NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|518073375|ref|WP_019243583|]
View 

MULTISPECIES: pyridoxal 5'-phosphate synthase lyase subunit PdxS [Bacillus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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: 579.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375   4 TQASEVVKRGMAQMQKGGVIMDVVNAEQAKIAEAAGAVAVMALERVPSDIRAAGGVARMADPRIVEEVMNAVSIPVMAKA 83
Cdd:PRK04180   2 ETGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375  84 RIGHIVEARVLEAMGVDYIDESEVLTPADEEFHLLKSAYKVPFVCGCRDLGEAARRIGEGASMLRTKGEPGTGNIVEAVR 163
Cdd:PRK04180  82 RIGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375 164 HMRKVNAQVRKVVNMNDDELMTESKLLGASYEILKQIKSEGRLPVVNFAAGGIATPADAALMMELGADGVFVGSGIFKSE 243
Cdd:PRK04180 162 HMRQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSG 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 518073375 244 NPEKFAAAIVQATTYYTDYELIGQLSKELGTAMKGIDISTLHPSERMQERGW 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: 579.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375   4 TQASEVVKRGMAQMQKGGVIMDVVNAEQAKIAEAAGAVAVMALERVPSDIRAAGGVARMADPRIVEEVMNAVSIPVMAKA 83
Cdd:PRK04180   2 ETGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375  84 RIGHIVEARVLEAMGVDYIDESEVLTPADEEFHLLKSAYKVPFVCGCRDLGEAARRIGEGASMLRTKGEPGTGNIVEAVR 163
Cdd:PRK04180  82 RIGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375 164 HMRKVNAQVRKVVNMNDDELMTESKLLGASYEILKQIKSEGRLPVVNFAAGGIATPADAALMMELGADGVFVGSGIFKSE 243
Cdd:PRK04180 162 HMRQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSG 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 518073375 244 NPEKFAAAIVQATTYYTDYELIGQLSKELGTAMKGIDISTLHPSERMQERGW 295
Cdd:PRK04180 242 DPEKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDELPPEERLQERGW 293
PdxS COG0214
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ...
 4-295 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: 570.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375   4 TQASEVVKRGMAQMQKGGVIMDVVNAEQAKIAEAAGAVAVMALERVPSDIRAAGGVARMADPRIVEEVMNAVSIPVMAKA 83
Cdd:COG0214    2 ETGTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAKV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375  84 RIGHIVEARVLEAMGVDYIDESEVLTPADEEFHLLKSAYKVPFVCGCRDLGEAARRIGEGASMLRTKGEPGTGNIVEAVR 163
Cdd:COG0214   82 RIGHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAVR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375 164 HMRKVNAQVRKVVNMNDDELMTESKLLGASYEILKQIKSEGRLPVVNFAAGGIATPADAALMMELGADGVFVGSGIFKSE 243
Cdd:COG0214  162 HMRTINSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSE 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 518073375 244 NPEKFAAAIVQATTYYTDYELIGQLSKELGTAMKGIDISTLHPSERMQERGW 295
Cdd:COG0214  242 DPEKRARAIVEATTHYDDPEVLAEVSEGLGEAMKGIDISTLPEEERLQERGW 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: 523.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375  12 RGMAQMQKGGVIMDVVNAEQAKIAEAAGAVAVMALERVPSDIRAAGGVARMADPRIVEEVMNAVSIPVMAKARIGHIVEA 91
Cdd:cd04727    1 RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375  92 RVLEAMGVDYIDESEVLTPADEEFHLLKSAYKVPFVCGCRDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRHMRKVNAQ 171
Cdd:cd04727   81 QILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375 172 VRKVVNMNDDELMTESKLLGASYEILKQIKSEGRLPVVNFAAGGIATPADAALMMELGADGVFVGSGIFKSENPEKFAAA 251
Cdd:cd04727  161 IRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARA 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 518073375 252 IVQATTYYTDYELIGQLSKELGTAMKGIDISTLHPSERMQERG 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 7.17e-177

