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Conserved domains on  [gi|489079348|ref|WP_002989286|]
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bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA [Streptococcus pyogenes]

Protein Classification

bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA( domain architecture ID 11485649)

bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor, forming a BirA-biotinyl-5'-adenylate complex that can either transfer the biotinyl moiety to the BCCP subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon

CATH:  1.10.10.10
EC:  6.3.4.15
Gene Symbol:  birA
Gene Ontology:  GO:0005524|GO:0004077|GO:0003677|GO:0006355
PubMed:  3899863
SCOP:  4000146

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
2-312 2.82e-144

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


:

Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 408.79  E-value: 2.82e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348   2 KTSEKIYQLLS--QTDDFVSGEYLADQLSISRTSVWKSIKSLENQGIQIDSLKHKGYRMVQG-DILLPKTISQGL-GMPV 77
Cdd:PRK11886   1 KTYTVMLQLLSllADGDFHSGEQLGEELGISRAAIWKHIQTLEEWGLDIFSVKGKGYRLAEPlDLLDPERISSQLpPGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348  78 TYTPHSQSTQLDAKQGIeAHNSAPRLYLAPSQEAAKGRLDRQFFSASTGGIYMSMYLKPNVPYADMPPYTMMVASSIVKA 157
Cdd:PRK11886  81 TVLPVIDSTNQYLLDRI-AELKSGDLCLAEYQTAGRGRRGRQWFSPFGGNLYLSLYWRLNQGPAQAMGLSLVVGIAIAEA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348 158 ISRLTGIDTEIKWVNDIYLGNHKVAGILTEAitSVETGLITDVIIGVGLNFFVTDFPEAIAQKAGSLF-TEKPTITRNDL 236
Cdd:PRK11886 160 LRRLGAIDVGLKWPNDIYLNDRKLAGILVEL--SGETGDAAHVVIGIGINVAMPDFPEELIDQPWSDLqEAGPTIDRNQL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348 237 IIDI-------WKLFLSIPVKDHVKVYKEKSLVLNKQVTFIENSQEKRAIAIDLTDQGHLIVQfENGDFQTLRSGEISLS 309
Cdd:PRK11886 238 AAELikqlraaLELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIARGIDEQGALLLE-DDGVEKPFNGGEISLR 316


                 ...
gi 489079348 310 SWE 312
Cdd:PRK11886 317 SWE 319
 
Name Accession Description Interval E-value
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
2-312 2.82e-144

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


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 408.79  E-value: 2.82e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348   2 KTSEKIYQLLS--QTDDFVSGEYLADQLSISRTSVWKSIKSLENQGIQIDSLKHKGYRMVQG-DILLPKTISQGL-GMPV 77
Cdd:PRK11886   1 KTYTVMLQLLSllADGDFHSGEQLGEELGISRAAIWKHIQTLEEWGLDIFSVKGKGYRLAEPlDLLDPERISSQLpPGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348  78 TYTPHSQSTQLDAKQGIeAHNSAPRLYLAPSQEAAKGRLDRQFFSASTGGIYMSMYLKPNVPYADMPPYTMMVASSIVKA 157
Cdd:PRK11886  81 TVLPVIDSTNQYLLDRI-AELKSGDLCLAEYQTAGRGRRGRQWFSPFGGNLYLSLYWRLNQGPAQAMGLSLVVGIAIAEA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348 158 ISRLTGIDTEIKWVNDIYLGNHKVAGILTEAitSVETGLITDVIIGVGLNFFVTDFPEAIAQKAGSLF-TEKPTITRNDL 236
Cdd:PRK11886 160 LRRLGAIDVGLKWPNDIYLNDRKLAGILVEL--SGETGDAAHVVIGIGINVAMPDFPEELIDQPWSDLqEAGPTIDRNQL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348 237 IIDI-------WKLFLSIPVKDHVKVYKEKSLVLNKQVTFIENSQEKRAIAIDLTDQGHLIVQfENGDFQTLRSGEISLS 309
Cdd:PRK11886 238 AAELikqlraaLELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIARGIDEQGALLLE-DDGVEKPFNGGEISLR 316


