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Conserved domains on  [gi|1827344640|ref|WP_167316877|]
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pyridoxal 5'-phosphate synthase lyase subunit PdxS [Bacillus cereus]

Protein Classification

pyridoxal 5'-phosphate synthase subunit PdxS( domain architecture ID 10012155)

pyridoxal 5'-phosphate synthase subunit PdxS combines ammonia with five- and three-carbon phosphosugars to form pyridoxal 5'-phosphate (PLP)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK04180 PRK04180
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
4-295 0e+00

pyridoxal 5'-phosphate synthase lyase subunit PdxS;


:

Pssm-ID: 179769  Cd Length: 293  Bit Score: 604.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640   4 VTGTERVKRGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMGAVSIPVMAKC 83
Cdd:PRK04180    2 ETGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640  84 RIGHLVEARVLESLGVDYIDESEVLTPADEVYHLNKRDYTVPFVCGCRDIGEAARRIAEGASMLRTKGEPGTGNIVEAVR 163
Cdd:PRK04180   82 RIGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640 164 HMRQVNAEIRQVASLREDELMTYAKNTGAPYEVLLEIKHLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSE 243
Cdd:PRK04180  162 HMRQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSG 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1827344640 244 NPEKFARAIVEATTHYEDYELIASLSKGLGNAMKGVEISTLLPEQRMQERGW 295
Cdd:PRK04180  242 DPEKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDELPPEERLQERGW 293
 
Name Accession Description Interval E-value
PRK04180 PRK04180
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
4-295 0e+00

pyridoxal 5'-phosphate synthase lyase subunit PdxS;


Pssm-ID: 179769  Cd Length: 293  Bit Score: 604.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640   4 VTGTERVKRGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMGAVSIPVMAKC 83
Cdd:PRK04180    2 ETGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640  84 RIGHLVEARVLESLGVDYIDESEVLTPADEVYHLNKRDYTVPFVCGCRDIGEAARRIAEGASMLRTKGEPGTGNIVEAVR 163
Cdd:PRK04180   82 RIGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640 164 HMRQVNAEIRQVASLREDELMTYAKNTGAPYEVLLEIKHLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSE 243
Cdd:PRK04180  162 HMRQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSG 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1827344640 244 NPEKFARAIVEATTHYEDYELIASLSKGLGNAMKGVEISTLLPEQRMQERGW 295
Cdd:PRK04180  242 DPEKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDELPPEERLQERGW 293
PdxS COG0214
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ...
 5-295 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: 591.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640   5 TGTERVKRGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMGAVSIPVMAKCR 84
Cdd:COG0214     3 TGTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAKVR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640  85 IGHLVEARVLESLGVDYIDESEVLTPADEVYHLNKRDYTVPFVCGCRDIGEAARRIAEGASMLRTKGEPGTGNIVEAVRH 164
Cdd:COG0214    83 IGHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAVRH 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640 165 MRQVNAEIRQVASLREDELMTYAKNTGAPYEVLLEIKHLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSEN 244
Cdd:COG0214   163 MRTINSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSED 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1827344640 245 PEKFARAIVEATTHYEDYELIASLSKGLGNAMKGVEISTLLPEQRMQERGW 295
Cdd:COG0214   243 PEKRARAIVEATTHYDDPEVLAEVSEGLGEAMKGIDISTLPEEERLQERGW 293
pdxS cd04727
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ...
 12-294 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: 539.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640  12 RGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMGAVSIPVMAKCRIGHLVEA 91
Cdd:cd04727     1 RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640  92 RVLESLGVDYIDESEVLTPADEVYHLNKRDYTVPFVCGCRDIGEAARRIAEGASMLRTKGEPGTGNIVEAVRHMRQVNAE 171
Cdd:cd04727    81 QILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640 172 IRQVASLREDELMTYAKNTGAPYEVLLEIKHLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKFARA 251
Cdd:cd04727   161 IRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARA 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1827344640 252 IVEATTHYEDYELIASLSKGLGNAMKGVEISTLLPEQRMQERG 294
Cdd:cd04727   241 IVEAVTHYDDPEILAEVSEGLGEAMVGIDIASLKEEERMQERG 283
TIGR00343 TIGR00343
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a ...
 10-295 0e+00