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: 489.67  E-value: 7.17e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375   10 VKRGMAQMQKGGVIMDVVNAEQAKIAEAAGAVAVMALERVPSDIRAAGGVARMADPRIVEEVMNAVSIPVMAKARIGHIV 89
Cdd:TIGR00343   1 LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375   90 EARVLEAMGVDYIDESEVLTPADEEFHLLKSAYKVPFVCGCRDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRHMRKVN 169
Cdd:TIGR00343  81 EAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375  170 AQVRKVVNMN-DDELMTESKLLGASYEILKQIKSEGRLPVVNFAAGGIATPADAALMMELGADGVFVGSGIFKSENPEKF 248
Cdd:TIGR00343 161 EEIRQIQNMLeEEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 518073375  249 AAAIVQATTYYTDYELIGQLSKELGTAMKGIDISTLHPSERMQERGW 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 2.32e-144

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: 404.17  E-value: 2.32e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375    7 SEVVKRGMAQMQKGGVIMDVVNAEQAKIAEAAGAVAVMALERVPSDIRAAGGVARMADPRIVEEVMNAVSIPVMAKARIG 86
Cdd:pfam01680   1 TFRVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375   87 HIVEARVLEAMGVDYIDESEVLTPADEEFHLLKSAYKVPFVCGCRDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRHMR 166
Cdd:pfam01680  81 HFVEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 518073375  167 KVNAQVRKVVNMNDDELMTESKLLGASYEILKQIKSEGRLPVVNFA 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: 579.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375   4 TQASEVVKRGMAQMQKGGVIMDVVNAEQAKIAEAAGAVAVMALERVPSDIRAAGGVARMADPRIVEEVMNAVSIPVMAKA 83
Cdd:PRK04180   2 ETGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375  84 RIGHIVEARVLEAMGVDYIDESEVLTPADEEFHLLKSAYKVPFVCGCRDLGEAARRIGEGASMLRTKGEPGTGNIVEAVR 163
Cdd:PRK04180  82 RIGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375 164 HMRKVNAQVRKVVNMNDDELMTESKLLGASYEILKQIKSEGRLPVVNFAAGGIATPADAALMMELGADGVFVGSGIFKSE 243
Cdd:PRK04180 162 HMRQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSG 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 518073375 244 NPEKFAAAIVQATTYYTDYELIGQLSKELGTAMKGIDISTLHPSERMQERGW 295
Cdd:PRK04180 242 DPEKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDELPPEERLQERGW 293
PdxS COG0214
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ...
 4-295 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: 570.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375   4 TQASEVVKRGMAQMQKGGVIMDVVNAEQAKIAEAAGAVAVMALERVPSDIRAAGGVARMADPRIVEEVMNAVSIPVMAKA 83
Cdd:COG0214    2 ETGTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAKV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375  84 RIGHIVEARVLEAMGVDYIDESEVLTPADEEFHLLKSAYKVPFVCGCRDLGEAARRIGEGASMLRTKGEPGTGNIVEAVR 163
Cdd:COG0214   82 RIGHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAVR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375 164 HMRKVNAQVRKVVNMNDDELMTESKLLGASYEILKQIKSEGRLPVVNFAAGGIATPADAALMMELGADGVFVGSGIFKSE 243
Cdd:COG0214  162 HMRTINSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSE 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 518073375 244 NPEKFAAAIVQATTYYTDYELIGQLSKELGTAMKGIDISTLHPSERMQERGW 295
Cdd:COG0214  242 DPEKRARAIVEATTHYDDPEVLAEVSEGLGEAMKGIDISTLPEEERLQERGW 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: 523.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375  12 RGMAQMQKGGVIMDVVNAEQAKIAEAAGAVAVMALERVPSDIRAAGGVARMADPRIVEEVMNAVSIPVMAKARIGHIVEA 91
Cdd:cd04727    1 RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375  92 RVLEAMGVDYIDESEVLTPADEEFHLLKSAYKVPFVCGCRDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRHMRKVNAQ 171
Cdd:cd04727   81 QILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375 172 VRKVVNMNDDELMTESKLLGASYEILKQIKSEGRLPVVNFAAGGIATPADAALMMELGADGVFVGSGIFKSENPEKFAAA 251
Cdd:cd04727  161 IRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARA 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 518073375 252 IVQATTYYTDYELIGQLSKELGTAMKGIDISTLHPSERMQERG 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 7.17e-177

