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Conserved domains on  [gi|500622390|gb|EOQ62381|]
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biotin-[acetyl-CoA-carboxylase] ligase [Acinetobacter calcoaceticus ANC 3811]

Protein Classification

biotin--[acetyl-CoA-carboxylase] ligase( domain architecture ID 11417403)

biotin--[acetyl-CoA-carboxylase] ligase catalyzes the formation of biotinyl-5'-AMP from biotin and ATP, and the succeeding biotinylation of the biotin carboxyl carrier protein

CATH:  3.30.930.10
EC:  6.3.4.-
Gene Ontology:  GO:0036211|GO:0005524|GO:0009374|GO:0042803
PubMed:  10470036

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 26-235 1.22e-54

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: 175.75  E-value: 1.22e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  26 ATTTSTNDDIREIAKKGITTGLVCSA-QQTQGRGQHQRQWISPEG-NIYLSTLVQTRTPLD--GRLALEVALNILQ-IPQ 100
Cdd:COG0340    6 DEVDSTNDEAKELAREGAPEGTVVVAeEQTAGRGRRGRSWVSPPGkGLYFSLLLRPDLPPArlPLLSLAAGLAVAEaLRE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390 101 LQALNLQVKWPNDLYSTHGKWGGILVE----PLSQHQAIVGVGINLKTPPVTDSD--QPITSLEDLGLEQMSRLELISEL 174
Cdd:COG0340   86 LTGVDVGLKWPNDILLNGKKLAGILIEasgeGDGIDWVVIGIGINVNQPPFDPEEldQPATSLKEETGKEVDREELLAAL 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500622390 175 YVAIQNA-ARWFDHGCYNLAGRFNHHAAWLNQLVQFEHSQGLVHGRFVGISNEGAVILETPE 235
Cdd:COG0340  166 LEELEELyDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEGIAVGIDEDGALLLETAD 227
 
Name Accession Description Interval E-value
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 26-235 1.22e-54

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: 175.75  E-value: 1.22e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  26 ATTTSTNDDIREIAKKGITTGLVCSA-QQTQGRGQHQRQWISPEG-NIYLSTLVQTRTPLD--GRLALEVALNILQ-IPQ 100
Cdd:COG0340    6 DEVDSTNDEAKELAREGAPEGTVVVAeEQTAGRGRRGRSWVSPPGkGLYFSLLLRPDLPPArlPLLSLAAGLAVAEaLRE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390 101 LQALNLQVKWPNDLYSTHGKWGGILVE----PLSQHQAIVGVGINLKTPPVTDSD--QPITSLEDLGLEQMSRLELISEL 174
Cdd:COG0340   86 LTGVDVGLKWPNDILLNGKKLAGILIEasgeGDGIDWVVIGIGINVNQPPFDPEEldQPATSLKEETGKEVDREELLAAL 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500622390 175 YVAIQNA-ARWFDHGCYNLAGRFNHHAAWLNQLVQFEHSQGLVHGRFVGISNEGAVILETPE 235
Cdd:COG0340  166 LEELEELyDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEGIAVGIDEDGALLLETAD 227
BPL cd16442
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
 22-185 1.22e-35

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: 124.68  E-value: 1.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  22 VLLKATTTSTNDDIREIAKKGITTGLVCSA-QQTQGRGQHQRQWISPEG-NIYLSTLVQTRTPLD--GRLALEVALNILQ 97
Cdd:cd16442    2 LIVLDEIDSTNDEAKELARSGAPEGTVVVAeEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPPAeaPLLTLLAAVAVAE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  98 -IPQLQALNLQVKWPNDLYSTHGKWGGILVE----PLSQHQAIVGVGINLKTPPVTDSDqPITSLEDLGLEQMSRLELIS 172
Cdd:cd16442   82 aLEKLGGIPVQIKWPNDILVNGKKLAGILTEasaeGEGVAAVVIGIGINVNNTPPPEPL-PDTSLATSLGKEVDRNELLE 160

                        170
                 ....*....|...
gi 500622390 173 ELYVAIQNAARWF 185
Cdd:cd16442  161 ELLAALENRLELF 173
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
10-233 3.53e-32

