|
Name |
Accession |
Description |
Interval |
E-value |
| RibF |
COG0196 |
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ... |
1-314 |
7.80e-126 |
|
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
Pssm-ID: 439966 [Multi-domain] Cd Length: 310 Bit Score: 362.82 E-value: 7.80e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 1 MQVINlkypvALSQIPE--GPIVLALGFFDGVHRGHQQVVATARQAAQAQHAKLAVMTFDQHPSVVFKHTDPqqVRYLTT 78
Cdd:COG0196 1 MKIIR-----GLSELPAdlRGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDKA--PKLLTT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 79 IDQKTALMSELGVDILYVLHFDATVGAMPPQTFVDQLIV-GLHAQTVVAGFDYTYGPAEIANMQRLNDYGHNR-FEIIEV 156
Cdd:COG0196 74 LEEKLELLEELGVDYVLVLPFTREFAALSPEEFVEEILVdKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYgFEVEVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 157 PKAELDAEKISSTRIRRALDAGDIDTANRLLGYQYETAGEVVHGEARGRTLGFPTANVAHGPNTRVPGIGIYATMVQIGT 236
Cdd:COG0196 154 PPVTIDGERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPEEKLLPADGVYAVRVRIDG 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489736620 237 RWVMGMASVGRNVTFGDHRPiTVEIYLLGFQGDLYGHNLTVRWGHRMRGEIKFAGADALVAQLKRDEQNTRDYYVAHP 314
Cdd:COG0196 234 RRYPGVANIGTRPTFDGGEP-TLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILAKLK 310
|
|
| PRK05627 |
PRK05627 |
bifunctional riboflavin kinase/FAD synthetase; |
21-309 |
4.19e-106 |
|
bifunctional riboflavin kinase/FAD synthetase;
Pssm-ID: 235536 [Multi-domain] Cd Length: 305 Bit Score: 312.47 E-value: 4.19e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 21 VLALGFFDGVHRGHQQVVATARQAAQAQHAKLAVMTFDQHPSVVFKHTDPqqVRYLTTIDQKTALMSELGVDILYVLHFD 100
Cdd:PRK05627 16 VLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKA--PARLTPLRDKAELLAELGVDYVLVLPFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 101 ATVGAMPPQTFVDQLIV-GLHAQTVVAGFDYTYGPAEIANMQRLNDYGHNR-FEIIEVPKAELDAEKISSTRIRRALDAG 178
Cdd:PRK05627 94 EEFAKLSAEEFIEDLLVkGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFgFEVTIVPEVKEDGERVSSTAIRQALAEG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 179 DIDTANRLLGYQYETAGEVVHGEARGRTLGFPTANVAHgPNTRVPGIGIYATMVQIGTRWVMGMASVGRNVTFGDHRPiT 258
Cdd:PRK05627 174 DLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPL-PDRVLPADGVYAVRVKVDGKPYPGVANIGTRPTVDGGRQ-L 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 489736620 259 VEIYLLGFQGDLYGHNLTVRWGHRMRGEIKFAGADALVAQLKRDEQNTRDY 309
Cdd:PRK05627 252 LEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAF 302
|
|
| ribF |
TIGR00083 |
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ... |
21-310 |
2.05e-68 |
|
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1.26) (flavokinase) / FMN adenylyltransferase (EC 2.7.7.2) (FAD pyrophosphorylase) (FAD synthetase). [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]
Pssm-ID: 272898 [Multi-domain] Cd Length: 288 Bit Score: 215.77 E-value: 2.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 21 VLALGFFDGVHRGHQQVVATARQAAQAQHAKLAVMTFDQHPSVVFkhtDPQQVRYLTTIDQKTALMSELGVDILYVLHFD 100
Cdd:TIGR00083 1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQF---NWLTAPALTPLEDKARQLQIKGVEQLLVVVFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 101 ATVGAMPPQTFVDQLIVG-LHAQTVVAGFDYTYGPAEIANMQRLNDYGHNRFEIIEVPKAELDAEKISSTRIRRALDAGD 179
Cdd:TIGR00083 78 EEFANLSALQFIDQLIVKhLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCVIVKQLFCQDIRISSSAIRQALKNGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 180 IDTANRLLGYQYETAGEVVHGEARGRTLGFPTANVAHGPNTRVPGIGIYATMVQIGTRWVMGMASVGRNVTFGDHRPItV 259
