|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04180 |
PRK04180 |
pyridoxal 5'-phosphate synthase lyase subunit PdxS; |
6-294 |
0e+00 |
|
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
Pssm-ID: 179769 Cd Length: 293 Bit Score: 567.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 6 TGTDRVKRGMAEMQKGGVIMDVINAEQARIAEAAGAVAVMALERVPSDIRAAGGVARMADPRITEEVMNAVTIPVMAKAR 85
Cdd:PRK04180 3 TGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 86 IGHISEARMLEAMGVDYIDESEVLTPADEEYHLIKSNFTVPFVCGNKDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRH 165
Cdd:PRK04180 83 IGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 166 LRKLNAQVRKIIHMNEDELMTEAKILGAPYHVLLEIKHLGRLPVVNFAAGGVATPADAALMMELGADGVFVGSGIFKSDN 245
Cdd:PRK04180 163 MRQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSGD 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 518242335 246 PEKFARAIVEATTHYQDYKLLVEISKDLGVPMKGIEISRLESKDRMQDR 294
Cdd:PRK04180 243 PEKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDELPPEERLQER 291
|
|
| PdxS |
COG0214 |
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ... |
6-294 |
0e+00 |
|
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5'-phosphate synthase subunit PdxS is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 439984 Cd Length: 293 Bit Score: 559.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 6 TGTDRVKRGMAEMQKGGVIMDVINAEQARIAEAAGAVAVMALERVPSDIRAAGGVARMADPRITEEVMNAVTIPVMAKAR 85
Cdd:COG0214 3 TGTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAKVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 86 IGHISEARMLEAMGVDYIDESEVLTPADEEYHLIKSNFTVPFVCGNKDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRH 165
Cdd:COG0214 83 IGHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAVRH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 166 LRKLNAQVRKIIHMNEDELMTEAKILGAPYHVLLEIKHLGRLPVVNFAAGGVATPADAALMMELGADGVFVGSGIFKSDN 245
Cdd:COG0214 163 MRTINSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSED 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 518242335 246 PEKFARAIVEATTHYQDYKLLVEISKDLGVPMKGIEISRLESKDRMQDR 294
Cdd:COG0214 243 PEKRARAIVEATTHYDDPEVLAEVSEGLGEAMKGIDISTLPEEERLQER 291
|
|
| pdxS |
cd04727 |
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ... |
13-294 |
0e+00 |
|
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in deoxyxylulose 5-phosphate (DXP)-independent pathway for de novo biosynthesis of PLP, present in some eubacteria, in archaea, fungi, plants, plasmodia, and some metazoa. Together with PdxT, PdxS forms the PLP synthase, a heteromeric glutamine amidotransferase (GATase), whereby PdxT produces ammonia from glutamine and PdxS combines ammonia with five- and three-carbon phosphosugars to form PLP. PLP is the biologically active form of vitamin B6, an essential cofactor in many biochemical processes. PdxS subunits form two hexameric rings.