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


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 119.51  E-value: 3.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  10 QLLSAK---NQLPE-VVLLKATTTSTNDDI-REIAkkGITTGLVCSA-QQTQGRGQHQRQWISPEG-NIYLS---TLVQT 79
Cdd:PRK11886  64 DLLDPErisSQLPPgRVTVLPVIDSTNQYLlDRIA--ELKSGDLCLAeYQTAGRGRRGRQWFSPFGgNLYLSlywRLNQG 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  80 RTPLDGrLALEVALNILQ-IPQLQALNLQVKWPNDLYSTHGKWGGILVE----PLSQHQAIVGVGINLKTPPVTDS--DQ 152
Cdd:PRK11886 142 PAQAMG-LSLVVGIAIAEaLRRLGAIDVGLKWPNDIYLNDRKLAGILVElsgeTGDAAHVVIGIGINVAMPDFPEEliDQ 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390 153 PITSLEDLGlEQMSRLELISELYVAIQNA-ARWFDHGCYNLAGRFNHHAAWLNQLVQFEHSQGLVHGRFVGISNEGAVIL 231
Cdd:PRK11886 221 PWSDLQEAG-PTIDRNQLAAELIKQLRAAlELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIARGIDEQGALLL 299


                 ..
gi 500622390 232 ET 233
Cdd:PRK11886 300 ED 301
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 28-233 1.57e-31

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: 115.96  E-value: 1.57e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390   28 TTSTNDDIREIAKKGITTGLVCSAQ-QTQGRGQHQRQWISPEGNIYLSTLVQTRTPLDG--RLALEVALNILQIPQLQAL 104
Cdd:TIGR00121   8 IDSTNQYALELAKEGKLKGDLVVAEyQTAGRGRRGRKWLSPEGGLYFSLILRPDLPKSPapGLTLVAGIAIAEVLKELGD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  105 NLQVKWPNDLYSTHGKWGGILVEpLSQH-----QAIVGVGINLKTPPVTDS--DQPITSLEDLGlEQMSRLELISELYVA 177
Cdd:TIGR00121  88 QVQVKWPNDILLKDKKLGGILTE-LTGKenradYVVIGIGINVQNRKPAESlrEQAISLSEEAG-IDLDRGELIEGFLRN 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 500622390  178 IQNAARWF-DHGCYNLAGRFNHHAAWLNQLVQFEHSQGLVHGRFVGISNEGAVILET 233
Cdd:TIGR00121 166 FEENLEWFeQEGIDEILSKWEKLSAHIGREVSLTTGNGEIEGIARGIDKDGALLLED 222
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 28-141 8.07e-13

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: 63.62  E-value: 8.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390   28 TTSTNDDIREIAKKGITTGLVCSAQ-QTQGRGQHQRQWISPEGNIYLSTLVQTRTPLD------------GRLALEVALn 94
Cdd:pfam03099   5 IKSTNTYLEELNSSELESGGVVVVRrQTGGRGRGGNVWHSPKGCLTYSLLLSKEHPNVdpsvlefyvlelVLAVLEALG- 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 500622390   95 iLQIPQLQALNLQVKWPNDLYSTHGKWGGILVEPLSQ---HQAIVGVGIN 141
Cdd:pfam03099  84 -LYKPGISGIPCFVKWPNDLYVNGRKLAGILQRSTRGgtlHHGVIGLGVN 132
 
Name Accession Description Interval E-value
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 26-235 1.22e-54

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: 175.75  E-value: 1.22e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  26 ATTTSTNDDIREIAKKGITTGLVCSA-QQTQGRGQHQRQWISPEG-NIYLSTLVQTRTPLD--GRLALEVALNILQ-IPQ 100
Cdd:COG0340    6 DEVDSTNDEAKELAREGAPEGTVVVAeEQTAGRGRRGRSWVSPPGkGLYFSLLLRPDLPPArlPLLSLAAGLAVAEaLRE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390 101 LQALNLQVKWPNDLYSTHGKWGGILVE----PLSQHQAIVGVGINLKTPPVTDSD--QPITSLEDLGLEQMSRLELISEL 174
Cdd:COG0340   86 LTGVDVGLKWPNDILLNGKKLAGILIEasgeGDGIDWVVIGIGINVNQPPFDPEEldQPATSLKEETGKEVDREELLAAL 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500622390 175 YVAIQNA-ARWFDHGCYNLAGRFNHHAAWLNQLVQFEHSQGLVHGRFVGISNEGAVILETPE 235
Cdd:COG0340  166 LEELEELyDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEGIAVGIDEDGALLLETAD 227
BPL cd16442
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
 22-185 1.22e-35