Cdd:TIGR00083 158 LELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLKNQVLPLKGGYYVVVVLLNGEPYPGVGNIGNRPTFIGQQLV-I 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 489736620 260 EIYLLGFQGDLYGHNLTVRWGHRMRGEIKFAGADALVAQLKRDEQNTRDYY 310
Cdd:TIGR00083 237 EVHLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWF 287
|
|
| FAD_synthetase_N |
cd02064 |
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ... |
21-200 |
3.87e-66 |
|
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal domain of the bifunctional riboflavin biosynthesis protein riboflavin kinase/FAD synthetase. These enzymes have both ATP:riboflavin 5'-phosphotransferase and ATP:FMN-adenylyltransferase activities. The N-terminal domain is believed to play a role in the adenylylation reaction of FAD synthetases. The C-terminal domain is thought to have kinase activity. FAD synthetase is present among all kingdoms of life. However, the bifunctional enzyme is not found in mammals, which use separate enzymes for FMN and FAD formation.
Pssm-ID: 185679 [Multi-domain] Cd Length: 180 Bit Score: 205.85 E-value: 3.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 21 VLALGFFDGVHRGHQQVVATARQAAQAQHAKLAVMTFDQHPSVVFKhtDPQQVRYLTTIDQKTALMSELGVDILYVLHFD 100
Cdd:cd02064 2 VVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFL--PDKAPPRLTTLEEKLELLESLGVDYLLVLPFD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 101 ATVGAMPPQTFVDQLIVGLHAQTVVAGFDYTYGPAEIANMQRLNDYGH-NRFEIIEVPKAELDAEKISSTRIRRALDAGD 179
Cdd:cd02064 80 KEFASLSAEEFVEDLLVKLNAKHVVVGFDFRFGKGRSGDAELLKELGKkYGFEVTVVPPVTLDGERVSSTRIREALAEGD 159
|
170 180
....*....|....*....|.
gi 489736620 180 IDTANRLLGYQYETAGEVVHG 200
Cdd:cd02064 160 VELANELLGRPYSIEGRVVHG 180
|
|
| Flavokinase |
smart00904 |
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ... |
186-309 |
4.68e-53 |
|
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) by the actions of riboflavin kinase, which converts it into FMN, and FAD synthetase, which adenylates FMN to FAD. Eukaryotes usually have two separate enzymes, while most prokaryotes have a single bifunctional protein that can carry out both catalyses, although exceptions occur in both cases. While eukaryotic monofunctional riboflavin kinase is orthologous to the bifunctional prokaryotic enzyme. the monofunctional FAD synthetase differs from its prokaryotic counterpart, and is instead related to the PAPS-reductase family. The bacterial FAD synthetase that is part of the bifunctional enzyme has remote similarity to nucleotidyl transferases and, hence, it may be involved in the adenylylation reaction of FAD synthetases. This entry represents riboflavin kinase, which occurs as part of a bifunctional enzyme or a stand-alone enzyme.
Pssm-ID: 214901 [Multi-domain] Cd Length: 124 Bit Score: 170.31 E-value: 4.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 186 LLGYQYETAGEVVHGEARGRTLGFPTANVAHGPNTRVPGIGIYATMVQIGTRWVMGMASVGRNVTFGDHRpiTVEIYLLG 265
Cdd:smart00904 1 LLGRPYSISGRVVHGDKRGRTLGFPTANLPLDDRLLLPKNGVYAVRVRVDGKIYPGVANIGTRPTFGGDR--SVEVHILD 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 489736620 266 FQGDLYGHNLTVRWGHRMRGEIKFAGADALVAQLKRDEQNTRDY 309
Cdd:smart00904 79 FSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREY 122
|
|
| Flavokinase |
pfam01687 |
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ... |
187-309 |
2.55e-48 |
|
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin biosynthesis protein known as RibC in Bacillus subtilis. The RibC protein from Bacillus subtilis has both flavokinase and flavin adenine dinucleotide synthetase (FAD-synthetase) activities. RibC plays an essential role in the flavin metabolism. This domain is thought to have kinase activity.
