|
Name |
Accession |
Description |
Interval |
E-value |
| BPL |
cd16442 |
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ... |
463-643 |
2.08e-36 |
|
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: 134.70 E-value: 2.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 463 KVILFAEVTSTtMSLLDGLMFEMPQEmGLIAIAVRQTQGKGRGPNAWLSPVGCALSTLLVFIPlrSQLGQRIPFVQHLMS 542
Cdd:cd16442 1 KLIVLDEIDST-NDEAKELARSGAPE-GTVVVAEEQTAGRGRRGRKWESPKGKGLYFSLLLRP--DVPPAEAPLLTLLAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 543 LAVVEAVRSIPGyedINLRVKWPNDIYYSDlMKIGGVLVNSTLMGET-FYILIGCGFNVTNSNPTICINDLIEEHNKQHG 621
Cdd:cd16442 77 VAVAEALEKLGG---IPVQIKWPNDILVNG-KKLAGILTEASAEGEGvAAVVIGIGINVNNTPPPEPLPDTSLATSLGKE 152
|
170 180
....*....|....*....|..
gi 1720386295 622 AGLKPLRADcLIARAVTVLEKL 643
Cdd:cd16442 153 VDRNELLEE-LLAALENRLELF 173
|
|
| BPL_C |
pfam02237 |
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ... |
665-712 |
5.47e-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: 40.91 E-value: 5.47e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1720386295 665 HGGQQVRLGSTEGP-QASIVGLDDSGFLQVHQEDGGvvtvHPDGNSFDM 712
Cdd:pfam02237 1 TLGREVRVLLGDGIvEGIAVGIDDDGALLLETDDGT----IRDINSGEV 45
|
|
| BPL_N super family |
cl48072 |
Biotin-protein ligase, N terminal; The function of this structural domain is unknown. It is ... |
162-384 |
8.23e-05 |
|
Biotin-protein ligase, N terminal; The function of this structural domain is unknown. It is found to the N terminus of the biotin protein ligase (BPL) catalytic domain. This domain is essential in BPL activity.
The actual alignment was detected with superfamily member pfam09825:
Pssm-ID: 462915 Cd Length: 277 Bit Score: 45.20 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 162 NILLYVGSG-SEEAlgrlqqVRSVLtdcvdtdsYTLYHLL----------EDSALRDPWSDNCLLLVI-ASRD-PIPKDI 228
Cdd:pfam09825 2 NVLVYSGPGtTPES------VRHTL--------ETLRRLLspyyavipvsAKVLLKEPWTSKCALLVFpGGADlPYCREL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 229 Q----HKFMAYLSQGGKVLGlsspFTLGG--------FRV--TRRDVLRN--------TVQNLVF------SKADGTEVR 280
Cdd:pfam09825 68 NgegnRRIKQFVRRGGAYLG----FCAGGyygsarceFEVgdPKLEVVGPrelaffpgTCRGPAFpgfvynSEAGARAAK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 281 LSVLSSG-----YVYEEGpslGrlqGHLENEDKDKMI---------VHVPFGTLGGEA-VLCQV----------HLELPP 335
Cdd:pfam09825 144 LKVNTSPvpdefKSYYNG---G---GVFVDADKYANVevlarytedLDVDGGDGGPAAvVYCKVgkgkalltgpHPEFAP 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720386295 336 GASLVQTADDFN------VLKSSNVRRHEVLKEILTALGLSC---DAPQVPALTPLYL 384
Cdd:pfam09825 218 SNLKPQEADGPGydkvvdELAADEKARLEFLRACLTKLGLKVneeEETTVPSLTPLHL 275
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BPL |
cd16442 |
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ... |
463-643 |
2.08e-36 |
|
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: 134.70 E-value: 2.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 463 KVILFAEVTSTtMSLLDGLMFEMPQEmGLIAIAVRQTQGKGRGPNAWLSPVGCALSTLLVFIPlrSQLGQRIPFVQHLMS 542
Cdd:cd16442 1 KLIVLDEIDST-NDEAKELARSGAPE-GTVVVAEEQTAGRGRRGRKWESPKGKGLYFSLLLRP--DVPPAEAPLLTLLAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 543 LAVVEAVRSIPGyedINLRVKWPNDIYYSDlMKIGGVLVNSTLMGET-FYILIGCGFNVTNSNPTICINDLIEEHNKQHG 621
Cdd:cd16442 77 VAVAEALEKLGG---IPVQIKWPNDILVNG-KKLAGILTEASAEGEGvAAVVIGIGINVNNTPPPEPLPDTSLATSLGKE 152
|
170 180
....*....|....*....|..