Pssm-ID: 240078 Cd Length: 283 Bit Score: 517.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 13 RGMAEMQKGGVIMDVINAEQARIAEAAGAVAVMALERVPSDIRAAGGVARMADPRITEEVMNAVTIPVMAKARIGHISEA 92
Cdd:cd04727 1 RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 93 RMLEAMGVDYIDESEVLTPADEEYHLIKSNFTVPFVCGNKDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRHLRKLNAQ 172
Cdd:cd04727 81 QILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 173 VRKIIHMNEDELMTEAKILGAPYHVLLEIKHLGRLPVVNFAAGGVATPADAALMMELGADGVFVGSGIFKSDNPEKFARA 252
Cdd:cd04727 161 IRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 518242335 253 IVEATTHYQDYKLLVEISKDLGVPMKGIEISRLESKDRMQDR 294
Cdd:cd04727 241 IVEAVTHYDDPEILAEVSEGLGEAMVGIDIASLKEEERMQER 282
|
|
| TIGR00343 |
TIGR00343 |
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a ... |
11-294 |
2.51e-171 |
|
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a singlet oxygen resistance protein. Subsequent work showed that it is a protein of pyridoxine (vitamin B6) biosynthesis, and that pyridoxine quenches the highly toxic singlet form of oxygen produced by light in the presence of certain chemicals. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 129443 Cd Length: 287 Bit Score: 475.41 E-value: 2.51e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 11 VKRGMAEMQKGGVIMDVINAEQARIAEAAGAVAVMALERVPSDIRAAGGVARMADPRITEEVMNAVTIPVMAKARIGHIS 90
Cdd:TIGR00343 1 LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 91 EARMLEAMGVDYIDESEVLTPADEEYHLIKSNFTVPFVCGNKDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRHLRKLN 170
Cdd:TIGR00343 81 EAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 171 AQVRKIIHMN-EDELMTEAKILGAPYHVLLEIKHLGRLPVVNFAAGGVATPADAALMMELGADGVFVGSGIFKSDNPEKF 249
Cdd:TIGR00343 161 EEIRQIQNMLeEEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 518242335 250 ARAIVEATTHYQDYKLLVEISKDLGVPMKGIEISRLESKDRMQDR 294
Cdd:TIGR00343 241 AKAIVEATTHYDNPEKLAEVSKDLGEAMKGISISSISEAERLQER 285
|
|
| SOR_SNZ |
pfam01680 |
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ... |
8-213 |
2.03e-139 |
|
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine/pyridoxal 5-phosphate biosynthesis. This family was formerly known as UPF0019.
Pssm-ID: 460291 Cd Length: 206 Bit Score: 391.46 E-value: 2.03e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 8 TDRVKRGMAEMQKGGVIMDVINAEQARIAEAAGAVAVMALERVPSDIRAAGGVARMADPRITEEVMNAVTIPVMAKARIG 87
Cdd:pfam01680 1 TFRVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 88 HISEARMLEAMGVDYIDESEVLTPADEEYHLIKSNFTVPFVCGNKDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRHLR 167
Cdd:pfam01680 81 HFVEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518242335 168 KLNAQVRKIIHMNEDELMTEAKILGAPYHVLLEIKHLGRLPVVNFA 213
Cdd:pfam01680 161 TINGEIRRLQNMDEEELYAFAKELGAPYELVKEVAELGRLPVVNFA 206
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04180 |
PRK04180 |
pyridoxal 5'-phosphate synthase lyase subunit PdxS; |
6-294 |
0e+00 |
|
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
Pssm-ID: 179769 Cd Length: 293 Bit Score: 567.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 6 TGTDRVKRGMAEMQKGGVIMDVINAEQARIAEAAGAVAVMALERVPSDIRAAGGVARMADPRITEEVMNAVTIPVMAKAR 85
Cdd:PRK04180 3 TGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 86 IGHISEARMLEAMGVDYIDESEVLTPADEEYHLIKSNFTVPFVCGNKDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRH 165
Cdd:PRK04180 83 IGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 166 LRKLNAQVRKIIHMNEDELMTEAKILGAPYHVLLEIKHLGRLPVVNFAAGGVATPADAALMMELGADGVFVGSGIFKSDN 245
Cdd:PRK04180 163 MRQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSGD 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 518242335 246 PEKFARAIVEATTHYQDYKLLVEISKDLGVPMKGIEISRLESKDRMQDR 294
Cdd:PRK04180 243 PEKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDELPPEERLQER 291
|
|
| PdxS |
COG0214 |
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ... |
6-294 |
0e+00 |
|