Pssm-ID: 460295 [Multi-domain] Cd Length: 123 Bit Score: 158.31 E-value: 2.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 187 LGYQYETAGEVVHGEARGRTLGFPTANVaHGPNTRVPGIGIYATMVQI-GTRWVMGMASVGRNVTFGDHRPiTVEIYLLG 265
Cdd:pfam01687 1 LGRPYSISGKVVHGDGRGRTLGFPTANL-PLPEKLLPANGVYAVWVRVdGGKVYPGVANIGTNPTFGNGKL-TVEVHILD 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 489736620 266 FQGDLYGHNLTVRWGHRMRGEIKFAGADALVAQLKRDEQNTRDY 309
Cdd:pfam01687 79 FDGDLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQARAI 122
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RibF |
COG0196 |
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ... |
1-314 |
7.80e-126 |
|
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
Pssm-ID: 439966 [Multi-domain] Cd Length: 310 Bit Score: 362.82 E-value: 7.80e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 1 MQVINlkypvALSQIPE--GPIVLALGFFDGVHRGHQQVVATARQAAQAQHAKLAVMTFDQHPSVVFKHTDPqqVRYLTT 78
Cdd:COG0196 1 MKIIR-----GLSELPAdlRGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDKA--PKLLTT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 79 IDQKTALMSELGVDILYVLHFDATVGAMPPQTFVDQLIV-GLHAQTVVAGFDYTYGPAEIANMQRLNDYGHNR-FEIIEV 156
Cdd:COG0196 74 LEEKLELLEELGVDYVLVLPFTREFAALSPEEFVEEILVdKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYgFEVEVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 157 PKAELDAEKISSTRIRRALDAGDIDTANRLLGYQYETAGEVVHGEARGRTLGFPTANVAHGPNTRVPGIGIYATMVQIGT 236
Cdd:COG0196 154 PPVTIDGERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPEEKLLPADGVYAVRVRIDG 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489736620 237 RWVMGMASVGRNVTFGDHRPiTVEIYLLGFQGDLYGHNLTVRWGHRMRGEIKFAGADALVAQLKRDEQNTRDYYVAHP 314
Cdd:COG0196 234 RRYPGVANIGTRPTFDGGEP-TLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILAKLK 310
|
|
| PRK05627 |
PRK05627 |
bifunctional riboflavin kinase/FAD synthetase; |
21-309 |
4.19e-106 |
|
bifunctional riboflavin kinase/FAD synthetase;
Pssm-ID: 235536 [Multi-domain] Cd Length: 305 Bit Score: 312.47 E-value: 4.19e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 21 VLALGFFDGVHRGHQQVVATARQAAQAQHAKLAVMTFDQHPSVVFKHTDPqqVRYLTTIDQKTALMSELGVDILYVLHFD 100
Cdd:PRK05627 16 VLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKA--PARLTPLRDKAELLAELGVDYVLVLPFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 101 ATVGAMPPQTFVDQLIV-GLHAQTVVAGFDYTYGPAEIANMQRLNDYGHNR-FEIIEVPKAELDAEKISSTRIRRALDAG 178
Cdd:PRK05627 94 EEFAKLSAEEFIEDLLVkGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFgFEVTIVPEVKEDGERVSSTAIRQALAEG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 179 DIDTANRLLGYQYETAGEVVHGEARGRTLGFPTANVAHgPNTRVPGIGIYATMVQIGTRWVMGMASVGRNVTFGDHRPiT 258
Cdd:PRK05627 174 DLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPL-PDRVLPADGVYAVRVKVDGKPYPGVANIGTRPTVDGGRQ-L 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 489736620 259 VEIYLLGFQGDLYGHNLTVRWGHRMRGEIKFAGADALVAQLKRDEQNTRDY 309
Cdd:PRK05627 252 LEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAF 302
|
|
| ribF |
TIGR00083 |
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ... |
21-310 |
2.05e-68 |
|
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1.26) (flavokinase) / FMN adenylyltransferase (EC 2.7.7.2) (FAD pyrophosphorylase) (FAD synthetase). [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]