                 ...
gi 489079348 310 SWE 312
Cdd:PRK11886 317 SWE 319
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 85-308 3.79e-68

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: 212.73  E-value: 3.79e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348  85 STQLDAKQGIEAHNSAPRLYLAPSQEAAKGRLDRQFFSASTGGIYMSMYLKPNVPYADMPPYTMMVASSIVKAISRLTGI 164
Cdd:COG0340   10 STNDEAKELAREGAPEGTVVVAEEQTAGRGRRGRSWVSPPGKGLYFSLLLRPDLPPARLPLLSLAAGLAVAEALRELTGV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348 165 DTEIKWVNDIYLGNHKVAGILTEaiTSVETGLITDVIIGVGLNFFVTDF-PEAIAQKAGSLFTEK-PTITRNDLIIDIWK 242
Cdd:COG0340   90 DVGLKWPNDILLNGKKLAGILIE--ASGEGDGIDWVVIGIGINVNQPPFdPEELDQPATSLKEETgKEVDREELLAALLE 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489079348 243 -------LFLSIPVKDHVKVYKEKSLVLNKQVTFIENSQEKRAIAIDLTDQGHLIVQFENGDFQTLRSGEISL 308
Cdd:COG0340  168 eleelydRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEGIAVGIDEDGALLLETADGEIRAVAAGEVSL 240
BPL cd16442
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
 85-245 2.13e-42

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: 144.33  E-value: 2.13e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348  85 STQLDAKQGIEAHNSAPRLYLAPSQEAAKGRLDRQFFSASTGGIYMSMYLKPNVPYADMPPYTMMVASSIVKAISRLTGI 164
Cdd:cd16442   10 STNDEAKELARSGAPEGTVVVAEEQTAGRGRRGRKWESPKGKGLYFSLLLRPDVPPAEAPLLTLLAAVAVAEALEKLGGI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348 165 DTEIKWVNDIYLGNHKVAGILTEAITSVETglITDVIIGVGLNFFVTDFPEAI---AQKAGSLFTEKPTITRNDLIIDIW 241
Cdd:cd16442   90 PVQIKWPNDILVNGKKLAGILTEASAEGEG--VAAVVIGIGINVNNTPPPEPLpdtSLATSLGKEVDRNELLEELLAALE 167


                 ....
gi 489079348 242 KLFL 245
Cdd:cd16442  168 NRLE 171
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 77-308 4.79e-32

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: 119.04  E-value: 4.79e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348   77 VTYTPHSQSTQLDAKQGIEAHNSAPRLYLAPSQEAAKGRLDRQFFSAStGGIYMSMYLKPNVPYADMPPYTMMVASSIVK 156
Cdd:TIGR00121   2 VIVLDVIDSTNQYALELAKEGKLKGDLVVAEYQTAGRGRRGRKWLSPE-GGLYFSLILRPDLPKSPAPGLTLVAGIAIAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348  157 AISRLtGIDTEIKWVNDIYLGNHKVAGILTEAitSVETGLITDVIIGVGLNFFVTDFPEAIAQKAGSLFTE-KPTITRND 235
Cdd:TIGR00121  81 VLKEL-GDQVQVKWPNDILLKDKKLGGILTEL--TGKENRADYVVIGIGINVQNRKPAESLREQAISLSEEaGIDLDRGE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348  236 LIIDI-------WKLFLSIPVKDHVKVYKEKSLVLNKQVTFIENSQEKRAIAIDLTDQGHLIVQfENGDFQTLRSGEISL 308
Cdd:TIGR00121 158 LIEGFlrnfeenLEWFEQEGIDEILSKWEKLSAHIGREVSLTTGNGEIEGIARGIDKDGALLLE-DGGGIKKIISGEISL 236
HTH_11 pfam08279
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.
 5-56 6.85e-14

HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.