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: 124.68  E-value: 1.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  22 VLLKATTTSTNDDIREIAKKGITTGLVCSA-QQTQGRGQHQRQWISPEG-NIYLSTLVQTRTPLD--GRLALEVALNILQ 97
Cdd:cd16442    2 LIVLDEIDSTNDEAKELARSGAPEGTVVVAeEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPPAeaPLLTLLAAVAVAE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  98 -IPQLQALNLQVKWPNDLYSTHGKWGGILVE----PLSQHQAIVGVGINLKTPPVTDSDqPITSLEDLGLEQMSRLELIS 172
Cdd:cd16442   82 aLEKLGGIPVQIKWPNDILVNGKKLAGILTEasaeGEGVAAVVIGIGINVNNTPPPEPL-PDTSLATSLGKEVDRNELLE 160

                        170
                 ....*....|...
gi 500622390 173 ELYVAIQNAARWF 185
Cdd:cd16442  161 ELLAALENRLELF 173
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
10-233 3.53e-32

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


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 119.51  E-value: 3.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  10 QLLSAK---NQLPE-VVLLKATTTSTNDDI-REIAkkGITTGLVCSA-QQTQGRGQHQRQWISPEG-NIYLS---TLVQT 79
Cdd:PRK11886  64 DLLDPErisSQLPPgRVTVLPVIDSTNQYLlDRIA--ELKSGDLCLAeYQTAGRGRRGRQWFSPFGgNLYLSlywRLNQG 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  80 RTPLDGrLALEVALNILQ-IPQLQALNLQVKWPNDLYSTHGKWGGILVE----PLSQHQAIVGVGINLKTPPVTDS--DQ 152
Cdd:PRK11886 142 PAQAMG-LSLVVGIAIAEaLRRLGAIDVGLKWPNDIYLNDRKLAGILVElsgeTGDAAHVVIGIGINVAMPDFPEEliDQ 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390 153 PITSLEDLGlEQMSRLELISELYVAIQNA-ARWFDHGCYNLAGRFNHHAAWLNQLVQFEHSQGLVHGRFVGISNEGAVIL 231
Cdd:PRK11886 221 PWSDLQEAG-PTIDRNQLAAELIKQLRAAlELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIARGIDEQGALLL 299


                 ..
gi 500622390 232 ET 233
Cdd:PRK11886 300 ED 301
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 28-233 1.57e-31

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: 115.96  E-value: 1.57e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390   28 TTSTNDDIREIAKKGITTGLVCSAQ-QTQGRGQHQRQWISPEGNIYLSTLVQTRTPLDG--RLALEVALNILQIPQLQAL 104
Cdd:TIGR00121   8 IDSTNQYALELAKEGKLKGDLVVAEyQTAGRGRRGRKWLSPEGGLYFSLILRPDLPKSPapGLTLVAGIAIAEVLKELGD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  105 NLQVKWPNDLYSTHGKWGGILVEpLSQH-----QAIVGVGINLKTPPVTDS--DQPITSLEDLGlEQMSRLELISELYVA 177
Cdd:TIGR00121  88 QVQVKWPNDILLKDKKLGGILTE-LTGKenradYVVIGIGINVQNRKPAESlrEQAISLSEEAG-IDLDRGELIEGFLRN 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 500622390  178 IQNAARWF-DHGCYNLAGRFNHHAAWLNQLVQFEHSQGLVHGRFVGISNEGAVILET 233
Cdd:TIGR00121 166 FEENLEWFeQEGIDEILSKWEKLSAHIGREVSLTTGNGEIEGIARGIDKDGALLLED 222
PTZ00276 PTZ00276
biotin/lipoate protein ligase; Provisional
 29-161 2.21e-20

biotin/lipoate protein ligase; Provisional


Pssm-ID: 140302 [Multi-domain]  Cd Length: 245  Bit Score: 86.84  E-value: 2.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  29 TSTNDDIREI-AKKGITTGLVCSAQQTQGRGQHQRQWISPEGNIYLSTLVQTRT---------PLDGRLALEVAlnILQI 98
Cdd:PTZ00276  16 TSTMDVARTMlAAAGGKPFAVLAESQTAGRGTGGRTWTSPKGNMYFTLCIPQKGvppelvpvlPLITGLACRAA--IMEV 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500622390  99 pqLQALNLQVKWPNDLYSTHGKWGGILVEPLSQHqAIVGVGINLK-TPPVTDSDQPITSL----EDLG 161
Cdd:PTZ00276  94 --LHGAAVHTKWPNDIIYAGKKIGGSLIESEGEY-LIIGIGMNIEvAPPVTDAGRESTMVneiaEDLG 158
PRK08330 PRK08330
biotin--protein ligase; Provisional
 29-235 2.18e-15

