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Conserved domains on  [gi|502978728|ref|WP_013213704|]
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MULTISPECIES: biotin--[acetyl-CoA-carboxylase] ligase [Ralstonia solanacearum species complex]

Protein Classification

PRK06955 family protein( domain architecture ID 11482511)

PRK06955 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK06955 PRK06955
biotin--[acetyl-CoA-carboxylase] ligase;
1-290 1.51e-120

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


:

Pssm-ID: 235896 [Multi-domain]  Cd Length: 300  Bit Score: 347.15  E-value: 1.51e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728   1 MSSAPTPARWRLTRDRIQPTGVAAG--WPVEVVESTGSTNADLMAAVRNAVWPAtvgtpagaAPLVGARVLAARRQTAGR 78
Cdd:PRK06955   6 PSSTPASGDWRIDRDRLDAHLAAAAraWPLEIVEETGSTNADLMARLKALPRSA--------DALPAPIVRVAYEQTAGR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728  79 GRQGRPWDGDHG--LTFSVACAFAGEPAQLAGLSLAVGVAVADAVATYAETHGgsaQALTLKWPNDVQIAGRKLAGILVE 156
Cdd:PRK06955  78 GRQGRPWFAQPGnaLLFSVACVLPRPVAALAGLSLAVGVALAEALAALPAALG---QRIALKWPNDLLIAGRKLAGILIE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728 157 TMRAAPGQTWAVIGIGLNLERP----------RALETALGRSLSGVEELV--DRPAPNAVLTTLLSALGEHLLRFGTHGL 224
Cdd:PRK06955 155 TVWATPDATAVVIGIGLNVRRAdavaaevdalRAREAALARGLPPVALAAacAGANLTDTLAAALNALAPALQAFGADGL 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502978728 225 APFVAPFAARDAFAGQPVRLWQDGAVVLEGVAHGIDAQGRLAIESGGRVQWIHSGEVSLRAADAEQ 290
Cdd:PRK06955 235 APFAARWHALHAYAGREVVLLEDGAELARGVAHGIDETGQLLLDTPAGRQAIAAGDVSLREADAAR 300
 
Name Accession Description Interval E-value
PRK06955 PRK06955
biotin--[acetyl-CoA-carboxylase] ligase;
1-290 1.51e-120

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


Pssm-ID: 235896 [Multi-domain]  Cd Length: 300  Bit Score: 347.15  E-value: 1.51e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728   1 MSSAPTPARWRLTRDRIQPTGVAAG--WPVEVVESTGSTNADLMAAVRNAVWPAtvgtpagaAPLVGARVLAARRQTAGR 78
Cdd:PRK06955   6 PSSTPASGDWRIDRDRLDAHLAAAAraWPLEIVEETGSTNADLMARLKALPRSA--------DALPAPIVRVAYEQTAGR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728  79 GRQGRPWDGDHG--LTFSVACAFAGEPAQLAGLSLAVGVAVADAVATYAETHGgsaQALTLKWPNDVQIAGRKLAGILVE 156
Cdd:PRK06955  78 GRQGRPWFAQPGnaLLFSVACVLPRPVAALAGLSLAVGVALAEALAALPAALG---QRIALKWPNDLLIAGRKLAGILIE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728 157 TMRAAPGQTWAVIGIGLNLERP----------RALETALGRSLSGVEELV--DRPAPNAVLTTLLSALGEHLLRFGTHGL 224
Cdd:PRK06955 155 TVWATPDATAVVIGIGLNVRRAdavaaevdalRAREAALARGLPPVALAAacAGANLTDTLAAALNALAPALQAFGADGL 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502978728 225 APFVAPFAARDAFAGQPVRLWQDGAVVLEGVAHGIDAQGRLAIESGGRVQWIHSGEVSLRAADAEQ 290
Cdd:PRK06955 235 APFAARWHALHAYAGREVVLLEDGAELARGVAHGIDETGQLLLDTPAGRQAIAAGDVSLREADAAR 300
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 27-284 3.46e-60

