|
Name |
Accession |
Description |
Interval |
E-value |
| BirA2 |
COG0340 |
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ... |
87-326 |
2.07e-97 |
|
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: 287.84 E-value: 2.07e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 87 RIVSYRTLGSTNEVAKQLADSGAPEGTLIVAEEQTKGRGRLGRSWHSPPKCGLYFTLILRPPIPPAKAPALSICAALAVV 166
Cdd:COG0340 1 RIEVFDEVDSTNDEAKELAREGAPEGTVVVAEEQTAGRGRRGRSWVSPPGKGLYFSLLLRPDLPPARLPLLSLAAGLAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 167 DSLGELFGIQLSTKWPNDVLINRKKVCGILTELVTRGNGVDSVIVGVGMNVNNRREDfPKDLRKTATSLAVELGEEVSRL 246
Cdd:COG0340 81 EALRELTGVDVGLKWPNDILLNGKKLAGILIEASGEGDGIDWVVIGIGINVNQPPFD-PEELDQPATSLKEETGKEVDRE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 247 GVLKRFLLEFERDYLQFSKSGLAPFRNHYRECSVGLGRSVKIRCGGKLLSGIAEDIDEEGSLILKK--GRRRLFLpGGEI 324
Cdd:COG0340 160 ELLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEGIAVGIDEDGALLLETadGEIRAVA-AGEV 238
|
..
gi 931359025 325 TH 326
Cdd:COG0340 239 SL 240
|
|
| BPL |
cd16442 |
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ... |
87-263 |
3.28e-68 |
|
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: 210.97 E-value: 3.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 87 RIVSYRTLGSTNEVAKQLADSGAPEGTLIVAEEQTKGRGRLGRSWHSPPKCGLYFTLILRPPIPPAKAPALSICAALAVV 166
Cdd:cd16442 1 KLIVLDEIDSTNDEAKELARSGAPEGTVVVAEEQTAGRGRRGRKWESPKGKGLYFSLLLRPDVPPAEAPLLTLLAAVAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 167 DSLGELFGIQLSTKWPNDVLINRKKVCGILTELVTRGNGVDSVIVGVGMNVNNRREDFPKDLrktaTSLAVELGEEVSRL 246
Cdd:cd16442 81 EALEKLGGIPVQIKWPNDILVNGKKLAGILTEASAEGEGVAAVVIGIGINVNNTPPPEPLPD----TSLATSLGKEVDRN 156
|
170
....*....|....*..
gi 931359025 247 GVLKRFLLEFERDYLQF 263
Cdd:cd16442 157 ELLEELLAALENRLELF 173
|
|
| birA_ligase |
TIGR00121 |
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ... |
94-326 |
3.93e-67 |
|
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: 210.72 E-value: 3.93e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 94 LGSTNEVAKQLADSGAPEGTLIVAEEQTKGRGRLGRSWHSPPKcGLYFTLILRPPIPPAKAPALSICAALAVVDSLGELf 173
Cdd:TIGR00121 8 IDSTNQYALELAKEGKLKGDLVVAEYQTAGRGRRGRKWLSPEG-GLYFSLILRPDLPKSPAPGLTLVAGIAIAEVLKEL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 174 GIQLSTKWPNDVLINRKKVCGILTELVTRGNGVDSVIVGVGMNVNNRRedFPKDLRKTATSLAVELGEEVSRLGVLKRFL 253
Cdd:TIGR00121 86 GDQVQVKWPNDILLKDKKLGGILTELTGKENRADYVVIGIGINVQNRK--PAESLREQAISLSEEAGIDLDRGELIEGFL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931359025 254 LEFERDYLQFSKSGLAPFRNHYRECSVGLGRSVKIRCGGKLLSGIAEDIDEEGSLILKKGRRRLFLPGGEITH 326
Cdd:TIGR00121 164 RNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSLTTGNGEIEGIARGIDKDGALLLEDGGGIKKIISGEISL 236
|
|
| PRK11886 |
PRK11886 |