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: 504.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640  10 VKRGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMGAVSIPVMAKCRIGHLV 89
Cdd:TIGR00343   1 LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640  90 EARVLESLGVDYIDESEVLTPADEVYHLNKRDYTVPFVCGCRDIGEAARRIAEGASMLRTKGEPGTGNIVEAVRHMRQVN 169
Cdd:TIGR00343  81 EAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640 170 AEIRQV-ASLREDELMTYAKNTGAPYEVLLEIKHLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKF 248
Cdd:TIGR00343 161 EEIRQIqNMLEEEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1827344640 249 ARAIVEATTHYEDYELIASLSKGLGNAMKGVEISTLLPEQRMQERGW 295
Cdd:TIGR00343 241 AKAIVEATTHYDNPEKLAEVSKDLGEAMKGISISSISEAERLQERGW 287
SOR_SNZ pfam01680
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ...
 7-212 1.93e-147

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: 411.87  E-value: 1.93e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640   7 TERVKRGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMGAVSIPVMAKCRIG 86
Cdd:pfam01680   1 TFRVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640  87 HLVEARVLESLGVDYIDESEVLTPADEVYHLNKRDYTVPFVCGCRDIGEAARRIAEGASMLRTKGEPGTGNIVEAVRHMR 166
Cdd:pfam01680  81 HFVEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1827344640 167 QVNAEIRQVASLREDELMTYAKNTGAPYEVLLEIKHLGRLPVVNFA 212
Cdd:pfam01680 161 TINGEIRRLQNMDEEELYAFAKELGAPYELVKEVAELGRLPVVNFA 206
 
Name Accession Description Interval E-value
PRK04180 PRK04180
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
4-295 0e+00

pyridoxal 5'-phosphate synthase lyase subunit PdxS;


Pssm-ID: 179769  Cd Length: 293  Bit Score: 604.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640   4 VTGTERVKRGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMGAVSIPVMAKC 83
Cdd:PRK04180    2 ETGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640  84 RIGHLVEARVLESLGVDYIDESEVLTPADEVYHLNKRDYTVPFVCGCRDIGEAARRIAEGASMLRTKGEPGTGNIVEAVR 163
Cdd:PRK04180   82 RIGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640 164 HMRQVNAEIRQVASLREDELMTYAKNTGAPYEVLLEIKHLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSE 243
Cdd:PRK04180  162 HMRQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSG 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1827344640 244 NPEKFARAIVEATTHYEDYELIASLSKGLGNAMKGVEISTLLPEQRMQERGW 295
Cdd:PRK04180  242 DPEKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDELPPEERLQERGW 293
PdxS COG0214
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ...
 5-295 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: 591.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640   5 TGTERVKRGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMGAVSIPVMAKCR 84
Cdd:COG0214     3 TGTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAKVR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640  85 IGHLVEARVLESLGVDYIDESEVLTPADEVYHLNKRDYTVPFVCGCRDIGEAARRIAEGASMLRTKGEPGTGNIVEAVRH 164
Cdd:COG0214    83 IGHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAVRH 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640 165 MRQVNAEIRQVASLREDELMTYAKNTGAPYEVLLEIKHLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSEN 244
Cdd:COG0214   163 MRTINSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSED 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1827344640 245 PEKFARAIVEATTHYEDYELIASLSKGLGNAMKGVEISTLLPEQRMQERGW 295
Cdd:COG0214   243 PEKRARAIVEATTHYDDPEVLAEVSEGLGEAMKGIDISTLPEEERLQERGW 293
pdxS cd04727
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ...
 12-294 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: 539.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640  12 RGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMGAVSIPVMAKCRIGHLVEA 91
Cdd:cd04727     1 RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640  92 RVLESLGVDYIDESEVLTPADEVYHLNKRDYTVPFVCGCRDIGEAARRIAEGASMLRTKGEPGTGNIVEAVRHMRQVNAE 171
Cdd:cd04727    81 QILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640 172 IRQVASLREDELMTYAKNTGAPYEVLLEIKHLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKFARA 251
Cdd:cd04727   161 IRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARA 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1827344640 252 IVEATTHYEDYELIASLSKGLGNAMKGVEISTLLPEQRMQERG 294
Cdd:cd04727   241 IVEAVTHYDDPEILAEVSEGLGEAMVGIDIASLKEEERMQERG 283
TIGR00343 TIGR00343
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a ...
 10-295 0e+00