biotin--protein ligase; Provisional


Pssm-ID: 169384 [Multi-domain]  Cd Length: 236  Bit Score: 72.85  E-value: 2.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  29 TSTNDDIREIAKKGITTGLVCSAQQTQGRGQHQRQWISPEGNIYLSTLVQTRTPLDG--RLALEVALNILQIPQLQALNL 106
Cdd:PRK08330  12 DSTNEYAKRIAPDEEEGTVIVADRQTAGHGRKGRAWASPEGGLWMSVILKPKVSPEHlpKLVFLGALAVVDTLREFGIEG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390 107 QVKWPNDLYSTHGKWGGILVEpLSQHQAIVGVGINLKTPPVTDSDQPITSL-EDLGLEqmsrLELISELYVAIQNAARWF 185
Cdd:PRK08330  92 KIKWPNDVLVNYKKIAGVLVE-GKGDFVVLGIGLNVNNEIPDELRETATSMkEVLGRE----VPLIEVFKRLVENLDRWY 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 500622390 186 -------DHGCYNLAGRfnhhAAWLNQLVQ-FEHSQGLVHGRFVGISNEGAVILETPE 235
Cdd:PRK08330 167 klflegpGEILEEVKGR----SMILGKRVKiIGDGEILVEGIAEDIDEFGALILRLDD 220
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 28-141 8.07e-13

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: 63.62  E-value: 8.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390   28 TTSTNDDIREIAKKGITTGLVCSAQ-QTQGRGQHQRQWISPEGNIYLSTLVQTRTPLD------------GRLALEVALn 94
Cdd:pfam03099   5 IKSTNTYLEELNSSELESGGVVVVRrQTGGRGRGGNVWHSPKGCLTYSLLLSKEHPNVdpsvlefyvlelVLAVLEALG- 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 500622390   95 iLQIPQLQALNLQVKWPNDLYSTHGKWGGILVEPLSQ---HQAIVGVGIN 141
Cdd:pfam03099  84 -LYKPGISGIPCFVKWPNDLYVNGRKLAGILQRSTRGgtlHHGVIGLGVN 132
BirA COG1654
Biotin operon repressor [Transcription];
7-232 1.94e-12

Biotin operon repressor [Transcription];


Pssm-ID: 441260 [Multi-domain]  Cd Length: 324  Bit Score: 65.78  E-value: 1.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390   7 QLQQLLSAKNQLPEVVLLKATTTSTNDDIREIAKKGITTGLVCSAQQTQGRGQHQRQWISPEG-NIYLSTLVQTRTPLDG 85
Cdd:COG1654   70 EIRAGLSTKRLGREILYVISSTSTNLLALELAAQGGDAGTVVAAEQQRGGRGRRRRSWSSPGGgGLLYSLLLRPPIAPAL 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  86 RLALEVALNILQIPQLQALNLQVKWPNDLYSTHGKWGGILVE------PLSQHQAIVGVGINLKTPPVTDSDQPITSLED 159
Cdd:COG1654  150 LSLLLLAAAVAVAAALAEGGGLVKWKKWPNDLLKKGKKILGIleeeggDADGVVIVVGGGGNNNNSNPEEEPQELAELAT 229

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500622390 160 LGLEQMSRLELISELYVAIQNAARWFDHGCYNLAGRFNHHAAWLNQLVQFEHSQGLVHGRFVGISNEGAVILE 232
Cdd:COG1654  230 SLLLILRLRLLRLLLLLLLLLLELLELLGFLEFFFLWERLDWELLRVLKLVVVVVEIGGGGGGGGALGGGLLG 302
PRK06955 PRK06955
biotin--[acetyl-CoA-carboxylase] ligase;
20-238 2.62e-11

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


Pssm-ID: 235896 [Multi-domain]  Cd Length: 300  Bit Score: 62.11  E-value: 2.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  20 EVVllkATTTSTNDDIREIAKK------GITTGLVCSAQ-QTQGRGQHQRQWISPEGNIYLST--LVQTRTP--LDG-RL 87
Cdd:PRK06955  36 EIV---EETGSTNADLMARLKAlprsadALPAPIVRVAYeQTAGRGRQGRPWFAQPGNALLFSvaCVLPRPVaaLAGlSL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  88 ALEVAL--NILQIPQLQALNLQVKWPNDLYSTHGKWGGILVEPL----SQHQAIVGVGINLKTPPVTDSDQPITSLEDLG 161
Cdd:PRK06955 113 AVGVALaeALAALPAALGQRIALKWPNDLLIAGRKLAGILIETVwatpDATAVVIGIGLNVRRADAVAAEVDALRAREAA 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390 162 L--------EQMSRLEL-ISELYVAIQNA-----ARWFDHGCYNLAGRFNHHAAWLNQLVQFEHsQGLVHGRFV--GISN 225
Cdd:PRK06955 193 LarglppvaLAAACAGAnLTDTLAAALNAlapalQAFGADGLAPFAARWHALHAYAGREVVLLE-DGAELARGVahGIDE 271

