NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1449613330|gb|RFB41790|]
View 

pyridoxal 5'-phosphate synthase lyase subunit PdxS [Bacillus sp. RC]

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;
1-293 0e+00

pyridoxal 5'-phosphate synthase lyase subunit PdxS;


:

Pssm-ID: 179769  Cd Length: 293  Bit Score: 605.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330   1 MRNGTDRVKRGMAEMQKGGVIMDVINAEQAKIAEAAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMNAVSIPVMAK 80
Cdd:PRK04180    1 LETGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330  81 ARIGHIVEARVLEAMGVDYIDESEVLTPADEEYHLNKSTFTVPFVCGCRDLGEAARRIGEGASMLRTKGEPGTGNIVEAV 160
Cdd:PRK04180   81 ARIGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330 161 RHMRQVNAQVRKVVGMDEDELMTEAKLLGAPYELLLQIKREGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKS 240
Cdd:PRK04180  161 RHMRQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1449613330 241 DNPEKFARAIVEATTHYQDYELIANLSKGLGSAMKGIEISSLLPENRMQERGW 293
Cdd:PRK04180  241 GDPEKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDELPPEERLQERGW 293
 
Name Accession Description Interval E-value
PRK04180 PRK04180
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
1-293 0e+00

pyridoxal 5'-phosphate synthase lyase subunit PdxS;


Pssm-ID: 179769  Cd Length: 293  Bit Score: 605.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330   1 MRNGTDRVKRGMAEMQKGGVIMDVINAEQAKIAEAAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMNAVSIPVMAK 80
Cdd:PRK04180    1 LETGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330  81 ARIGHIVEARVLEAMGVDYIDESEVLTPADEEYHLNKSTFTVPFVCGCRDLGEAARRIGEGASMLRTKGEPGTGNIVEAV 160
Cdd:PRK04180   81 ARIGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330 161 RHMRQVNAQVRKVVGMDEDELMTEAKLLGAPYELLLQIKREGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKS 240
Cdd:PRK04180  161 RHMRQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1449613330 241 DNPEKFARAIVEATTHYQDYELIANLSKGLGSAMKGIEISSLLPENRMQERGW 293
Cdd:PRK04180  241 GDPEKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDELPPEERLQERGW 293
PdxS COG0214
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ...
 1-293 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: 593.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330   1 MRNGTDRVKRGMAEMQKGGVIMDVINAEQAKIAEAAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMNAVSIPVMAK 80
Cdd:COG0214     1 LETGTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330  81 ARIGHIVEARVLEAMGVDYIDESEVLTPADEEYHLNKSTFTVPFVCGCRDLGEAARRIGEGASMLRTKGEPGTGNIVEAV 160
Cdd:COG0214    81 VRIGHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330 161 RHMRQVNAQVRKVVGMDEDELMTEAKLLGAPYELLLQIKREGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKS 240
Cdd:COG0214   161 RHMRTINSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1449613330 241 DNPEKFARAIVEATTHYQDYELIANLSKGLGSAMKGIEISSLLPENRMQERGW 293
Cdd:COG0214   241 EDPEKRARAIVEATTHYDDPEVLAEVSEGLGEAMKGIDISTLPEEERLQERGW 293
pdxS cd04727
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ...
 10-292 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: 540.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330  10 RGMAEMQKGGVIMDVINAEQAKIAEAAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMNAVSIPVMAKARIGHIVEA 89
Cdd:cd04727     1 RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330  90 RVLEAMGVDYIDESEVLTPADEEYHLNKSTFTVPFVCGCRDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRHMRQVNAQ 169
Cdd:cd04727    81 QILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330 170 VRKVVGMDEDELMTEAKLLGAPYELLLQIKREGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSDNPEKFARA 249
Cdd:cd04727   161 IRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARA 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1449613330 250 IVEATTHYQDYELIANLSKGLGSAMKGIEISSLLPENRMQERG 292
Cdd:cd04727   241 IVEAVTHYDDPEILAEVSEGLGEAMVGIDIASLKEEERMQERG 283
TIGR00343 TIGR00343
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a ...
 8-293 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: 503.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330   8 VKRGMAEMQKGGVIMDVINAEQAKIAEAAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMNAVSIPVMAKARIGHIV 87
Cdd:TIGR00343   1 LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330  88 EARVLEAMGVDYIDESEVLTPADEEYHLNKSTFTVPFVCGCRDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRHMRQVN 167
Cdd:TIGR00343  81 EAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330 168 AQVRKVVGM-DEDELMTEAKLLGAPYELLLQIKREGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSDNPEKF 246
Cdd:TIGR00343 161 EEIRQIQNMlEEEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1449613330 247 ARAIVEATTHYQDYELIANLSKGLGSAMKGIEISSLLPENRMQERGW 293
Cdd:TIGR00343 241 AKAIVEATTHYDNPEKLAEVSKDLGEAMKGISISSISEAERLQERGW 287
SOR_SNZ pfam01680
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ...
 5-210 1.06e-148