Pssm-ID: 429896 [Multi-domain]  Cd Length: 52  Bit Score: 65.15  E-value: 6.85e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489079348    5 EKIYQLLSQTDDFVSGEYLADQLSISRTSVWKSIKSLENQGIQIDSLKHKGY 56
Cdd:pfam08279   1 LQILQLLLEARGPISGQELAEKLGVSRRTIRRDIKILEELGVPIEAEPGRGY 52
 
Name Accession Description Interval E-value
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
2-312 2.82e-144

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


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 408.79  E-value: 2.82e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348   2 KTSEKIYQLLS--QTDDFVSGEYLADQLSISRTSVWKSIKSLENQGIQIDSLKHKGYRMVQG-DILLPKTISQGL-GMPV 77
Cdd:PRK11886   1 KTYTVMLQLLSllADGDFHSGEQLGEELGISRAAIWKHIQTLEEWGLDIFSVKGKGYRLAEPlDLLDPERISSQLpPGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348  78 TYTPHSQSTQLDAKQGIeAHNSAPRLYLAPSQEAAKGRLDRQFFSASTGGIYMSMYLKPNVPYADMPPYTMMVASSIVKA 157
Cdd:PRK11886  81 TVLPVIDSTNQYLLDRI-AELKSGDLCLAEYQTAGRGRRGRQWFSPFGGNLYLSLYWRLNQGPAQAMGLSLVVGIAIAEA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348 158 ISRLTGIDTEIKWVNDIYLGNHKVAGILTEAitSVETGLITDVIIGVGLNFFVTDFPEAIAQKAGSLF-TEKPTITRNDL 236
Cdd:PRK11886 160 LRRLGAIDVGLKWPNDIYLNDRKLAGILVEL--SGETGDAAHVVIGIGINVAMPDFPEELIDQPWSDLqEAGPTIDRNQL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348 237 IIDI-------WKLFLSIPVKDHVKVYKEKSLVLNKQVTFIENSQEKRAIAIDLTDQGHLIVQfENGDFQTLRSGEISLS 309
Cdd:PRK11886 238 AAELikqlraaLELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIARGIDEQGALLLE-DDGVEKPFNGGEISLR 316


                 ...
gi 489079348 310 SWE 312
Cdd:PRK11886 317 SWE 319
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 85-308 3.79e-68

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: 212.73  E-value: 3.79e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348  85 STQLDAKQGIEAHNSAPRLYLAPSQEAAKGRLDRQFFSASTGGIYMSMYLKPNVPYADMPPYTMMVASSIVKAISRLTGI 164
Cdd:COG0340   10 STNDEAKELAREGAPEGTVVVAEEQTAGRGRRGRSWVSPPGKGLYFSLLLRPDLPPARLPLLSLAAGLAVAEALRELTGV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348 165 DTEIKWVNDIYLGNHKVAGILTEaiTSVETGLITDVIIGVGLNFFVTDF-PEAIAQKAGSLFTEK-PTITRNDLIIDIWK 242
Cdd:COG0340   90 DVGLKWPNDILLNGKKLAGILIE--ASGEGDGIDWVVIGIGINVNQPPFdPEELDQPATSLKEETgKEVDREELLAALLE 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489079348 243 -------LFLSIPVKDHVKVYKEKSLVLNKQVTFIENSQEKRAIAIDLTDQGHLIVQFENGDFQTLRSGEISL 308
Cdd:COG0340  168 eleelydRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEGIAVGIDEDGALLLETADGEIRAVAAGEVSL 240
BirA COG1654
Biotin operon repressor [Transcription];
1-308 5.23e-45

Biotin operon repressor [Transcription];