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: 504.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640  10 VKRGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMGAVSIPVMAKCRIGHLV 89
Cdd:TIGR00343   1 LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640  90 EARVLESLGVDYIDESEVLTPADEVYHLNKRDYTVPFVCGCRDIGEAARRIAEGASMLRTKGEPGTGNIVEAVRHMRQVN 169
Cdd:TIGR00343  81 EAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640 170 AEIRQV-ASLREDELMTYAKNTGAPYEVLLEIKHLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKF 248
Cdd:TIGR00343 161 EEIRQIqNMLEEEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1827344640 249 ARAIVEATTHYEDYELIASLSKGLGNAMKGVEISTLLPEQRMQERGW 295
Cdd:TIGR00343 241 AKAIVEATTHYDNPEKLAEVSKDLGEAMKGISISSISEAERLQERGW 287
SOR_SNZ pfam01680
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ...
 7-212 1.93e-147

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: 411.87  E-value: 1.93e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640   7 TERVKRGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMGAVSIPVMAKCRIG 86
Cdd:pfam01680   1 TFRVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640  87 HLVEARVLESLGVDYIDESEVLTPADEVYHLNKRDYTVPFVCGCRDIGEAARRIAEGASMLRTKGEPGTGNIVEAVRHMR 166
Cdd:pfam01680  81 HFVEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1827344640 167 QVNAEIRQVASLREDELMTYAKNTGAPYEVLLEIKHLGRLPVVNFA 212
Cdd:pfam01680 161 TINGEIRRLQNMDEEELYAFAKELGAPYELVKEVAELGRLPVVNFA 206
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 29-237 2.92e-10

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: 58.75  E-value: 2.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640  29 AEQAKIAEEAGAVAVMALERVPADIRAAGgvsrmADPTIVEEVMGAVSIPVMAKCRIGHLVE-----ARVLESLGVDYID 103
Cdd:cd04722    15 VELAKAAAEAGADAIIVGTRSSDPEEAET-----DDKEVLKEVAAETDLPLGVQLAINDAAAavdiaAAAARAAGADGVE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640 104 ESEVLTPADE-----VYHLNKRDYTVPFVCGCRDIGEAARRIAE--GASMLRTKGEPGTGNIVEAVrhmrqvnaeirqva 176
Cdd:cd04722    90 IHGAVGYLARedlelIRELREAVPDVKVVVKLSPTGELAAAAAEeaGVDEVGLGNGGGGGGGRDAV-------------- 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827344640 177 slredelmtyakntgaPYEVLLEIKHLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGS 237
Cdd:cd04722   156 ----------------PIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
thiG CHL00162
thiamin biosynthesis protein G; Validated
 205-252 9.17e-07

thiamin biosynthesis protein G; Validated


Pssm-ID: 214380  Cd Length: 267  Bit Score: 49.32  E-value: 9.17e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1827344640 205 RLPVVNFAagGVATPADAALMMQLGADGVFVGSGIFKSENPEKFARAI 252
Cdd:CHL00162  189 KIPVIIDA--GIGTPSEASQAMELGASGVLLNTAVAQAKNPEQMAKAM 234
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 195-254 1.42e-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: 1.42e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640 195 EVLLEIKHLGRLPVVnfAAGGVaTPADAALMMQLGADGVFVGSGIFKSENPEKFARAIVE 254
Cdd:cd00564   140 ELLREIAELVEIPVV--AIGGI-TPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
PRK11840 PRK11840
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
 193-255 9.61e-06

bifunctional sulfur carrier protein/thiazole synthase protein; Provisional


Pssm-ID: 236998 [Multi-domain]  Cd Length: 326  Bit Score: 46.28  E-value: 9.61e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827344640 193 PYEVLLeIKHLGRLPVVNFAagGVATPADAALMMQLGADGVFVGSGIFKSENPEKFARAI---VEA 255
Cdd:PRK11840  238 PYTIRL-IVEGATVPVLVDA--GVGTASDAAVAMELGCDGVLMNTAIAEAKNPVLMARAMklaVEA 300
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 29-245 9.73e-06

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: 46.24  E-value: 9.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640  29 AEQAKIAEEAGAVAVmalervpaDI----------RAAGGVSRMADP----TIVEEVMGAVSIPVMAKCRIGhlvearvl 94
Cdd:COG0042    77 AEAARIAEELGADEI--------DInmgcpvkkvtKGGAGAALLRDPelvaEIVKAVVEAVDVPVTVKIRLG-------- 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640  95 eslgvdyIDESEvltpadevyhlnkrdytvpfvcgcRDIGEAARRIAE-GASML----RTKgepgtgniveavrhmrqVN 169
Cdd:COG0042   141 -------WDDDD------------------------ENALEFARIAEDaGAAALtvhgRTR-----------------EQ 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827344640 170 AEIRQvaslredelmtyakntgAPYEVLLEIKHLGRLPVVnfAAGGVATPADAALMMQL-GADGVFVGSGIFKseNP 245
Cdd:COG0042   173 RYKGP-----------------ADWDAIARVKEAVSIPVI--GNGDIFSPEDAKRMLEEtGCDGVMIGRGALG--NP 228
thiG PRK00208
thiazole synthase; Reviewed
 215-255 1.42e-05