gi 1720386295 622 AGLKPLRADcLIARAVTVLEKL 643
Cdd:cd16442 153 VDRNELLEE-LLAALENRLELF 173
|
|
| BPL_LplA_LipB |
pfam03099 |
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ... |
467-599 |
4.45e-35 |
|
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: 129.48 E-value: 4.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 467 FAEVTSTTMSLLDGLMFEmPQEMGLIAIAVRQTQGKGRGPNAWLSPVGCALSTLLVFIPLRSQLGQRIPFVQHLMSLAVV 546
Cdd:pfam03099 1 LGERIKSTNTYLEELNSS-ELESGGVVVVRRQTGGRGRGGNVWHSPKGCLTYSLLLSKEHPNVDPSVLEFYVLELVLAVL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1720386295 547 EAVR-SIPGYEDINLRVKWPNDIYYSDlMKIGGVLVNSTLMGETFYILIGCGFN 599
Cdd:pfam03099 80 EALGlYKPGISGIPCFVKWPNDLYVNG-RKLAGILQRSTRGGTLHHGVIGLGVN 132
|
|
| BirA2 |
COG0340 |
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ... |
463-704 |
2.21e-34 |
|
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: 131.45 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 463 KVILFAEVTSTtMSLLDGLMFEMPQEmGLIAIAVRQTQGKGRGPNAWLSPVGCAL--STLLVF-IPLrsqlgQRIPFVQH 539
Cdd:COG0340 1 RIEVFDEVDST-NDEAKELAREGAPE-GTVVVAEEQTAGRGRRGRSWVSPPGKGLyfSLLLRPdLPP-----ARLPLLSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 540 LMSLAVVEAVRSIPGyedINLRVKWPNDIYYSDLmKIGGVLV-NSTLMGETFYILIGCGFNVTNSnpticinDLIEEHNK 618
Cdd:COG0340 74 AAGLAVAEALRELTG---VDVGLKWPNDILLNGK-KLAGILIeASGEGDGIDWVVIGIGINVNQP-------PFDPEELD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 619 QHGAGLK-----PLRADCLIARAVTVLEKLIDRFQDQGPDGVLPLYYKYWVHGGQQVRLGSTEGP-QASIVGLDDSGFLQ 692
Cdd:COG0340 143 QPATSLKeetgkEVDREELLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETlEGIAVGIDEDGALL 222
|
250
....*....|..
gi 1720386295 693 VHQEDGGVVTVH 704
Cdd:COG0340 223 LETADGEIRAVA 234
|
|
| birA_ligase |
TIGR00121 |
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ... |
463-699 |
8.42e-23 |
|
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: 97.86 E-value: 8.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 463 KVILFAEVTSTTMSLLDglMFEMPQEMGLIAIAVRQTQGKGRGPNAWLSPVGcalsTLLVFIPLRSQLG-QRIPFVQHLM 541
Cdd:TIGR00121 1 EVIVLDVIDSTNQYALE--LAKEGKLKGDLVVAEYQTAGRGRRGRKWLSPEG----GLYFSLILRPDLPkSPAPGLTLVA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 542 SLAVVEAVRSipgyEDINLRVKWPNDIYYSDlMKIGGVLVNSTLMGETF-YILIGCGFNVTNSNPTiciNDLIEEHNKQH 620
Cdd:TIGR00121 75 GIAIAEVLKE----LGDQVQVKWPNDILLKD-KKLGGILTELTGKENRAdYVVIGIGINVQNRKPA---ESLREQAISLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 621 GAGLKPLRADCLIARAVTVLEKLIDRFQDQGPDGVLPLYYKYWVHGGQQVRL----GSTEGPQASIvglDDSGFLQVhqE 696
Cdd:TIGR00121 147 EEAGIDLDRGELIEGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSLttgnGEIEGIARGI---DKDGALLL--E 221
|
...