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: 414.95  E-value: 1.06e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330   5 TDRVKRGMAEMQKGGVIMDVINAEQAKIAEAAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMNAVSIPVMAKARIG 84
Cdd:pfam01680   1 TFRVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330  85 HIVEARVLEAMGVDYIDESEVLTPADEEYHLNKSTFTVPFVCGCRDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRHMR 164
Cdd:pfam01680  81 HFVEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1449613330 165 QVNAQVRKVVGMDEDELMTEAKLLGAPYELLLQIKREGRLPVVNFA 210
Cdd:pfam01680 161 TINGEIRRLQNMDEEELYAFAKELGAPYELVKEVAELGRLPVVNFA 206
 
Name Accession Description Interval E-value
PRK04180 PRK04180
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
1-293 0e+00

pyridoxal 5'-phosphate synthase lyase subunit PdxS;


Pssm-ID: 179769  Cd Length: 293  Bit Score: 605.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330   1 MRNGTDRVKRGMAEMQKGGVIMDVINAEQAKIAEAAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMNAVSIPVMAK 80
Cdd:PRK04180    1 LETGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330  81 ARIGHIVEARVLEAMGVDYIDESEVLTPADEEYHLNKSTFTVPFVCGCRDLGEAARRIGEGASMLRTKGEPGTGNIVEAV 160
Cdd:PRK04180   81 ARIGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330 161 RHMRQVNAQVRKVVGMDEDELMTEAKLLGAPYELLLQIKREGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKS 240
Cdd:PRK04180  161 RHMRQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1449613330 241 DNPEKFARAIVEATTHYQDYELIANLSKGLGSAMKGIEISSLLPENRMQERGW 293
Cdd:PRK04180  241 GDPEKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDELPPEERLQERGW 293
PdxS COG0214
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ...
 1-293 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: 593.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330   1 MRNGTDRVKRGMAEMQKGGVIMDVINAEQAKIAEAAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMNAVSIPVMAK 80
Cdd:COG0214     1 LETGTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330  81 ARIGHIVEARVLEAMGVDYIDESEVLTPADEEYHLNKSTFTVPFVCGCRDLGEAARRIGEGASMLRTKGEPGTGNIVEAV 160
Cdd:COG0214    81 VRIGHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330 161 RHMRQVNAQVRKVVGMDEDELMTEAKLLGAPYELLLQIKREGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKS 240
Cdd:COG0214   161 RHMRTINSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1449613330 241 DNPEKFARAIVEATTHYQDYELIANLSKGLGSAMKGIEISSLLPENRMQERGW 293
Cdd:COG0214   241 EDPEKRARAIVEATTHYDDPEVLAEVSEGLGEAMKGIDISTLPEEERLQERGW 293
pdxS cd04727
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ...
 10-292 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: 540.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330  10 RGMAEMQKGGVIMDVINAEQAKIAEAAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMNAVSIPVMAKARIGHIVEA 89
Cdd:cd04727     1 RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330  90 RVLEAMGVDYIDESEVLTPADEEYHLNKSTFTVPFVCGCRDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRHMRQVNAQ 169
Cdd:cd04727    81 QILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330 170 VRKVVGMDEDELMTEAKLLGAPYELLLQIKREGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSDNPEKFARA 249
Cdd:cd04727   161 IRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARA 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1449613330 250 IVEATTHYQDYELIANLSKGLGSAMKGIEISSLLPENRMQERG 292
Cdd:cd04727   241 IVEAVTHYDDPEILAEVSEGLGEAMVGIDIASLKEEERMQERG 283
TIGR00343 TIGR00343
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a ...
 8-293 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: 503.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330   8 VKRGMAEMQKGGVIMDVINAEQAKIAEAAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMNAVSIPVMAKARIGHIV 87
Cdd:TIGR00343   1 LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330  88 EARVLEAMGVDYIDESEVLTPADEEYHLNKSTFTVPFVCGCRDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRHMRQVN 167
Cdd:TIGR00343  81 EAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330 168 AQVRKVVGM-DEDELMTEAKLLGAPYELLLQIKREGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSDNPEKF 246
Cdd:TIGR00343 161 EEIRQIQNMlEEEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1449613330 247 ARAIVEATTHYQDYELIANLSKGLGSAMKGIEISSLLPENRMQERGW 293
Cdd:TIGR00343 241 AKAIVEATTHYDNPEKLAEVSKDLGEAMKGISISSISEAERLQERGW 287
SOR_SNZ pfam01680
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ...
 5-210 1.06e-148