Pssm-ID: 441260 [Multi-domain]  Cd Length: 324  Bit Score: 155.53  E-value: 5.23e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348   1 MKTSEKIYQLLSQtDDFVSGEYLADQLSISRTSVWKSIKSLENQGIQIDSLKHKGYRMVQG-DILLPKTISQGL-----G 74
Cdd:COG1654    3 SSTRLKLLRLLAD-GEFHSGEELAEELGVSRAAVWKHIKALRELGYEIESVPGKGYRLAEPpDLLDPEEIRAGLstkrlG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348  75 MPVTYTPHSQSTQLDAKQGIEAHNSAPRLYLAPSQEAAKGRLDRQFFSASTGGIYMSMYLKPNVPYADMPPYTMMVASSI 154
Cdd:COG1654   82 REILYVISSTSTNLLALELAAQGGDAGTVVAAEQQRGGRGRRRRSWSSPGGGGLLYSLLLRPPIAPALLSLLLLAAAVAV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348 155 VKAISRLTGIDTEIKWVNDIYLGNHKVAGILTEAITSVETGLITDVIIGVGLNFFVTDFPEAIAQKAGSLFTEKPTITRN 234
Cdd:COG1654  162 AAALAEGGGLVKWKKWPNDLLKKGKKILGILEEEGGDADGVVIVVGGGGNNNNSNPEEEPQELAELATSLLLILRLRLLR 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348 235 DLII--------DIWKLFLSIPVKDHVKVYKEKSLVLNKQVTFIENSQEKRAIAIDLTDQGHLIVQFENGDFQTLRSGEI 306
Cdd:COG1654  242 LLLLllllllelLELLGFLEFFFLWERLDWELLRVLKLVVVVVEIGGGGGGGGALGGGLLGLLLLGGGGGGGEGSLSAVV 321


                 ..
gi 489079348 307 SL 308
Cdd:COG1654  322 VL 323
BPL cd16442
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
 85-245 2.13e-42

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: 144.33  E-value: 2.13e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348  85 STQLDAKQGIEAHNSAPRLYLAPSQEAAKGRLDRQFFSASTGGIYMSMYLKPNVPYADMPPYTMMVASSIVKAISRLTGI 164
Cdd:cd16442   10 STNDEAKELARSGAPEGTVVVAEEQTAGRGRRGRKWESPKGKGLYFSLLLRPDVPPAEAPLLTLLAAVAVAEALEKLGGI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348 165 DTEIKWVNDIYLGNHKVAGILTEAITSVETglITDVIIGVGLNFFVTDFPEAI---AQKAGSLFTEKPTITRNDLIIDIW 241
Cdd:cd16442   90 PVQIKWPNDILVNGKKLAGILTEASAEGEG--VAAVVIGIGINVNNTPPPEPLpdtSLATSLGKEVDRNELLEELLAALE 167


                 ....
gi 489079348 242 KLFL 245
Cdd:cd16442  168 NRLE 171
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 77-308 4.79e-32

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: 119.04  E-value: 4.79e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348   77 VTYTPHSQSTQLDAKQGIEAHNSAPRLYLAPSQEAAKGRLDRQFFSAStGGIYMSMYLKPNVPYADMPPYTMMVASSIVK 156
Cdd:TIGR00121   2 VIVLDVIDSTNQYALELAKEGKLKGDLVVAEYQTAGRGRRGRKWLSPE-GGLYFSLILRPDLPKSPAPGLTLVAGIAIAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348  157 AISRLtGIDTEIKWVNDIYLGNHKVAGILTEAitSVETGLITDVIIGVGLNFFVTDFPEAIAQKAGSLFTE-KPTITRND 235
Cdd:TIGR00121  81 VLKEL-GDQVQVKWPNDILLKDKKLGGILTEL--TGKENRADYVVIGIGINVQNRKPAESLREQAISLSEEaGIDLDRGE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348  236 LIIDI-------WKLFLSIPVKDHVKVYKEKSLVLNKQVTFIENSQEKRAIAIDLTDQGHLIVQfENGDFQTLRSGEISL 308
Cdd:TIGR00121 158 LIEGFlrnfeenLEWFEQEGIDEILSKWEKLSAHIGREVSLTTGNGEIEGIARGIDKDGALLLE-DGGGIKKIISGEISL 236
PRK08330 PRK08330
biotin--protein ligase; Provisional
 106-308 2.97e-23