gi 1720386295 697 DGG 699
Cdd:TIGR00121 222 DGG 224
|
|
| PRK11886 |
PRK11886 |
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA; |
461-700 |
4.20e-18 |
|
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
Pssm-ID: 237010 [Multi-domain] Cd Length: 319 Bit Score: 85.99 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 461 LGKVILFAEVTSTTMSLLDGLMfemPQEMGLIAIAVRQTQGKGRGPNAWLSPVGCAL--STLLVFiplrsqlgqRIPFVQ 538
Cdd:PRK11886 77 PGRVTVLPVIDSTNQYLLDRIA---ELKSGDLCLAEYQTAGRGRRGRQWFSPFGGNLylSLYWRL---------NQGPAQ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 539 hLMSL------AVVEAVRSIpGYEDInlRVKWPNDIYYSDLmKIGGVLVNstLMGET---FYILIGCGFNVT-NSNPTIC 608
Cdd:PRK11886 145 -AMGLslvvgiAIAEALRRL-GAIDV--GLKWPNDIYLNDR-KLAGILVE--LSGETgdaAHVVIGIGINVAmPDFPEEL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 609 IN----DLIEEhnkqhgaGLKPLRADcLIARAVTVLEKLIDRFQDQGPDGVLPLYYKYWVHGGQQVRLgsTEGPQA--SI 682
Cdd:PRK11886 218 IDqpwsDLQEA-------GPTIDRNQ-LAAELIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKL--IIGDKEisGI 287
|
250
....*....|....*....
gi 1720386295 683 V-GLDDSGFLQVhQEDGGV 700
Cdd:PRK11886 288 ArGIDEQGALLL-EDDGVE 305
|
|
| BPL_C |
pfam02237 |
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ... |
665-712 |
5.47e-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: 40.91 E-value: 5.47e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1720386295 665 HGGQQVRLGSTEGP-QASIVGLDDSGFLQVHQEDGGvvtvHPDGNSFDM 712
Cdd:pfam02237 1 TLGREVRVLLGDGIvEGIAVGIDDDGALLLETDDGT----IRDINSGEV 45
|
|
| BPL_N |
pfam09825 |
Biotin-protein ligase, N terminal; The function of this structural domain is unknown. It is ... |
162-384 |
8.23e-05 |
|
Biotin-protein ligase, N terminal; The function of this structural domain is unknown. It is found to the N terminus of the biotin protein ligase (BPL) catalytic domain. This domain is essential in BPL activity.
