|
Name |
Accession |
Description |
Interval |
E-value |
| RibF |
COG0196 |
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ... |
30-323 |
1.79e-136 |
|
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: 389.79 E-value: 1.79e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 30 VATIGFFDGVHRGHQFLIGRVRDEAERSGMASAVITFDLHPRQVLQAGYQPQLLSTLDGKLLLLSKTRVDNIIVLHFDES 109
Cdd:COG0196 18 VVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDKAPKLLTTLEEKLELLEELGVDYVLVLPFTRE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 110 LAALPAREFMKEVLYRQLNVKKLIIGYDNRFGHNRSEGFEHYVQYGRELGIEVILADAFLPDDEKVSSSVIRNHIQQGEI 189
Cdd:COG0196 98 FAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYGFEVEVVPPVTIDGERVSSTRIREALAEGDV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 190 EAANRLLGYDYTIESTIVNGCQNGRRMGFPTANLDVNGcRQLLPAAGVYAVTVRLKDsvGWKRGMMNIGKRPTFNGTTTS 269
Cdd:COG0196 178 EEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPE-EKLLPADGVYAVRVRIDG--RRYPGVANIGTRPTFDGGEPT 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 913019572 270 MEVNLFNFTGNLYGQELLVSFISKIRDERRFDSLDALSAQLMQDRDSVNRLFDE 323
Cdd:COG0196 255 LEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILAK 308
|
|
| PRK05627 |
PRK05627 |
bifunctional riboflavin kinase/FAD synthetase; |
27-313 |
8.52e-117 |
|
bifunctional riboflavin kinase/FAD synthetase;
Pssm-ID: 235536 [Multi-domain] Cd Length: 305 Bit Score: 339.43 E-value: 8.52e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 27 PEQVATIGFFDGVHRGHQFLIGRVRDEAERSGMASAVITFDLHPRQVLQAGYQPQLLSTLDGKLLLLSKTRVDNIIVLHF 106
Cdd:PRK05627 13 PDCVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKAPARLTPLRDKAELLAELGVDYVLVLPF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 107 DESLAALPAREFMKEVLYRQLNVKKLIIGYDNRFGHNRSEGFEHYVQYGRELGIEVILADAFLPDDEKVSSSVIRNHIQQ 186
Cdd:PRK05627 93 DEEFAKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFGFEVTIVPEVKEDGERVSSTAIRQALAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 187 GEIEAANRLLGYDYTIESTIVNGCQNGRRMGFPTANLDVNgcRQLLPAAGVYAVTVRLKDSvgWKRGMMNIGKRPTFNGT 266
Cdd:PRK05627 173 GDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPLP--DRVLPADGVYAVRVKVDGK--PYPGVANIGTRPTVDGG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 913019572 267 TTSMEVNLFNFTGNLYGQELLVSFISKIRDERRFDSLDALSAQLMQD 313
Cdd:PRK05627 249 RQLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKD 295
|
|
| ribF |
TIGR00083 |
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ... |
30-321 |
2.19e-81 |
|
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: 248.90 E-value: 2.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 30 VATIGFFDGVHRGHQFLIGRVRDEAERSGMASAVITFDLHPRQVLQAGYQPqLLSTLDGKLLLLSKTRVDNIIVLHFDES 109
Cdd:TIGR00083 1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWLTAP-ALTPLEDKARQLQIKGVEQLLVVVFDEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 110 LAALPAREFMKEVLYRQLNVKKLIIGYDNRFGHNRSEGFEHYVQYGRELGIEVILADAFLpDDEKVSSSVIRNHIQQGEI 189