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA; |
10-324 |
4.76e-65 |
|
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
Pssm-ID: 237010 [Multi-domain] Cd Length: 319 Bit Score: 207.72 E-value: 4.76e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 10 EILTLLrrSPGEYVSGRFLAESLDLKRESIYHTISQLRQFGYGIESDRRLGYRYRTAPDLLIASEIREGLKTKlfakRIV 89
Cdd:PRK11886 8 QLLSLL--ADGDFHSGEQLGEELGISRAAIWKHIQTLEEWGLDIFSVKGKGYRLAEPLDLLDPERISSQLPPG----RVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 90 SYRTLGSTNEVAKQLAdSGAPEGTLIVAEEQTKGRGRLGRSWHSPPKCGLYFTLILRPPIPPAKAPALSICAALAVVDSL 169
Cdd:PRK11886 82 VLPVIDSTNQYLLDRI-AELKSGDLCLAEYQTAGRGRRGRQWFSPFGGNLYLSLYWRLNQGPAQAMGLSLVVGIAIAEAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 170 GELFGIQLSTKWPNDVLINRKKVCGILTELVTRGNGVDSVIVGVGMNVNNRreDFPKDLRKTATSLAVELGEEVSRLGVL 249
Cdd:PRK11886 161 RRLGAIDVGLKWPNDIYLNDRKLAGILVELSGETGDAAHVVIGIGINVAMP--DFPEELIDQPWSDLQEAGPTIDRNQLA 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931359025 250 KRFLLEFERDYLQFSKSGLAPFRNHYRECSVGLGRSVKIRCGGKLLSGIAEDIDEEGSLILKK-GRRRLFLpGGEI 324
Cdd:PRK11886 239 AELIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIARGIDEQGALLLEDdGVEKPFN-GGEI 313
|
|
| BPL_LplA_LipB |
pfam03099 |
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ... |
96-216 |
5.42e-21 |
|
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: 87.11 E-value: 5.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 96 STNEVAKQLADSGAPEGTLIVAEEQTKGRGRLGRSWHSPPKCgLYFTLILRPPIPPAKAPALSI---CAALAVVDSLG-- 170
Cdd:pfam03099 7 STNTYLEELNSSELESGGVVVVRRQTGGRGRGGNVWHSPKGC-LTYSLLLSKEHPNVDPSVLEFyvlELVLAVLEALGly 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 931359025 171 --ELFGIQLSTKWPNDVLINRKKVCGILTElVTRGNGVDSVIVGVGMN 216
Cdd:pfam03099 86 kpGISGIPCFVKWPNDLYVNGRKLAGILQR-STRGGTLHHGVIGLGVN 132
|
|
| HTH_11 |
pfam08279 |
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins. |
11-61 |
8.23e-06 |
|
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: 42.42 E-value: 8.23e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 931359025 11 ILTLLRRSPgEYVSGRFLAESLDLKRESIYHTISQLRQFGYGIESDRRLGY 61
Cdd:pfam08279 3 ILQLLLEAR-GPISGQELAEKLGVSRRTIRRDIKILEELGVPIEAEPGRGY 52
|
|
| NiaR |
COG1827 |
Transcriptional regulator of NAD metabolism, contains HTH and 3H domains [Transcription, ... |
5-81 |
2.13e-03 |
|
Transcriptional regulator of NAD metabolism, contains HTH and 3H domains [Transcription, Coenzyme transport and metabolism];
Pssm-ID: 441432 [Multi-domain] Cd Length: 171 Bit Score: 38.19 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 5 SEHRDEILTLLRRSPgEYVSGRFLAESLDLKRESIYHTISQLRQFGYGIESDRRlGYRYRTAPDL-----LIA-----SE 74
Cdd:COG1827 4 EERREKILEILKESK-EPISGSELAKKFGVSRQVIVQDIALLRAKGEPIIATPR-GYILLKAESSkgftrVIAckhtpEE 81
|
....*..