thiazole synthase; Reviewed


Pssm-ID: 234687  Cd Length: 250  Bit Score: 45.44  E-value: 1.42e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1827344640 215 GVATPADAALMMQLGADGVFVGSGIFKSENPEKFARAI---VEA 255
Cdd:PRK00208  183 GIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFklaVEA 226
IGPS cd00331
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ...
 212-252 2.41e-05

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: 44.38  E-value: 2.41e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1827344640 212 AAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKFARAI 252
Cdd:cd00331   177 SESGISTPEDVKRLAEAGADAVLIGESLMRAPDPGAALREL 217
ThiG cd04728
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ...
 215-255 2.46e-05

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: 44.79  E-value: 2.46e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1827344640 215 GVATPADAALMMQLGADGVFVGSGIFKSENPEKFARAI---VEA 255
Cdd:cd04728   183 GIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFklaVEA 226
Dus pfam01207
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ...
 29-250 3.96e-05

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: 44.24  E-value: 3.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640  29 AEQAKIAEEAGAVAVMALERVPAD--IRAAGGVSRMADP----TIVEEVMGAVSIPVMAKCRIGhlvearvleslgvdyI 102
Cdd:pfam01207  69 AEAAKLVEDRGADGIDINMGCPSKkvTRGGGGAALLRNPdlvaQIVKAVVKAVGIPVTVKIRIG---------------W 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640 103 DESevltpadevyhlnkrdytvpfvcgCRDIGEAARRI-AEGASML----RTKGEpgtgniveavrhMRQVNAEIRQVAS 177
Cdd:pfam01207 134 DDS------------------------HENAVEIAKIVeDAGAQALtvhgRTRAQ------------NYEGTADWDAIKQ 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827344640 178 LREDelmtyakntgapyevlleikhlgrLPVVNFAAGGVATPADA-ALMMQLGADGVFVGSGIFksENPEKFAR 250
Cdd:pfam01207 178 VKQA------------------------VSIPVIANGDITDPEDAqRCLAYTGADGVMIGRGAL--GNPWLFAE 225
ThiG pfam05690
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ...
 193-255 5.24e-05

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: 43.78  E-value: 5.24e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827344640 193 PYEVLLEIKHLgRLPVVNFAagGVATPADAALMMQLGADGVFVGSGIFKSENPEKFARAI---VEA 255
Cdd:pfam05690 164 PYNLKIIIEEA-DVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFklaVEA 226
thiE PRK00043
thiamine phosphate synthase;
195-259 8.27e-05

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 42.86  E-value: 8.27e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827344640 195 EVLLEIKHLGR-LPVVnfAAGGVaTPADAALMMQLGADGVFVGSGIFKSENPEKFARAIVEATTHY 259
Cdd:PRK00043  149 EGLREIRAAVGdIPIV--AIGGI-TPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAA 211
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 192-237 1.33e-04

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: 42.47  E-value: 1.33e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1827344640 192 APYEVLLEIKHLGRLPVVnfAAGGVATPADAALMMQLGADGVFVGS 237
Cdd:cd04730   143 GTFALVPEVRDAVDIPVI--AAGGIADGRGIAAALALGADGVQMGT 186
trpC PRK00278
indole-3-glycerol phosphate synthase TrpC;
215-255 2.61e-04

indole-3-glycerol phosphate synthase TrpC;


Pssm-ID: 234710  Cd Length: 260  Bit Score: 41.68  E-value: 2.61e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1827344640 215 GVATPADAALMMQLGADGVFVGSGIFKSENPEKFARAIVEA 255
Cdd:PRK00278  219 GIFTPEDLKRLAKAGADAVLVGESLMRADDPGAALRELLGA 259
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 187-239 4.53e-04

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: 40.64  E-value: 4.53e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1827344640 187 AKNTGAPYEVLLEIKHLGRLPVVnfAAGGVATPADAALMMQLGADGVFVGSGI 239
Cdd:cd04729   159 AKTEDPDFELLKELRKALGIPVI--AEGRINSPEQAAKALELGADAVVVGSAI 209
PRK07695 PRK07695
thiazole tautomerase TenI;
195-255 5.01e-04