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: 191.54  E-value: 3.46e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728  27 PVEVVESTGSTNADLMAAVRNavwpatvGTPAGAaplvgarVLAARRQTAGRGRQGRPWDGDHG--LTFSVACAFAGEPA 104
Cdd:COG0340    1 RIEVFDEVDSTNDEAKELARE-------GAPEGT-------VVVAEEQTAGRGRRGRSWVSPPGkgLYFSLLLRPDLPPA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728 105 QLAGLSLAvgvavadavatyaethGGSA--QAL--------TLKWPNDVQIAGRKLAGILVETMRAAPGQTWAVIGIGLN 174
Cdd:COG0340   67 RLPLLSLA----------------AGLAvaEALreltgvdvGLKWPNDILLNGKKLAGILIEASGEGDGIDWVVIGIGIN 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728 175 LERPRALETALGR---SLSgvEELVDRPAPNAVLTTLLSALGEHLLRFGTHGLAPFVAPFAARDAFAGQPVRLWQDGAVV 251
Cdd:COG0340  131 VNQPPFDPEELDQpatSLK--EETGKEVDREELLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETL 208

                        250       260       270
                 ....*....|....*....|....*....|....
gi 502978728 252 lEGVAHGIDAQGRLAIE-SGGRVQWIHSGEVSLR 284
Cdd:COG0340  209 -EGIAVGIDEDGALLLEtADGEIRAVAAGEVSLR 241
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 71-284 2.86e-34

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: 124.44  E-value: 2.86e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728   71 ARRQTAGRGRQGRPWDGDHG-LTFSVACAFAGEPAQLAGLSLAVGVAVADAVatyaETHGGSAQaltLKWPNDVQIAGRK 149
Cdd:TIGR00121  31 AEYQTAGRGRRGRKWLSPEGgLYFSLILRPDLPKSPAPGLTLVAGIAIAEVL----KELGDQVQ---VKWPNDILLKDKK 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728  150 LAGILVETMRAAPGQTWAVIGIGLNLERPRALETALGRSLSGVEEL---VDRpapNAVLTTLLSALGEHLLRFGTHGLAP 226
Cdd:TIGR00121 104 LGGILTELTGKENRADYVVIGIGINVQNRKPAESLREQAISLSEEAgidLDR---GELIEGFLRNFEENLEWFEQEGIDE 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 502978728  227 FVAPFAARDAFAGQPVRLWQDGAVVlEGVAHGIDAQGRLAIESGGRVQWIHSGEVSLR 284
Cdd:TIGR00121 181 ILSKWEKLSAHIGREVSLTTGNGEI-EGIARGIDKDGALLLEDGGGIKKIISGEISLR 237
BPL cd16442
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
 27-219 1.21e-28

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: 107.73  E-value: 1.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728  27 PVEVVESTGSTNADLMAAVRNavwpatvGTPAGAaplvgarVLAARRQTAGRGRQGRPWDG--DHGLTFSVACAFAGEPA 104
Cdd:cd16442    1 KLIVLDEIDSTNDEAKELARS-------GAPEGT-------VVVAEEQTAGRGRRGRKWESpkGKGLYFSLLLRPDVPPA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728 105 QLAGLSLAVGVAVADAVATYAETHGGsaqaltLKWPNDVQIAGRKLAGILVETMRAAPGQTWAVIGIGLNLERPRalETA 184
Cdd:cd16442   67 EAPLLTLLAAVAVAEALEKLGGIPVQ------IKWPNDILVNGKKLAGILTEASAEGEGVAAVVIGIGINVNNTP--PPE 138

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 502978728 185 LGRSLSGVEELVDRPAPNAVLTTLLSALGEHLLRF 219
Cdd:cd16442  139 PLPDTSLATSLGKEVDRNELLEELLAALENRLELF 173
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 67-174 1.25e-10

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: 58.22  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728   67 RVLAARRQTAGRGRQGRPW-DGDHGLTFSVACAFAGEPAQLAGLSLAVGVAVADAVATYAETHGGSAQALT-LKWPNDVQ 144
Cdd:pfam03099  24 GVVVVRRQTGGRGRGGNVWhSPKGCLTYSLLLSKEHPNVDPSVLEFYVLELVLAVLEALGLYKPGISGIPCfVKWPNDLY 103