gi 931359025 75 IREGLKT 81
Cdd:COG1827 82 IEEELNT 88
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| BirA2 |
COG0340 |
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ... |
87-326 |
2.07e-97 |
|
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: 287.84 E-value: 2.07e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 87 RIVSYRTLGSTNEVAKQLADSGAPEGTLIVAEEQTKGRGRLGRSWHSPPKCGLYFTLILRPPIPPAKAPALSICAALAVV 166
Cdd:COG0340 1 RIEVFDEVDSTNDEAKELAREGAPEGTVVVAEEQTAGRGRRGRSWVSPPGKGLYFSLLLRPDLPPARLPLLSLAAGLAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 167 DSLGELFGIQLSTKWPNDVLINRKKVCGILTELVTRGNGVDSVIVGVGMNVNNRREDfPKDLRKTATSLAVELGEEVSRL 246
Cdd:COG0340 81 EALRELTGVDVGLKWPNDILLNGKKLAGILIEASGEGDGIDWVVIGIGINVNQPPFD-PEELDQPATSLKEETGKEVDRE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 247 GVLKRFLLEFERDYLQFSKSGLAPFRNHYRECSVGLGRSVKIRCGGKLLSGIAEDIDEEGSLILKK--GRRRLFLpGGEI 324
Cdd:COG0340 160 ELLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEGIAVGIDEDGALLLETadGEIRAVA-AGEV 238
|
..
gi 931359025 325 TH 326
Cdd:COG0340 239 SL 240
|
|
| BPL |
cd16442 |
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ... |
87-263 |
3.28e-68 |
|
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: 210.97 E-value: 3.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 87 RIVSYRTLGSTNEVAKQLADSGAPEGTLIVAEEQTKGRGRLGRSWHSPPKCGLYFTLILRPPIPPAKAPALSICAALAVV 166
Cdd:cd16442 1 KLIVLDEIDSTNDEAKELARSGAPEGTVVVAEEQTAGRGRRGRKWESPKGKGLYFSLLLRPDVPPAEAPLLTLLAAVAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 167 DSLGELFGIQLSTKWPNDVLINRKKVCGILTELVTRGNGVDSVIVGVGMNVNNRREDFPKDLrktaTSLAVELGEEVSRL 246
Cdd:cd16442 81 EALEKLGGIPVQIKWPNDILVNGKKLAGILTEASAEGEGVAAVVIGIGINVNNTPPPEPLPD----TSLATSLGKEVDRN 156
|
170
....*....|....*..
gi 931359025 247 GVLKRFLLEFERDYLQF 263
Cdd:cd16442 157 ELLEELLAALENRLELF 173
|
|
| birA_ligase |
TIGR00121 |
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ... |
94-326 |
3.93e-67 |
|
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: 210.72 E-value: 3.93e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 94 LGSTNEVAKQLADSGAPEGTLIVAEEQTKGRGRLGRSWHSPPKcGLYFTLILRPPIPPAKAPALSICAALAVVDSLGELf 173
Cdd:TIGR00121 8 IDSTNQYALELAKEGKLKGDLVVAEYQTAGRGRRGRKWLSPEG-GLYFSLILRPDLPKSPAPGLTLVAGIAIAEVLKEL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 174 GIQLSTKWPNDVLINRKKVCGILTELVTRGNGVDSVIVGVGMNVNNRRedFPKDLRKTATSLAVELGEEVSRLGVLKRFL 253
Cdd:TIGR00121 86 GDQVQVKWPNDILLKDKKLGGILTELTGKENRADYVVIGIGINVQNRK--PAESLREQAISLSEEAGIDLDRGELIEGFL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931359025 254 LEFERDYLQFSKSGLAPFRNHYRECSVGLGRSVKIRCGGKLLSGIAEDIDEEGSLILKKGRRRLFLPGGEITH 326
Cdd:TIGR00121 164 RNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSLTTGNGEIEGIARGIDKDGALLLEDGGGIKKIISGEISL 236
|
|
| PRK11886 |
PRK11886 |
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA; |
10-324 |
4.76e-65 |
|