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: 414.95  E-value: 1.06e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330   5 TDRVKRGMAEMQKGGVIMDVINAEQAKIAEAAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMNAVSIPVMAKARIG 84
Cdd:pfam01680   1 TFRVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330  85 HIVEARVLEAMGVDYIDESEVLTPADEEYHLNKSTFTVPFVCGCRDLGEAARRIGEGASMLRTKGEPGTGNIVEAVRHMR 164
Cdd:pfam01680  81 HFVEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1449613330 165 QVNAQVRKVVGMDEDELMTEAKLLGAPYELLLQIKREGRLPVVNFA 210
Cdd:pfam01680 161 TINGEIRRLQNMDEEELYAFAKELGAPYELVKEVAELGRLPVVNFA 206
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 27-235 5.69e-11

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: 60.68  E-value: 5.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330  27 AEQAKIAEAAGAVAVMALERVPADIRAAGgvsrmADPTIVEEVMNAVSIPVMAKARIGHIVE-----ARVLEAMGVDYID 101
Cdd:cd04722    15 VELAKAAAEAGADAIIVGTRSSDPEEAET-----DDKEVLKEVAAETDLPLGVQLAINDAAAavdiaAAAARAAGADGVE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330 102 ESEVLTPADEEYH-----LNKSTFTVPFVCGCRDLGEAARR--IGEGASMLRTKGEPGTGNIVEAVrhmrqvnaqvrkvv 174
Cdd:cd04722    90 IHGAVGYLAREDLelireLREAVPDVKVVVKLSPTGELAAAaaEEAGVDEVGLGNGGGGGGGRDAV-------------- 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1449613330 175 gmdedelmteakllgaPYELLLQIKREGRLPVVNFAAGGVATPADAALMMQLGADGVFVGS 235
Cdd:cd04722   156 ----------------PIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 193-252 3.27e-07

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: 49.82  E-value: 3.27e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330 193 ELLLQIKREGRLPVVnfAAGGVaTPADAALMMQLGADGVFVGSGIFKSDNPEKFARAIVE 252
Cdd:cd00564   140 ELLREIAELVEIPVV--AIGGI-TPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
thiG CHL00162
thiamin biosynthesis protein G; Validated
 196-250 1.51e-06

thiamin biosynthesis protein G; Validated


Pssm-ID: 214380  Cd Length: 267  Bit Score: 48.55  E-value: 1.51e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1449613330 196 LQIKRE-GRLPVVNFAagGVATPADAALMMQLGADGVFVGSGIFKSDNPEKFARAI 250
Cdd:CHL00162  181 LQIIIEnAKIPVIIDA--GIGTPSEASQAMELGASGVLLNTAVAQAKNPEQMAKAM 234
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 190-254 3.05e-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: 47.48  E-value: 3.05e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1449613330 190 APYELLLQIKREGRLPVVnfAAGGVATPADAALMMQLGADGVFVGSgIF----KSDNPEKFARAIVEAT 254
Cdd:cd04730   143 GTFALVPEVRDAVDIPVI--AAGGIADGRGIAAALALGADGVQMGT-RFlateESGASPAYKQALLAAT 208
ThiG pfam05690
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ...
 193-253 3.19e-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: 47.24  E-value: 3.19e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1449613330 193 ELLLQIKREGRLPVVNFAagGVATPADAALMMQLGADGVFVGSGIFKSDNPEKFARAI---VEA 253
Cdd:pfam05690 165 YNLKIIIEEADVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFklaVEA 226
ThiG cd04728
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ...
 193-253 3.24e-06

Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the thiazole moiety of thiamin pyrophosphate, an essential ubiquitous cofactor that plays an important role in carbohydrate and amino acid metabolism. ThiG catalyzes the formation of thiazole from 1-deoxy-D-xylulose 5-phosphate (DXP) and dehydroglycine, with the help of the sulfur carrier protein ThiS that carries the sulfur needed for thiazole assembly on its carboxy terminus (ThiS-COSH).