                          90       100       110
                  ....*....|....*....|....*....|
gi 502978728  145 IAGRKLAGILVETMRAAPGQTwAVIGIGLN 174
Cdd:pfam03099 104 VNGRKLAGILQRSTRGGTLHH-GVIGLGVN 132
 
Name Accession Description Interval E-value
PRK06955 PRK06955
biotin--[acetyl-CoA-carboxylase] ligase;
1-290 1.51e-120

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


Pssm-ID: 235896 [Multi-domain]  Cd Length: 300  Bit Score: 347.15  E-value: 1.51e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728   1 MSSAPTPARWRLTRDRIQPTGVAAG--WPVEVVESTGSTNADLMAAVRNAVWPAtvgtpagaAPLVGARVLAARRQTAGR 78
Cdd:PRK06955   6 PSSTPASGDWRIDRDRLDAHLAAAAraWPLEIVEETGSTNADLMARLKALPRSA--------DALPAPIVRVAYEQTAGR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728  79 GRQGRPWDGDHG--LTFSVACAFAGEPAQLAGLSLAVGVAVADAVATYAETHGgsaQALTLKWPNDVQIAGRKLAGILVE 156
Cdd:PRK06955  78 GRQGRPWFAQPGnaLLFSVACVLPRPVAALAGLSLAVGVALAEALAALPAALG---QRIALKWPNDLLIAGRKLAGILIE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728 157 TMRAAPGQTWAVIGIGLNLERP----------RALETALGRSLSGVEELV--DRPAPNAVLTTLLSALGEHLLRFGTHGL 224
Cdd:PRK06955 155 TVWATPDATAVVIGIGLNVRRAdavaaevdalRAREAALARGLPPVALAAacAGANLTDTLAAALNALAPALQAFGADGL 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502978728 225 APFVAPFAARDAFAGQPVRLWQDGAVVLEGVAHGIDAQGRLAIESGGRVQWIHSGEVSLRAADAEQ 290
Cdd:PRK06955 235 APFAARWHALHAYAGREVVLLEDGAELARGVAHGIDETGQLLLDTPAGRQAIAAGDVSLREADAAR 300
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 27-284 3.46e-60

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: 191.54  E-value: 3.46e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728  27 PVEVVESTGSTNADLMAAVRNavwpatvGTPAGAaplvgarVLAARRQTAGRGRQGRPWDGDHG--LTFSVACAFAGEPA 104
Cdd:COG0340    1 RIEVFDEVDSTNDEAKELARE-------GAPEGT-------VVVAEEQTAGRGRRGRSWVSPPGkgLYFSLLLRPDLPPA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728 105 QLAGLSLAvgvavadavatyaethGGSA--QAL--------TLKWPNDVQIAGRKLAGILVETMRAAPGQTWAVIGIGLN 174
Cdd:COG0340   67 RLPLLSLA----------------AGLAvaEALreltgvdvGLKWPNDILLNGKKLAGILIEASGEGDGIDWVVIGIGIN 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728 175 LERPRALETALGR---SLSgvEELVDRPAPNAVLTTLLSALGEHLLRFGTHGLAPFVAPFAARDAFAGQPVRLWQDGAVV 251
Cdd:COG0340  131 VNQPPFDPEELDQpatSLK--EETGKEVDREELLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETL 208

                        250       260       270
                 ....*....|....*....|....*....|....
gi 502978728 252 lEGVAHGIDAQGRLAIE-SGGRVQWIHSGEVSLR 284
Cdd:COG0340  209 -EGIAVGIDEDGALLLEtADGEIRAVAAGEVSLR 241
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
25-287 1.57e-49

