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Conserved domains on  [gi|18400914|ref|NP_565605|]
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holocarboxylase synthase 1 [Arabidopsis thaliana]

Protein Classification

lipoate--protein ligase family protein( domain architecture ID 11612795)

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 cd16442
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
 113-288 8.10e-48

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: 159.74  E-value: 8.10e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914 113 FLIWSPRLSSTHDVVSHNFSEL-PVGSVCVTDIQFKGRGRTKNVWESPKG-CLMYSFTLEMEDG-RVVPLIQYVVSLAVT 189
Cdd:cd16442   1 KLIVLDEIDSTNDEAKELARSGaPEGTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPpAEAPLLTLLAAVAVA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914 190 EAVKDVCDkkglpyIDVKIKWPNDLYVNGLKVGGILCTSTYR-SKKFNVSVGVGLNVDNGQPTTCLNAVLKGMAPESNlL 268
Cdd:cd16442  81 EALEKLGG------IPVQIKWPNDILVNGKKLAGILTEASAEgEGVAAVVIGIGINVNNTPPPEPLPDTSLATSLGKE-V 153

                       170       180
                ....*....|....*....|
gi 18400914 269 KREEILGAFFHKFEKFFDLF 288
Cdd:cd16442 154 DRNELLEELLAALENRLELF 173
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
 306-361 1.05e-04

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: 39.37  E-value: 1.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 18400914   306 HSEQRVIVEDkvEDQVVqnVVTIQGLTSSGYLLAVGDDNQmyelHPDGNSFDFFKG 361
Cdd:pfam02237   1 TLGREVRVLL--GDGIV--EGIAVGIDDDGALLLETDDGT----IRDINSGEVSLR 48
 
Name Accession Description Interval E-value
BPL cd16442
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
 113-288 8.10e-48

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: 159.74  E-value: 8.10e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914 113 FLIWSPRLSSTHDVVSHNFSEL-PVGSVCVTDIQFKGRGRTKNVWESPKG-CLMYSFTLEMEDG-RVVPLIQYVVSLAVT 189
Cdd:cd16442   1 KLIVLDEIDSTNDEAKELARSGaPEGTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPpAEAPLLTLLAAVAVA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914 190 EAVKDVCDkkglpyIDVKIKWPNDLYVNGLKVGGILCTSTYR-SKKFNVSVGVGLNVDNGQPTTCLNAVLKGMAPESNlL 268
Cdd:cd16442  81 EALEKLGG------IPVQIKWPNDILVNGKKLAGILTEASAEgEGVAAVVIGIGINVNNTPPPEPLPDTSLATSLGKE-V 153

                       170       180
                ....*....|....*....|
gi 18400914 269 KREEILGAFFHKFEKFFDLF 288
Cdd:cd16442 154 DRNELLEELLAALENRLELF 173
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 116-244 8.51e-43

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: 145.28  E-value: 8.51e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914   116 WSPRLSSTHDVV-SHNFSELPVGSVCVTDIQFKGRGRTKNVWESPKGCLMYSFTLEME----DGRVVPLIQYVVSLAVTE 190
Cdd:pfam03099   1 LGERIKSTNTYLeELNSSELESGGVVVVRRQTGGRGRGGNVWHSPKGCLTYSLLLSKEhpnvDPSVLEFYVLELVLAVLE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 18400914   191 AVKDvcDKKGLPYIDVKIKWPNDLYVNGLKVGGILCTSTYRSKKFNVSVGVGLN 244
Cdd:pfam03099  81 ALGL--YKPGISGIPCFVKWPNDLYVNGRKLAGILQRSTRGGTLHHGVIGLGVN 132
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 114-350 1.16e-40

