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Conserved domains on  [gi|1063704848|ref|NP_001324830|]
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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 ...
 75-250 2.97e-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: 2.97e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848  75 FLIWSPRLSSTHDVVSHNFSEL-PVGSVCVTDIQFKGRGRTKNVWESPKG-CLMYSFTLEMEDG-RVVPLIQYVVSLAVT 151
Cdd:cd16442     1 KLIVLDEIDSTNDEAKELARSGaPEGTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPpAEAPLLTLLAAVAVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 152 EAVKDVCDkkglpyIDVKIKWPNDLYVNGLKVGGILCTSTYR-SKKFNVSVGVGLNVDNGQPTTCLNAVLKGMAPESNlL 230
Cdd:cd16442    81 EALEKLGG------IPVQIKWPNDILVNGKKLAGILTEASAEgEGVAAVVIGIGINVNNTPPPEPLPDTSLATSLGKE-V 153

                         170       180
                  ....*....|....*....|
gi 1063704848 231 KREEILGAFFHKFEKFFDLF 250
Cdd:cd16442   154 DRNELLEELLAALENRLELF 173
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
 268-323 1.58e-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: 38.60  E-value: 1.58e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063704848 268 HSEQRVIVEDkvEDQVVqnVVTIQGLTSSGYLLAVGDDNQmyelHPDGNSFDFFKG 323
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 ...
 75-250 2.97e-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: 2.97e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848  75 FLIWSPRLSSTHDVVSHNFSEL-PVGSVCVTDIQFKGRGRTKNVWESPKG-CLMYSFTLEMEDG-RVVPLIQYVVSLAVT 151
Cdd:cd16442     1 KLIVLDEIDSTNDEAKELARSGaPEGTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPpAEAPLLTLLAAVAVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 152 EAVKDVCDkkglpyIDVKIKWPNDLYVNGLKVGGILCTSTYR-SKKFNVSVGVGLNVDNGQPTTCLNAVLKGMAPESNlL 230
Cdd:cd16442    81 EALEKLGG------IPVQIKWPNDILVNGKKLAGILTEASAEgEGVAAVVIGIGINVNNTPPPEPLPDTSLATSLGKE-V 153

                         170       180
                  ....*....|....*....|
gi 1063704848 231 KREEILGAFFHKFEKFFDLF 250
Cdd:cd16442   154 DRNELLEELLAALENRLELF 173
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 78-206 5.54e-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: 144.89  E-value: 5.54e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848  78 WSPRLSSTHDVV-SHNFSELPVGSVCVTDIQFKGRGRTKNVWESPKGCLMYSFTLEME----DGRVVPLIQYVVSLAVTE 152
Cdd:pfam03099   1 LGERIKSTNTYLeELNSSELESGGVVVVRRQTGGRGRGGNVWHSPKGCLTYSLLLSKEhpnvDPSVLEFYVLELVLAVLE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063704848 153 AVKDvcDKKGLPYIDVKIKWPNDLYVNGLKVGGILCTSTYRSKKFNVSVGVGLN 206
Cdd:pfam03099  81 ALGL--YKPGISGIPCFVKWPNDLYVNGRKLAGILQRSTRGGTLHHGVIGLGVN 132
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 76-312 4.60e-41

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: 4.60e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848  76 LIWSPRLSSTHDVVSHNFSE-LPVGSVCVTDIQFKGRGRTKNVWESPKG-CLMYSFTLEMEDG-RVVPLIQYVVSLAVTE 152
Cdd:COG0340     2 IEVFDEVDSTNDEAKELAREgAPEGTVVVAEEQTAGRGRRGRSWVSPPGkGLYFSLLLRPDLPpARLPLLSLAAGLAVAE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 153 AVKDVCDkkglpyIDVKIKWPNDLYVNGLKVGGILCTSTYRSKKFNVSV-GVGLNVDN--------GQPTTCLNAVLkGM 223
Cdd:COG0340    82 ALRELTG------VDVGLKWPNDILLNGKKLAGILIEASGEGDGIDWVViGIGINVNQppfdpeelDQPATSLKEET-GK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 224 APEsnllkREEILGAFFHKFEKFFDLFMDQGFKSLEELYYRTWLHSEQRVIVEDkvEDQVVQNvvTIQGLTSSGYLLAVG 303
Cdd:COG0340   155 EVD-----REELLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVET--GGETLEG--IAVGIDEDGALLLET 225