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
Pssm-ID: 237010 [Multi-domain] Cd Length: 319 Bit Score: 207.72 E-value: 4.76e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 10 EILTLLrrSPGEYVSGRFLAESLDLKRESIYHTISQLRQFGYGIESDRRLGYRYRTAPDLLIASEIREGLKTKlfakRIV 89
Cdd:PRK11886 8 QLLSLL--ADGDFHSGEQLGEELGISRAAIWKHIQTLEEWGLDIFSVKGKGYRLAEPLDLLDPERISSQLPPG----RVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 90 SYRTLGSTNEVAKQLAdSGAPEGTLIVAEEQTKGRGRLGRSWHSPPKCGLYFTLILRPPIPPAKAPALSICAALAVVDSL 169
Cdd:PRK11886 82 VLPVIDSTNQYLLDRI-AELKSGDLCLAEYQTAGRGRRGRQWFSPFGGNLYLSLYWRLNQGPAQAMGLSLVVGIAIAEAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 170 GELFGIQLSTKWPNDVLINRKKVCGILTELVTRGNGVDSVIVGVGMNVNNRreDFPKDLRKTATSLAVELGEEVSRLGVL 249
Cdd:PRK11886 161 RRLGAIDVGLKWPNDIYLNDRKLAGILVELSGETGDAAHVVIGIGINVAMP--DFPEELIDQPWSDLQEAGPTIDRNQLA 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931359025 250 KRFLLEFERDYLQFSKSGLAPFRNHYRECSVGLGRSVKIRCGGKLLSGIAEDIDEEGSLILKK-GRRRLFLpGGEI 324
Cdd:PRK11886 239 AELIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIARGIDEQGALLLEDdGVEKPFN-GGEI 313
|
|
| BirA |
COG1654 |
Biotin operon repressor [Transcription]; |
5-315 |
7.86e-62 |
|
Biotin operon repressor [Transcription];
Pssm-ID: 441260 [Multi-domain] Cd Length: 324 Bit Score: 199.83 E-value: 7.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 5 SEHRDEILTLLRRspGEYVSGRFLAESLDLKRESIYHTISQLRQFGYGIESDRRLGYRYRTAPDLLIASEIREGLKTKLF 84
Cdd:COG1654 3 SSTRLKLLRLLAD--GEFHSGEELAEELGVSRAAVWKHIKALRELGYEIESVPGKGYRLAEPPDLLDPEEIRAGLSTKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 85 AKRIVSYRTLGSTNEVAKQLADSGAPEGTLIVAEEQTKGRGRLGRSWHSPPKCGLYFTLILRPPIPPAKAPALSICAALA 164
Cdd:COG1654 81 GREILYVISSTSTNLLALELAAQGGDAGTVVAAEQQRGGRGRRRRSWSSPGGGGLLYSLLLRPPIAPALLSLLLLAAAVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 165 VVDSLGELFGIQLSTKWPNDVLINRKKVCGILTELVTRGNGVDSVIVGVGMNVNNRREDFPKDLRKTATSLAVELGEEVS 244
Cdd:COG1654 161 VAAALAEGGGLVKWKKWPNDLLKKGKKILGILEEEGGDADGVVIVVGGGGNNNNSNPEEEPQELAELATSLLLILRLRLL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931359025 245 RLGVLKRFLLEFERDYLQFSKSGLAPFRNHYRECSVGLGRSVKIRCGGKLLSGIAEDIDEEGSLILKKGRR 315
Cdd:COG1654 241 RLLLLLLLLLLELLELLGFLEFFFLWERLDWELLRVLKLVVVVVEIGGGGGGGGALGGGLLGLLLLGGGGG 311
|
|
| PRK08330 |
PRK08330 |
biotin--protein ligase; Provisional |
86-311 |
4.29e-58 |
|
biotin--protein ligase; Provisional
Pssm-ID: 169384 [Multi-domain] Cd Length: 236 Bit Score: 187.26 E-value: 4.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 86 KRIVSYRTLGSTNEVAKQLAdSGAPEGTLIVAEEQTKGRGRLGRSWHSPPKcGLYFTLILRPPIPPAKAPALSICAALAV 165
Cdd:PRK08330 3 RNIIYFDEVDSTNEYAKRIA-PDEEEGTVIVADRQTAGHGRKGRAWASPEG-GLWMSVILKPKVSPEHLPKLVFLGALAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 166 VDSLGElFGIQLSTKWPNDVLINRKKVCGILTElvtrGNGvDSVIVGVGMNVNNrreDFPKDLRKTATSLAVELGEEVSR 245