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: 143.39  E-value: 1.16e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914 114 LIWSPRLSSTHDVVSHNFSE-LPVGSVCVTDIQFKGRGRTKNVWESPKG-CLMYSFTLEMEDG-RVVPLIQYVVSLAVTE 190
Cdd:COG0340   2 IEVFDEVDSTNDEAKELAREgAPEGTVVVAEEQTAGRGRRGRSWVSPPGkGLYFSLLLRPDLPpARLPLLSLAAGLAVAE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914 191 AVKDVCDkkglpyIDVKIKWPNDLYVNGLKVGGILCTSTYRSKKFNVSV-GVGLNVDN--------GQPTTCLNAVLkGM 261
Cdd:COG0340  82 ALRELTG------VDVGLKWPNDILLNGKKLAGILIEASGEGDGIDWVViGIGINVNQppfdpeelDQPATSLKEET-GK 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914 262 APEsnllkREEILGAFFHKFEKFFDLFMDQGFKSLEELYYRTWLHSEQRVIVEDkvEDQVVQNvvTIQGLTSSGYLLAVG 341
Cdd:COG0340 155 EVD-----REELLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVET--GGETLEG--IAVGIDEDGALLLET 225


                ....*....
gi 18400914 342 DDNQMYELH 350
Cdd:COG0340 226 ADGEIRAVA 234
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 114-342 5.59e-26

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: 104.02  E-value: 5.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914   114 LIWSPRLSSTHDVVSHNFSEL-PVGSVCVTDIQFKGRGRTKNVWESPKGCLMYSFTLEMEDGRV-VPLIQYVVSLAVTEA 191
Cdd:TIGR00121   2 VIVLDVIDSTNQYALELAKEGkLKGDLVVAEYQTAGRGRRGRKWLSPEGGLYFSLILRPDLPKSpAPGLTLVAGIAIAEV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914   192 VKDVCDkkglpyiDVKIKWPNDLYVNGLKVGGILCTSTYRSKKF-NVSVGVGLNVDNGQPTTCLNAVLKGMAPESNL-LK 269
Cdd:TIGR00121  82 LKELGD-------QVQVKWPNDILLKDKKLGGILTELTGKENRAdYVVIGIGINVQNRKPAESLREQAISLSEEAGIdLD 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18400914   270 REEILGAFFHKFEKFFDLFMDQGFKSLEELYYRTWLHSEQRVivedKVEDQVVQNVVTIQGLTSSGYLLAVGD 342
Cdd:TIGR00121 155 RGELIEGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREV----SLTTGNGEIEGIARGIDKDGALLLEDG 223
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
118-345 1.17e-22

bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 96.78  E-value: 1.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914  118 PRLSSTHDVVSHNFSELPVGSVCVTDIQFKGRGRTKNVWESPKGC-LMYSFTLEMEDGrVVPLIQY--VVSLAVTEAVKD 194
Cdd:PRK11886  84 PVIDSTNQYLLDRIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGnLYLSLYWRLNQG-PAQAMGLslVVGIAIAEALRR 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914  195 vcdkkgLPYIDVKIKWPNDLYVNGLKVGGIL----------CtstyrskkfNVSVGVGLNV---DN-----GQPTTCLNA 256
Cdd:PRK11886 163 ------LGAIDVGLKWPNDIYLNDRKLAGILvelsgetgdaA---------HVVIGIGINVampDFpeeliDQPWSDLQE 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914  257 VLKgmapesnLLKREEILGAFFHKFEKFFDLFMDQGFKSLEELYYRT--WLHSEQRVIVEDKVEDQVVqnvvtiQGLTSS 334
Cdd:PRK11886 228 AGP-------TIDRNQLAAELIKQLRAALELFEQEGLAPFLERWKKLdlFLGREVKLIIGDKEISGIA------RGIDEQ 294

                        250
                 ....*....|.
gi 18400914  335 GYLLaVGDDNQ 345
Cdd:PRK11886 295 GALL-LEDDGV 304
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
 306-361 1.05e-04

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: 39.37  E-value: 1.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 18400914   306 HSEQRVIVEDkvEDQVVqnVVTIQGLTSSGYLLAVGDDNQmyelHPDGNSFDFFKG 361
Cdd:pfam02237   1 TLGREVRVLL--GDGIV--EGIAVGIDDDGALLLETDDGT----IRDINSGEVSLR 48
 
Name Accession Description Interval E-value
BPL cd16442
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
 113-288 8.10e-48