                  ....*....
gi 1063704848 304 DDNQMYELH 312
Cdd:COG0340   226 ADGEIRAVA 234
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 76-304 4.74e-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: 103.64  E-value: 4.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848  76 LIWSPRLSSTHDVVSHNFSEL-PVGSVCVTDIQFKGRGRTKNVWESPKGCLMYSFTLEMEDGRV-VPLIQYVVSLAVTEA 153
Cdd:TIGR00121   2 VIVLDVIDSTNQYALELAKEGkLKGDLVVAEYQTAGRGRRGRKWLSPEGGLYFSLILRPDLPKSpAPGLTLVAGIAIAEV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 154 VKDVCDkkglpyiDVKIKWPNDLYVNGLKVGGILCTSTYRSKKF-NVSVGVGLNVDNGQPTTCLNAVLKGMAPESNL-LK 231
Cdd:TIGR00121  82 LKELGD-------QVQVKWPNDILLKDKKLGGILTELTGKENRAdYVVIGIGINVQNRKPAESLREQAISLSEEAGIdLD 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063704848 232 REEILGAFFHKFEKFFDLFMDQGFKSLEELYYRTWLHSEQRVivedKVEDQVVQNVVTIQGLTSSGYLLAVGD 304
Cdd:TIGR00121 155 RGELIEGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREV----SLTTGNGEIEGIARGIDKDGALLLEDG 223
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
80-307 6.45e-23

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


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 96.78  E-value: 6.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848  80 PRLSSTHDVVSHNFSELPVGSVCVTDIQFKGRGRTKNVWESPKGC-LMYSFTLEMEDGrVVPLIQY--VVSLAVTEAVKD 156
Cdd:PRK11886   84 PVIDSTNQYLLDRIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGnLYLSLYWRLNQG-PAQAMGLslVVGIAIAEALRR 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 157 vcdkkgLPYIDVKIKWPNDLYVNGLKVGGIL----------CtstyrskkfNVSVGVGLNV---DN-----GQPTTCLNA 218
Cdd:PRK11886  163 ------LGAIDVGLKWPNDIYLNDRKLAGILvelsgetgdaA---------HVVIGIGINVampDFpeeliDQPWSDLQE 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 219 VLKgmapesnLLKREEILGAFFHKFEKFFDLFMDQGFKSLEELYYRT--WLHSEQRVIVEDKVEDQVVqnvvtiQGLTSS 296
Cdd:PRK11886  228 AGP-------TIDRNQLAAELIKQLRAALELFEQEGLAPFLERWKKLdlFLGREVKLIIGDKEISGIA------RGIDEQ 294

                         250
                  ....*....|.
gi 1063704848 297 GYLLaVGDDNQ 307
Cdd:PRK11886  295 GALL-LEDDGV 304
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
 268-323 1.58e-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: 38.60  E-value: 1.58e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063704848 268 HSEQRVIVEDkvEDQVVqnVVTIQGLTSSGYLLAVGDDNQmyelHPDGNSFDFFKG 323
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 ...
 75-250 2.97e-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: 2.97e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848  75 FLIWSPRLSSTHDVVSHNFSEL-PVGSVCVTDIQFKGRGRTKNVWESPKG-CLMYSFTLEMEDG-RVVPLIQYVVSLAVT 151
Cdd:cd16442     1 KLIVLDEIDSTNDEAKELARSGaPEGTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPpAEAPLLTLLAAVAVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 152 EAVKDVCDkkglpyIDVKIKWPNDLYVNGLKVGGILCTSTYR-SKKFNVSVGVGLNVDNGQPTTCLNAVLKGMAPESNlL 230
Cdd:cd16442    81 EALEKLGG------IPVQIKWPNDILVNGKKLAGILTEASAEgEGVAAVVIGIGINVNNTPPPEPLPDTSLATSLGKE-V 153