Pssm-ID: 462915 Cd Length: 277 Bit Score: 45.20 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 162 NILLYVGSG-SEEAlgrlqqVRSVLtdcvdtdsYTLYHLL----------EDSALRDPWSDNCLLLVI-ASRD-PIPKDI 228
Cdd:pfam09825 2 NVLVYSGPGtTPES------VRHTL--------ETLRRLLspyyavipvsAKVLLKEPWTSKCALLVFpGGADlPYCREL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 229 Q----HKFMAYLSQGGKVLGlsspFTLGG--------FRV--TRRDVLRN--------TVQNLVF------SKADGTEVR 280
Cdd:pfam09825 68 NgegnRRIKQFVRRGGAYLG----FCAGGyygsarceFEVgdPKLEVVGPrelaffpgTCRGPAFpgfvynSEAGARAAK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 281 LSVLSSG-----YVYEEGpslGrlqGHLENEDKDKMI---------VHVPFGTLGGEA-VLCQV----------HLELPP 335
Cdd:pfam09825 144 LKVNTSPvpdefKSYYNG---G---GVFVDADKYANVevlarytedLDVDGGDGGPAAvVYCKVgkgkalltgpHPEFAP 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720386295 336 GASLVQTADDFN------VLKSSNVRRHEVLKEILTALGLSC---DAPQVPALTPLYL 384
Cdd:pfam09825 218 SNLKPQEADGPGydkvvdELAADEKARLEFLRACLTKLGLKVneeEETTVPSLTPLHL 275
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BPL |
cd16442 |
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ... |
463-643 |
2.08e-36 |
|
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: 134.70 E-value: 2.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 463 KVILFAEVTSTtMSLLDGLMFEMPQEmGLIAIAVRQTQGKGRGPNAWLSPVGCALSTLLVFIPlrSQLGQRIPFVQHLMS 542
Cdd:cd16442 1 KLIVLDEIDST-NDEAKELARSGAPE-GTVVVAEEQTAGRGRRGRKWESPKGKGLYFSLLLRP--DVPPAEAPLLTLLAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 543 LAVVEAVRSIPGyedINLRVKWPNDIYYSDlMKIGGVLVNSTLMGET-FYILIGCGFNVTNSNPTICINDLIEEHNKQHG 621
Cdd:cd16442 77 VAVAEALEKLGG---IPVQIKWPNDILVNG-KKLAGILTEASAEGEGvAAVVIGIGINVNNTPPPEPLPDTSLATSLGKE 152
|
170 180
....*....|....*....|..
gi 1720386295 622 AGLKPLRADcLIARAVTVLEKL 643
Cdd:cd16442 153 VDRNELLEE-LLAALENRLELF 173
|
|
| BPL_LplA_LipB |
pfam03099 |
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ... |
467-599 |
4.45e-35 |
|
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: 129.48 E-value: 4.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 467 FAEVTSTTMSLLDGLMFEmPQEMGLIAIAVRQTQGKGRGPNAWLSPVGCALSTLLVFIPLRSQLGQRIPFVQHLMSLAVV 546
Cdd:pfam03099 1 LGERIKSTNTYLEELNSS-ELESGGVVVVRRQTGGRGRGGNVWHSPKGCLTYSLLLSKEHPNVDPSVLEFYVLELVLAVL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1720386295 547 EAVR-SIPGYEDINLRVKWPNDIYYSDlMKIGGVLVNSTLMGETFYILIGCGFN 599
Cdd:pfam03099 80 EALGlYKPGISGIPCFVKWPNDLYVNG-RKLAGILQRSTRGGTLHHGVIGLGVN 132
|
|
| BirA2 |
COG0340 |
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ... |
463-704 |
2.21e-34 |
|
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: 131.45 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 463 KVILFAEVTSTtMSLLDGLMFEMPQEmGLIAIAVRQTQGKGRGPNAWLSPVGCAL--STLLVF-IPLrsqlgQRIPFVQH 539
Cdd:COG0340 1 RIEVFDEVDST-NDEAKELAREGAPE-GTVVVAEEQTAGRGRRGRSWVSPPGKGLyfSLLLRPdLPP-----ARLPLLSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 540 LMSLAVVEAVRSIPGyedINLRVKWPNDIYYSDLmKIGGVLV-NSTLMGETFYILIGCGFNVTNSnpticinDLIEEHNK 618
Cdd:COG0340 74 AAGLAVAEALRELTG---VDVGLKWPNDILLNGK-KLAGILIeASGEGDGIDWVVIGIGINVNQP-------PFDPEELD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 619 QHGAGLK-----PLRADCLIARAVTVLEKLIDRFQDQGPDGVLPLYYKYWVHGGQQVRLGSTEGP-QASIVGLDDSGFLQ 692
Cdd:COG0340 143 QPATSLKeetgkEVDREELLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETlEGIAVGIDEDGALL 222
|
250
....*....|..
gi 1720386295 693 VHQEDGGVVTVH 704
Cdd:COG0340 223 LETADGEIRAVA 234
|
|
| birA_ligase |
TIGR00121 |
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ... |
463-699 |
8.42e-23 |
|
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: 97.86 E-value: 8.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 463 KVILFAEVTSTTMSLLDglMFEMPQEMGLIAIAVRQTQGKGRGPNAWLSPVGcalsTLLVFIPLRSQLG-QRIPFVQHLM 541
Cdd:TIGR00121 1 EVIVLDVIDSTNQYALE--LAKEGKLKGDLVVAEYQTAGRGRRGRKWLSPEG----GLYFSLILRPDLPkSPAPGLTLVA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 542 SLAVVEAVRSipgyEDINLRVKWPNDIYYSDlMKIGGVLVNSTLMGETF-YILIGCGFNVTNSNPTiciNDLIEEHNKQH 620
Cdd:TIGR00121 75 GIAIAEVLKE----LGDQVQVKWPNDILLKD-KKLGGILTELTGKENRAdYVVIGIGINVQNRKPA---ESLREQAISLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 621 GAGLKPLRADCLIARAVTVLEKLIDRFQDQGPDGVLPLYYKYWVHGGQQVRL----GSTEGPQASIvglDDSGFLQVhqE 696
Cdd:TIGR00121 147 EEAGIDLDRGELIEGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSLttgnGEIEGIARGI---DKDGALLL--E 221
|
...
gi 1720386295 697 DGG 699
Cdd:TIGR00121 222 DGG 224
|
|
| PRK11886 |
PRK11886 |
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA; |
461-700 |
4.20e-18 |
|
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
Pssm-ID: 237010 [Multi-domain] Cd Length: 319 Bit Score: 85.99 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 461 LGKVILFAEVTSTTMSLLDGLMfemPQEMGLIAIAVRQTQGKGRGPNAWLSPVGCAL--STLLVFiplrsqlgqRIPFVQ 538
Cdd:PRK11886 77 PGRVTVLPVIDSTNQYLLDRIA---ELKSGDLCLAEYQTAGRGRRGRQWFSPFGGNLylSLYWRL---------NQGPAQ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 539 hLMSL------AVVEAVRSIpGYEDInlRVKWPNDIYYSDLmKIGGVLVNstLMGET---FYILIGCGFNVT-NSNPTIC 608
Cdd:PRK11886 145 -AMGLslvvgiAIAEALRRL-GAIDV--GLKWPNDIYLNDR-KLAGILVE--LSGETgdaAHVVIGIGINVAmPDFPEEL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 609 IN----DLIEEhnkqhgaGLKPLRADcLIARAVTVLEKLIDRFQDQGPDGVLPLYYKYWVHGGQQVRLgsTEGPQA--SI 682
Cdd:PRK11886 218 IDqpwsDLQEA-------GPTIDRNQ-LAAELIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKL--IIGDKEisGI 287
|
250
....*....|....*....
gi 1720386295 683 V-GLDDSGFLQVhQEDGGV 700
Cdd:PRK11886 288 ArGIDEQGALLL-EDDGVE 305
|
|
| PRK08330 |
PRK08330 |
biotin--protein ligase; Provisional |
463-605 |
1.33e-12 |
|
biotin--protein ligase; Provisional
Pssm-ID: 169384 [Multi-domain] Cd Length: 236 Bit Score: 67.85 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 463 KVILFAEVTSTTMSLLDGLMFEmpqEMGLIAIAVRQTQGKGRGPNAWLSPVGcALSTLLVFIPLRSQlgQRIPFVQHLMS 542