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5'-phosphate synthase subunit PdxS is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 439984 Cd Length: 293 Bit Score: 559.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 6 TGTDRVKRGMAEMQKGGVIMDVINAEQARIAEAAGAVAVMALERVPSDIRAAGGVARMADPRITEEVMNAVTIPVMAKAR 85
Cdd:COG0214 3 TGTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAKVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 86 IGHISEARMLEAMGVDYIDESEVLTPADEEYHLIKSNFTVPFVCGNKDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRH 165
Cdd:COG0214 83 IGHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAVRH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 166 LRKLNAQVRKIIHMNEDELMTEAKILGAPYHVLLEIKHLGRLPVVNFAAGGVATPADAALMMELGADGVFVGSGIFKSDN 245
Cdd:COG0214 163 MRTINSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSED 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 518242335 246 PEKFARAIVEATTHYQDYKLLVEISKDLGVPMKGIEISRLESKDRMQDR 294
Cdd:COG0214 243 PEKRARAIVEATTHYDDPEVLAEVSEGLGEAMKGIDISTLPEEERLQER 291
|
|
| pdxS |
cd04727 |
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ... |
13-294 |
0e+00 |
|
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in deoxyxylulose 5-phosphate (DXP)-independent pathway for de novo biosynthesis of PLP, present in some eubacteria, in archaea, fungi, plants, plasmodia, and some metazoa. Together with PdxT, PdxS forms the PLP synthase, a heteromeric glutamine amidotransferase (GATase), whereby PdxT produces ammonia from glutamine and PdxS combines ammonia with five- and three-carbon phosphosugars to form PLP. PLP is the biologically active form of vitamin B6, an essential cofactor in many biochemical processes. PdxS subunits form two hexameric rings.
Pssm-ID: 240078 Cd Length: 283 Bit Score: 517.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 13 RGMAEMQKGGVIMDVINAEQARIAEAAGAVAVMALERVPSDIRAAGGVARMADPRITEEVMNAVTIPVMAKARIGHISEA 92
Cdd:cd04727 1 RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 93 RMLEAMGVDYIDESEVLTPADEEYHLIKSNFTVPFVCGNKDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRHLRKLNAQ 172
Cdd:cd04727 81 QILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 173 VRKIIHMNEDELMTEAKILGAPYHVLLEIKHLGRLPVVNFAAGGVATPADAALMMELGADGVFVGSGIFKSDNPEKFARA 252
Cdd:cd04727 161 IRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 518242335 253 IVEATTHYQDYKLLVEISKDLGVPMKGIEISRLESKDRMQDR 294
Cdd:cd04727 241 IVEAVTHYDDPEILAEVSEGLGEAMVGIDIASLKEEERMQER 282
|
|
| TIGR00343 |
TIGR00343 |
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a ... |
11-294 |
2.51e-171 |
|
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a singlet oxygen resistance protein. Subsequent work showed that it is a protein of pyridoxine (vitamin B6) biosynthesis, and that pyridoxine quenches the highly toxic singlet form of oxygen produced by light in the presence of certain chemicals. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 129443 Cd Length: 287 Bit Score: 475.41 E-value: 2.51e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 11 VKRGMAEMQKGGVIMDVINAEQARIAEAAGAVAVMALERVPSDIRAAGGVARMADPRITEEVMNAVTIPVMAKARIGHIS 90
Cdd:TIGR00343 1 LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 91 EARMLEAMGVDYIDESEVLTPADEEYHLIKSNFTVPFVCGNKDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRHLRKLN 170
Cdd:TIGR00343 81 EAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 171 AQVRKIIHMN-EDELMTEAKILGAPYHVLLEIKHLGRLPVVNFAAGGVATPADAALMMELGADGVFVGSGIFKSDNPEKF 249
Cdd:TIGR00343 161 EEIRQIQNMLeEEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 518242335 250 ARAIVEATTHYQDYKLLVEISKDLGVPMKGIEISRLESKDRMQDR 294
Cdd:TIGR00343 241 AKAIVEATTHYDNPEKLAEVSKDLGEAMKGISISSISEAERLQER 285
|
|
| SOR_SNZ |
pfam01680 |
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ... |
8-213 |
2.03e-139 |
|
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine/pyridoxal 5-phosphate biosynthesis. This family was formerly known as UPF0019.