biotin--protein ligase; Provisional


Pssm-ID: 169384 [Multi-domain]  Cd Length: 236  Bit Score: 95.58  E-value: 2.97e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348 106 APSQEAAKGRLDRQFFSAStGGIYMSMYLKPNVPYADMPPYTMMVASSIVKAISRLtGIDTEIKWVNDIYLGNHKVAGIL 185
Cdd:PRK08330  33 ADRQTAGHGRKGRAWASPE-GGLWMSVILKPKVSPEHLPKLVFLGALAVVDTLREF-GIEGKIKWPNDVLVNYKKIAGVL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348 186 TEAITSVetglitdVIIGVGLNfFVTDFPEAIAQKAGS----LFTEKPTI-TRNDLI--IDIW-KLFLSIPvKDHVKVYK 257
Cdd:PRK08330 111 VEGKGDF-------VVLGIGLN-VNNEIPDELRETATSmkevLGREVPLIeVFKRLVenLDRWyKLFLEGP-GEILEEVK 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489079348 258 EKSLVLNKQVTFIEN-SQEKRAIAIDLTDQGHLIVQFENGDFQTLRSGEISL 308
Cdd:PRK08330 182 GRSMILGKRVKIIGDgEILVEGIAEDIDEFGALILRLDDGTVKKVLYGDVSL 233
HTH_11 pfam08279
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.
 5-56 6.85e-14

HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.


Pssm-ID: 429896 [Multi-domain]  Cd Length: 52  Bit Score: 65.15  E-value: 6.85e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489079348    5 EKIYQLLSQTDDFVSGEYLADQLSISRTSVWKSIKSLENQGIQIDSLKHKGY 56
Cdd:pfam08279   1 LQILQLLLEARGPISGQELAEKLGVSRRTIRRDIKILEELGVPIEAEPGRGY 52
PTZ00276 PTZ00276
biotin/lipoate protein ligase; Provisional
 75-301 8.56e-11

biotin/lipoate protein ligase; Provisional


Pssm-ID: 140302 [Multi-domain]  Cd Length: 245  Bit Score: 61.03  E-value: 8.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348  75 MPVTYTPHSQ------STQLDAKQGIEAHNSAPRLYLAPSQEAAKGRLDRQFFSAStGGIYMSMylkpNVPYADMPPYTM 148
Cdd:PTZ00276   1 MPADVPPNIHfvgevtSTMDVARTMLAAAGGKPFAVLAESQTAGRGTGGRTWTSPK-GNMYFTL----CIPQKGVPPELV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348 149 MVASSIVKAISR------LTGIDTEIKWVNDIYLGNHKVAGILTEAITSvetglitDVIIGVGLNFFVTdfPE------- 215
Cdd:PTZ00276  76 PVLPLITGLACRaaimevLHGAAVHTKWPNDIIYAGKKIGGSLIESEGE-------YLIIGIGMNIEVA--PPvtdagre 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348 216 -----AIAQKAGslfteKPTITRNDLIIDIWKLFLSI---------PVKDHVKVYKEKSLVLNKQVTFIENSQEKRAIAi 281
Cdd:PTZ00276 147 stmvnEIAEDLG-----VKSVTPQDLAEAVWKHFFDIcsdpeltreILIESFDAAMDKSLKLHKRTPTGRDPEELTALS- 220

                        250       260
                 ....*....|....*....|
gi 489079348 282 dLTDQGHLIVQFENGDFQTL 301
Cdd:PTZ00276 221 -LNEWGHLIVRRPDGTEEDL 239
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 100-207 3.93e-09