Cdd:PRK08330 4 NIIYFDEVDSTNEYAKRIAPDE---EEGTVIVADRQTAGHGRKGRAWASPEG-GLWMSVILKPKVSP--EHLPKLVFLGA 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720386295 543 LAVVEAVRSIpgyeDINLRVKWPNDIYYsDLMKIGGVLVNstlmGETFYILIGCGFNVTNSNP 605
Cdd:PRK08330 78 LAVVDTLREF----GIEGKIKWPNDVLV-NYKKIAGVLVE----GKGDFVVLGIGLNVNNEIP 131
|
|
| PTZ00276 |
PTZ00276 |
biotin/lipoate protein ligase; Provisional |
463-600 |
1.29e-09 |
|
biotin/lipoate protein ligase; Provisional
Pssm-ID: 140302 [Multi-domain] Cd Length: 245 Bit Score: 59.49 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 463 KVILFAEVTSTtmslLDgLMFEMPQEMGLIAIAV---RQTQGKGRGPNAWLSPVGCALSTLLvfIPLRSQLGQRIPFVQH 539
Cdd:PTZ00276 8 NIHFVGEVTST----MD-VARTMLAAAGGKPFAVlaeSQTAGRGTGGRTWTSPKGNMYFTLC--IPQKGVPPELVPVLPL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720386295 540 LMSLAVVEAVRSIpgYEDINLRVKWPNDIYYsDLMKIGGVLVNSTlmGEtfYILIGCGFNV 600
Cdd:PTZ00276 81 ITGLACRAAIMEV--LHGAAVHTKWPNDIIY-AGKKIGGSLIESE--GE--YLIIGIGMNI 134
|
|
| PRK06955 |
PRK06955 |
biotin--[acetyl-CoA-carboxylase] ligase; |
491-698 |
2.95e-07 |
|
biotin--[acetyl-CoA-carboxylase] ligase;
Pssm-ID: 235896 [Multi-domain] Cd Length: 300 Bit Score: 52.86 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 491 LIAIAVRQTQGKGRGPNAWLSPVGCAL--STLLVFIPLRSQLGQripfvqhlMSLAV----VEAVRSIPGYEDINLRVKW 564
Cdd:PRK06955 66 IVRVAYEQTAGRGRQGRPWFAQPGNALlfSVACVLPRPVAALAG--------LSLAVgvalAEALAALPAALGQRIALKW 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 565 PNDIYYSDlMKIGGVLVNSTLMG-ETFYILIGCGFNVTNSNPTICINDLIEEHNKQHGAGLKP--LRADC-------LIA 634
Cdd:PRK06955 138 PNDLLIAG-RKLAGILIETVWATpDATAVVIGIGLNVRRADAVAAEVDALRAREAALARGLPPvaLAAACaganltdTLA 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720386295 635 RAVTVLEKLIDRFQDQGPDGVLPLYYKYWVHGGQQVRL--GSTEGPQASIVGLDDSGFLQVHQEDG 698
Cdd:PRK06955 217 AALNALAPALQAFGADGLAPFAARWHALHAYAGREVVLleDGAELARGVAHGIDETGQLLLDTPAG 282
|
|
| BPL_C |
pfam02237 |
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ... |
665-712 |
5.47e-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: 40.91 E-value: 5.47e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1720386295 665 HGGQQVRLGSTEGP-QASIVGLDDSGFLQVHQEDGGvvtvHPDGNSFDM 712
Cdd:pfam02237 1 TLGREVRVLLGDGIvEGIAVGIDDDGALLLETDDGT----IRDINSGEV 45
|
|
| BPL_N |
pfam09825 |
Biotin-protein ligase, N terminal; The function of this structural domain is unknown. It is ... |
162-384 |
8.23e-05 |
|
Biotin-protein ligase, N terminal; The function of this structural domain is unknown. It is found to the N terminus of the biotin protein ligase (BPL) catalytic domain. This domain is essential in BPL activity.