Pssm-ID: 240079  Cd Length: 248  Bit Score: 47.48  E-value: 3.24e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1449613330 193 ELLLQIKREGRLPVVNFAagGVATPADAALMMQLGADGVFVGSGIFKSDNPEKFARAI---VEA 253
Cdd:cd04728   165 YNLRIIIERADVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFklaVEA 226
thiG PRK00208
thiazole synthase; Reviewed
 198-253 4.83e-06

thiazole synthase; Reviewed


Pssm-ID: 234687  Cd Length: 250  Bit Score: 46.98  E-value: 4.83e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1449613330 198 IKREGRLPVVNFAagGVATPADAALMMQLGADGVFVGSGIFKSDNPEKFARAI---VEA 253
Cdd:PRK00208  170 IIEQADVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFklaVEA 226
PRK11840 PRK11840
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
 191-253 9.47e-06

bifunctional sulfur carrier protein/thiazole synthase protein; Provisional


Pssm-ID: 236998 [Multi-domain]  Cd Length: 326  Bit Score: 46.28  E-value: 9.47e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1449613330 191 PYELLLqIKREGRLPVVNFAagGVATPADAALMMQLGADGVFVGSGIFKSDNPEKFARAI---VEA 253
Cdd:PRK11840  238 PYTIRL-IVEGATVPVLVDA--GVGTASDAAVAMELGCDGVLMNTAIAEAKNPVLMARAMklaVEA 300
IGPS cd00331
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ...
 17-250 1.41e-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: 45.15  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330  17 KGGVIMDVINAEQAKIAEAAGAVAVMALervpADIRAAGGvsrmaDPTIVEEVMNAVSIPVMAKARIGH---IVEARVLE 93
Cdd:cd00331    24 KGLIREDFDPVEIAKAYEKAGAAAISVL----TEPKYFQG-----SLEDLRAVREAVSLPVLRKDFIIDpyqIYEARAAG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330  94 AMGVDYIdeSEVLTPADeeyhlnkstftvpfvcgCRDLGEAARRIGegasMlrtkgEPgtgnIVEAvrHmrqvnaqvrkv 173
Cdd:cd00331    95 ADAVLLI--VAALDDEQ-----------------LKELYELARELG----M-----EV----LVEV--H----------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330 174 vgmDEDEL----MTEAKLLG-------------APYELLLQIKREGRLPVvnfAAGGVATPADAALMMQLGADGVFVGSG 236
Cdd:cd00331   130 ---DEEELeralALGAKIIGinnrdlktfevdlNTTERLAPLIPKDVILV---SESGISTPEDVKRLAEAGADAVLIGES 203

                         250
                  ....*....|....
gi 1449613330 237 IFKSDNPEKFARAI 250
Cdd:cd00331   204 LMRAPDPGAALREL 217
thiE PRK00043
thiamine phosphate synthase;
193-257 1.81e-05

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 44.79  E-value: 1.81e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1449613330 193 ELLLQIKREGR-LPVVnfAAGGVaTPADAALMMQLGADGVFVGSGIFKSDNPEKFARAIVEATTHY 257
Cdd:PRK00043  149 EGLREIRAAVGdIPIV--AIGGI-TPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAA 211
PRK07695 PRK07695
thiazole tautomerase TenI;
193-253 4.88e-05

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 43.47  E-value: 4.88e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1449613330 193 ELLLQIKREGRLPVVnfAAGGVaTPADAALMMQLGADGVFVGSGIFKSDNPEKFARAIVEA 253
Cdd:PRK07695  139 EELSDIARALSIPVI--AIGGI-TPENTRDVLAAGVSGIAVMSGIFSSANPYSKAKRYAES 196
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 191-253 7.01e-05