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: 489.67  E-value: 7.17e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375   10 VKRGMAQMQKGGVIMDVVNAEQAKIAEAAGAVAVMALERVPSDIRAAGGVARMADPRIVEEVMNAVSIPVMAKARIGHIV 89
Cdd:TIGR00343   1 LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375   90 EARVLEAMGVDYIDESEVLTPADEEFHLLKSAYKVPFVCGCRDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRHMRKVN 169
Cdd:TIGR00343  81 EAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375  170 AQVRKVVNMN-DDELMTESKLLGASYEILKQIKSEGRLPVVNFAAGGIATPADAALMMELGADGVFVGSGIFKSENPEKF 248
Cdd:TIGR00343 161 EEIRQIQNMLeEEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 518073375  249 AAAIVQATTYYTDYELIGQLSKELGTAMKGIDISTLHPSERMQERGW 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 2.32e-144

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: 404.17  E-value: 2.32e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375    7 SEVVKRGMAQMQKGGVIMDVVNAEQAKIAEAAGAVAVMALERVPSDIRAAGGVARMADPRIVEEVMNAVSIPVMAKARIG 86
Cdd:pfam01680   1 TFRVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375   87 HIVEARVLEAMGVDYIDESEVLTPADEEFHLLKSAYKVPFVCGCRDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRHMR 166
Cdd:pfam01680  81 HFVEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 518073375  167 KVNAQVRKVVNMNDDELMTESKLLGASYEILKQIKSEGRLPVVNFA 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 4.91e-12

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: 63.76  E-value: 4.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375  29 AEQAKIAEAAGAVAVMALERVPSDIRAAGgvarmADPRIVEEVMNAVSIPVMAKARIGHIVE-----ARVLEAMGVDYID 103
Cdd:cd04722   15 VELAKAAAEAGADAIIVGTRSSDPEEAET-----DDKEVLKEVAAETDLPLGVQLAINDAAAavdiaAAAARAAGADGVE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375 104 ESEVLTPADEEFH-----LLKSAYKVPFVCGCRDLGEAARR--IGEGASMLRTKGEPGTGNIVEAVRHmrkvnaqvrkvv 176
Cdd:cd04722   90 IHGAVGYLAREDLelireLREAVPDVKVVVKLSPTGELAAAaaEEAGVDEVGLGNGGGGGGGRDAVPI------------ 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518073375 177 nmnddelmteskllgaSYEILKQIKSEGRLPVvnFAAGGIATPADAALMMELGADGVFVGS 237
Cdd:cd04722  158 ----------------ADLLLILAKRGSKVPV--IAGGGINDPEDAAEALALGADGVIVGS 200
thiG CHL00162
thiamin biosynthesis protein G; Validated
 197-255 3.44e-08

thiamin biosynthesis protein G; Validated


Pssm-ID: 214380  Cd Length: 267  Bit Score: 53.56  E-value: 3.44e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518073375 197 LKQIKSEGRLPVVNFAagGIATPADAALMMELGADGVFVGSGIFKSENPEKFAAAI---VQA 255
Cdd:CHL00162 181 LQIIIENAKIPVIIDA--GIGTPSEASQAMELGASGVLLNTAVAQAKNPEQMAKAMklaVQA 240
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 195-254 4.08e-08