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


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 166.50  E-value: 1.57e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728  25 GWPVEVVESTGSTNADLMAavrnavwpatvgtpaGAAPLVGARVLAARRQTAGRGRQGRPW---DGdHGLTFSVACAFAG 101
Cdd:PRK11886  77 PGRVTVLPVIDSTNQYLLD---------------RIAELKSGDLCLAEYQTAGRGRRGRQWfspFG-GNLYLSLYWRLNQ 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728 102 EPAQLAGLSLAVgvavadavatyaethGGS-AQALT--------LKWPNDVQIAGRKLAGILVETMRAAPGQTWAVIGIG 172
Cdd:PRK11886 141 GPAQAMGLSLVV---------------GIAiAEALRrlgaidvgLKWPNDIYLNDRKLAGILVELSGETGDAAHVVIGIG 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728 173 LNLERPRALETALGR---SLSGVEELVDRpapNAVLTTLLSALGEHLLRFGTHGLAPFVAPFAARDAFAGQPVRLwQDGA 249
Cdd:PRK11886 206 INVAMPDFPEELIDQpwsDLQEAGPTIDR---NQLAAELIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKL-IIGD 281

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 502978728 250 VVLEGVAHGIDAQGRLAIESGGRVQWIHSGEVSLRAAD 287
Cdd:PRK11886 282 KEISGIARGIDEQGALLLEDDGVEKPFNGGEISLRSWE 319
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 71-284 2.86e-34

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: 124.44  E-value: 2.86e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728   71 ARRQTAGRGRQGRPWDGDHG-LTFSVACAFAGEPAQLAGLSLAVGVAVADAVatyaETHGGSAQaltLKWPNDVQIAGRK 149
Cdd:TIGR00121  31 AEYQTAGRGRRGRKWLSPEGgLYFSLILRPDLPKSPAPGLTLVAGIAIAEVL----KELGDQVQ---VKWPNDILLKDKK 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728  150 LAGILVETMRAAPGQTWAVIGIGLNLERPRALETALGRSLSGVEEL---VDRpapNAVLTTLLSALGEHLLRFGTHGLAP 226
Cdd:TIGR00121 104 LGGILTELTGKENRADYVVIGIGINVQNRKPAESLREQAISLSEEAgidLDR---GELIEGFLRNFEENLEWFEQEGIDE 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 502978728  227 FVAPFAARDAFAGQPVRLWQDGAVVlEGVAHGIDAQGRLAIESGGRVQWIHSGEVSLR 284
Cdd:TIGR00121 181 ILSKWEKLSAHIGREVSLTTGNGEI-EGIARGIDKDGALLLEDGGGIKKIISGEISLR 237
BPL cd16442
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
 27-219 1.21e-28

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: 107.73  E-value: 1.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728  27 PVEVVESTGSTNADLMAAVRNavwpatvGTPAGAaplvgarVLAARRQTAGRGRQGRPWDG--DHGLTFSVACAFAGEPA 104
Cdd:cd16442    1 KLIVLDEIDSTNDEAKELARS-------GAPEGT-------VVVAEEQTAGRGRRGRKWESpkGKGLYFSLLLRPDVPPA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728 105 QLAGLSLAVGVAVADAVATYAETHGGsaqaltLKWPNDVQIAGRKLAGILVETMRAAPGQTWAVIGIGLNLERPRalETA 184
Cdd:cd16442   67 EAPLLTLLAAVAVAEALEKLGGIPVQ------IKWPNDILVNGKKLAGILTEASAEGEGVAAVVIGIGINVNNTP--PPE 138

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 502978728 185 LGRSLSGVEELVDRPAPNAVLTTLLSALGEHLLRF 219
Cdd:cd16442  139 PLPDTSLATSLGKEVDRNELLEELLAALENRLELF 173
PRK13325 PRK13325
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase;
74-284 3.93e-25

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


Pssm-ID: 183976 [Multi-domain]  Cd Length: 592  Bit Score: 104.79  E-value: 3.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728  74 QTAGRGRQGRPWDGDHG--LTFSVACAFAGEPAQLAGLSlavgvavADAVATYAETHGGSAQALTLKWPNDVQIAGRKLA 151
Cdd:PRK13325 118 QSKGRGRQGRKWSHRLGecLMFSFGWVFDRPQYELGSLS-------PVAAVACRRALSRLGLKTQIKWPNDLVVGRDKLG 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728 152 GILVETMRAApGQTWAVIGIGLNLERPRALETALG-RSLSGVEELVDRPAPNAVLTTLLSALGEHLLRFGTHGLAPFVAP 230
Cdd:PRK13325 191 GILIETVRTG-GKTVAVVGIGINFVLPKEVENAASvQSLFQTASRRGNADAAVLLETLLAELDAVLLQYARDGFAPFVAE 269