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: 53.99  E-value: 3.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348  100 APRLYLAPSQEAAKGRLDRQFFSAStGGIYMSMYLKPNVPYADMPPYTMMVASSIVKAI-------SRLTGIDTEIKWVN 172
Cdd:pfam03099  22 SGGVVVVRRQTGGRGRGGNVWHSPK-GCLTYSLLLSKEHPNVDPSVLEFYVLELVLAVLealglykPGISGIPCFVKWPN 100

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 489079348  173 DIYLGNHKVAGIlteAITSVETGLITDVIIGVGLN 207
Cdd:pfam03099 101 DLYVNGRKLAGI---LQRSTRGGTLHHGVIGLGVN 132
birA_repr_reg TIGR00122
BirA biotin operon repressor domain; This model represents the amino-terminal helix-turn-helix ...
 10-66 1.62e-06

BirA biotin operon repressor domain; This model represents the amino-terminal helix-turn-helix repressor region of the biotin--acetyl-CoA-carboxylase ligase/biotin operon repressor bifunctional protein BirA. In many species, the biotin--acetyl-CoA-carboxylase ligase ortholog lacks this DNA-binding repressor region and therefore is not equivalent to the well-characterized BirA of E. coli. This model may recognize some other putative repressor proteins, such as DnrO of Streptomyces peucetius with scores below the noise cutoff but with significance shown by low E-value. [Regulatory functions, DNA interactions]


Pssm-ID: 272918 [Multi-domain]  Cd Length: 69  Bit Score: 44.76  E-value: 1.62e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489079348   10 LLSQTDDFVSGEYLADQLSISRTSVWKSIKSLENQGIQIDSLKhKGYRMVQGDILLP 66
Cdd:TIGR00122   6 LALLADNPFSGEKLGEALGMSRTAVNKHIQTLREWGVDVLTVG-KGYRLPPPIPLLN 61
PRK08477 PRK08477
biotin--[acetyl-CoA-carboxylase] ligase;
85-209 2.19e-06

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


Pssm-ID: 236273 [Multi-domain]  Cd Length: 211  Bit Score: 47.64  E-value: 2.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348  85 STQLDAKQGIEAHN-SAPRLYLAPSQEAAKGRLDRQFFSAStGGIYMSMYLKPNVPYADMPpytmMVASSI-----VKAI 158
Cdd:PRK08477  11 STQTYLIEKIKNGElKAPFAIVAKEQTAGIGSRGNSWEGKK-GNLFFSFALKESDLPKDLP----LQSSSIyfgflLKEV 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489079348 159 SRLTGIDTEIKWVNDIYLGNHKVAGILTEAITSVetglitdVIIGVGLNFF 209
Cdd:PRK08477  86 LKELGSKVWLKWPNDLYLDDKKIGGVITNKIKNF-------IVCGIGLNLK 129
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
 262-308 1.35e-05

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: 41.68  E-value: 1.35e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 489079348  262 VLNKQVTFIENSQEKRAIAIDLTDQGHLIVQFENGDFQTLRSGEISL 308
Cdd:pfam02237   1 TLGREVRVLLGDGIVEGIAVGIDDDGALLLETDDGTIRDINSGEVSL 47
PRK13325 PRK13325
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase;
142-225 1.40e-05

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


Pssm-ID: 183976 [Multi-domain]  Cd Length: 592  Bit Score: 46.63  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348 142 DMPPYTMMVASSIVKAISRLT----GIDTEIKWVNDIYLGNHKVAGILTEaitSVETGLITDVIIGVGLNFFVtdfPEAI 217
Cdd:PRK13325 146 DRPQYELGSLSPVAAVACRRAlsrlGLKTQIKWPNDLVVGRDKLGGILIE---TVRTGGKTVAVVGIGINFVL---PKEV 219

                         90
                 ....*....|
gi 489079348 218 AQKAG--SLF 225
Cdd:PRK13325 220 ENAASvqSLF 229
YobV COG2378
Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains ...
 1-66 2.26e-05

Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains [Transcription];


Pssm-ID: 441945 [Multi-domain]  Cd Length: 314  Bit Score: 45.45  E-value: 2.26e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348   1 MKTSEKIYQLLS--QTDDFVSGEYLADQLSISRTSVWKSIKSLENQGIQIDSL--KHKGYRMVQGDILLP 66
Cdd:COG2378    1 MSRLERLLALLQllQSRRGVTAAELAERLEVSERTIYRDIDALRELGVPIEAErgRGGGYRLRDGYRLPP 70
PRK06955 PRK06955
biotin--[acetyl-CoA-carboxylase] ligase;
100-233 2.71e-05

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


Pssm-ID: 235896 [Multi-domain]  Cd Length: 300  Bit Score: 45.16  E-value: 2.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348 100 APRLYLAPSQEAAKGRLDRQFFSASTGGIYMSMYLKPNVPYADMPPYTMMVASSIVKAISRL---TGIDTEIKWVNDIYL 176
Cdd:PRK06955  64 APIVRVAYEQTAGRGRQGRPWFAQPGNALLFSVACVLPRPVAALAGLSLAVGVALAEALAALpaaLGQRIALKWPNDLLI 143

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489079348 177 GNHKVAGILTEAITSveTGLITDVIIGVGLNFfvtDFPEAIAQKAGSLFTEKPTITR 233
Cdd:PRK06955 144 AGRKLAGILIETVWA--TPDATAVVIGIGLNV---RRADAVAAEVDALRAREAALAR 195
PRK05935 PRK05935
biotin--protein ligase; Provisional
 85-224 2.79e-04

biotin--protein ligase; Provisional


Pssm-ID: 235649 [Multi-domain]  Cd Length: 190  Bit Score: 40.96  E-value: 2.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348  85 STQLDAKQGIEAHN-SAPRLYLAPSQEAAKGRLDRQFFSaSTGGIYMSMYLKPNVPYADMPPYTMMVASSIVKAISRLTG 163
Cdd:PRK05935  13 STNTTAKEGMHLWDpYALTVISTREQTAGKGKFGKSWHS-SDQDLLASFCFFITVLNIDVSLLFRLGTEAVMRLGEDLGI 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489079348 164 IDTEIKWVNDIYLGNHKVAGILTEAItSVETGLitDVIIGVGLNFFVT-DFPEAIAQKAGSL 224
Cdd:PRK05935  92 TEAVIKWPNDVLVHGEKLCGVLCETI-PVKGGL--GVILGIGVNGNTTkDELLGIDQPATSL 150
BPL_LplA_LipB cd16435
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ...
 96-207 3.64e-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: 40.98  E-value: 3.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079348  96 AHNSAPRLYLAPSQEAAKGRLDRQF----FSASTGGIYMSMYLKPNVPYaDMPPYTMMVASSIVKAISRLtGIDTEIKWV 171
Cdd:cd16435   46 LDRELPHLELAKKIERGYELVVRNRggraVSHDPGQLVFSPVIGPNVEF-MISKFNLIIEEGIRDAIADF-GQSAEVKWG 123

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489079348 172 -NDIYLGNHKVAGILTEAITSVetglitdVIIGVGLN 207
Cdd:cd16435  124 rNDLWIDNRKVCGIAVRVVKEA-------IFHGIALN 153
HTH_24 pfam13412
Winged helix-turn-helix DNA-binding;
2-46 7.83e-03

Winged helix-turn-helix DNA-binding;


Pssm-ID: 404317 [Multi-domain]  Cd Length: 45  Bit Score: 33.95  E-value: 7.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 489079348    2 KTSEKIYQLLsQTDDFVSGEYLADQLSISRTSVWKSIKSLENQGI 46
Cdd:pfam13412   1 ETDRKILNLL-QENPRISQRELAERLGLSPSTVNRRLKRLEEEGV 44
 
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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