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: 52.52  E-value: 4.08e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375 195 EILKQIKSEGRLPVVnfAAGGIaTPADAALMMELGADGVFVGSGIFKSENPEKFAAAIVQ 254
Cdd:cd00564  140 ELLREIAELVEIPVV--AIGGI-TPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 29-245 9.40e-08

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: 52.40  E-value: 9.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375  29 AEQAKIAEAAGAVAVmalervpsDI----------RAAGGVARMADP----RIVEEVMNAVSIPVMAKARIGhivearvl 94
Cdd:COG0042   77 AEAARIAEELGADEI--------DInmgcpvkkvtKGGAGAALLRDPelvaEIVKAVVEAVDVPVTVKIRLG-------- 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375  95 eamgvdyIDEsevltpaDEEFhllksaykvpfvcgCRDLGEAARRigEGASMLrtkgepgtgnIVEAvrhmrkvnaqvRK 174
Cdd:COG0042  141 -------WDD-------DDEN--------------ALEFARIAED--AGAAAL----------TVHG-----------RT 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518073375 175 VVNMNDDElmteskllgASYEILKQIKSEGRLPVVnfAAGGIATPADAALMMEL-GADGVFVGSGIFKseNP 245
Cdd:COG0042  170 REQRYKGP---------ADWDAIARVKEAVSIPVI--GNGDIFSPEDAKRMLEEtGCDGVMIGRGALG--NP 228
ThiG cd04728
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ...
 197-256 4.05e-07

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: 50.18  E-value: 4.05e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375 197 LKQIKSEGRLPVVNFAagGIATPADAALMMELGADGVFVGSGIFKSENPEKFAAAIVQAT 256
Cdd:cd04728  167 LRIIIERADVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFKLAV 224
IGPS cd00331
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ...
 19-252 4.90e-07

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: 49.38  E-value: 4.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375  19 KGGVIMDVVNAEQAKIAEAAGAVAVMALervpSDIRAAGGvarmaDPRIVEEVMNAVSIPVMAKARIGH---IVEARVLE 95
Cdd:cd00331   24 KGLIREDFDPVEIAKAYEKAGAAAISVL----TEPKYFQG-----SLEDLRAVREAVSLPVLRKDFIIDpyqIYEARAAG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375  96 AMGVDYIdeSEVLTPAD-EEFHLLksaykvpfvcgCRDLGEAArrigegasmlrtkgepgtgnIVEA--VRHMRKVNAQV 172
Cdd:cd00331   95 ADAVLLI--VAALDDEQlKELYEL-----------ARELGMEV--------------------LVEVhdEEELERALALG 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375 173 RKVVNMNDDELMTESKLLGASYEILKQIKsEGRLPVvnfAAGGIATPADAALMMELGADGVFVGSGIFKSENPEKFAAAI 252
Cdd:cd00331  142 AKIIGINNRDLKTFEVDLNTTERLAPLIP-KDVILV---SESGISTPEDVKRLAEAGADAVLIGESLMRAPDPGAALREL 217
thiG PRK00208
thiazole synthase; Reviewed
 197-255 5.73e-07

thiazole synthase; Reviewed


Pssm-ID: 234687  Cd Length: 250  Bit Score: 49.67  E-value: 5.73e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 518073375 197 LKQIKSEGRLPVVNFAagGIATPADAALMMELGADGVFVGSGIFKSENPEKFAAAIVQA 255
Cdd:PRK00208 167 LRIIIEQADVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFKLA 223
ThiG pfam05690
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ...
 195-256 1.09e-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: 48.79  E-value: 1.09e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518073375  195 EILKQIKSEGRLPVVNFAagGIATPADAALMMELGADGVFVGSGIFKSENPEKFAAAIVQAT 256
Cdd:pfam05690 165 YNLKIIIEEADVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFKLAV 224
Dus pfam01207
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ...
 29-250 1.90e-06