Pssm-ID: 460291 Cd Length: 206 Bit Score: 391.46 E-value: 2.03e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 8 TDRVKRGMAEMQKGGVIMDVINAEQARIAEAAGAVAVMALERVPSDIRAAGGVARMADPRITEEVMNAVTIPVMAKARIG 87
Cdd:pfam01680 1 TFRVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 88 HISEARMLEAMGVDYIDESEVLTPADEEYHLIKSNFTVPFVCGNKDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRHLR 167
Cdd:pfam01680 81 HFVEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518242335 168 KLNAQVRKIIHMNEDELMTEAKILGAPYHVLLEIKHLGRLPVVNFA 213
Cdd:pfam01680 161 TINGEIRRLQNMDEEELYAFAKELGAPYELVKEVAELGRLPVVNFA 206
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
30-238 |
1.79e-09 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 56.44 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 30 AEQARIAEAAGAVAVMALERVPSDIRAAGgvarmADPRITEEVMNAVTIPVMAKARIGHISE-----ARMLEAMGVDYID 104
Cdd:cd04722 15 VELAKAAAEAGADAIIVGTRSSDPEEAET-----DDKEVLKEVAAETDLPLGVQLAINDAAAavdiaAAAARAAGADGVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 105 ESEVLTPADEEYH-----LIKSNFTVPFV--CGNKDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRHLrklnaqvrkii 177
Cdd:cd04722 90 IHGAVGYLAREDLelireLREAVPDVKVVvkLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIA----------- 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518242335 178 hmnedelmteakilgapyhVLLEIKHLGRLPVVNFAAGGVATPADAALMMELGADGVFVGS 238
Cdd:cd04722 159 -------------------DLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| thiG |
CHL00162 |
thiamin biosynthesis protein G; Validated |
117-253 |
3.51e-07 |
|
thiamin biosynthesis protein G; Validated
Pssm-ID: 214380 Cd Length: 267 Bit Score: 50.48 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 117 HLIKSNFTV-PFVCGNKDLGEAARRIGEGASMlrTKGEP-GTGnivEAVRHLRKLnaqvrKIIHMNedelmteAKIlgap 194
Cdd:CHL00162 132 FLVKKGFTVlPYINADPMLAKHLEDIGCATVM--PLGSPiGSG---QGLQNLLNL-----QIIIEN-------AKI---- 190
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 518242335 195 yhvlleikhlgrlPVVNFAagGVATPADAALMMELGADGVFVGSGIFKSDNPEKFARAI 253
Cdd:CHL00162 191 -------------PVIIDA--GIGTPSEASQAMELGASGVLLNTAVAQAKNPEQMAKAM 234
|
|
| thiG |
PRK00208 |
thiazole synthase; Reviewed |
216-256 |
1.52e-06 |
|
thiazole synthase; Reviewed
Pssm-ID: 234687 Cd Length: 250 Bit Score: 48.52 E-value: 1.52e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 518242335 216 GVATPADAALMMELGADGVFVGSGIFKSDNPEKFARAI---VEA 256
Cdd:PRK00208 183 GIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFklaVEA 226
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
198-255 |
1.57e-06 |
|
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.
Pssm-ID: 238317 [Multi-domain] Cd Length: 196 Bit Score: 47.90 E-value: 1.57e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 518242335 198 LLEIKHLGRLPVVnfAAGGVaTPADAALMMELGADGVFVGSGIFKSDNPEKFARAIVE 255
Cdd:cd00564 142 LREIAELVEIPVV--AIGGI-TPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
|
|
| ThiG |
cd04728 |
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ... |
216-256 |
2.01e-06 |
|
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the thiazole moiety of thiamin pyrophosphate, an essential ubiquitous cofactor that plays an important role in carbohydrate and amino acid metabolism. ThiG catalyzes the formation of thiazole from 1-deoxy-D-xylulose 5-phosphate (DXP) and dehydroglycine, with the help of the sulfur carrier protein ThiS that carries the sulfur needed for thiazole assembly on its carboxy terminus (ThiS-COSH).