Cdd:TIGR00083 80 FANLSALQFIDQLIVKHLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCVIVKQLFC-QDIRISSSAIRQALKNGDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 190 EAANRLLGYDYTIESTIVNGCQNGRRMGFPTANLDVNgcRQLLPAAGVYAVTVRLKDSVGWKrGMMNIGKRPTFNGTTTS 269
Cdd:TIGR00083 159 ELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLK--NQVLPLKGGYYVVVVLLNGEPYP-GVGNIGNRPTFIGQQLV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 913019572 270 MEVNLFNFTGNLYGQELLVSFISKIRDERRFDSLDALSAQLMQDRDSVNRLF 321
Cdd:TIGR00083 236 IEVHLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWF 287
|
|
| FAD_synthetase_N |
cd02064 |
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ... |
30-209 |
1.84e-70 |
|
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: 217.02 E-value: 1.84e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 30 VATIGFFDGVHRGHQFLIGRVRDEAERSGMASAVITFDLHPRQVLQAGYQPQLLSTLDGKLLLLSKTRVDNIIVLHFDES 109
Cdd:cd02064 2 VVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPDKAPPRLTTLEEKLELLESLGVDYLLVLPFDKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 110 LAALPAREFMKEVLyRQLNVKKLIIGYDNRFGHNRSEGFEHYVQYGRELGIEVILADAFLPDDEKVSSSVIRNHIQQGEI 189
Cdd:cd02064 82 FASLSAEEFVEDLL-VKLNAKHVVVGFDFRFGKGRSGDAELLKELGKKYGFEVTVVPPVTLDGERVSSTRIREALAEGDV 160
|
170 180
....*....|....*....|
gi 913019572 190 EAANRLLGYDYTIESTIVNG 209
Cdd:cd02064 161 ELANELLGRPYSIEGRVVHG 180
|
|
| FAD_syn |
pfam06574 |
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ... |
30-178 |
2.54e-54 |
|
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: 175.06 E-value: 2.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 30 VATIGFFDGVHRGHQFLIGRVRDEAERSGMASAVITFDLHPRQVLQAGYQPQLLSTLDGKLLLLSKTRVDNIIVLHFDES 109
Cdd:pfam06574 9 VVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNPDSAPFRLTTLEEKIELLAELGVDYLLVLPFTKE 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 913019572 110 LAALPAREFMKEVLYRQLNVKKLIIGYDNRFGHNRSEGFEHYVQYGRELGIEVILADAFLPDDEKVSSS 178
Cdd:pfam06574 89 FASLSAEEFIENVLVDGLNVKHVVVGFDFRFGKGRKGDVELLKELGAKLGFEVTIVPPVELDGEKISST 157
|
|
| Flavokinase |
smart00904 |
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ... |
195-322 |
4.76e-47 |
|
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: 154.90 E-value: 4.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 195 LLGYDYTIESTIVNGCQNGRRMGFPTANLDVNGcRQLLPAAGVYAVTVRLKDsvGWKRGMMNIGKRPTFNGTTTsMEVNL 274
Cdd:smart00904 1 LLGRPYSISGRVVHGDKRGRTLGFPTANLPLDD-RLLLPKNGVYAVRVRVDG--KIYPGVANIGTRPTFGGDRS-VEVHI 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 913019572 275 FNFTGNLYGQELLVSFISKIRDERRFDSLDALSAQLMQDRDSVNRLFD 322
Cdd:smart00904 77 LDFSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYLA 124
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| RibF |
COG0196 |
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ... |
30-323 |
1.79e-136 |
|
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: 389.79 E-value: 1.79e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 30 VATIGFFDGVHRGHQFLIGRVRDEAERSGMASAVITFDLHPRQVLQAGYQPQLLSTLDGKLLLLSKTRVDNIIVLHFDES 109