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: 48.48  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375   29 AEQAKIAEAAGAVAVMALERVPSD--IRAAGGVARMADP----RIVEEVMNAVSIPVMAKARIGhivearvleamgvdyI 102
Cdd:pfam01207  69 AEAAKLVEDRGADGIDINMGCPSKkvTRGGGGAALLRNPdlvaQIVKAVVKAVGIPVTVKIRIG---------------W 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375  103 DESevltpadeefhllksaykvpfvcgCRDLGEAARRI-GEGASML----RTKGEPGTGNiveavrhmrkvnaqvrkvvn 177
Cdd:pfam01207 134 DDS------------------------HENAVEIAKIVeDAGAQALtvhgRTRAQNYEGT-------------------- 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518073375  178 mnddelmteskllgASYEILKQIKSEGRLPVvnFAAGGIATPADA-ALMMELGADGVFVGSGIFksENPEKFAA 250
Cdd:pfam01207 170 --------------ADWDAIKQVKQAVSIPV--IANGDITDPEDAqRCLAYTGADGVMIGRGAL--GNPWLFAE 225
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 29-245 3.50e-06

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: 47.10  E-value: 3.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375  29 AEQAKIAEAAGAVAV---MAlerVPSD--IRAAGGVARMADP----RIVEEVMNAVSIPVMAKARIGHivearvleamgv 99
Cdd:cd02801   70 AEAAKIVEELGADGIdlnMG---CPSPkvTKGGAGAALLKDPelvaEIVRAVREAVPIPVTVKIRLGW------------ 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375 100 dyidesevltpaDEEFHLLKsaykvpFVCGCRDlgeaarrigEGASML----RTKGEPGTGNiveavrhmrkvnaqvrkv 175
Cdd:cd02801  135 ------------DDEEETLE------LAKALED---------AGASALtvhgRTREQRYSGP------------------ 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518073375 176 vnmnddelmteskllgASYEILKQIKSEGRLPVvnFAAGGIATPADAALMMEL-GADGVFVGSGIFksENP 245
Cdd:cd02801  170 ----------------ADWDYIAEIKEAVSIPV--IANGDIFSLEDALRCLEQtGVDGVMIGRGAL--GNP 220
IGPS pfam00218
Indole-3-glycerol phosphate synthase;
10-251 4.33e-06

Indole-3-glycerol phosphate synthase;


Pssm-ID: 395163  Cd Length: 252  Bit Score: 46.91  E-value: 4.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375   10 VKRgmAQMQKGGVIMDVVNAEQAKIAEAAGAVAVMALERVP------SDIRAaggvarmadpriveeVMNAVSIPVMAKA 83
Cdd:pfam00218  53 VKK--ASPSKGLIREDFDPAEIARVYEAAGASAISVLTDPKyfqgsiEYLRA---------------VRQAVSLPVLRKD 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375   84 RI---GHIVEARVLEAMGVDYIdeSEVLTpaDEEFHllksaykvpfvcgcrDLGEAARRIGegasMlrtkgEPgtgnIVE 160
Cdd:pfam00218 116 FIideYQIDEARLAGADAILLI--VAVLD--DELLE---------------ELYAYARSLG----M-----EV----LVE 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375  161 aVRHMRKVNAQVR---KVVNMNDDELMTESKLLGASYEILKQIKSEgrlpVVNFAAGGIATPADAALMMELGADGVFVGS 237
Cdd:pfam00218 164 -VHNEEELERALAlgaKIIGVNNRNLKTFEVDLNTTRRLAPLIPAD----VLLVAESGIYTPADVRELKEHGANAFLVGE 238

                         250
                  ....*....|....
gi 518073375  238 GIFKSENPEKFAAA 251
Cdd:pfam00218 239 SLMRQEDVRAAIRE 252
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
188-239 5.00e-06

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


Pssm-ID: 234907  Cd Length: 221  Bit Score: 46.68  E-value: 5.00e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 518073375 188 KLLGASYEILKQIKSEGRLPVVnfAAGGIATPADAALMMELGADGVFVGSGI 239
Cdd:PRK01130 156 KPEEPDFALLKELLKAVGCPVI--AEGRINTPEQAKKALELGAHAVVVGGAI 205
thiE PRK00043
thiamine phosphate synthase;
195-256 5.87e-06