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


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 43.86  E-value: 7.01e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1449613330 191 PYELLLQIKREGRLPVVnfAAGGVaTPADAALMMQLGADGVFVGSGIFKSDNPEKFARAIVEA 253
Cdd:PRK07028  150 PLELLKEVSEEVSIPIA--VAGGL-DAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIREA 209
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
192-237 2.17e-04

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


Pssm-ID: 234907  Cd Length: 221  Bit Score: 41.67  E-value: 2.17e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1449613330 192 YELLLQIKREGRLPVVnfAAGGVATPADAALMMQLGADGVFVGSGI 237
Cdd:PRK01130  162 FALLKELLKAVGCPVI--AEGRINTPEQAKKALELGAHAVVVGGAI 205
trpC PRK00278
indole-3-glycerol phosphate synthase TrpC;
213-253 2.25e-04

indole-3-glycerol phosphate synthase TrpC;


Pssm-ID: 234710  Cd Length: 260  Bit Score: 41.68  E-value: 2.25e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1449613330 213 GVATPADAALMMQLGADGVFVGSGIFKSDNPEKFARAIVEA 253
Cdd:PRK00278  219 GIFTPEDLKRLAKAGADAVLVGESLMRADDPGAALRELLGA 259
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 191-254 2.28e-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: 42.02  E-value: 2.28e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1449613330 191 PYELLLQIKREGRLPVVnfAAGGVATPADAALMMQLGADGVFVGSGiF----KSDNPEKFARAIVEAT 254
Cdd:COG2070   146 TFALVPEVRDAVDIPVI--AAGGIADGRGIAAALALGADGVQMGTR-FlateESPAHEAYKQALVDAK 210
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 27-243 2.58e-04

tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439812 [Multi-domain]  Cd Length: 310  Bit Score: 42.00  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330  27 AEQAKIAEAAGAVAVmalervpaDI----------RAAGGVSRMADP----TIVEEVMNAVSIPVMAKARIGhivearvl 92
Cdd:COG0042    77 AEAARIAEELGADEI--------DInmgcpvkkvtKGGAGAALLRDPelvaEIVKAVVEAVDVPVTVKIRLG-------- 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330  93 eamgvdyIDESevltpadeeyHLNkstftvpfvcgCRDLGEAARRigEGASML----RTKGEpgtGNIVEAvrhmrqvna 168
Cdd:COG0042   141 -------WDDD----------DEN-----------ALEFARIAED--AGAAALtvhgRTREQ---RYKGPA--------- 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1449613330 169 qvrkvvgmDedelmteakllgapYELLLQIKREGRLPVVnfAAGGVATPADAALMMQL-GADGVFVGSGIFKsdNP 243
Cdd:COG0042   179 --------D--------------WDAIARVKEAVSIPVI--GNGDIFSPEDAKRMLEEtGCDGVMIGRGALG--NP 228
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 192-237 3.49e-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: 41.02  E-value: 3.49e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1449613330 192 YELLLQIKREGRLPVVnfAAGGVATPADAALMMQLGADGVFVGSGI 237
Cdd:cd04729   166 FELLKELRKALGIPVI--AEGRINSPEQAAKALELGADAVVVGSAI 209
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 184-250 9.04e-04

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: 39.49  E-value: 9.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1449613330 184 EAKLLGAPYELLLQIKREGRLPVVnfAAGGVaTPADAALMMQLGADGVFVGSGIFKSDNPEKFARAI 250
Cdd:cd04726   139 QAAGGWWPEDDLKKVKKLLGVKVA--VAGGI-TPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
Dus pfam01207
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ...
 27-236 2.87e-03

Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.


Pssm-ID: 426126  Cd Length: 309  Bit Score: 38.85  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330  27 AEQAKIAEAAGAVAVMALERVPAD--IRAAGGVSRMADP----TIVEEVMNAVSIPVMAKARIGhivearvleamgvdyI 100
Cdd:pfam01207  69 AEAAKLVEDRGADGIDINMGCPSKkvTRGGGGAALLRNPdlvaQIVKAVVKAVGIPVTVKIRIG---------------W 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330 101 DESevltpadeeyhlnkstftvpfvcgCRDLGEAARRI-GEGASML----RTKGEPGTGNiveavrhmrqvnaqvrkvvg 175
Cdd:pfam01207 134 DDS------------------------HENAVEIAKIVeDAGAQALtvhgRTRAQNYEGT-------------------- 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1449613330 176 mdedelmteakllgAPYELLLQIKREGRLPVvnFAAGGVATPADA-ALMMQLGADGVFVGSG 236
Cdd:pfam01207 170 --------------ADWDAIKQVKQAVSIPV--IANGDITDPEDAqRCLAYTGADGVMIGRG 215
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 201-282 3.80e-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: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330 201 EGRLPVVnfAAGGVATPADAALMMQLGADGVFVGSGIFksdnpekfaraiveatthYQDYELIANLSKGLGSAMKGIEIS 280
Cdd:COG0167   234 GGDIPII--GVGGISTAEDALEFILAGASAVQVGTALF------------------YEGPGLVRRIIRGLEAYLEEKGFS 293


                  ..
gi 1449613330 281 SL 282
Cdd:COG0167   294 SI 295
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 186-238 4.10e-03

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]; Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439876  Cd Length: 236  Bit Score: 37.71  E-value: 4.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1449613330 186 KLLGAPYELLLQIKREGRLPVVnfAAGGVATPADAALMMQLGADGVFVGSGIF 238
Cdd:COG0106   172 TLQGPNLELYRELAAATGIPVI--ASGGVSSLDDLRALKELGVEGAIVGKALY 222
PRK04302 PRK04302
triosephosphate isomerase; Provisional
 209-253 4.36e-03

triosephosphate isomerase; Provisional


Pssm-ID: 235274  Cd Length: 223  Bit Score: 37.54  E-value: 4.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1449613330 209 FAAGGVATPADAALMMQLGADGVFVGSGIFKSDNPEKFARAIVEA 253
Cdd:PRK04302  177 LCGAGISTGEDVKAALELGADGVLLASGVVKAKDPEAALRDLVSP 221
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
158-250 5.41e-03

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 37.54  E-value: 5.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330 158 EAVRHMRQVNAQVRKVVGMDE--DELMTEAKLLGAPY----------ELLLQIKREGrLPVVnfaAGGVATPADAALMMQ 225
Cdd:COG0584   143 EALRRLRELAPDVPLGLLVEElpADPLELARALGADGvgpdydlltpELVAAAHAAG-LKVH---VWTVNDPEEMRRLLD 218

                          90       100
                  ....*....|....*....|....*
gi 1449613330 226 LGADGVFvgsgifkSDNPEKFARAI 250
Cdd:COG0584   219 LGVDGII-------TDRPDLLRAVL 236
trpA TIGR00262
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ...
 192-252 8.04e-03

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: 36.94  E-value: 8.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1449613330 192 YELLLQIKREGRLPV-VNFaagGVATPADAALMMQLGADGVFVGSGIFK-----SDNPEKFARAIVE 252
Cdd:TIGR00262 187 NELVKRLKAYSAKPVlVGF---GISKPEQVKQAIDAGADGVIVGSAIVKiieenLNTPEKMLQALEE 250
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 204-239 8.71e-03

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


Pssm-ID: 184165  Cd Length: 241  Bit Score: 36.81  E-value: 8.71e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1449613330 204 LPVVnfAAGGVATPADAALMMQLGADGVFVGSGIFK 239
Cdd:PRK13585  194 IPVI--ASGGVTTLDDLRALKEAGAAGVVVGSALYK 227
trpA PRK13111
tryptophan synthase subunit alpha; Provisional
 183-254 8.95e-03

tryptophan synthase subunit alpha; Provisional


Pssm-ID: 237285  Cd Length: 258  Bit Score: 37.01  E-value: 8.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449613330 183 TEAKLLGAPYELLLQIKREGRLPVvnfAAG-GVATPADAALMMQlGADGVFVGSGIFK--SDNPE------KFARAIVEA 253
Cdd:PRK13111  180 ARSADAADLAELVARLKAHTDLPV---AVGfGISTPEQAAAIAA-VADGVIVGSALVKiiEENPEalealaAFVKELKAA 255


                  .
gi 1449613330 254 T 254
Cdd:PRK13111  256 L 256
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 187-235 9.19e-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: 36.69  E-value: 9.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1449613330 187 LLGAPYELLLQIKREGRLPVVnfAAGGVATPADAALMMQLGADGVFVGS 235
Cdd:cd04732   174 LSGPNFELYKELAAATGIPVI--ASGGVSSLDDIKALKELGVAGVIVGK 220
 
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