Pssm-ID: 240079 Cd Length: 248 Bit Score: 47.87 E-value: 2.01e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 518242335 216 GVATPADAALMMELGADGVFVGSGIFKSDNPEKFARAI---VEA 256
Cdd:cd04728 183 GIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFklaVEA 226
|
|
| PRK11840 |
PRK11840 |
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional |
194-256 |
2.17e-06 |
|
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
Pssm-ID: 236998 [Multi-domain] Cd Length: 326 Bit Score: 48.20 E-value: 2.17e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518242335 194 PYHVLLeIKHLGRLPVVNFAagGVATPADAALMMELGADGVFVGSGIFKSDNPEKFARAI---VEA 256
Cdd:PRK11840 238 PYTIRL-IVEGATVPVLVDA--GVGTASDAAVAMELGCDGVLMNTAIAEAKNPVLMARAMklaVEA 300
|
|
| ThiG |
pfam05690 |
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ... |
194-256 |
5.06e-06 |
|
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole biosynthesis protein G sequences. ThiG, together with ThiF and ThiH, is proposed to be involved in the synthesis of 4-methyl-5-(b-hydroxyethyl)thiazole (THZ) which is an intermediate in the thiazole production pathway. This family also includes triosephosphate isomerase and pyridoxal 5'-phosphate synthase subunit PdxS.
Pssm-ID: 428589 Cd Length: 247 Bit Score: 46.86 E-value: 5.06e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518242335 194 PYHVLLEIKHLgRLPVVNFAagGVATPADAALMMELGADGVFVGSGIFKSDNPEKFARAI---VEA 256
Cdd:pfam05690 164 PYNLKIIIEEA-DVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFklaVEA 226
|
|
| IGPS |
cd00331 |
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
213-253 |
7.57e-06 |
|
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, catalyzing the ring closure reaction of 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate (CdRP) to indole-3-glycerol phosphate (IGP), accompanied by the release of carbon dioxide and water. IGPS is active as a separate monomer in most organisms, but is also found fused to other enzymes as part of a bifunctional or multifunctional enzyme involved in tryptophan biosynthesis.
Pssm-ID: 238203 Cd Length: 217 Bit Score: 45.92 E-value: 7.57e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 518242335 213 AAGGVATPADAALMMELGADGVFVGSGIFKSDNPEKFARAI 253
Cdd:cd00331 177 SESGISTPEDVKRLAEAGADAVLIGESLMRAPDPGAALREL 217
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
200-280 |
3.99e-05 |
|
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.