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 46.33  E-value: 5.87e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518073375 195 EILKQIKSEGR-LPVVnfAAGGIaTPADAALMMELGADGVFVGSGIFKSENPEKFAAAIVQAT 256
Cdd:PRK00043 149 EGLREIRAAVGdIPIV--AIGGI-TPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAF 208
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 192-237 6.37e-06

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: 46.32  E-value: 6.37e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 518073375 192 ASYEILKQIKSEGRLPVVnfAAGGIATPADAALMMELGADGVFVGS 237
Cdd:cd04730  143 GTFALVPEVRDAVDIPVI--AAGGIADGRGIAAALALGADGVQMGT 186
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 194-239 7.77e-06

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: 46.03  E-value: 7.77e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 518073375 194 YEILKQIKSEGRLPVVnfAAGGIATPADAALMMELGADGVFVGSGI 239
Cdd:cd04729  166 FELLKELRKALGIPVI--AEGRINSPEQAAKALELGADAVVVGSAI 209
PRK07695 PRK07695
thiazole tautomerase TenI;
185-251 2.03e-05

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 44.63  E-value: 2.03e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518073375 185 TESK--LLGASYEILKQIKSEGRLPVVnfAAGGIaTPADAALMMELGADGVFVGSGIFKSENPEKFAAA 251
Cdd:PRK07695 127 TDCKkgVPARGLEELSDIARALSIPVI--AIGGI-TPENTRDVLAAGVSGIAVMSGIFSSANPYSKAKR 192
trpA TIGR00262
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ...
 186-252 3.02e-05

tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the biosynthesis of tryptophan. The alpha chain is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. In bacteria and plants each domain is found on a separate subunit (alpha and beta chains), while in fungi the two domains are fused together on a single multifunctional protein. The signature pattern for trpA contains three conserved acidic residues. [LIVM]-E-[LIVM]-G-x(2)-[FYC]-[ST]-[DE]-[PA]-[LIVMY]-[AGLI]-[DE]-G and this is located between residues 43-58 of the model. The Sulfolobus solfataricus trpA is known to be quite divergent from other known trpA sequences. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 161792  Cd Length: 256  Bit Score: 44.64  E-value: 3.02e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518073375  186 ESKLLGASYEILKQIKSEGRLPV-VNFaagGIATPADAALMMELGADGVFVGSGIFK-----SENPEKFAAAI 252
Cdd:TIGR00262 179 RNRAASALNELVKRLKAYSAKPVlVGF---GISKPEQVKQAIDAGADGVIVGSAIVKiieenLNTPEKMLQAL 248
PRK11840 PRK11840
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
 197-255 3.86e-05

bifunctional sulfur carrier protein/thiazole synthase protein; Provisional


Pssm-ID: 236998 [Multi-domain]  Cd Length: 326  Bit Score: 44.35  E-value: 3.86e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 518073375 197 LKQIKSEGRLPVVNFAagGIATPADAALMMELGADGVFVGSGIFKSENPEKFAAAIVQA 255
Cdd:PRK11840 241 IRLIVEGATVPVLVDA--GVGTASDAAVAMELGCDGVLMNTAIAEAKNPVLMARAMKLA 297
trpC PRK00278
indole-3-glycerol phosphate synthase TrpC;
190-255 1.93e-04

indole-3-glycerol phosphate synthase TrpC;


Pssm-ID: 234710  Cd Length: 260  Bit Score: 42.07  E-value: 1.93e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518073375 190 LGASYEILKQIKSEgRLPVvnfAAGGIATPADAALMMELGADGVFVGSGIFKSENPEKFAAAIVQA 255
Cdd:PRK00278 198 LETTERLAPLIPSD-RLVV---SESGIFTPEDLKRLAKAGADAVLVGESLMRADDPGAALRELLGA 259
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 195-255 2.46e-04