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 40.39  E-value: 5.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827344640 195 EVLLEIKHLGRLPVVnfAAGGVaTPADAALMMQLGADGVFVGSGIFKSENPEKFARAIVEA 255
Cdd:PRK07695  139 EELSDIARALSIPVI--AIGGI-TPENTRDVLAAGVSGIAVMSGIFSSANPYSKAKRYAES 196
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
187-239 5.47e-04

putative N-acetylmannosamine-6-phosphate 2-epimerase;


Pssm-ID: 234907  Cd Length: 221  Bit Score: 40.52  E-value: 5.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1827344640 187 AKNTGAPYEVLLEIKHLGRLPVVnfAAGGVATPADAALMMQLGADGVFVGSGI 239
Cdd:PRK01130  155 KKPEEPDFALLKELLKAVGCPVI--AEGRINTPEQAKKALELGAHAVVVGGAI 205
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 29-102 5.69e-04

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: 40.56  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827344640  29 AEQAKIAEEAGAVAVmalervpaDI----------RAAGGVSRMADP----TIVEEVMGAVSIPVMAKCRIG-----HLV 89
Cdd:cd02801    70 AEAAKIVEELGADGI--------DLnmgcpspkvtKGGAGAALLKDPelvaEIVRAVREAVPIPVTVKIRLGwddeeETL 141

                          90
                  ....*....|....
gi 1827344640  90 E-ARVLESLGVDYI 102
Cdd:cd02801   142 ElAKALEDAGASAL 155
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 193-255 1.18e-03

bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 40.00  E-value: 1.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827344640 193 PYEVLLEIKHLGRLPVVnfAAGGVaTPADAALMMQLGADGVFVGSGIFKSENPEKFARAIVEA 255
Cdd:PRK07028  150 PLELLKEVSEEVSIPIA--VAGGL-DAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIREA 209
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 199-252 1.85e-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: 38.72  E-value: 1.85e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1827344640 199 EIKHLGRLPVVNFA-AGGVaTPADAALMMQLGADGVFVGSGIFKSENPEKFARAI 252
Cdd:cd04726   149 DLKKVKKLLGVKVAvAGGI-TPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 204-277 4.43e-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: 38.13  E-value: 4.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827344640 204 GRLPVVnfAAGGVATPADAALMMQLGADGVFVGSGIFksenpekfaraiveatthYEDYELIASLSKGLGNAMK 277
Cdd:COG0167   235 GDIPII--GVGGISTAEDALEFILAGASAVQVGTALF------------------YEGPGLVRRIIRGLEAYLE 288
thiE TIGR00693
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ...
 195-252 7.91e-03

thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate pyrophosphorylase, ThiE, of a number of bacteria, and N-terminal domains of bifunctional thiamine proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe, in which the C-terminal domain corresponds to the bacterial hydroxyethylthiazole kinase (EC 2.7.1.50), ThiM. This model includes ThiE from Bacillus subtilis but excludes its paralog, the regulatory protein TenI (SP:P25053), and neighbors of TenI. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 273222 [Multi-domain]  Cd Length: 196  Bit Score: 36.84  E-value: 7.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1827344640 195 EVLLEIKHLG-RLPVVnfAAGGVaTPADAALMMQLGADGVFVGSGIFKSENPEKFARAI 252
Cdd:TIGR00693 141 ELLREIAATLiDIPIV--AIGGI-TLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 206-241 8.73e-03

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;


Pssm-ID: 184165  Cd Length: 241  Bit Score: 36.81  E-value: 8.73e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1827344640 206 LPVVnfAAGGVATPADAALMMQLGADGVFVGSGIFK 241
Cdd:PRK13585  194 IPVI--ASGGVTTLDDLRALKEAGAAGVVVGSALYK 227
PRK04302 PRK04302
triosephosphate isomerase; Provisional
 211-255 9.32e-03

triosephosphate isomerase; Provisional


Pssm-ID: 235274  Cd Length: 223  Bit Score: 36.77  E-value: 9.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1827344640 211 FAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKFARAIVEA 255
Cdd:PRK04302  177 LCGAGISTGEDVKAALELGADGVLLASGVVKAKDPEAALRDLVSP 221
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 193-237 9.39e-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: 37.01  E-value: 9.39e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1827344640 193 PYEVLLEIKHLGRLPVVnfAAGGVATPADAALMMQLGADGVFVGS 237
Cdd:COG2070   146 TFALVPEVRDAVDIPVI--AAGGIADGRGIAAALALGADGVQMGT 188
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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