Pssm-ID: 240081 [Multi-domain] Cd Length: 236 Bit Score: 44.01 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 200 EIKHLGRLPVVnfAAGGVATPADAALMMELGADGVFVGSgIF----KSDNPEKFARAIVEATTHYqdyklLVEISKDLGV 275
Cdd:cd04730 150 EVRDAVDIPVI--AAGGIADGRGIAAALALGADGVQMGT-RFlateESGASPAYKQALLAATAED-----TVLTRAFSGR 221
|
....*
gi 518242335 276 PMKGI 280
Cdd:cd04730 222 PARGL 226
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
200-260 |
1.00e-04 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 42.48 E-value: 1.00e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518242335 200 EIKHLGR-LPVVnfAAGGVaTPADAALMMELGADGVFVGSGIFKSDNPEKFARAIVEATTHY 260
Cdd:PRK00043 153 EIRAAVGdIPIV--AIGGI-TPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAA 211
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
30-141 |
1.29e-04 |
|
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439812 [Multi-domain] Cd Length: 310 Bit Score: 42.77 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 30 AEQARIAEAAGAVAVmalervpsDI----------RAAGGVARMADP----RITEEVMNAVTIPVMAKARIG--HISE-- 91
Cdd:COG0042 77 AEAARIAEELGADEI--------DInmgcpvkkvtKGGAGAALLRDPelvaEIVKAVVEAVDVPVTVKIRLGwdDDDEna 148
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518242335 92 ---ARMLEAMGVDyideseVLT------------PADEEY-HLIKSNFTVPfVCGNKDL--GEAARRI 141
Cdd:COG0042 149 lefARIAEDAGAA------ALTvhgrtreqrykgPADWDAiARVKEAVSIP-VIGNGDIfsPEDAKRM 209
|
|
| trpC |
PRK00278 |
indole-3-glycerol phosphate synthase TrpC; |
216-256 |
2.21e-04 |
|
indole-3-glycerol phosphate synthase TrpC;
Pssm-ID: 234710 Cd Length: 260 Bit Score: 42.07 E-value: 2.21e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 518242335 216 GVATPADAALMMELGADGVFVGSGIFKSDNPEKFARAIVEA 256
Cdd:PRK00278 219 GIFTPEDLKRLAKAGADAVLVGESLMRADDPGAALRELLGA 259
|
|
| PRK07028 |
PRK07028 |
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated |
159-256 |
3.12e-04 |
|
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
Pssm-ID: 235912 [Multi-domain] Cd Length: 430 Bit Score: 41.93 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 159 IVEAVRHLRKLNAQVRK--IIHMNEDELMTEAKILGAPY---HVLLEIKHLGRLPV-----------VNFAAGGVATPAD 222
Cdd:PRK07028 96 IEDAVRAARKYGVRLMAdlINVPDPVKRAVELEELGVDYinvHVGIDQQMLGKDPLellkevseevsIPIAVAGGLDAET 175
|
90 100 110
....*....|....*....|....*....|....
gi 518242335 223 AALMMELGADGVFVGSGIFKSDNPEKFARAIVEA 256
Cdd:PRK07028 176 AAKAVAAGADIVIVGGNIIKSADVTEAARKIREA 209
|
|
| PRK07695 |
PRK07695 |
thiazole tautomerase TenI; |
196-256 |
7.23e-04 |
|
thiazole tautomerase TenI;
Pssm-ID: 181086 [Multi-domain] Cd Length: 201 Bit Score: 40.00 E-value: 7.23e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518242335 196 HVLLEIKHLGRLPVVnfAAGGVaTPADAALMMELGADGVFVGSGIFKSDNPEKFARAIVEA 256
Cdd:PRK07695 139 EELSDIARALSIPVI--AIGGI-TPENTRDVLAAGVSGIAVMSGIFSSANPYSKAKRYAES 196
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
212-256 |
1.10e-03 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 39.47 E-value: 1.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 518242335 212 FAAGGVATPADAALMMELGADGVFVGSGIFKSDNPEKFARAIVEA 256
Cdd:PRK04302 177 LCGAGISTGEDVKAALELGADGVLLASGVVKAKDPEAALRDLVSP 221
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
195-240 |
2.28e-03 |
|
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.
Pssm-ID: 240080 [Multi-domain] Cd Length: 219 Bit Score: 38.71 E-value: 2.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 518242335 195 YHVLLEIKHLGRLPVVnfAAGGVATPADAALMMELGADGVFVGSGI 240
Cdd:cd04729 166 FELLKELRKALGIPVI--AEGRINSPEQAAKALELGADAVVVGSAI 209
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
195-240 |
2.35e-03 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 38.59 E-value: 2.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 518242335 195 YHVLLEIKHLGRLPVVnfAAGGVATPADAALMMELGADGVFVGSGI 240
Cdd:PRK01130 162 FALLKELLKAVGCPVI--AEGRINTPEQAKKALELGAHAVVVGGAI 205
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
176-253 |
2.74e-03 |
|
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates.