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


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 42.31  E-value: 2.46e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518073375 195 EILKQIKSEGRLPVVnfAAGGIaTPADAALMMELGADGVFVGSGIFKSENPEKFAAAIVQA 255
Cdd:PRK07028 152 ELLKEVSEEVSIPIA--VAGGL-DAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIREA 209
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 193-237 4.46e-04

NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 41.25  E-value: 4.46e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 518073375 193 SYEILKQIKSEGRLPVVnfAAGGIATPADAALMMELGADGVFVGS 237
Cdd:COG2070  146 TFALVPEVRDAVDIPVI--AAGGIADGRGIAAALALGADGVQMGT 188
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
 195-239 4.99e-04

Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes 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. This Pfam family also includes the regulatory protein TENI, a protein from Bacillus subtilis that regulates the production of several extracellular enzymes by reducing alkaline protease production. While TenI shows high sequence similarity with thiamin phosphate synthase, the purified protein has no thiamin phosphate synthase activity. Instead, it is a thiazole tautomerase.


Pssm-ID: 426849 [Multi-domain]  Cd Length: 180  Bit Score: 40.22  E-value: 4.99e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 518073375  195 EILKQIKSEGRLPVVnfAAGGIaTPADAALMMELGADGVFVGSGI 239
Cdd:pfam02581 139 EGLKAIAEAVEIPVV--AIGGI-TPENVPEVIEAGADGVAVVSAI 180
PRK04302 PRK04302
triosephosphate isomerase; Provisional
 211-247 1.76e-03

triosephosphate isomerase; Provisional


Pssm-ID: 235274  Cd Length: 223  Bit Score: 39.08  E-value: 1.76e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 518073375 211 FAAGGIATPADAALMMELGADGVFVGSGIFKSENPEK 247
Cdd:PRK04302 177 LCGAGISTGEDVKAALELGADGVLLASGVVKAKDPEA 213
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 189-237 1.83e-03

HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene.


Pssm-ID: 240083  Cd Length: 234  Bit Score: 39.00  E-value: 1.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 518073375 189 LLGASYEILKQIKSEGRLPVVnfAAGGIATPADAALMMELGADGVFVGS 237
Cdd:cd04732  174 LSGPNFELYKELAAATGIPVI--ASGGVSSLDDIKALKELGVAGVIVGK 220
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
 196-239 1.87e-03

Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 240086 [Multi-domain]  Cd Length: 353  Bit Score: 39.50  E-value: 1.87e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 518073375 196 ILKQIKSE--GRLPVVnfAAGGIATPADAALMMELGADGVFVGSGI 239
Cdd:cd04735  273 IMELVKERiaGRLPLI--AVGSINTPDDALEALETGADLVAIGRGL 316
trpA PRK13111
tryptophan synthase subunit alpha; Provisional
 195-256 2.25e-03

tryptophan synthase subunit alpha; Provisional


Pssm-ID: 237285  Cd Length: 258  Bit Score: 38.94  E-value: 2.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518073375 195 EILKQIKSEGRLPVvnfAAG-GIATPADAALMMElGADGVFVGSGIFK--SENPE------KFAAAIVQAT 256
Cdd:PRK13111 190 ELVARLKAHTDLPV---AVGfGISTPEQAAAIAA-VADGVIVGSALVKiiEENPEalealaAFVKELKAAL 256
PRK05286 PRK05286
quinone-dependent dihydroorotate dehydrogenase;
189-231 2.71e-03

quinone-dependent dihydroorotate dehydrogenase;


Pssm-ID: 235388  Cd Length: 344  Bit Score: 38.99  E-value: 2.71e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 518073375 189 LLGASYEILKQIKSE--GRLPVVnfAAGGIATPADAALMMELGAD 231
Cdd:PRK05286 271 LFERSTEVIRRLYKElgGRLPII--GVGGIDSAEDAYEKIRAGAS 313
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 185-241 2.96e-03