                        250
                 ....*....|...
gi 500622390 226 EGAVILETPEPQQ 238
Cdd:PRK06955 272 TGQLLLDTPAGRQ 284
PRK05935 PRK05935
biotin--protein ligase; Provisional
 26-188 4.29e-11

biotin--protein ligase; Provisional


Pssm-ID: 235649 [Multi-domain]  Cd Length: 190  Bit Score: 60.22  E-value: 4.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  26 ATTTSTNddirEIAKKGITT------GLVCSAQQTQGRGQHQRQWISPEGNIYLS-----TLVQTRTPLDGRLALEVALN 94
Cdd:PRK05935   9 AETPSTN----TTAKEGMHLwdpyalTVISTREQTAGKGKFGKSWHSSDQDLLASfcffiTVLNIDVSLLFRLGTEAVMR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  95 ILQipQLQALNLQVKWPNDLYSTHGKWGGILVEPLSQHQ---AIVGVGINLKT--PPVTDSDQPITSLEDL-----GLEQ 164
Cdd:PRK05935  85 LGE--DLGITEAVIKWPNDVLVHGEKLCGVLCETIPVKGglgVILGIGVNGNTtkDELLGIDQPATSLQELlghpiDLEE 162

                        170       180
                 ....*....|....*....|....*....
gi 500622390 165 MsRLELISEL-YVAIQNA----ARWFDHG 188
Cdd:PRK05935 163 Q-RERLIKHIkHVLIQTLpkllARESNHG 190
PRK08477 PRK08477
biotin--[acetyl-CoA-carboxylase] ligase;
30-146 1.33e-09

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


Pssm-ID: 236273 [Multi-domain]  Cd Length: 211  Bit Score: 56.50  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  30 STNDDIREIAKKGITTG--LVCSAQQTQGRGQHQRQWISPEGNIYLS-TLVQTRTPLDgrLALEVA---LNILQIPQLQA 103
Cdd:PRK08477  11 STQTYLIEKIKNGELKApfAIVAKEQTAGIGSRGNSWEGKKGNLFFSfALKESDLPKD--LPLQSSsiyFGFLLKEVLKE 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 500622390 104 LNLQV--KWPNDLYSTHGKWGGILVEpLSQHQAIVGVGINLKTPP 146
Cdd:PRK08477  89 LGSKVwlKWPNDLYLDDKKIGGVITN-KIKNFIVCGIGLNLKFSP 132
PRK13325 PRK13325
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase;
24-238 4.13e-09

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


Pssm-ID: 183976 [Multi-domain]  Cd Length: 592  Bit Score: 56.26  E-value: 4.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  24 LKATTTSTNDDIREIAKKGITTG--LVCSAQ-QTQGRGQHQRQWISPEGNIYLSTL--VQTRTPLD-GRLALEVALNILQ 97
Cdd:PRK13325  86 LKHECASSNDEILELARIAPDKAhkTICVTHlQSKGRGRQGRKWSHRLGECLMFSFgwVFDRPQYElGSLSPVAAVACRR 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390  98 IPQLQALNLQVKWPNDLYSTHGKWGGILVEPL---SQHQAIVGVGINLKTPPVTDSDQPITSLedlgLEQMSR------- 167
Cdd:PRK13325 166 ALSRLGLKTQIKWPNDLVVGRDKLGGILIETVrtgGKTVAVVGIGINFVLPKEVENAASVQSL----FQTASRrgnadaa 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622390 168 --LE-LISELYVAIQNAArwfDHGC------YNLAGRFNHHAAWLnqlvqFEHSQGLVHGRFVGISNEGAVILETPEPQQ 238
Cdd:PRK13325 242 vlLEtLLAELDAVLLQYA---RDGFapfvaeYQAANRDHGKAVLL-----LRDGETVFEGTVKGVDGQGVLHLETAEGKQ 313
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
 203-238 3.82e-03

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: 34.36  E-value: 3.82e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 500622390  203 LNQLVQFEHSQGLVHGRFVGISNEGAVILETPEPQQ 238
Cdd:pfam02237   2 LGREVRVLLGDGIVEGIAVGIDDDGALLLETDDGTI 37
 
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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