Cdd:COG0196 18 VVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDKAPKLLTTLEEKLELLEELGVDYVLVLPFTRE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 110 LAALPAREFMKEVLYRQLNVKKLIIGYDNRFGHNRSEGFEHYVQYGRELGIEVILADAFLPDDEKVSSSVIRNHIQQGEI 189
Cdd:COG0196 98 FAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYGFEVEVVPPVTIDGERVSSTRIREALAEGDV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 190 EAANRLLGYDYTIESTIVNGCQNGRRMGFPTANLDVNGcRQLLPAAGVYAVTVRLKDsvGWKRGMMNIGKRPTFNGTTTS 269
Cdd:COG0196 178 EEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPE-EKLLPADGVYAVRVRIDG--RRYPGVANIGTRPTFDGGEPT 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 913019572 270 MEVNLFNFTGNLYGQELLVSFISKIRDERRFDSLDALSAQLMQDRDSVNRLFDE 323
Cdd:COG0196 255 LEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILAK 308
|
|
| PRK05627 |
PRK05627 |
bifunctional riboflavin kinase/FAD synthetase; |
27-313 |
8.52e-117 |
|
bifunctional riboflavin kinase/FAD synthetase;
Pssm-ID: 235536 [Multi-domain] Cd Length: 305 Bit Score: 339.43 E-value: 8.52e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 27 PEQVATIGFFDGVHRGHQFLIGRVRDEAERSGMASAVITFDLHPRQVLQAGYQPQLLSTLDGKLLLLSKTRVDNIIVLHF 106
Cdd:PRK05627 13 PDCVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKAPARLTPLRDKAELLAELGVDYVLVLPF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 107 DESLAALPAREFMKEVLYRQLNVKKLIIGYDNRFGHNRSEGFEHYVQYGRELGIEVILADAFLPDDEKVSSSVIRNHIQQ 186
Cdd:PRK05627 93 DEEFAKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFGFEVTIVPEVKEDGERVSSTAIRQALAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 187 GEIEAANRLLGYDYTIESTIVNGCQNGRRMGFPTANLDVNgcRQLLPAAGVYAVTVRLKDSvgWKRGMMNIGKRPTFNGT 266
Cdd:PRK05627 173 GDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPLP--DRVLPADGVYAVRVKVDGK--PYPGVANIGTRPTVDGG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 913019572 267 TTSMEVNLFNFTGNLYGQELLVSFISKIRDERRFDSLDALSAQLMQD 313
Cdd:PRK05627 249 RQLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKD 295
|
|
| ribF |
TIGR00083 |
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ... |
30-321 |
2.19e-81 |
|
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: 248.90 E-value: 2.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 30 VATIGFFDGVHRGHQFLIGRVRDEAERSGMASAVITFDLHPRQVLQAGYQPqLLSTLDGKLLLLSKTRVDNIIVLHFDES 109
Cdd:TIGR00083 1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWLTAP-ALTPLEDKARQLQIKGVEQLLVVVFDEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 110 LAALPAREFMKEVLYRQLNVKKLIIGYDNRFGHNRSEGFEHYVQYGRELGIEVILADAFLpDDEKVSSSVIRNHIQQGEI 189
Cdd:TIGR00083 80 FANLSALQFIDQLIVKHLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCVIVKQLFC-QDIRISSSAIRQALKNGDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 190 EAANRLLGYDYTIESTIVNGCQNGRRMGFPTANLDVNgcRQLLPAAGVYAVTVRLKDSVGWKrGMMNIGKRPTFNGTTTS 269
Cdd:TIGR00083 159 ELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLK--NQVLPLKGGYYVVVVLLNGEPYP-GVGNIGNRPTFIGQQLV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 913019572 270 MEVNLFNFTGNLYGQELLVSFISKIRDERRFDSLDALSAQLMQDRDSVNRLF 321