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: 159.74  E-value: 8.10e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914 113 FLIWSPRLSSTHDVVSHNFSEL-PVGSVCVTDIQFKGRGRTKNVWESPKG-CLMYSFTLEMEDG-RVVPLIQYVVSLAVT 189
Cdd:cd16442   1 KLIVLDEIDSTNDEAKELARSGaPEGTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPpAEAPLLTLLAAVAVA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914 190 EAVKDVCDkkglpyIDVKIKWPNDLYVNGLKVGGILCTSTYR-SKKFNVSVGVGLNVDNGQPTTCLNAVLKGMAPESNlL 268
Cdd:cd16442  81 EALEKLGG------IPVQIKWPNDILVNGKKLAGILTEASAEgEGVAAVVIGIGINVNNTPPPEPLPDTSLATSLGKE-V 153

                       170       180
                ....*....|....*....|
gi 18400914 269 KREEILGAFFHKFEKFFDLF 288
Cdd:cd16442 154 DRNELLEELLAALENRLELF 173
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 116-244 8.51e-43

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: 145.28  E-value: 8.51e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914   116 WSPRLSSTHDVV-SHNFSELPVGSVCVTDIQFKGRGRTKNVWESPKGCLMYSFTLEME----DGRVVPLIQYVVSLAVTE 190
Cdd:pfam03099   1 LGERIKSTNTYLeELNSSELESGGVVVVRRQTGGRGRGGNVWHSPKGCLTYSLLLSKEhpnvDPSVLEFYVLELVLAVLE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 18400914   191 AVKDvcDKKGLPYIDVKIKWPNDLYVNGLKVGGILCTSTYRSKKFNVSVGVGLN 244
Cdd:pfam03099  81 ALGL--YKPGISGIPCFVKWPNDLYVNGRKLAGILQRSTRGGTLHHGVIGLGVN 132
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 114-350 1.16e-40

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: 143.39  E-value: 1.16e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914 114 LIWSPRLSSTHDVVSHNFSE-LPVGSVCVTDIQFKGRGRTKNVWESPKG-CLMYSFTLEMEDG-RVVPLIQYVVSLAVTE 190
Cdd:COG0340   2 IEVFDEVDSTNDEAKELAREgAPEGTVVVAEEQTAGRGRRGRSWVSPPGkGLYFSLLLRPDLPpARLPLLSLAAGLAVAE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914 191 AVKDVCDkkglpyIDVKIKWPNDLYVNGLKVGGILCTSTYRSKKFNVSV-GVGLNVDN--------GQPTTCLNAVLkGM 261
Cdd:COG0340  82 ALRELTG------VDVGLKWPNDILLNGKKLAGILIEASGEGDGIDWVViGIGINVNQppfdpeelDQPATSLKEET-GK 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914 262 APEsnllkREEILGAFFHKFEKFFDLFMDQGFKSLEELYYRTWLHSEQRVIVEDkvEDQVVQNvvTIQGLTSSGYLLAVG 341
Cdd:COG0340 155 EVD-----REELLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVET--GGETLEG--IAVGIDEDGALLLET 225


                ....*....
gi 18400914 342 DDNQMYELH 350
Cdd:COG0340 226 ADGEIRAVA 234
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 114-342 5.59e-26

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: 104.02  E-value: 5.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914   114 LIWSPRLSSTHDVVSHNFSEL-PVGSVCVTDIQFKGRGRTKNVWESPKGCLMYSFTLEMEDGRV-VPLIQYVVSLAVTEA 191
Cdd:TIGR00121   2 VIVLDVIDSTNQYALELAKEGkLKGDLVVAEYQTAGRGRRGRKWLSPEGGLYFSLILRPDLPKSpAPGLTLVAGIAIAEV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914   192 VKDVCDkkglpyiDVKIKWPNDLYVNGLKVGGILCTSTYRSKKF-NVSVGVGLNVDNGQPTTCLNAVLKGMAPESNL-LK 269
Cdd:TIGR00121  82 LKELGD-------QVQVKWPNDILLKDKKLGGILTELTGKENRAdYVVIGIGINVQNRKPAESLREQAISLSEEAGIdLD 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18400914   270 REEILGAFFHKFEKFFDLFMDQGFKSLEELYYRTWLHSEQRVivedKVEDQVVQNVVTIQGLTSSGYLLAVGD 342
Cdd:TIGR00121 155 RGELIEGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREV----SLTTGNGEIEGIARGIDKDGALLLEDG 223
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
118-345 1.17e-22

bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 96.78  E-value: 1.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914  118 PRLSSTHDVVSHNFSELPVGSVCVTDIQFKGRGRTKNVWESPKGC-LMYSFTLEMEDGrVVPLIQY--VVSLAVTEAVKD 194
Cdd:PRK11886  84 PVIDSTNQYLLDRIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGnLYLSLYWRLNQG-PAQAMGLslVVGIAIAEALRR 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914  195 vcdkkgLPYIDVKIKWPNDLYVNGLKVGGIL----------CtstyrskkfNVSVGVGLNV---DN-----GQPTTCLNA 256
Cdd:PRK11886 163 ------LGAIDVGLKWPNDIYLNDRKLAGILvelsgetgdaA---------HVVIGIGINVampDFpeeliDQPWSDLQE 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914  257 VLKgmapesnLLKREEILGAFFHKFEKFFDLFMDQGFKSLEELYYRT--WLHSEQRVIVEDKVEDQVVqnvvtiQGLTSS 334
Cdd:PRK11886 228 AGP-------TIDRNQLAAELIKQLRAALELFEQEGLAPFLERWKKLdlFLGREVKLIIGDKEISGIA------RGIDEQ 294

                        250
                 ....*....|.
gi 18400914  335 GYLLaVGDDNQ 345
Cdd:PRK11886 295 GALL-LEDDGV 304
PRK08330 PRK08330
biotin--protein ligase; Provisional
 111-318 3.07e-19

biotin--protein ligase; Provisional


Pssm-ID: 169384 [Multi-domain]  Cd Length: 236  Bit Score: 85.57  E-value: 3.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914  111 GRFLIWSPRLSSTHDVVSHNFSELPVGSVCVTDIQFKGRGRTKNVWESPKGCLMYSFTL----EMEDgrvVPLIQYVVSL 186
Cdd:PRK08330   2 GRNIIYFDEVDSTNEYAKRIAPDEEEGTVIVADRQTAGHGRKGRAWASPEGGLWMSVILkpkvSPEH---LPKLVFLGAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914  187 AVTEAVKDVCdkkglpyIDVKIKWPNDLYVNGLKVGGILCtstyRSKKFNVSVGVGLNVDNGQP------TTCLNAVLKG 260
Cdd:PRK08330  79 AVVDTLREFG-------IEGKIKWPNDVLVNYKKIAGVLV----EGKGDFVVLGIGLNVNNEIPdelretATSMKEVLGR 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18400914  261 MAPESNLLKReeilgaFFHKFEKFFDLFMDQGFKSLEELYYRTW-LHSEQRVIVEDKVE 318
Cdd:PRK08330 148 EVPLIEVFKR------LVENLDRWYKLFLEGPGEILEEVKGRSMiLGKRVKIIGDGEIL 200
PRK08477 PRK08477
biotin--[acetyl-CoA-carboxylase] ligase;
141-284 2.60e-12

biotin--[acetyl-CoA-carboxylase] ligase;


Pssm-ID: 236273 [Multi-domain]  Cd Length: 211  Bit Score: 65.36  E-value: 2.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914  141 VTDIQFKGRGRTKNVWESPKGCLMYSFTLEMED-GRVVPLIQyvVSLAVTEAVKDVCDKKGLpyiDVKIKWPNDLYVNGL 219
Cdd:PRK08477  32 VAKEQTAGIGSRGNSWEGKKGNLFFSFALKESDlPKDLPLQS--SSIYFGFLLKEVLKELGS---KVWLKWPNDLYLDDK 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18400914  220 KVGGILcTSTYRSkkfNVSVGVGLNVDNG-QPTTCLNAVlkgmapesnlLKREEILGAFFHKFEKF 284
Cdd:PRK08477 107 KIGGVI-TNKIKN---FIVCGIGLNLKFSpKNFACLDIE----------ISDDLLLEGFLQKIEKK 158
PTZ00276 PTZ00276
biotin/lipoate protein ligase; Provisional
 141-294 3.92e-12