Pssm-ID: 462915 Cd Length: 277 Bit Score: 45.20 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 162 NILLYVGSG-SEEAlgrlqqVRSVLtdcvdtdsYTLYHLL----------EDSALRDPWSDNCLLLVI-ASRD-PIPKDI 228
Cdd:pfam09825 2 NVLVYSGPGtTPES------VRHTL--------ETLRRLLspyyavipvsAKVLLKEPWTSKCALLVFpGGADlPYCREL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 229 Q----HKFMAYLSQGGKVLGlsspFTLGG--------FRV--TRRDVLRN--------TVQNLVF------SKADGTEVR 280
Cdd:pfam09825 68 NgegnRRIKQFVRRGGAYLG----FCAGGyygsarceFEVgdPKLEVVGPrelaffpgTCRGPAFpgfvynSEAGARAAK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 281 LSVLSSG-----YVYEEGpslGrlqGHLENEDKDKMI---------VHVPFGTLGGEA-VLCQV----------HLELPP 335
Cdd:pfam09825 144 LKVNTSPvpdefKSYYNG---G---GVFVDADKYANVevlarytedLDVDGGDGGPAAvVYCKVgkgkalltgpHPEFAP 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720386295 336 GASLVQTADDFN------VLKSSNVRRHEVLKEILTALGLSC---DAPQVPALTPLYL 384
Cdd:pfam09825 218 SNLKPQEADGPGydkvvdELAADEKARLEFLRACLTKLGLKVneeEETTVPSLTPLHL 275
|
|
| PRK05935 |
PRK05935 |
biotin--protein ligase; Provisional |
463-599 |
1.92e-03 |
|
biotin--protein ligase; Provisional
Pssm-ID: 235649 [Multi-domain] Cd Length: 190 Bit Score: 40.19 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 463 KVILF--AEVTSTTMSLLDGLMFEMPQEMGLIAIAvRQTQGKGRGPNAWLSPVGCALSTLLVFIplrSQLGQRIPFVQHL 540
Cdd:PRK05935 2 KVIYYeiAETPSTNTTAKEGMHLWDPYALTVISTR-EQTAGKGKFGKSWHSSDQDLLASFCFFI---TVLNIDVSLLFRL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720386295 541 MSLAVVEAVRS--IPgyediNLRVKWPNDIYYSDlMKIGGVLVNSTLMGETFYILIGCGFN 599
Cdd:PRK05935 78 GTEAVMRLGEDlgIT-----EAVIKWPNDVLVHG-EKLCGVLCETIPVKGGLGVILGIGVN 132
|
|
| PRK13325 |
PRK13325 |
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase; |
492-721 |
2.45e-03 |
|
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase;
Pssm-ID: 183976 [Multi-domain] Cd Length: 592 Bit Score: 41.23 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 492 IAIAVRQTQGKGRGPNAWLSPVG-CALSTL-LVFIPLRSQLGQripfvqhlMSLAVVEAVRSIPGYEDINLRVKWPNDIY 569
Cdd:PRK13325 112 ICVTHLQSKGRGRQGRKWSHRLGeCLMFSFgWVFDRPQYELGS--------LSPVAAVACRRALSRLGLKTQIKWPNDLV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 570 YSDlMKIGGVLVNSTLMGETFYILIGCGFNVT---NSNPTICINDLIEEHNKQHGAGLKPLrADCLIARAVTVLEKLIDr 646
Cdd:PRK13325 184 VGR-DKLGGILIETVRTGGKTVAVVGIGINFVlpkEVENAASVQSLFQTASRRGNADAAVL-LETLLAELDAVLLQYAR- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720386295 647 fqdqgpDGVLPLYYKYWV----HGGQQVRLGSTEGP-QASIVGLDDSGFLQVHQEDG------GVVTVHPDGnsfdmlRN 715
Cdd:PRK13325 261 ------DGFAPFVAEYQAanrdHGKAVLLLRDGETVfEGTVKGVDGQGVLHLETAEGkqtvvsGEISLRSDD------RP 328
|
....*.
gi 1720386295 716 LIVPKR 721
Cdd:PRK13325 329 VSVPKR 334
|
|
| PRK08477 |
PRK08477 |
biotin--[acetyl-CoA-carboxylase] ligase; |
562-604 |
3.84e-03 |
|
biotin--[acetyl-CoA-carboxylase] ligase;
Pssm-ID: 236273 [Multi-domain] Cd Length: 211 Bit Score: 39.17 E-value: 3.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1720386295 562 VKWPNDIYYSDLmKIGGVLVNstLMGEtfYILIGCGFNVTNSN 604
Cdd:PRK08477 95 LKWPNDLYLDDK-KIGGVITN--KIKN--FIVCGIGLNLKFSP 132
|
|
| |