                         170       180
                  ....*....|....*....|
gi 1063704848 231 KREEILGAFFHKFEKFFDLF 250
Cdd:cd16442   154 DRNELLEELLAALENRLELF 173
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 78-206 5.54e-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: 144.89  E-value: 5.54e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848  78 WSPRLSSTHDVV-SHNFSELPVGSVCVTDIQFKGRGRTKNVWESPKGCLMYSFTLEME----DGRVVPLIQYVVSLAVTE 152
Cdd:pfam03099   1 LGERIKSTNTYLeELNSSELESGGVVVVRRQTGGRGRGGNVWHSPKGCLTYSLLLSKEhpnvDPSVLEFYVLELVLAVLE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063704848 153 AVKDvcDKKGLPYIDVKIKWPNDLYVNGLKVGGILCTSTYRSKKFNVSVGVGLN 206
Cdd:pfam03099  81 ALGL--YKPGISGIPCFVKWPNDLYVNGRKLAGILQRSTRGGTLHHGVIGLGVN 132
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 76-312 4.60e-41

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: 4.60e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848  76 LIWSPRLSSTHDVVSHNFSE-LPVGSVCVTDIQFKGRGRTKNVWESPKG-CLMYSFTLEMEDG-RVVPLIQYVVSLAVTE 152
Cdd:COG0340     2 IEVFDEVDSTNDEAKELAREgAPEGTVVVAEEQTAGRGRRGRSWVSPPGkGLYFSLLLRPDLPpARLPLLSLAAGLAVAE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 153 AVKDVCDkkglpyIDVKIKWPNDLYVNGLKVGGILCTSTYRSKKFNVSV-GVGLNVDN--------GQPTTCLNAVLkGM 223
Cdd:COG0340    82 ALRELTG------VDVGLKWPNDILLNGKKLAGILIEASGEGDGIDWVViGIGINVNQppfdpeelDQPATSLKEET-GK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 224 APEsnllkREEILGAFFHKFEKFFDLFMDQGFKSLEELYYRTWLHSEQRVIVEDkvEDQVVQNvvTIQGLTSSGYLLAVG 303
Cdd:COG0340   155 EVD-----REELLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVET--GGETLEG--IAVGIDEDGALLLET 225


                  ....*....
gi 1063704848 304 DDNQMYELH 312
Cdd:COG0340   226 ADGEIRAVA 234
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 76-304 4.74e-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: 103.64  E-value: 4.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848  76 LIWSPRLSSTHDVVSHNFSEL-PVGSVCVTDIQFKGRGRTKNVWESPKGCLMYSFTLEMEDGRV-VPLIQYVVSLAVTEA 153
Cdd:TIGR00121   2 VIVLDVIDSTNQYALELAKEGkLKGDLVVAEYQTAGRGRRGRKWLSPEGGLYFSLILRPDLPKSpAPGLTLVAGIAIAEV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 154 VKDVCDkkglpyiDVKIKWPNDLYVNGLKVGGILCTSTYRSKKF-NVSVGVGLNVDNGQPTTCLNAVLKGMAPESNL-LK 231
Cdd:TIGR00121  82 LKELGD-------QVQVKWPNDILLKDKKLGGILTELTGKENRAdYVVIGIGINVQNRKPAESLREQAISLSEEAGIdLD 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063704848 232 REEILGAFFHKFEKFFDLFMDQGFKSLEELYYRTWLHSEQRVivedKVEDQVVQNVVTIQGLTSSGYLLAVGD 304
Cdd:TIGR00121 155 RGELIEGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREV----SLTTGNGEIEGIARGIDKDGALLLEDG 223
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
80-307 6.45e-23

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


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 96.78  E-value: 6.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848  80 PRLSSTHDVVSHNFSELPVGSVCVTDIQFKGRGRTKNVWESPKGC-LMYSFTLEMEDGrVVPLIQY--VVSLAVTEAVKD 156
Cdd:PRK11886   84 PVIDSTNQYLLDRIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGnLYLSLYWRLNQG-PAQAMGLslVVGIAIAEALRR 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 157 vcdkkgLPYIDVKIKWPNDLYVNGLKVGGIL----------CtstyrskkfNVSVGVGLNV---DN-----GQPTTCLNA 218
Cdd:PRK11886  163 ------LGAIDVGLKWPNDIYLNDRKLAGILvelsgetgdaA---------HVVIGIGINVampDFpeeliDQPWSDLQE 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 219 VLKgmapesnLLKREEILGAFFHKFEKFFDLFMDQGFKSLEELYYRT--WLHSEQRVIVEDKVEDQVVqnvvtiQGLTSS 296
Cdd:PRK11886  228 AGP-------TIDRNQLAAELIKQLRAALELFEQEGLAPFLERWKKLdlFLGREVKLIIGDKEISGIA------RGIDEQ 294

                         250
                  ....*....|.
gi 1063704848 297 GYLLaVGDDNQ 307
Cdd:PRK11886  295 GALL-LEDDGV 304
PRK08330 PRK08330
biotin--protein ligase; Provisional
 73-280 3.30e-19

biotin--protein ligase; Provisional


Pssm-ID: 169384 [Multi-domain]  Cd Length: 236  Bit Score: 84.80  E-value: 3.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848  73 GRFLIWSPRLSSTHDVVSHNFSELPVGSVCVTDIQFKGRGRTKNVWESPKGCLMYSFTL----EMEDgrvVPLIQYVVSL 148
Cdd:PRK08330    2 GRNIIYFDEVDSTNEYAKRIAPDEEEGTVIVADRQTAGHGRKGRAWASPEGGLWMSVILkpkvSPEH---LPKLVFLGAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 149 AVTEAVKDVCdkkglpyIDVKIKWPNDLYVNGLKVGGILCtstyRSKKFNVSVGVGLNVDNGQP------TTCLNAVLKG 222
Cdd:PRK08330   79 AVVDTLREFG-------IEGKIKWPNDVLVNYKKIAGVLV----EGKGDFVVLGIGLNVNNEIPdelretATSMKEVLGR 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063704848 223 MAPESNLLKReeilgaFFHKFEKFFDLFMDQGFKSLEELYYRTW-LHSEQRVIVEDKVE 280
Cdd:PRK08330  148 EVPLIEVFKR------LVENLDRWYKLFLEGPGEILEEVKGRSMiLGKRVKIIGDGEIL 200
PRK08477 PRK08477
biotin--[acetyl-CoA-carboxylase] ligase;
103-246 2.42e-12

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


Pssm-ID: 236273 [Multi-domain]  Cd Length: 211  Bit Score: 64.98  E-value: 2.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 103 VTDIQFKGRGRTKNVWESPKGCLMYSFTLEMED-GRVVPLIQyvVSLAVTEAVKDVCDKKGLpyiDVKIKWPNDLYVNGL 181
Cdd:PRK08477   32 VAKEQTAGIGSRGNSWEGKKGNLFFSFALKESDlPKDLPLQS--SSIYFGFLLKEVLKELGS---KVWLKWPNDLYLDDK 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063704848 182 KVGGILcTSTYRSkkfNVSVGVGLNVDNG-QPTTCLNAVlkgmapesnlLKREEILGAFFHKFEKF 246
Cdd:PRK08477  107 KIGGVI-TNKIKN---FIVCGIGLNLKFSpKNFACLDIE----------ISDDLLLEGFLQKIEKK 158
PTZ00276 PTZ00276
biotin/lipoate protein ligase; Provisional
 103-256 3.01e-12

biotin/lipoate protein ligase; Provisional


Pssm-ID: 140302 [Multi-domain]  Cd Length: 245  Bit Score: 65.66  E-value: 3.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 103 VTDIQFKGRGRTKNVWESPKGCLMYSFTL--EMEDGRVVPLIQYVVSLAVTEAVKDVCDKKGlpyidVKIKWPNDLYVNG 180
Cdd:PTZ00276   37 LAESQTAGRGTGGRTWTSPKGNMYFTLCIpqKGVPPELVPVLPLITGLACRAAIMEVLHGAA-----VHTKWPNDIIYAG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 181 LKVGGILCTSTYRSkkfnVSVGVGLNV-------DNGQPTTCLNAVLKGMAPESnlLKREEILGAFFHkfeKFFDLFMDQ 253
Cdd:PTZ00276  112 KKIGGSLIESEGEY----LIIGIGMNIevappvtDAGRESTMVNEIAEDLGVKS--VTPQDLAEAVWK---HFFDICSDP 182


                  ...
gi 1063704848 254 GFK 256
Cdd:PTZ00276  183 ELT 185
PRK05935 PRK05935
biotin--protein ligase; Provisional
 100-254 8.46e-11

biotin--protein ligase; Provisional


Pssm-ID: 235649 [Multi-domain]  Cd Length: 190  Bit Score: 60.22  E-value: 8.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 100 SVCVTDIQFKGRGRTKNVWESPKGCLMYSFTLEMEDGRVVpliqyvVSLAV---TEAVKDVCDKKGLPyiDVKIKWPNDL 176
Cdd:PRK05935   31 TVISTREQTAGKGKFGKSWHSSDQDLLASFCFFITVLNID------VSLLFrlgTEAVMRLGEDLGIT--EAVIKWPNDV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 177 YVNGLKVGGILCTSTYRSKKFNVSVGVGLN--------VDNGQPTTCLNAVLKGMAPESNLLKR--EEILGAFFHKFEKF 246
Cdd:PRK05935  103 LVHGEKLCGVLCETIPVKGGLGVILGIGVNgnttkdelLGIDQPATSLQELLGHPIDLEEQRERliKHIKHVLIQTLPKL 182


                  ....*...
gi 1063704848 247 FDLFMDQG 254
Cdd:PRK05935  183 LARESNHG 190
PRK13325 PRK13325
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase;
100-253 8.70e-11

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


Pssm-ID: 183976 [Multi-domain]  Cd Length: 592  Bit Score: 62.81  E-value: 8.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 100 SVCVTDIQFKGRGRTKNVWESPKG-CLMYSFTL-----EMEDGRVVPliqyVVSLAVTEAVkdvcdkkGLPYIDVKIKWP 173
Cdd:PRK13325  111 TICVTHLQSKGRGRQGRKWSHRLGeCLMFSFGWvfdrpQYELGSLSP----VAAVACRRAL-------SRLGLKTQIKWP 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 174 NDLYVNGLKVGGILCTSTYRSKKFNVSVGVGLN------VDNGQPTTCL--NAVLKGMAPESNLLKR-EEILGAFFHKF- 243
Cdd:PRK13325  180 NDLVVGRDKLGGILIETVRTGGKTVAVVGIGINfvlpkeVENAASVQSLfqTASRRGNADAAVLLETlLAELDAVLLQYa 259

                         170
                  ....*....|
gi 1063704848 244 EKFFDLFMDQ 253
Cdd:PRK13325  260 RDGFAPFVAE 269
BirA COG1654
Biotin operon repressor [Transcription];
69-293 2.07e-10

Biotin operon repressor [Transcription];


Pssm-ID: 441260 [Multi-domain]  Cd Length: 324  Bit Score: 60.77  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848  69 THRFGRFLIWSPRLSSTHDVV-SHNFSELPVGSVCVTDIQFKGRGRTKNVWESPKGCLMYSFTLEmedgRVVPLIQYVVS 147
Cdd:COG1654    77 TKRLGREILYVISSTSTNLLAlELAAQGGDAGTVVAAEQQRGGRGRRRRSWSSPGGGGLLYSLLL----RPPIAPALLSL 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 148 LAVTEAVKDVCDKKGLPYIDVKIKWPNDLYVNGLKVGGILCTSTYRSKKFNVSVGVGLNVDN----GQPTTCLNAVLKGM 223
Cdd:COG1654   153 LLLAAAVAVAAALAEGGGLVKWKKWPNDLLKKGKKILGILEEEGGDADGVVIVVGGGGNNNNsnpeEEPQELAELATSLL 232

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 224 APESNLLKREEILGAFFHKFEKFFDLFMDQGFKSLEELYYRTWLHSEQRVIVEDKVEDQVVQNVVTIQGL 293
Cdd:COG1654   233 LILRLRLLRLLLLLLLLLLELLELLGFLEFFFLWERLDWELLRVLKLVVVVVEIGGGGGGGGALGGGLLG 302
PRK06955 PRK06955
biotin--[acetyl-CoA-carboxylase] ligase;
96-207 1.75e-05

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


Pssm-ID: 235896 [Multi-domain]  Cd Length: 300  Bit Score: 45.93  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848  96 LPVGSVCVTDIQFKGRGRTKNVWES-PKGCLMYSFTLemedgrVVPL-------IQYVVSLAVTEAVKDVCDKKGLpyiD 167
Cdd:PRK06955   62 LPAPIVRVAYEQTAGRGRQGRPWFAqPGNALLFSVAC------VLPRpvaalagLSLAVGVALAEALAALPAALGQ---R 132

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1063704848 168 VKIKWPNDLYVNGLKVGGILCTSTYRS-KKFNVSVGVGLNV 207
Cdd:PRK06955  133 IALKWPNDLLIAGRKLAGILIETVWATpDATAVVIGIGLNV 173
PTZ00275 PTZ00275
biotin-acetyl-CoA-carboxylase ligase; Provisional
 105-312 6.23e-05

biotin-acetyl-CoA-carboxylase ligase; Provisional


Pssm-ID: 185536 [Multi-domain]  Cd Length: 285  Bit Score: 44.04  E-value: 6.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 105 DIQFKG---RGRTKN---VWESPKGCLMYSFTL--EMEDGRVVPLIQYVVSLAVTEAVKDVcdkkglpYIDVKIKWPNDL 176
Cdd:PTZ00275   56 NEQTNGigtRDTKKNqdrIWLSEKGNLFTTFVFlwNRNDIEKVKYLAQTCTVAISKTLEYF-------HLVTQIKWINDV 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 177 YVNGLKVGGILCTSTY-------RSKKFNVSVGVGLNV----DNGQPTTCLNAVLKGMAPESNLLKR----EEILGAFFH 241
Cdd:PTZ00275  129 LVNYKKIAGCLVHLYYlddfpnlNSRYVCVMVGIGINVtledKHNLLNNNYTSIKKELQRDFNTPKSipsvEQVTEKLII 208

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063704848 242 KFEKFFDLFMDQGFKSLEELYYRTWLHSEQRVIVedkveDQVVQNVVT-IQGLTSSGYLLAVGDDNQMYELH 312
Cdd:PTZ00275  209 NLKAVINKLRKEGFSSFLDYITPRLLYKDKKVLI-----DQDNELIVGyLQGLLHDGSLLLLREKNKLVRVN 275
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
 268-323 1.58e-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: 38.60  E-value: 1.58e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063704848 268 HSEQRVIVEDkvEDQVVqnVVTIQGLTSSGYLLAVGDDNQmyelHPDGNSFDFFKG 323
Cdd:pfam02237   1 TLGREVRVLL--GDGIV--EGIAVGIDDDGALLLETDDGT----IRDINSGEVSLR 48
BPL_LplA_LipB cd16435
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ...
 111-208 2.64e-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: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704848 111 RGRTKNVWESPKGCLMYSFTLemedGRVVPLIQYVVSLAVTEAVKDVCDKKGLPyidVKIKW-PNDLYVNGLKVGGILct 189
Cdd:cd16435    68 RNRGGRAVSHDPGQLVFSPVI----GPNVEFMISKFNLIIEEGIRDAIADFGQS---AEVKWgRNDLWIDNRKVCGIA-- 138

                          90
                  ....*....|....*....
gi 1063704848 190 stYRSKKFNVSVGVGLNVD 208
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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