 82.17 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 12 RVIYFQ--EITSTNEFAKtSYLE-----EGTVIVADKQTMGHGRLNRKWESPEGGLWLSIVLSPKVPQKDLPKIVFLGAV 84
Cdd:PRK05935 2 KVIYYEiaETPSTNTTAK-EGMHlwdpyALTVISTREQTAGKGKFGKSWHSSDQDLLASFCFFITVLNIDVSLLFRLGTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 85 GVVETLKEFSI-DGRIKWPNDVLVNYKAIAGVLVEG----KGDKIVLGIGLNVN------NKVPNGATSMKLELGSEVPL 153
Cdd:PRK05935 81 AVMRLGEDLGItEAVIKWPNDVLVHGEKLCGVLCETipvkGGLGVILGIGVNGNttkdelLGIDQPATSLQELLGHPIDL 160
|
....*...
2DJZ_A 154 LSVFRSLI 161
Cdd:PRK05935 161 EEQRERLI 168
|
|
| PTZ00276 |
PTZ00276 |
biotin/lipoate protein ligase; Provisional |
15-132 |
5.47e-17 |
|
biotin/lipoate protein ligase; Provisional
Pssm-ID: 140302 [Multi-domain] Cd Length: 245 Bit Score: 77.21 E-value: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 15 YFQEITSTNEFAKTSYLEEGTV---IVADKQTMGHGRLNRKWESPEGGLWLSIVlspkVPQKD--------LPKIVFLGA 83
Cdd:PTZ00276 11 FVGEVTSTMDVARTMLAAAGGKpfaVLAESQTAGRGTGGRTWTSPKGNMYFTLC----IPQKGvppelvpvLPLITGLAC 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
2DJZ_A 84 -VGVVETLKEFSIdgRIKWPNDVLVNYKAIAGVLVEGKGDKIVLGIGLNV 132
Cdd:PTZ00276 87 rAAIMEVLHGAAV--HTKWPNDIIYAGKKIGGSLIESEGEYLIIGIGMNI 134
|
|
| PRK08477 |
PRK08477 |
biotin--[acetyl-CoA-carboxylase] ligase; |
13-165 |
7.78e-17 |
|
biotin--[acetyl-CoA-carboxylase] ligase;
Pssm-ID: 236273 [Multi-domain] Cd Length: 211 Bit Score: 76.15 E-value: 7.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 13 VIYFQEITSTNEFAKTsYLEEGTV-----IVADKQTMGHGRLNRKWESPEGGLWLSIVLSPKVPQKDLPKI---VFLGAV 84
Cdd:PRK08477 3 IRVFESLDSTQTYLIE-KIKNGELkapfaIVAKEQTAGIGSRGNSWEGKKGNLFFSFALKESDLPKDLPLQsssIYFGFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 85 gVVETLKEFSIDGRIKWPNDVLVNYKAIAGVLVEGKGDKIVLGIGLNVNNkVPNGATSmkleLGSEVPLLSVFRSLITNL 164
Cdd:PRK08477 82 -LKEVLKELGSKVWLKWPNDLYLDDKKIGGVITNKIKNFIVCGIGLNLKF-SPKNFAC----LDIEISDDLLLEGFLQKI 155
|
.