biotin/lipoate protein ligase; Provisional


Pssm-ID: 140302 [Multi-domain]  Cd Length: 245  Bit Score: 65.66  E-value: 3.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914  141 VTDIQFKGRGRTKNVWESPKGCLMYSFTL--EMEDGRVVPLIQYVVSLAVTEAVKDVCDKKGlpyidVKIKWPNDLYVNG 218
Cdd:PTZ00276  37 LAESQTAGRGTGGRTWTSPKGNMYFTLCIpqKGVPPELVPVLPLITGLACRAAIMEVLHGAA-----VHTKWPNDIIYAG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914  219 LKVGGILCTSTYRSkkfnVSVGVGLNV-------DNGQPTTCLNAVLKGMAPESnlLKREEILGAFFHkfeKFFDLFMDQ 291
Cdd:PTZ00276 112 KKIGGSLIESEGEY----LIIGIGMNIevappvtDAGRESTMVNEIAEDLGVKS--VTPQDLAEAVWK---HFFDICSDP 182


                 ...
gi 18400914  292 GFK 294
Cdd:PTZ00276 183 ELT 185
PRK05935 PRK05935
biotin--protein ligase; Provisional
 138-292 1.09e-10

biotin--protein ligase; Provisional


Pssm-ID: 235649 [Multi-domain]  Cd Length: 190  Bit Score: 60.22  E-value: 1.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914  138 SVCVTDIQFKGRGRTKNVWESPKGCLMYSFTLEMEDGRVVpliqyvVSLAV---TEAVKDVCDKKGLPyiDVKIKWPNDL 214
Cdd:PRK05935  31 TVISTREQTAGKGKFGKSWHSSDQDLLASFCFFITVLNID------VSLLFrlgTEAVMRLGEDLGIT--EAVIKWPNDV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914  215 YVNGLKVGGILCTSTYRSKKFNVSVGVGLN--------VDNGQPTTCLNAVLKGMAPESNLLKR--EEILGAFFHKFEKF 284
Cdd:PRK05935 103 LVHGEKLCGVLCETIPVKGGLGVILGIGVNgnttkdelLGIDQPATSLQELLGHPIDLEEQRERliKHIKHVLIQTLPKL 182


                 ....*...
gi 18400914  285 FDLFMDQG 292
Cdd:PRK05935 183 LARESNHG 190
PRK13325 PRK13325
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase;
138-291 1.21e-10

bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase;


Pssm-ID: 183976 [Multi-domain]  Cd Length: 592  Bit Score: 62.81  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914  138 SVCVTDIQFKGRGRTKNVWESPKG-CLMYSFTL-----EMEDGRVVPliqyVVSLAVTEAVkdvcdkkGLPYIDVKIKWP 211
Cdd:PRK13325 111 TICVTHLQSKGRGRQGRKWSHRLGeCLMFSFGWvfdrpQYELGSLSP----VAAVACRRAL-------SRLGLKTQIKWP 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914  212 NDLYVNGLKVGGILCTSTYRSKKFNVSVGVGLN------VDNGQPTTCL--NAVLKGMAPESNLLKR-EEILGAFFHKF- 281
Cdd:PRK13325 180 NDLVVGRDKLGGILIETVRTGGKTVAVVGIGINfvlpkeVENAASVQSLfqTASRRGNADAAVLLETlLAELDAVLLQYa 259

                        170
                 ....*....|
gi 18400914  282 EKFFDLFMDQ 291
Cdd:PRK13325 260 RDGFAPFVAE 269
BirA COG1654
Biotin operon repressor [Transcription];
107-331 2.69e-10

Biotin operon repressor [Transcription];


Pssm-ID: 441260 [Multi-domain]  Cd Length: 324  Bit Score: 60.77  E-value: 2.69e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914 107 THRFGRFLIWSPRLSSTHDVV-SHNFSELPVGSVCVTDIQFKGRGRTKNVWESPKGCLMYSFTLEmedgRVVPLIQYVVS 185
Cdd:COG1654  77 TKRLGREILYVISSTSTNLLAlELAAQGGDAGTVVAAEQQRGGRGRRRRSWSSPGGGGLLYSLLL----RPPIAPALLSL 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914 186 LAVTEAVKDVCDKKGLPYIDVKIKWPNDLYVNGLKVGGILCTSTYRSKKFNVSVGVGLNVDN----GQPTTCLNAVLKGM 261
Cdd:COG1654 153 LLLAAAVAVAAALAEGGGLVKWKKWPNDLLKKGKKILGILEEEGGDADGVVIVVGGGGNNNNsnpeEEPQELAELATSLL 232