Pssm-ID: 272898 [Multi-domain] Cd Length: 288 Bit Score: 215.77 E-value: 2.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 21 VLALGFFDGVHRGHQQVVATARQAAQAQHAKLAVMTFDQHPSVVFkhtDPQQVRYLTTIDQKTALMSELGVDILYVLHFD 100
Cdd:TIGR00083 1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQF---NWLTAPALTPLEDKARQLQIKGVEQLLVVVFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 101 ATVGAMPPQTFVDQLIVG-LHAQTVVAGFDYTYGPAEIANMQRLNDYGHNRFEIIEVPKAELDAEKISSTRIRRALDAGD 179
Cdd:TIGR00083 78 EEFANLSALQFIDQLIVKhLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCVIVKQLFCQDIRISSSAIRQALKNGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 180 IDTANRLLGYQYETAGEVVHGEARGRTLGFPTANVAHGPNTRVPGIGIYATMVQIGTRWVMGMASVGRNVTFGDHRPItV 259
Cdd:TIGR00083 158 LELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLKNQVLPLKGGYYVVVVLLNGEPYPGVGNIGNRPTFIGQQLV-I 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 489736620 260 EIYLLGFQGDLYGHNLTVRWGHRMRGEIKFAGADALVAQLKRDEQNTRDYY 310
Cdd:TIGR00083 237 EVHLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWF 287
|
|
| FAD_synthetase_N |
cd02064 |
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ... |
21-200 |
3.87e-66 |
|
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal domain of the bifunctional riboflavin biosynthesis protein riboflavin kinase/FAD synthetase. These enzymes have both ATP:riboflavin 5'-phosphotransferase and ATP:FMN-adenylyltransferase activities. The N-terminal domain is believed to play a role in the adenylylation reaction of FAD synthetases. The C-terminal domain is thought to have kinase activity. FAD synthetase is present among all kingdoms of life. However, the bifunctional enzyme is not found in mammals, which use separate enzymes for FMN and FAD formation.
Pssm-ID: 185679 [Multi-domain] Cd Length: 180 Bit Score: 205.85 E-value: 3.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 21 VLALGFFDGVHRGHQQVVATARQAAQAQHAKLAVMTFDQHPSVVFKhtDPQQVRYLTTIDQKTALMSELGVDILYVLHFD 100
Cdd:cd02064 2 VVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFL--PDKAPPRLTTLEEKLELLESLGVDYLLVLPFD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 101 ATVGAMPPQTFVDQLIVGLHAQTVVAGFDYTYGPAEIANMQRLNDYGH-NRFEIIEVPKAELDAEKISSTRIRRALDAGD 179
Cdd:cd02064 80 KEFASLSAEEFVEDLLVKLNAKHVVVGFDFRFGKGRSGDAELLKELGKkYGFEVTVVPPVTLDGERVSSTRIREALAEGD 159
|
170 180
....*....|....*....|.
gi 489736620 180 IDTANRLLGYQYETAGEVVHG 200
Cdd:cd02064 160 VELANELLGRPYSIEGRVVHG 180
|
|
| Flavokinase |
smart00904 |
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ... |
186-309 |
4.68e-53 |
|
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) by the actions of riboflavin kinase, which converts it into FMN, and FAD synthetase, which adenylates FMN to FAD. Eukaryotes usually have two separate enzymes, while most prokaryotes have a single bifunctional protein that can carry out both catalyses, although exceptions occur in both cases. While eukaryotic monofunctional riboflavin kinase is orthologous to the bifunctional prokaryotic enzyme. the monofunctional FAD synthetase differs from its prokaryotic counterpart, and is instead related to the PAPS-reductase family. The bacterial FAD synthetase that is part of the bifunctional enzyme has remote similarity to nucleotidyl transferases and, hence, it may be involved in the adenylylation reaction of FAD synthetases. This entry represents riboflavin kinase, which occurs as part of a bifunctional enzyme or a stand-alone enzyme.