Cdd:TIGR00083 236 IEVHLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWF 287
|
|
| FAD_synthetase_N |
cd02064 |
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ... |
30-209 |
1.84e-70 |
|
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: 217.02 E-value: 1.84e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 30 VATIGFFDGVHRGHQFLIGRVRDEAERSGMASAVITFDLHPRQVLQAGYQPQLLSTLDGKLLLLSKTRVDNIIVLHFDES 109
Cdd:cd02064 2 VVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPDKAPPRLTTLEEKLELLESLGVDYLLVLPFDKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 110 LAALPAREFMKEVLyRQLNVKKLIIGYDNRFGHNRSEGFEHYVQYGRELGIEVILADAFLPDDEKVSSSVIRNHIQQGEI 189
Cdd:cd02064 82 FASLSAEEFVEDLL-VKLNAKHVVVGFDFRFGKGRSGDAELLKELGKKYGFEVTVVPPVTLDGERVSSTRIREALAEGDV 160
|
170 180
....*....|....*....|
gi 913019572 190 EAANRLLGYDYTIESTIVNG 209
Cdd:cd02064 161 ELANELLGRPYSIEGRVVHG 180
|
|
| FAD_syn |
pfam06574 |
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ... |
30-178 |
2.54e-54 |
|
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: 175.06 E-value: 2.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 30 VATIGFFDGVHRGHQFLIGRVRDEAERSGMASAVITFDLHPRQVLQAGYQPQLLSTLDGKLLLLSKTRVDNIIVLHFDES 109
Cdd:pfam06574 9 VVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNPDSAPFRLTTLEEKIELLAELGVDYLLVLPFTKE 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 913019572 110 LAALPAREFMKEVLYRQLNVKKLIIGYDNRFGHNRSEGFEHYVQYGRELGIEVILADAFLPDDEKVSSS 178
Cdd:pfam06574 89 FASLSAEEFIENVLVDGLNVKHVVVGFDFRFGKGRKGDVELLKELGAKLGFEVTIVPPVELDGEKISST 157
|
|
| Flavokinase |
pfam01687 |
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ... |
196-321 |
2.62e-50 |
|
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: 163.32 E-value: 2.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 196 LGYDYTIESTIVNGCQNGRRMGFPTANLDVNgcRQLLPAAGVYAVTVRLKDSVGWKrGMMNIGKRPTFNGTTTSMEVNLF 275
Cdd:pfam01687 1 LGRPYSISGKVVHGDGRGRTLGFPTANLPLP--EKLLPANGVYAVWVRVDGGKVYP-GVANIGTNPTFGNGKLTVEVHIL 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 913019572 276 NFTGNLYGQELLVSFISKIRDERRFDSLDALSAQLMQDRDSVNRLF 321
Cdd:pfam01687 78 DFDGDLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQARAIL 123
|
|
| Flavokinase |
smart00904 |
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ... |
195-322 |
4.76e-47 |
|
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: 154.90 E-value: 4.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 195 LLGYDYTIESTIVNGCQNGRRMGFPTANLDVNGcRQLLPAAGVYAVTVRLKDsvGWKRGMMNIGKRPTFNGTTTsMEVNL 274
Cdd:smart00904 1 LLGRPYSISGRVVHGDKRGRTLGFPTANLPLDD-RLLLPKNGVYAVRVRVDG--KIYPGVANIGTRPTFGGDRS-VEVHI 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 913019572 275 FNFTGNLYGQELLVSFISKIRDERRFDSLDALSAQLMQDRDSVNRLFD 322
Cdd:smart00904 77 LDFSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYLA 124
|
|
| PRK07143 |
PRK07143 |
hypothetical protein; Provisional |
33-207 |
9.31e-15 |
|
hypothetical protein; Provisional