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914 262 APESNLLKREEILGAFFHKFEKFFDLFMDQGFKSLEELYYRTWLHSEQRVIVEDKVEDQVVQNVVTIQGL 331
Cdd:COG1654 233 LILRLRLLRLLLLLLLLLLELLELLGFLEFFFLWERLDWELLRVLKLVVVVVEIGGGGGGGGALGGGLLG 302
PRK06955 PRK06955
biotin--[acetyl-CoA-carboxylase] ligase;
134-245 2.12e-05

biotin--[acetyl-CoA-carboxylase] ligase;


Pssm-ID: 235896 [Multi-domain]  Cd Length: 300  Bit Score: 45.93  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914  134 LPVGSVCVTDIQFKGRGRTKNVWES-PKGCLMYSFTLemedgrVVPL-------IQYVVSLAVTEAVKDVCDKKGLpyiD 205
Cdd:PRK06955  62 LPAPIVRVAYEQTAGRGRQGRPWFAqPGNALLFSVAC------VLPRpvaalagLSLAVGVALAEALAALPAALGQ---R 132

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 18400914  206 VKIKWPNDLYVNGLKVGGILCTSTYRS-KKFNVSVGVGLNV 245
Cdd:PRK06955 133 IALKWPNDLLIAGRKLAGILIETVWATpDATAVVIGIGLNV 173
PTZ00275 PTZ00275
biotin-acetyl-CoA-carboxylase ligase; Provisional
 143-350 5.93e-05

biotin-acetyl-CoA-carboxylase ligase; Provisional


Pssm-ID: 185536 [Multi-domain]  Cd Length: 285  Bit Score: 44.43  E-value: 5.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914  143 DIQFKG---RGRTKN---VWESPKGCLMYSFTL--EMEDGRVVPLIQYVVSLAVTEAVKDVcdkkglpYIDVKIKWPNDL 214
Cdd:PTZ00275  56 NEQTNGigtRDTKKNqdrIWLSEKGNLFTTFVFlwNRNDIEKVKYLAQTCTVAISKTLEYF-------HLVTQIKWINDV 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914  215 YVNGLKVGGILCTSTY-------RSKKFNVSVGVGLNV----DNGQPTTCLNAVLKGMAPESNLLKR----EEILGAFFH 279
Cdd:PTZ00275 129 LVNYKKIAGCLVHLYYlddfpnlNSRYVCVMVGIGINVtledKHNLLNNNYTSIKKELQRDFNTPKSipsvEQVTEKLII 208

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18400914  280 KFEKFFDLFMDQGFKSLEELYYRTWLHSEQRVIVedkveDQVVQNVVT-IQGLTSSGYLLAVGDDNQMYELH 350
Cdd:PTZ00275 209 NLKAVINKLRKEGFSSFLDYITPRLLYKDKKVLI-----DQDNELIVGyLQGLLHDGSLLLLREKNKLVRVN 275
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
 306-361 1.05e-04

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: 39.37  E-value: 1.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 18400914   306 HSEQRVIVEDkvEDQVVqnVVTIQGLTSSGYLLAVGDDNQmyelHPDGNSFDFFKG 361
Cdd:pfam02237   1 TLGREVRVLL--GDGIV--EGIAVGIDDDGALLLETDDGT----IRDINSGEVSLR 48
BPL_LplA_LipB cd16435
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ...
 149-246 3.05e-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: 38.29  E-value: 3.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400914 149 RGRTKNVWESPKGCLMYSFTLemedGRVVPLIQYVVSLAVTEAVKDVCDKKGLPyidVKIKW-PNDLYVNGLKVGGILct 227
Cdd:cd16435  68 RNRGGRAVSHDPGQLVFSPVI----GPNVEFMISKFNLIIEEGIRDAIADFGQS---AEVKWgRNDLWIDNRKVCGIA-- 138

                        90
                ....*....|....*....
gi 18400914 228 stYRSKKFNVSVGVGLNVD 246
Cdd:cd16435 139 --VRVVKEAIFHGIALNLN 155
 
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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