Pssm-ID: 214901 [Multi-domain] Cd Length: 124 Bit Score: 170.31 E-value: 4.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 186 LLGYQYETAGEVVHGEARGRTLGFPTANVAHGPNTRVPGIGIYATMVQIGTRWVMGMASVGRNVTFGDHRpiTVEIYLLG 265
Cdd:smart00904 1 LLGRPYSISGRVVHGDKRGRTLGFPTANLPLDDRLLLPKNGVYAVRVRVDGKIYPGVANIGTRPTFGGDR--SVEVHILD 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 489736620 266 FQGDLYGHNLTVRWGHRMRGEIKFAGADALVAQLKRDEQNTRDY 309
Cdd:smart00904 79 FSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREY 122
|
|
| Flavokinase |
pfam01687 |
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ... |
187-309 |
2.55e-48 |
|
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin biosynthesis protein known as RibC in Bacillus subtilis. The RibC protein from Bacillus subtilis has both flavokinase and flavin adenine dinucleotide synthetase (FAD-synthetase) activities. RibC plays an essential role in the flavin metabolism. This domain is thought to have kinase activity.
Pssm-ID: 460295 [Multi-domain] Cd Length: 123 Bit Score: 158.31 E-value: 2.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 187 LGYQYETAGEVVHGEARGRTLGFPTANVaHGPNTRVPGIGIYATMVQI-GTRWVMGMASVGRNVTFGDHRPiTVEIYLLG 265
Cdd:pfam01687 1 LGRPYSISGKVVHGDGRGRTLGFPTANL-PLPEKLLPANGVYAVWVRVdGGKVYPGVANIGTNPTFGNGKL-TVEVHILD 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 489736620 266 FQGDLYGHNLTVRWGHRMRGEIKFAGADALVAQLKRDEQNTRDY 309
Cdd:pfam01687 79 FDGDLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQARAI 122
|
|
| FAD_syn |
pfam06574 |
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ... |
19-170 |
2.00e-43 |
|
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme riboflavin kinase / FAD synthetase. These enzymes have both ATP:riboflavin 5'-phospho transferase and ATP:FMN-adenylyltransferase activity. They catalyze the 5'-phosphorylation of riboflavin to FMN and the adenylylation of FMN to FAD. This domain is thought to have the flavin mononucleotide (FMN) adenylyltransferase activity.
Pssm-ID: 429011 [Multi-domain] Cd Length: 158 Bit Score: 146.94 E-value: 2.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 19 PIVLALGFFDGVHRGHQQVVATARQAAQAQHAKLAVMTFDQHPSVVFKhTDPQQVRyLTTIDQKTALMSELGVDILYVLH 98
Cdd:pfam06574 7 GCVVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFN-PDSAPFR-LTTLEEKIELLAELGVDYLLVLP 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489736620 99 FDATVGAMPPQTFVDQLIV-GLHAQTVVAGFDYTYGPAEIANMQRLNDYGHNR-FEIIEVPKAELDAEKISSTR 170
Cdd:pfam06574 85 FTKEFASLSAEEFIENVLVdGLNVKHVVVGFDFRFGKGRKGDVELLKELGAKLgFEVTIVPPVELDGEKISSTR 158
|
|
| PRK07143 |
PRK07143 |
hypothetical protein; Provisional |
1-192 |
4.42e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 235946 [Multi-domain] Cd Length: 279 Bit Score: 62.32 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 1 MQVInlKYPvaLSQIPEGPIVLALGFFDGVHRGHQQVVATARQAAQAQHaklaVMTFdQHPSVVFKHTDpqqvRYLTtiD 80
Cdd:PRK07143 2 MKVY--TFP--LKNFKFEKPTFVLGGFESFHLGHLELFKKAKESNDEIV----IVIF-KNPENLPKNTN----KKFS--D 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 81 QKTAL--MSELGVDILYVLHFDATVGAMPPQTFVDQLIVGLHAQtVVAGFDYTYGPAEIANMQRLNDYgHNRFEIIEVPK 158
Cdd:PRK07143 67 LNSRLqtLANLGFKNIILLDFNEELQNLSGNDFIEKLTKNQVSF-FVVGKDFRFGKNASWNADDLKEY-FPNVHIVEILK 144
|
170 180 190
....*....|....*....|....*....|....