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


Pssm-ID: 184165  Cd Length: 241  Bit Score: 38.35  E-value: 2.96e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 518073375 185 TESKLLGASYEILKQIKSEGRLPVVnfAAGGIATPADAALMMELGADGVFVGSGIFK 241
Cdd:PRK13585 173 VEGLLEGVNTEPVKELVDSVDIPVI--ASGGVTTLDDLRALKEAGAAGVVVGSALYK 227
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 193-240 3.07e-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: 38.52  E-value: 3.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 518073375 193 SYEILKQIKSE--GRLPVVnfAAGGIATPADAALMMELGADGVFVGSGIF 240
Cdd:COG0167  222 ALRMVREVAQAvgGDIPII--GVGGISTAEDALEFILAGASAVQVGTALF 269
thiE TIGR00693
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ...
 195-252 3.11e-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: 38.00  E-value: 3.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 518073375  195 EILKQIKSEG-RLPVVnfAAGGIaTPADAALMMELGADGVFVGSGIFKSENPEKFAAAI 252
Cdd:TIGR00693 141 ELLREIAATLiDIPIV--AIGGI-TLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
DUF561 pfam04481
Protein of unknown function (DUF561); Protein of unknown function found in a cyanobacterium, ...
 63-262 4.72e-03

Protein of unknown function (DUF561); Protein of unknown function found in a cyanobacterium, and the chloroplasts of algae.


Pssm-ID: 113257  Cd Length: 243  Bit Score: 37.81  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375   63 ADPRIVEEVMNAVSIPVMAKArighiVEARVL---EAMGVD---------------YIDESEVLTPADEEFHLLKSA--- 121
Cdd:pfam04481  48 ADPQLVKVVKSVSNIPICVSA-----VEPELLyeaVLAGADlveignfdsfykqgrVLSVCEIIALVKETRKLLPHTplc 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518073375  122 YKVPFVCGCRDLGEAARRIGE-GASMLRTKGepGTGNIVEAvrhmRKVNAQVRKVVNMnddelmtesklLGASYEILKQI 200
Cdd:pfam04481 123 VTIPHILKLKEQINLAKQLESlGIDLIQTEG--KITSISKN----HCVNDLIEKSAST-----------LASTYEISKHV 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518073375  201 ksegRLPVVnfAAGGIaTPADAALMMELGADGVFVGSGIFKSENPEKFAAAI--VQATTYYTDY 262
Cdd:pfam04481 186 ----QLPVI--CASGL-SDVTVPLAFSYGASGIGIGSAVSKLNDIEKMVNYIseIKKAISGTRV 242
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 195-252 5.48e-03

Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.


Pssm-ID: 238244  Cd Length: 211  Bit Score: 37.46  E-value: 5.48e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 518073375 195 EILKQIKSEGRLPVVNFAAGGIaTPADAALMMELGADGVFVGSGIFKSENPEKFAAAI 252
Cdd:cd00429  154 RKLRELIPENNLNLLIEVDGGI-NLETIPLLAEAGADVLVAGSALFGSDDYAEAIKEL 210
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 197-255 6.86e-03

Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; Pentose-5-phosphate-3-epimerase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 439806  Cd Length: 218  Bit Score: 36.98  E-value: 6.86e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 518073375 197 LKQIKSEGRLPVVNFAAGGIaTPADAALMMELGADGVFVGSGIFKSENPEKFAAAIVQA 255
Cdd:COG0036  157 LRELIDERGLDILIEVDGGI-NAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREA 214
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 191-239 7.21e-03

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The ProFAR isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.


Pssm-ID: 240074 [Multi-domain]  Cd Length: 233  Bit Score: 37.25  E-value: 7.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 518073375 191 GASYEILKQIKSEGRLPVVnfAAGGIATPADAALMMELGADGVFVGSGI 239
Cdd:cd04723  175 GPDLELLERLAARADIPVI--AAGGVRSVEDLELLKKLGASGALVASAL 221
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH