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Conserved domains on  [gi|1333097845|ref|XP_023517017|]
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biotin--protein ligase 2-like [Cucurbita pepo subsp. pepo]

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 ...
 133-308 1.29e-49

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: 165.13  E-value: 1.29e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 133 FLIWCSRIPSTQDVISQNFSDL-PLGAVCVADVQFKGRGRSKNLWESPPG-CLMFSFTIQMEDGRI-VPLLQYVVSLAIT 209
Cdd:cd16442     1 KLIVLDEIDSTNDEAKELARSGaPEGTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPPAeAPLLTLLAAVAVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 210 EAVKDICDkkglpyIDLKIKWPNDLYVNGLKVGGILCTSTYR-SKKFNVTAGIGLNVDNDKPTTCLNEALANLsSTPYKF 288
Cdd:cd16442    81 EALEKLGG------IPVQIKWPNDILVNGKKLAGILTEASAEgEGVAAVVIGIGINVNNTPPPEPLPDTSLAT-SLGKEV 153

                         170       180
                  ....*....|....*....|
gi 1333097845 289 RREDILAFFFNKFEGLYDIF 308
Cdd:cd16442   154 DRNELLEELLAALENRLELF 173
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
 326-381 4.73e-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: 37.44  E-value: 4.73e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333097845 326 HSGQRVIVqeKKEDQVVEnvVTIQGLTPTGYLLAIGDDNQmcelHPDGNSLDFFKG 381
Cdd:pfam02237   1 TLGREVRV--LLGDGIVE--GIAVGIDDDGALLLETDDGT----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 ...
 133-308 1.29e-49

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: 165.13  E-value: 1.29e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 133 FLIWCSRIPSTQDVISQNFSDL-PLGAVCVADVQFKGRGRSKNLWESPPG-CLMFSFTIQMEDGRI-VPLLQYVVSLAIT 209
Cdd:cd16442     1 KLIVLDEIDSTNDEAKELARSGaPEGTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPPAeAPLLTLLAAVAVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 210 EAVKDICDkkglpyIDLKIKWPNDLYVNGLKVGGILCTSTYR-SKKFNVTAGIGLNVDNDKPTTCLNEALANLsSTPYKF 288
Cdd:cd16442    81 EALEKLGG------IPVQIKWPNDILVNGKKLAGILTEASAEgEGVAAVVIGIGINVNNTPPPEPLPDTSLAT-SLGKEV 153

                         170       180
                  ....*....|....*....|
gi 1333097845 289 RREDILAFFFNKFEGLYDIF 308
Cdd:cd16442   154 DRNELLEELLAALENRLELF 173
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 134-370 8.73e-45

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: 154.56  E-value: 8.73e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 134 LIWCSRIPSTQDVISQNF-SDLPLGAVCVADVQFKGRGRSKNLWESPPG-CLMFS----FTIQMEDgriVPLLQYVVSLA 207
Cdd:COG0340     2 IEVFDEVDSTNDEAKELArEGAPEGTVVVAEEQTAGRGRRGRSWVSPPGkGLYFSlllrPDLPPAR---LPLLSLAAGLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 208 ITEAVKDICDkkglpyIDLKIKWPNDLYVNGLKVGGILC-TSTYRSKKFNVTAGIGLNVDN--------DKPTTCLNEAl 278
Cdd:COG0340    79 VAEALRELTG------VDVGLKWPNDILLNGKKLAGILIeASGEGDGIDWVVIGIGINVNQppfdpeelDQPATSLKEE- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 279 anlssTPYKFRREDILAFFFNKFEGLYDIFINQGFQALEELYCQTWLHSGQRVIVqeKKEDQVVENvvTIQGLTPTGYLL 358
Cdd:COG0340   152 -----TGKEVDREELLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRV--ETGGETLEG--IAVGIDEDGALL 222

                         250
                  ....*....|..
gi 1333097845 359 AIGDDNQMCELH 370
Cdd:COG0340   223 LETADGEIRAVA 234
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 139-264 6.32e-36

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: 127.94  E-value: 6.32e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 139 RIPSTQDVISQ-NFSDLPLGAVCVADVQFKGRGRSKNLWESPPGCLMFSFTIQME----DGRIVPLLQYVVSLAITEAVK 213
Cdd:pfam03099   4 RIKSTNTYLEElNSSELESGGVVVVRRQTGGRGRGGNVWHSPKGCLTYSLLLSKEhpnvDPSVLEFYVLELVLAVLEALG 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1333097845 214 DicDKKGLPYIDLKIKWPNDLYVNGLKVGGILCTSTYRSKKFNVTAGIGLN 264
Cdd:pfam03099  84 L--YKPGISGIPCFVKWPNDLYVNGRKLAGILQRSTRGGTLHHGVIGLGVN 132
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 140-362 5.67e-30

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: 115.19  E-value: 5.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 140 IPSTQDVISQNFSDL-PLGAVCVADVQFKGRGRSKNLWESPPGCLMFSFTIQMEDGRI-VPLLQYVVSLAITEAVKDICD 217
Cdd:TIGR00121   8 IDSTNQYALELAKEGkLKGDLVVAEYQTAGRGRRGRKWLSPEGGLYFSLILRPDLPKSpAPGLTLVAGIAIAEVLKELGD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 218 kkglpyiDLKIKWPNDLYVNGLKVGGILCTSTYRSKKF-NVTAGIGLNVDNDKPTTCLNE-ALANLSSTPYKFRREDILA 295
Cdd:TIGR00121  88 -------QVQVKWPNDILLKDKKLGGILTELTGKENRAdYVVIGIGINVQNRKPAESLREqAISLSEEAGIDLDRGELIE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333097845 296 FFFNKFEGLYDIFINQGFQALEELYCQTWLHSGQRVIVqeKKEDQVVENVVtiQGLTPTGYLLAIGD 362
Cdd:TIGR00121 161 GFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSL--TTGNGEIEGIA--RGIDKDGALLLEDG 223
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
140-358 7.05e-27

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


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 108.72  E-value: 7.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 140 IPSTQDVISQNFSDLPLGAVCVADVQFKGRGRSKNLWESPPGC-LMFSFTIQMEDG-RIVPLLQYVVSLAITEAVKDicd 217
Cdd:PRK11886   86 IDSTNQYLLDRIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGnLYLSLYWRLNQGpAQAMGLSLVVGIAIAEALRR--- 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 218 kkgLPYIDLKIKWPNDLYVNGLKVGGIL----------CtstyrskkfNVTAGIGLNVD-NDKPTTCLNEALANLSSTPY 286
Cdd:PRK11886  163 ---LGAIDVGLKWPNDIYLNDRKLAGILvelsgetgdaA---------HVVIGIGINVAmPDFPEELIDQPWSDLQEAGP 230

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333097845 287 KFRREDILAFFFNKFEGLYDIFINQGFQALEELYCQTWLHSGQRVIVQEkkEDQVVENVVtiQGLTPTGYLL 358
Cdd:PRK11886  231 TIDRNQLAAELIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLII--GDKEISGIA--RGIDEQGALL 298
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
 326-381 4.73e-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: 37.44  E-value: 4.73e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333097845 326 HSGQRVIVqeKKEDQVVEnvVTIQGLTPTGYLLAIGDDNQmcelHPDGNSLDFFKG 381
Cdd:pfam02237   1 TLGREVRV--LLGDGIVE--GIAVGIDDDGALLLETDDGT----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 ...
 133-308 1.29e-49

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: 165.13  E-value: 1.29e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 133 FLIWCSRIPSTQDVISQNFSDL-PLGAVCVADVQFKGRGRSKNLWESPPG-CLMFSFTIQMEDGRI-VPLLQYVVSLAIT 209
Cdd:cd16442     1 KLIVLDEIDSTNDEAKELARSGaPEGTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPPAeAPLLTLLAAVAVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 210 EAVKDICDkkglpyIDLKIKWPNDLYVNGLKVGGILCTSTYR-SKKFNVTAGIGLNVDNDKPTTCLNEALANLsSTPYKF 288
Cdd:cd16442    81 EALEKLGG------IPVQIKWPNDILVNGKKLAGILTEASAEgEGVAAVVIGIGINVNNTPPPEPLPDTSLAT-SLGKEV 153

                         170       180
                  ....*....|....*....|
gi 1333097845 289 RREDILAFFFNKFEGLYDIF 308
Cdd:cd16442   154 DRNELLEELLAALENRLELF 173
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 134-370 8.73e-45

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: 154.56  E-value: 8.73e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 134 LIWCSRIPSTQDVISQNF-SDLPLGAVCVADVQFKGRGRSKNLWESPPG-CLMFS----FTIQMEDgriVPLLQYVVSLA 207
Cdd:COG0340     2 IEVFDEVDSTNDEAKELArEGAPEGTVVVAEEQTAGRGRRGRSWVSPPGkGLYFSlllrPDLPPAR---LPLLSLAAGLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 208 ITEAVKDICDkkglpyIDLKIKWPNDLYVNGLKVGGILC-TSTYRSKKFNVTAGIGLNVDN--------DKPTTCLNEAl 278
Cdd:COG0340    79 VAEALRELTG------VDVGLKWPNDILLNGKKLAGILIeASGEGDGIDWVVIGIGINVNQppfdpeelDQPATSLKEE- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 279 anlssTPYKFRREDILAFFFNKFEGLYDIFINQGFQALEELYCQTWLHSGQRVIVqeKKEDQVVENvvTIQGLTPTGYLL 358
Cdd:COG0340   152 -----TGKEVDREELLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRV--ETGGETLEG--IAVGIDEDGALL 222

                         250
                  ....*....|..
gi 1333097845 359 AIGDDNQMCELH 370
Cdd:COG0340   223 LETADGEIRAVA 234
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 139-264 6.32e-36

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: 127.94  E-value: 6.32e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 139 RIPSTQDVISQ-NFSDLPLGAVCVADVQFKGRGRSKNLWESPPGCLMFSFTIQME----DGRIVPLLQYVVSLAITEAVK 213
Cdd:pfam03099   4 RIKSTNTYLEElNSSELESGGVVVVRRQTGGRGRGGNVWHSPKGCLTYSLLLSKEhpnvDPSVLEFYVLELVLAVLEALG 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1333097845 214 DicDKKGLPYIDLKIKWPNDLYVNGLKVGGILCTSTYRSKKFNVTAGIGLN 264
Cdd:pfam03099  84 L--YKPGISGIPCFVKWPNDLYVNGRKLAGILQRSTRGGTLHHGVIGLGVN 132
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 140-362 5.67e-30

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: 115.19  E-value: 5.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 140 IPSTQDVISQNFSDL-PLGAVCVADVQFKGRGRSKNLWESPPGCLMFSFTIQMEDGRI-VPLLQYVVSLAITEAVKDICD 217
Cdd:TIGR00121   8 IDSTNQYALELAKEGkLKGDLVVAEYQTAGRGRRGRKWLSPEGGLYFSLILRPDLPKSpAPGLTLVAGIAIAEVLKELGD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 218 kkglpyiDLKIKWPNDLYVNGLKVGGILCTSTYRSKKF-NVTAGIGLNVDNDKPTTCLNE-ALANLSSTPYKFRREDILA 295
Cdd:TIGR00121  88 -------QVQVKWPNDILLKDKKLGGILTELTGKENRAdYVVIGIGINVQNRKPAESLREqAISLSEEAGIDLDRGELIE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333097845 296 FFFNKFEGLYDIFINQGFQALEELYCQTWLHSGQRVIVqeKKEDQVVENVVtiQGLTPTGYLLAIGD 362
Cdd:TIGR00121 161 GFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSL--TTGNGEIEGIA--RGIDKDGALLLEDG 223
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
140-358 7.05e-27

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


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 108.72  E-value: 7.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 140 IPSTQDVISQNFSDLPLGAVCVADVQFKGRGRSKNLWESPPGC-LMFSFTIQMEDG-RIVPLLQYVVSLAITEAVKDicd 217
Cdd:PRK11886   86 IDSTNQYLLDRIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGnLYLSLYWRLNQGpAQAMGLSLVVGIAIAEALRR--- 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 218 kkgLPYIDLKIKWPNDLYVNGLKVGGIL----------CtstyrskkfNVTAGIGLNVD-NDKPTTCLNEALANLSSTPY 286
Cdd:PRK11886  163 ---LGAIDVGLKWPNDIYLNDRKLAGILvelsgetgdaA---------HVVIGIGINVAmPDFPEELIDQPWSDLQEAGP 230

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333097845 287 KFRREDILAFFFNKFEGLYDIFINQGFQALEELYCQTWLHSGQRVIVQEkkEDQVVENVVtiQGLTPTGYLL 358
Cdd:PRK11886  231 TIDRNQLAAELIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLII--GDKEISGIA--RGIDEQGALL 298
PRK08330 PRK08330
biotin--protein ligase; Provisional
 131-364 5.07e-22

biotin--protein ligase; Provisional


Pssm-ID: 169384 [Multi-domain]  Cd Length: 236  Bit Score: 93.66  E-value: 5.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 131 GRFLIWCSRIPSTQDVISQNFSDLPLGAVCVADVQFKGRGRSKNLWESPPGCLMFSFTIQ--MEDgRIVPLLQYVVSLAI 208
Cdd:PRK08330    2 GRNIIYFDEVDSTNEYAKRIAPDEEEGTVIVADRQTAGHGRKGRAWASPEGGLWMSVILKpkVSP-EHLPKLVFLGALAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 209 TEAVKDICdkkglpyIDLKIKWPNDLYVNGLKVGGILCtstyRSKKFNVTAGIGLNVDNDKP------TTCLNEALAnlS 282
Cdd:PRK08330   81 VDTLREFG-------IEGKIKWPNDVLVNYKKIAGVLV----EGKGDFVVLGIGLNVNNEIPdelretATSMKEVLG--R 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 283 STPYkfrrEDILAFFFNKFEGLYDIFINQGFQALEELYCQTWLhSGQRVIVQEKKEDQVVENVVTIQGLtptGYLLAIGD 362
Cdd:PRK08330  148 EVPL----IEVFKRLVENLDRWYKLFLEGPGEILEEVKGRSMI-LGKRVKIIGDGEILVEGIAEDIDEF---GALILRLD 219


                  ..
gi 1333097845 363 DN 364
Cdd:PRK08330  220 DG 221
PRK08477 PRK08477
biotin--[acetyl-CoA-carboxylase] ligase;
140-302 4.21e-12

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


Pssm-ID: 236273 [Multi-domain]  Cd Length: 211  Bit Score: 64.98  E-value: 4.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 140 IPSTQDVISQNFSDLPLGA-VC-VADVQFKGRGRSKNLWESPPGCLMFSFTIQMED-GRIVPLlqyvVSLAITEAV--KD 214
Cdd:PRK08477    9 LDSTQTYLIEKIKNGELKApFAiVAKEQTAGIGSRGNSWEGKKGNLFFSFALKESDlPKDLPL----QSSSIYFGFllKE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 215 ICDKKGLpyiDLKIKWPNDLYVNGLKVGGILcTSTYRSkkfNVTAGIGLNVDNdkpttcLNEALANLSStpyKFRREDIL 294
Cdd:PRK08477   85 VLKELGS---KVWLKWPNDLYLDDKKIGGVI-TNKIKN---FIVCGIGLNLKF------SPKNFACLDI---EISDDLLL 148


                  ....*...
gi 1333097845 295 AFFFNKFE 302
Cdd:PRK08477  149 EGFLQKIE 156
BirA COG1654
Biotin operon repressor [Transcription];
109-351 2.81e-11

Biotin operon repressor [Transcription];


Pssm-ID: 441260 [Multi-domain]  Cd Length: 324  Bit Score: 63.85  E-value: 2.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 109 KSLKESGFQIGSYMNS-------------------LSTDTFGRFLIWCSRIPSTQDVISQNFSD-LPLGAVCVADVQFKG 168
Cdd:COG1654    40 KALRELGYEIESVPGKgyrlaeppdlldpeeiragLSTKRLGREILYVISSTSTNLLALELAAQgGDAGTVVAAEQQRGG 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 169 RGRSKNLWESPPGCLMFSFTIqmEDGRIVPLLQYVVSLAITEAVKDICDKKGLpyIDLKIKWPNDLYVNGLKVGGILCTS 248
Cdd:COG1654   120 RGRRRRSWSSPGGGGLLYSLL--LRPPIAPALLSLLLLAAAVAVAAALAEGGG--LVKWKKWPNDLLKKGKKILGILEEE 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 249 TYRSKKFNVTAGIGLNVDN----DKPTTCLNEALANLSSTPYKFRREDILAFFFNKFEGLYDIFINQGFQALEELYCQTW 324
Cdd:COG1654   196 GGDADGVVIVVGGGGNNNNsnpeEEPQELAELATSLLLILRLRLLRLLLLLLLLLLELLELLGFLEFFFLWERLDWELLR 275

                         250       260
                  ....*....|....*....|....*..
gi 1333097845 325 LHSGQRVIVQEKKEDQVVENVVTIQGL 351
Cdd:COG1654   276 VLKLVVVVVEIGGGGGGGGALGGGLLG 302
PTZ00276 PTZ00276
biotin/lipoate protein ligase; Provisional
 161-285 2.83e-11

biotin/lipoate protein ligase; Provisional


Pssm-ID: 140302 [Multi-domain]  Cd Length: 245  Bit Score: 62.96  E-value: 2.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 161 VADVQFKGRGRSKNLWESPPGCLMFSFTI--QMEDGRIVPLLQYVVSLAITEAVKDICDKKGlpyidLKIKWPNDLYVNG 238
Cdd:PTZ00276   37 LAESQTAGRGTGGRTWTSPKGNMYFTLCIpqKGVPPELVPVLPLITGLACRAAIMEVLHGAA-----VHTKWPNDIIYAG 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333097845 239 LKVGGILCTSTYRSkkfnVTAGIGLNV-------DNDKPTTCLN---EALANLSSTP 285
Cdd:PTZ00276  112 KKIGGSLIESEGEY----LIIGIGMNIevappvtDAGRESTMVNeiaEDLGVKSVTP 164
PRK13325 PRK13325
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase;
159-264 3.75e-10

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


Pssm-ID: 183976 [Multi-domain]  Cd Length: 592  Bit Score: 61.65  E-value: 3.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 159 VCVADVQFKGRGRSKNLWESPPG-CLMFSF-----TIQMEDGRIVPllqyVVSLAITEAVkdicdkkGLPYIDLKIKWPN 232
Cdd:PRK13325  112 ICVTHLQSKGRGRQGRKWSHRLGeCLMFSFgwvfdRPQYELGSLSP----VAAVACRRAL-------SRLGLKTQIKWPN 180

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1333097845 233 DLYVNGLKVGGILCTSTYRSKKFNVTAGIGLN 264
Cdd:PRK13325  181 DLVVGRDKLGGILIETVRTGGKTVAVVGIGIN 212
PRK05935 PRK05935
biotin--protein ligase; Provisional
 165-278 1.74e-09

biotin--protein ligase; Provisional


Pssm-ID: 235649 [Multi-domain]  Cd Length: 190  Bit Score: 56.75  E-value: 1.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 165 QFKGRGRSKNLWESPPGCLMFSFTIQMEDGRIVPLLQYVVSlaiTEAVKDICDKKGLPyiDLKIKWPNDLYVNGLKVGGI 244
Cdd:PRK05935   38 QTAGKGKFGKSWHSSDQDLLASFCFFITVLNIDVSLLFRLG---TEAVMRLGEDLGIT--EAVIKWPNDVLVHGEKLCGV 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1333097845 245 LCTSTYRSKKFNVTAGIGLN--------VDNDKPTTCLNEAL 278
Cdd:PRK05935  113 LCETIPVKGGLGVILGIGVNgnttkdelLGIDQPATSLQELL 154
PRK06955 PRK06955
biotin--[acetyl-CoA-carboxylase] ligase;
154-284 4.44e-08