Pssm-ID: 235946 [Multi-domain] Cd Length: 279 Bit Score: 73.11 E-value: 9.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 33 IGFFDGVHRGHQFLIGRVRDEAERsgmasAVITFDLHPRQVLQagYQPQLLSTLDGKLLLLSKTRVDNIIVLHFDESLAA 112
Cdd:PRK07143 21 LGGFESFHLGHLELFKKAKESNDE-----IVIVIFKNPENLPK--NTNKKFSDLNSRLQTLANLGFKNIILLDFNEELQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 113 LPAREFMKEVLyrQLNVKKLIIGYDNRFGHNRSEGFEHYvqygRELGIEVILADAFLPDDEKVSSSVIRNHIQQGEIEAA 192
Cdd:PRK07143 94 LSGNDFIEKLT--KNQVSFFVVGKDFRFGKNASWNADDL----KEYFPNVHIVEILKINQQKISTSLLKEFIEFGDIELL 167
|
170
....*....|....*
gi 913019572 193 NRLLGYDYTIESTIV 207
Cdd:PRK07143 168 NSLLLYNYSISITIN 182
|
|
| PLN02940 |
PLN02940 |
riboflavin kinase |
202-322 |
1.30e-09 |
|
riboflavin kinase
Pssm-ID: 178528 [Multi-domain] Cd Length: 382 Bit Score: 58.69 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 202 IESTIVNGCQNGRR-MGFPTANLDVNGCRQLLPA--AGVYavtvrlkdsVGW----KRGM----MNIGKRPTFNGTTTSM 270
Cdd:PLN02940 241 IGGPVIKGFGRGSKvLGIPTANLSTENYSDVLSEhpSGVY---------FGWaglsTRGVykmvMSIGWNPYFNNTEKTI 311
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 913019572 271 EVNLF-NFTGNLYGQELLVSFISKIRDERRFDSLDALSAQLMQDRDSVNRLFD 322
Cdd:PLN02940 312 EPWLLhDFGEDFYGEELRLVIVGYIRPEANFPSLESLIAKIHEDRRIAEKALD 364
|
|
| cytidylyltransferase_like |
cd02039 |
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ... |
30-182 |
3.68e-05 |
|
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: 43.20 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 30 VATIGFFDGVHRGHQFLIGRVRDEAERSGMasaVITFDlHPRQVLqagyQPQLLSTLDGKLLLLSK--TRVDNIIVLHFD 107
Cdd:cd02039 2 GIIIGRFEPFHLGHLKLIKEALEEALDEVI---IIIVS-NPPKKK----RNKDPFSLHERVEMLKEilKDRLKVVPVDFP 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 913019572 108 ESLAALPAREFMKEVLyrQLNVKKLIIGYDNRFGHNRSEG---FEHYvqygreLGIEVILADAFLpDDEKVSSSVIRN 182
Cdd:cd02039 74 EVKILLAVVFILKILL--KVGPDKVVVGEDFAFGKNASYNkdlKELF------LDIEIVEVPRVR-DGKKISSTLIRE 142
|
|
| PBP1_ABC_HAAT-like |
cd19988 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
124-220 |
5.92e-03 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids or peptides; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.
Pssm-ID: 380643 [Multi-domain] Cd Length: 302 Bit Score: 38.03 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 124 YRQLNVKKLIIGYDN-RFGhnRSeGFEHYVQYGRELGIEVILADAFLPDDEKVSSSVIRnhIQQGEIEAanrLLGYDYTI 202
Cdd:cd19988 131 FEKLKVTKIAVLYVNdDYG--RG-GIDAFKDAAKKYGIEVVVEESYNRGDKDFSPQLEK--IKDSGAQA---IVMWGQYT 202
|
90
....*....|....*...
gi 913019572 203 ESTIVngCQNGRRMGFPT 220
Cdd:cd19988 203 EGALI--AKQARELGLKQ 218
|
|
| cyt_tran_rel |
TIGR00125 |
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
30-56 |
8.51e-03 |
|
cytidyltransferase-like domain; 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. Many of these proteins are known to use CTP or ATP and release pyrophosphate.
Pssm-ID: 272920 [Multi-domain] Cd Length: 66 Bit Score: 34.59 E-value: 8.51e-03
10 20
....*....|....*....|....*..
gi 913019572 30 VATIGFFDGVHRGHQFLIGRVRDEAER 56
Cdd:TIGR00125 2 VIFVGTFDPFHLGHLDLLERAKELFDE 28
|
|
|