gi 489736620 159 aeLDAEKISSTRIRRALDAGDIDTANRLLGYQYE 192
Cdd:PRK07143 145 --INQQKISTSLLKEFIEFGDIELLNSLLLYNYS 176
|
|
| cytidylyltransferase_like |
cd02039 |
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ... |
20-174 |
2.45e-07 |
|
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are known to use CTP or ATP and release pyrophosphate. Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown.
Pssm-ID: 185678 [Multi-domain] Cd Length: 143 Bit Score: 49.36 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736620 20 IVLALGFFDGVHRGHQQVVATARQAAqaqhaklavmtFDQHPSVVFKHTD-PQQVRYLTTIDQKTALMSELGVDILYVLH 98
Cdd:cd02039 1 VGIIIGRFEPFHLGHLKLIKEALEEA-----------LDEVIIIIVSNPPkKKRNKDPFSLHERVEMLKEILKDRLKVVP 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489736620 99 FDA-TVGAMPPQTFVDQLIVGLHAQTVVAGFDYTYGPAEIANMQRLNDYghNRFEIIEVPKAElDAEKISSTRIRRA 174
Cdd:cd02039 70 VDFpEVKILLAVVFILKILLKVGPDKVVVGEDFAFGKNASYNKDLKELF--LDIEIVEVPRVR-DGKKISSTLIREL 143
|
|
| CAB4 |
COG1019 |
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ... |
127-187 |
2.08e-06 |
|
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 440642 Cd Length: 154 Bit Score: 46.73 E-value: 2.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489736620 127 GFDY------TYGPAEIANMQRLNDyGHNRFEIIEVP--KAElDAEKISSTRIRRaldaGDIDTANRLL 187
Cdd:COG1019 89 DFDAlvvspeTEPGAEKINEIRRER-GLKPLEIVVVPhvLAE-DGKPISSTRIRN----GEIDEHGRLL 151
|
|
| PRK00777 |
PRK00777 |
pantetheine-phosphate adenylyltransferase; |
123-187 |
1.64e-04 |
|
pantetheine-phosphate adenylyltransferase;
Pssm-ID: 234834 Cd Length: 153 Bit Score: 41.36 E-value: 1.64e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489736620 123 TVVAGFDY------TYGPAEIANMQRLNDyGHNRFEIIEVP--KAElDAEKISSTRIRRaldaGDIDTANRLL 187
Cdd:PRK00777 84 ALEDDFDAivvspeTYPGALKINEIRRER-GLKPLEIVVIDfvLAE-DGKPISSTRIRR----GEIDEHGNLI 150
|
|
| PPAT_CoAS |
cd02164 |
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ... |
131-173 |
2.34e-03 |
|
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; The PPAT domain of the bifunctional enzyme with PPAT and DPCK functions. The final two steps of the CoA biosynthesis pathway are catalyzed by phosphopantetheine adenylyltransferase (PPAT) and dephospho-CoA (dPCoA) kinase (DPCK). The PPAT reaction involves the reversible adenylation of 4'-phosphopantetheine to form 3'-dPCoA and PPi, and DPCK catalyses phosphorylation of the 3'-hydroxy group of the ribose moiety of dPCoA. In eukaryotes the two enzymes are part of a large multienzyme complex . Studies in Corynebacterium ammoniagenes suggested that separate enzymes were present, and this was confirmed through identification of the bacterial PPAT/CoAD.
Pssm-ID: 173915 Cd Length: 143 Bit Score: 37.64 E-value: 2.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 489736620 131 TYGPAEIANMQRLNDyGHNRFEIIEVP--KAELDAEKISSTRIRR 173
Cdd:cd02164 99 TYPGALKINRKREEN-GLSPLEIVVVPlvKADEDGEKISSTRIRR 142
|
|
| |