Cdd:PRK08330 81 VDTLRE-FGIEGKIKWPNDVLVNYKKIAGVLVE----GKG-DFVVLGIGLNVNN---EIPDELRETATSMKEVLGREVPL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931359025 246 LGVLKRFLLEFERDYLQFSKSGLAPFRNHYRECSVgLGRSVKIRCGGKLLS-GIAEDIDEEGSLILK 311
Cdd:PRK08330 152 IEVFKRLVENLDRWYKLFLEGPGEILEEVKGRSMI-LGKRVKIIGDGEILVeGIAEDIDEFGALILR 217
|
|
| PRK06955 |
PRK06955 |
biotin--[acetyl-CoA-carboxylase] ligase; |
95-325 |
3.10e-28 |
|
biotin--[acetyl-CoA-carboxylase] ligase;
Pssm-ID: 235896 [Multi-domain] Cd Length: 300 Bit Score: 111.03 E-value: 3.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 95 GSTN----EVAKQLA--DSGAPEGTLIVAEEQTKGRGRLGRSWHSPPKCGLYFTLILRPPIPPAKAPALSICAALAVVDS 168
Cdd:PRK06955 42 GSTNadlmARLKALPrsADALPAPIVRVAYEQTAGRGRQGRPWFAQPGNALLFSVACVLPRPVAALAGLSLAVGVALAEA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 169 LGEL---FGIQLSTKWPNDVLINRKKVCGILTELVTRGNGVDSVIVGVGMNVNNRREDFPK--DLRKTATSLAVEL-GEE 242
Cdd:PRK06955 122 LAALpaaLGQRIALKWPNDLLIAGRKLAGILIETVWATPDATAVVIGIGLNVRRADAVAAEvdALRAREAALARGLpPVA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 243 VSRLG-------VLKRFLLEFERDYLQFSKSGLAPFRNHYRECSVGLGRSVKI-RCGGKLLSGIAEDIDEEGSLILKKGR 314
Cdd:PRK06955 202 LAAACaganltdTLAAALNALAPALQAFGADGLAPFAARWHALHAYAGREVVLlEDGAELARGVAHGIDETGQLLLDTPA 281
|
250
....*....|.
gi 931359025 315 RRLFLPGGEIT 325
Cdd:PRK06955 282 GRQAIAAGDVS 292
|
|
| PRK05935 |
PRK05935 |
biotin--protein ligase; Provisional |
96-274 |
1.80e-21 |
|
biotin--protein ligase; Provisional
Pssm-ID: 235649 [Multi-domain] Cd Length: 190 Bit Score: 89.88 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 96 STNEVAKQLADSGAPEG-TLIVAEEQTKGRGRLGRSWHSPPKcGLYFTLILRPPIPPAKAPALSICAALAVVdSLGELFG 174
Cdd:PRK05935 13 STNTTAKEGMHLWDPYAlTVISTREQTAGKGKFGKSWHSSDQ-DLLASFCFFITVLNIDVSLLFRLGTEAVM-RLGEDLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 175 IQLST-KWPNDVLINRKKVCGILTELVTRGNGVdSVIVGVGMNVNNRREDFpKDLRKTATSLAVELGEEVSRLGVLKRFL 253
Cdd:PRK05935 91 ITEAViKWPNDVLVHGEKLCGVLCETIPVKGGL-GVILGIGVNGNTTKDEL-LGIDQPATSLQELLGHPIDLEEQRERLI 168
|
170 180
....*....|....*....|..
gi 931359025 254 LEFERDYLQ-FSKSgLAPFRNH 274
Cdd:PRK05935 169 KHIKHVLIQtLPKL-LARESNH 189
|
|
| BPL_LplA_LipB |
pfam03099 |
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ... |
96-216 |
5.42e-21 |
|
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: 87.11 E-value: 5.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 96 STNEVAKQLADSGAPEGTLIVAEEQTKGRGRLGRSWHSPPKCgLYFTLILRPPIPPAKAPALSI---CAALAVVDSLG-- 170
Cdd:pfam03099 7 STNTYLEELNSSELESGGVVVVRRQTGGRGRGGNVWHSPKGC-LTYSLLLSKEHPNVDPSVLEFyvlELVLAVLEALGly 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 931359025 171 --ELFGIQLSTKWPNDVLINRKKVCGILTElVTRGNGVDSVIVGVGMN 216
Cdd:pfam03099 86 kpGISGIPCFVKWPNDLYVNGRKLAGILQR-STRGGTLHHGVIGLGVN 132
|
|
| PRK13325 |
PRK13325 |
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase; |
113-325 |
8.79e-19 |
|
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase;