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 502978728 231 FAARDAFAGQPVRLWQDGAVVLEGVAHGIDAQGRLAIESGGRVQWIHSGEVSLR 284
Cdd:PRK13325 270 YQAANRDHGKAVLLLRDGETVFEGTVKGVDGQGVLHLETAEGKQTVVSGEISLR 323
PRK08330 PRK08330
biotin--protein ligase; Provisional
 68-284 1.25e-21

biotin--protein ligase; Provisional


Pssm-ID: 169384 [Multi-domain]  Cd Length: 236  Bit Score: 90.96  E-value: 1.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728  68 VLAARRQTAGRGRQGRPWDG-DHGLTFSVACAFAGEPAQLAGLSLAVGVAVAdavatyaET-HGGSAQAlTLKWPNDVQI 145
Cdd:PRK08330  30 VIVADRQTAGHGRKGRAWASpEGGLWMSVILKPKVSPEHLPKLVFLGALAVV-------DTlREFGIEG-KIKWPNDVLV 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728 146 AGRKLAGILVEtmraAPGQtWAVIGIGLNL--ERPRAL-ETA------LGRSLSGVEelvdrpapnaVLTTLLSALgEHL 216
Cdd:PRK08330 102 NYKKIAGVLVE----GKGD-FVVLGIGLNVnnEIPDELrETAtsmkevLGREVPLIE----------VFKRLVENL-DRW 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502978728 217 LRFGTHGLAPFVAPFAARDAFAGQPVRLWQDGAVVLEGVAHGIDAQGRLAIE-SGGRVQWIHSGEVSLR 284
Cdd:PRK08330 166 YKLFLEGPGEILEEVKGRSMILGKRVKIIGDGEILVEGIAEDIDEFGALILRlDDGTVKKVLYGDVSLR 234
BirA COG1654
Biotin operon repressor [Transcription];
11-284 1.06e-11

Biotin operon repressor [Transcription];


Pssm-ID: 441260 [Multi-domain]  Cd Length: 324  Bit Score: 64.24  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728  11 RLTRDRIQP--TGVAAGWPVEVVESTGSTNADLMAAvrnavwpatvgtpAGAAPLVGArVLAARRQTAGRGRQGRPWD-- 86
Cdd:COG1654   65 LLDPEEIRAglSTKRLGREILYVISSTSTNLLALEL-------------AAQGGDAGT-VVAAEQQRGGRGRRRRSWSsp 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728  87 GDHGLTFSVACAFAGEPAQLAGLSLAVGVAVADAVATYAETHGGsaqaltLKWPNDVQIAGRKLAGILVETMRAAPGQTW 166
Cdd:COG1654  131 GGGGLLYSLLLRPPIAPALLSLLLLAAAVAVAAALAEGGGLVKW------KKWPNDLLKKGKKILGILEEEGGDADGVVI 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728 167 AVIGIGLNLERPRALETALGRSLSGVEELVDRPAPNAVLTTLLSALGEHLLRFgthGLAPFVAPFAARDAFAGQPVRLWQ 246
Cdd:COG1654  205 VVGGGGNNNNSNPEEEPQELAELATSLLLILRLRLLRLLLLLLLLLLELLELL---GFLEFFFLWERLDWELLRVLKLVV 281

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 502978728 247 DGAVVLEGVAHGIDAQGRLAIESGGRVQWIHSGEVSLR 284
Cdd:COG1654  282 VVVEIGGGGGGGGALGGGLLGLLLLGGGGGGGEGSLSA 319
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 67-174 1.25e-10

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: 58.22  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728   67 RVLAARRQTAGRGRQGRPW-DGDHGLTFSVACAFAGEPAQLAGLSLAVGVAVADAVATYAETHGGSAQALT-LKWPNDVQ 144
Cdd:pfam03099  24 GVVVVRRQTGGRGRGGNVWhSPKGCLTYSLLLSKEHPNVDPSVLEFYVLELVLAVLEALGLYKPGISGIPCfVKWPNDLY 103