Pssm-ID: 240077 [Multi-domain] Cd Length: 202 Bit Score: 38.33 E-value: 2.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518242335 176 IIHMNEDElmtEAKILGAPYHVLLEIKHLGRLPVVnfAAGGVaTPADAALMMELGADGVFVGSGIFKSDNPEKFARAI 253
Cdd:cd04726 131 ILHRGIDA---QAAGGWWPEDDLKKVKKLLGVKVA--VAGGI-TPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
206-257 |
3.82e-03 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 38.17 E-value: 3.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 518242335 206 RLPVVnfAAGGVATPADAALMMELGADGVFVGSGiF----KSDNPEKFARAIVEAT 257
Cdd:COG2070 158 DIPVI--AAGGIADGRGIAAALALGADGVQMGTR-FlateESPAHEAYKQALVDAK 210
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
30-103 |
4.00e-03 |
|
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.
Pssm-ID: 426126 Cd Length: 309 Bit Score: 38.08 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 30 AEQARIAEAAGAVAVMALERVPSD--IRAAGGVARMADP----RITEEVMNAVTIPVMAKARIG--HISE-----ARMLE 96
Cdd:pfam01207 69 AEAAKLVEDRGADGIDINMGCPSKkvTRGGGGAALLRNPdlvaQIVKAVVKAVGIPVTVKIRIGwdDSHEnaveiAKIVE 148
|
....*..
gi 518242335 97 AMGVDYI 103
Cdd:pfam01207 149 DAGAQAL 155
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
207-242 |
4.40e-03 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 37.96 E-value: 4.40e-03
10 20 30
....*....|....*....|....*....|....*.
gi 518242335 207 LPVVnfAAGGVATPADAALMMELGADGVFVGSGIFK 242
Cdd:PRK13585 194 IPVI--ASGGVTTLDDLRALKEAGAAGVVVGSALYK 227
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
205-262 |
5.15e-03 |
|
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439937 [Multi-domain] Cd Length: 296 Bit Score: 37.74 E-value: 5.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 518242335 205 GRLPVVnfAAGGVATPADAALMMELGADGVFVGSGIFKsDNPEKFARaIVEATTHYQD 262
Cdd:COG0167 235 GDIPII--GVGGISTAEDALEFILAGASAVQVGTALFY-EGPGLVRR-IIRGLEAYLE 288
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
202-239 |
6.75e-03 |
|
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.
Pssm-ID: 238223 [Multi-domain] Cd Length: 325 Bit Score: 37.50 E-value: 6.75e-03
10 20 30
....*....|....*....|....*....|....*...
gi 518242335 202 KHLGRLPVVnfaAGGVATPADAALMMELGADGVFVGSG 239
Cdd:cd00381 131 KKYPNVDVI---AGNVVTAEAARDLIDAGADGVKVGIG 165
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
30-145 |
9.82e-03 |
|
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.
Pssm-ID: 239200 [Multi-domain] Cd Length: 231 Bit Score: 36.70 E-value: 9.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518242335 30 AEQARIAEAAGAVAV---MAlerVPSD--IRAAGGVARMADP----RITEEVMNAVTIPVMAKARIGHISE------ARM 94
Cdd:cd02801 70 AEAAKIVEELGADGIdlnMG---CPSPkvTKGGAGAALLKDPelvaEIVRAVREAVPIPVTVKIRLGWDDEeetlelAKA 146
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518242335 95 LEAMGVDYI-------DESEVlTPADEEY-HLIKSNFTVPFVcGN---KDLGEAARR----------IGEGA 145
Cdd:cd02801 147 LEDAGASALtvhgrtrEQRYS-GPADWDYiAEIKEAVSIPVI-ANgdiFSLEDALRCleqtgvdgvmIGRGA 216
|
|
| |