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


Pssm-ID: 235896 [Multi-domain]  Cd Length: 300  Bit Score: 54.02  E-value: 4.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 154 LPLGAVCVADVQFKGRGRSKNLWESPPG-CLMFSFtiqmedGRIVPL-------LQYVVSLAITEAVKDICDKKGLpyiD 225
Cdd:PRK06955   62 LPAPIVRVAYEQTAGRGRQGRPWFAQPGnALLFSV------ACVLPRpvaalagLSLAVGVALAEALAALPAALGQ---R 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 226 LKIKWPNDLYVNGLKVGGILCTSTYRS-KKFNVTAGIGLNVDNDKPTTCLNEALANLSST 284
Cdd:PRK06955  133 IALKWPNDLLIAGRKLAGILIETVWATpDATAVVIGIGLNVRRADAVAAEVDALRAREAA 192
PTZ00275 PTZ00275
biotin-acetyl-CoA-carboxylase ligase; Provisional
 175-370 3.61e-05

biotin-acetyl-CoA-carboxylase ligase; Provisional


Pssm-ID: 185536 [Multi-domain]  Cd Length: 285  Bit Score: 45.20  E-value: 3.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 175 LWESPPGCLMFSFTIQMEDGRI--VPLLQYVVSLAITeavkdicdkKGLPYIDL--KIKWPNDLYVNGLKVGGILCTSTY 250
Cdd:PTZ00275   74 IWLSEKGNLFTTFVFLWNRNDIekVKYLAQTCTVAIS---------KTLEYFHLvtQIKWINDVLVNYKKIAGCLVHLYY 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 251 -------RSKKFNVTAGIGLNVD-NDKPT------TCLNEALANLSSTPYKFRR-EDILAFFFNKFEGLYDIFINQGFQA 315
Cdd:PTZ00275  145 lddfpnlNSRYVCVMVGIGINVTlEDKHNllnnnyTSIKKELQRDFNTPKSIPSvEQVTEKLIINLKAVINKLRKEGFSS 224

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333097845 316 LEELYCQTWLHSGQRVIVqekkeDQVVENVVT-IQGLTPTGYLLAIGDDNQMCELH 370
Cdd:PTZ00275  225 FLDYITPRLLYKDKKVLI-----DQDNELIVGyLQGLLHDGSLLLLREKNKLVRVN 275
BPL_LplA_LipB cd16435
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ...
 169-268 1.72e-04

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: 42.14  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333097845 169 RGRSKNLWESPPGCLMFSFTIqmedGRIVPLLQYVVSLAITEAVKDICDKKGLPyidLKIKW-PNDLYVNGLKVGGILct 247
Cdd:cd16435    68 RNRGGRAVSHDPGQLVFSPVI----GPNVEFMISKFNLIIEEGIRDAIADFGQS---AEVKWgRNDLWIDNRKVCGIA-- 138

                          90       100
                  ....*....|....*....|.
gi 1333097845 248 stYRSKKFNVTAGIGLNVDND 268
Cdd:cd16435   139 --VRVVKEAIFHGIALNLNQD 157
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
 326-381 4.73e-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: 37.44  E-value: 4.73e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333097845 326 HSGQRVIVqeKKEDQVVEnvVTIQGLTPTGYLLAIGDDNQmcelHPDGNSLDFFKG 381
Cdd:pfam02237   1 TLGREVRV--LLGDGIVE--GIAVGIDDDGALLLETDDGT----IRDINSGEVSLR 48
 
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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