Pssm-ID: 183976 [Multi-domain] Cd Length: 592 Bit Score: 87.07 E-value: 8.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 113 TLIVAEEQTKGRGRLGRSW-HSPPKCgLYFTLILRPPIPPAKAPALSICAALAVVDSLGELfGIQLSTKWPNDVLINRKK 191
Cdd:PRK13325 111 TICVTHLQSKGRGRQGRKWsHRLGEC-LMFSFGWVFDRPQYELGSLSPVAAVACRRALSRL-GLKTQIKWPNDLVVGRDK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 192 VCGILTELVtRGNGVDSVIVGVGMNVNnrredFPKDLRKTATslAVELGEEVSRLG------VLKRFLLEFERDYLQFSK 265
Cdd:PRK13325 189 LGGILIETV-RTGGKTVAVVGIGINFV-----LPKEVENAAS--VQSLFQTASRRGnadaavLLETLLAELDAVLLQYAR 260
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931359025 266 SGLAPFRNHYRECSVGLGRSV-KIRCGGKLLSGIAEDIDEEGSLILKKGRRRLFLPGGEIT 325
Cdd:PRK13325 261 DGFAPFVAEYQAANRDHGKAVlLLRDGETVFEGTVKGVDGQGVLHLETAEGKQTVVSGEIS 321
|
|
| PTZ00276 |
PTZ00276 |
biotin/lipoate protein ligase; Provisional |
94-217 |
3.03e-17 |
|
biotin/lipoate protein ligase; Provisional
Pssm-ID: 140302 [Multi-domain] Cd Length: 245 Bit Score: 79.91 E-value: 3.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 94 LGSTNEVAKQLADSGAPEGTLIVAEEQTKGRGRLGRSWHSpPKCGLYFTL-ILRPPIPPAKAPALSICAALAVVDSLGEL 172
Cdd:PTZ00276 15 VTSTMDVARTMLAAAGGKPFAVLAESQTAGRGTGGRTWTS-PKGNMYFTLcIPQKGVPPELVPVLPLITGLACRAAIMEV 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 931359025 173 F-GIQLSTKWPNDVLINRKKVCGILTElvtrgNGVDSVIVGVGMNV 217
Cdd:PTZ00276 94 LhGAAVHTKWPNDIIYAGKKIGGSLIE-----SEGEYLIIGIGMNI 134
|
|
| PRK08477 |
PRK08477 |
biotin--[acetyl-CoA-carboxylase] ligase; |
88-311 |
7.35e-11 |
|
biotin--[acetyl-CoA-carboxylase] ligase;
Pssm-ID: 236273 [Multi-domain] Cd Length: 211 Bit Score: 60.74 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 88 IVSYRTLGSTNEVAKQLADSG---APegTLIVAEEQTKGRGRLGRSWHSPpKCGLYFTLILRPPIPPA--KAPALSICAA 162
Cdd:PRK08477 3 IRVFESLDSTQTYLIEKIKNGelkAP--FAIVAKEQTAGIGSRGNSWEGK-KGNLFFSFALKESDLPKdlPLQSSSIYFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 163 LAVVDSLGELfGIQLSTKWPNDVLINRKKVCGILTELVTrgngvDSVIVGVGMNVNNRREDFPKdlrktatslaveLGEE 242
Cdd:PRK08477 80 FLLKEVLKEL-GSKVWLKWPNDLYLDDKKIGGVITNKIK-----NFIVCGIGLNLKFSPKNFAC------------LDIE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931359025 243 VSRLGVLKRFLLEFE---------RDY-LQFSKSglapfrnhyrecsvglgRSVKIRCGGKLLSGIAEDIDEEGSLILK 311
Cdd:PRK08477 142 ISDDLLLEGFLQKIEkkilwkqifSKYkLEFEKS-----------------KSFSFHIDGKLVSLKDAELLEDGSILIN 203
|
|
| BPL_LplA_LipB |
cd16435 |
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ... |
124-256 |
8.58e-08 |
|
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: 51.77 E-value: 8.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 124 RGRLGRSWHSPPKcGLYFTLILRPPIPPAKAPALSIcAALAVVDSLGElFGIQLSTKW-PNDVLINRKKVCGILTELVTr 202
Cdd:cd16435 68 RNRGGRAVSHDPG-QLVFSPVIGPNVEFMISKFNLI-IEEGIRDAIAD-FGQSAEVKWgRNDLWIDNRKVCGIAVRVVK- 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 931359025 203 gngvDSVIVGVGMNVNNRREDFPKDLR-----KTATSLAVELGEEVSRLGVLKRFLLEF 256