2DJZ_A 165 D 165
Cdd:PRK08477 156 E 156
|
|
| PRK06955 |
PRK06955 |
biotin--[acetyl-CoA-carboxylase] ligase; |
31-233 |
8.84e-14 |
|
biotin--[acetyl-CoA-carboxylase] ligase;
Pssm-ID: 235896 [Multi-domain] Cd Length: 300 Bit Score: 69.04 E-value: 8.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 31 LEEGTVIVADKQTMGHGRLNRKWESPEG-GLWLSIVLSPKVPQKDLPKIVFLGAVGVVETLKEFSIDGR----IKWPNDV 105
Cdd:PRK06955 62 LPAPIVRVAYEQTAGRGRQGRPWFAQPGnALLFSVACVLPRPVAALAGLSLAVGVALAEALAALPAALGqriaLKWPNDL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 106 LVNYKAIAGVLVEG--KGDK---IVLGIGLNVNNKVPNGATSMKLE-----LGSEVP------------LLSVFRSLITN 163
Cdd:PRK06955 142 LIAGRKLAGILIETvwATPDataVVIGIGLNVRRADAVAAEVDALRareaaLARGLPpvalaaacaganLTDTLAAALNA 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2DJZ_A 164 LDRLYLNFLKN---PMDILNLVRDnMILGVRVKILGDGS--FEGIAEDIDDFGRLIirLDSGE-VKKVIYGDVSLR 233
Cdd:PRK06955 222 LAPALQAFGADglaPFAARWHALH-AYAGREVVLLEDGAelARGVAHGIDETGQLL--LDTPAgRQAIAAGDVSLR 294
|
|
| PTZ00275 |
PTZ00275 |
biotin-acetyl-CoA-carboxylase ligase; Provisional |
14-147 |
2.82e-12 |
|
biotin-acetyl-CoA-carboxylase ligase; Provisional
Pssm-ID: 185536 [Multi-domain] Cd Length: 285 Bit Score: 64.46 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 14 IYFQEITSTNEFAKTS---YLEEGT-------VIVADKQTMGHG------RLNRKWESPEGGLWLSIVLSPKvpQKDLPK 77
Cdd:PTZ00275 20 LHFDVLDSTQLYCKRNmkrFIQNGKlqddnmiIVSCNEQTNGIGtrdtkkNQDRIWLSEKGNLFTTFVFLWN--RNDIEK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 78 IVFLG---AVGVVETLKEFSIDGRIKWPNDVLVNYKAIAGVLVE-----------GKGDKIVLGIGLNVN-----NKVPN 138
Cdd:PTZ00275 98 VKYLAqtcTVAISKTLEYFHLVTQIKWINDVLVNYKKIAGCLVHlyylddfpnlnSRYVCVMVGIGINVTledkhNLLNN 177
|
....*....
2DJZ_A 139 GATSMKLEL 147
Cdd:PTZ00275 178 NYTSIKKEL 186
|
|
| PRK13325 |
PRK13325 |
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase; |
35-233 |
4.20e-10 |
|
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase;
Pssm-ID: 183976 [Multi-domain] Cd Length: 592 Bit Score: 58.95 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 35 TVIVADKQTMGHGRLNRKWESPEGG-LWLSIVLSPKVPQKDLPKIVFLGAVGVVETLKEFSIDGRIKWPNDVLVNYKAIA 113
Cdd:PRK13325 111 TICVTHLQSKGRGRQGRKWSHRLGEcLMFSFGWVFDRPQYELGSLSPVAAVACRRALSRLGLKTQIKWPNDLVVGRDKLG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 114 GVLVE----GKGDKIVLGIGLN--VNNKVPNGATSMKL--------ELGSEVPLLSVFRSLITNLDRL----YLNFLkNP 175
Cdd:PRK13325 191 GILIEtvrtGGKTVAVVGIGINfvLPKEVENAASVQSLfqtasrrgNADAAVLLETLLAELDAVLLQYardgFAPFV-AE 269
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
2DJZ_A 176 MDILNlvRDNmilGVRVKILGDGSF--EGIAEDIDdfGRLIIRLDSGEVKK-VIYGDVSLR 233
Cdd:PRK13325 270 YQAAN--RDH---GKAVLLLRDGETvfEGTVKGVD--GQGVLHLETAEGKQtVVSGEISLR 323
|
|
| BPL_C |
pfam02237 |
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ... |
187-233 |
5.61e-10 |
|
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It is found to the C terminus of the biotin protein ligase catalytic domain pfam01317.
Pssm-ID: 426672 [Multi-domain] Cd Length: 48 Bit Score: 53.23 E-value: 5.61e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
2DJZ_A 187 ILGVRVKI-LGDGSFEGIAEDIDDFGRLIIRLDSGEVKKVIYGDVSLR 233
Cdd:pfam02237 1 TLGREVRVlLGDGIVEGIAVGIDDDGALLLETDDGTIRDINSGEVSLR 48
|
|
| BPL_LplA_LipB |
cd16435 |
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ... |
48-152 |
2.87e-07 |
|
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: 49.46 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DJZ_A 48 RLNRKWESPEGGLWLSIVLsPKVPQKDLPKIVFLGAVGVVETLKEFSIDGRIKW-PNDVLVNYKAIAGVLVEGKGDKIVL 126
Cdd:cd16435 70 RGGRAVSHDPGQLVFSPVI-GPNVEFMISKFNLIIEEGIRDAIADFGQSAEVKWgRNDLWIDNRKVCGIAVRVVKEAIFH 148
|
90 100 110
....*....|....*....|....*....|....*...
2DJZ_A 127 GIGLNVN------------NKVPNGATSMKLELGSEVP 152
Cdd:cd16435 149 GIALNLNqdlenfteiipcGYKPERVTSLSLELGRKVT 186
|
|
| |