                          90       100       110
                  ....*....|....*....|....*....|
gi 502978728  145 IAGRKLAGILVETMRAAPGQTwAVIGIGLN 174
Cdd:pfam03099 104 VNGRKLAGILQRSTRGGTLHH-GVIGLGVN 132
PRK05935 PRK05935
biotin--protein ligase; Provisional
 31-223 9.63e-10

biotin--protein ligase; Provisional


Pssm-ID: 235649 [Multi-domain]  Cd Length: 190  Bit Score: 56.75  E-value: 9.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728  31 VESTGSTNAdlMAAVRNAVWPATVGTpagaaplvgarVLAARRQTAGRGRQGRPW---DGDHGLTFsvaCAFAGE----P 103
Cdd:PRK05935   8 IAETPSTNT--TAKEGMHLWDPYALT-----------VISTREQTAGKGKFGKSWhssDQDLLASF---CFFITVlnidV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728 104 AQL------AGLSLAVGVavadavatyaethgGSAQAlTLKWPNDVQIAGRKLAGILVETMrAAPGQTWAVIGIGLN--- 174
Cdd:PRK05935  72 SLLfrlgteAVMRLGEDL--------------GITEA-VIKWPNDVLVHGEKLCGVLCETI-PVKGGLGVILGIGVNgnt 135

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 502978728 175 -------LERP-RALETALGRSLSgVEELVDRPAPNaVLTTLLSALGEHLLRFGTHG 223
Cdd:PRK05935 136 tkdellgIDQPaTSLQELLGHPID-LEEQRERLIKH-IKHVLIQTLPKLLARESNHG 190
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
 237-284 9.64e-09

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: 50.54  E-value: 9.64e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 502978728  237 FAGQPVRLWQDGAVVlEGVAHGIDAQGRLAIE-SGGRVQWIHSGEVSLR 284
Cdd:pfam02237   1 TLGREVRVLLGDGIV-EGIAVGIDDDGALLLEtDDGTIRDINSGEVSLR 48
PTZ00276 PTZ00276
biotin/lipoate protein ligase; Provisional
 28-176 3.14e-07

biotin/lipoate protein ligase; Provisional


Pssm-ID: 140302 [Multi-domain]  Cd Length: 245  Bit Score: 50.25  E-value: 3.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728  28 VEVVESTGSTnadlMAAVRnavwpaTVGTPAGAAPLVgarVLAARrQTAGRGRQGRPWDGDHG-LTFSVACAFAGEPAQL 106
Cdd:PTZ00276   9 IHFVGEVTST----MDVAR------TMLAAAGGKPFA---VLAES-QTAGRGTGGRTWTSPKGnMYFTLCIPQKGVPPEL 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502978728 107 AG-LSLAVGVAVADAVATYAEthggsAQALTLKWPNDVQIAGRKLAGILVEtmraAPGQtWAVIGIGLNLE 176
Cdd:PTZ00276  75 VPvLPLITGLACRAAIMEVLH-----GAAVHTKWPNDIIYAGKKIGGSLIE----SEGE-YLIIGIGMNIE 135
PRK08477 PRK08477
biotin--[acetyl-CoA-carboxylase] ligase;
28-178 1.74e-04

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


Pssm-ID: 236273 [Multi-domain]  Cd Length: 211  Bit Score: 41.86  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978728  28 VEVVESTGSTNADLMAAVRNAVWPATVGtpagaaplvgarvLAARRQTAGRGRQGRPWDGDHG-LTFSVACAFAGEPA-- 104
Cdd:PRK08477   3 IRVFESLDSTQTYLIEKIKNGELKAPFA-------------IVAKEQTAGIGSRGNSWEGKKGnLFFSFALKESDLPKdl 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502978728 105 QLAGLSLAVGVAVAdavatyaETHGGSAQALTLKWPNDVQIAGRKLAGILVETMRaapgqTWAVIGIGLNLERP 178
Cdd:PRK08477  70 PLQSSSIYFGFLLK-------EVLKELGSKVWLKWPNDLYLDDKKIGGVITNKIK-----NFIVCGIGLNLKFS 131
 
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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