Cdd:cd16435 144 ----EAIFHGIALNLNQDLENFTEIIPcgykpERVTSLSLELGRKVTVEQVLERVLAAF 198
|
|
| PTZ00275 |
PTZ00275 |
biotin-acetyl-CoA-carboxylase ligase; Provisional |
111-317 |
5.24e-07 |
|
biotin-acetyl-CoA-carboxylase ligase; Provisional
Pssm-ID: 185536 [Multi-domain] Cd Length: 285 Bit Score: 50.21 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 111 EGTLIVA-EEQTKGRG------RLGRSWHSPpKCGLYFTLI-LRPPIPPAKAPALSICAALAVVDSLgELFGIQLSTKWP 182
Cdd:PTZ00275 48 DNMIIVScNEQTNGIGtrdtkkNQDRIWLSE-KGNLFTTFVfLWNRNDIEKVKYLAQTCTVAISKTL-EYFHLVTQIKWI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 183 NDVLINRKKVCGILTELVTRGNGVD------SVIVGVGMNVNNRREDfpKDLRKTATSLAVELGEEV-------SRLGVL 249
Cdd:PTZ00275 126 NDVLVNYKKIAGCLVHLYYLDDFPNlnsryvCVMVGIGINVTLEDKH--NLLNNNYTSIKKELQRDFntpksipSVEQVT 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931359025 250 KRFLLEFERDYLQFSKSGLAPFRNH------YREcsvglgRSVKIRCGGKLLSGIAEDIDEEGSLILKKGRRRL 317
Cdd:PTZ00275 204 EKLIINLKAVINKLRKEGFSSFLDYitprllYKD------KKVLIDQDNELIVGYLQGLLHDGSLLLLREKNKL 271
|
|
| HTH_11 |
pfam08279 |
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins. |
11-61 |
8.23e-06 |
|
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: 42.42 E-value: 8.23e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 931359025 11 ILTLLRRSPgEYVSGRFLAESLDLKRESIYHTISQLRQFGYGIESDRRLGY 61
Cdd:pfam08279 3 ILQLLLEAR-GPISGQELAEKLGVSRRTIRRDIKILEELGVPIEAEPGRGY 52
|
|
| BPL_C |
pfam02237 |
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ... |
282-326 |
1.89e-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: 35.90 E-value: 1.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 931359025 282 LGRSVKIRCGGKLLSGIAEDIDEEGSLILK--KGRRRLFlPGGEITH 326
Cdd:pfam02237 2 LGREVRVLLGDGIVEGIAVGIDDDGALLLEtdDGTIRDI-NSGEVSL 47
|
|
| NiaR |
COG1827 |
Transcriptional regulator of NAD metabolism, contains HTH and 3H domains [Transcription, ... |
5-81 |
2.13e-03 |
|
Transcriptional regulator of NAD metabolism, contains HTH and 3H domains [Transcription, Coenzyme transport and metabolism];
Pssm-ID: 441432 [Multi-domain] Cd Length: 171 Bit Score: 38.19 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931359025 5 SEHRDEILTLLRRSPgEYVSGRFLAESLDLKRESIYHTISQLRQFGYGIESDRRlGYRYRTAPDL-----LIA-----SE 74
Cdd:COG1827 4 EERREKILEILKESK-EPISGSELAKKFGVSRQVIVQDIALLRAKGEPIIATPR-GYILLKAESSkgftrVIAckhtpEE 81
|
....*..
gi 931359025 75 IREGLKT 81
Cdd:COG1827 82 IEEELNT 88
|
|
| YobV |
COG2378 |
Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains ... |
10-69 |
2.39e-03 |
|
Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains [Transcription];
Pssm-ID: 441945 [Multi-domain] Cd Length: 314 Bit Score: 39.29 E-value: 2.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931359025 10 EILTLLRRSPGeyVSGRFLAESLDLKRESIYHTISQLRQFGYGIESDR--RLGYRYRTAPDL 69
Cdd:COG2378 9 ALLQLLQSRRG--VTAAELAERLEVSERTIYRDIDALRELGVPIEAERgrGGGYRLRDGYRL 68
|
|
|