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Conserved domains on  [gi|1672633255|ref|WP_138277935|]
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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

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List of domain hits

 Name Accession Description Interval E-value
PRK04180 PRK04180
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
4-294 0e+00

pyridoxal 5'-phosphate synthase lyase subunit PdxS;


:

Pssm-ID: 179769  Cd Length: 293  Bit Score: 599.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255   4 KGTERVKRGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPRIVEEVQNAVTIPVMAKAR 83
Cdd:PRK04180    3 TGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKAR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255  84 IGHIVEARVLEALGVDYIDESEVLTPADEEFHLNKNEYTVPFVCGCRDLGEATRRIAEGASMLRTKGEPGTGNIVEAVRH 163
Cdd:PRK04180   83 IGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRH 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255 164 MRKVNAQIRKVAAMSEDELMTEAKNLGAPYELLVQIKKDGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSDN 243
Cdd:PRK04180  163 MRQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSGD 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1672633255 244 PAKFAKAIVEATTHFTDYRLIAELSKELGTAMKGIEISNLLPEERMQERGW 294
Cdd:PRK04180  243 PEKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDELPPEERLQERGW 293
 
Name Accession Description Interval E-value
PRK04180 PRK04180
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
4-294 0e+00

pyridoxal 5'-phosphate synthase lyase subunit PdxS;


Pssm-ID: 179769  Cd Length: 293  Bit Score: 599.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255   4 KGTERVKRGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPRIVEEVQNAVTIPVMAKAR 83
Cdd:PRK04180    3 TGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKAR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255  84 IGHIVEARVLEALGVDYIDESEVLTPADEEFHLNKNEYTVPFVCGCRDLGEATRRIAEGASMLRTKGEPGTGNIVEAVRH 163
Cdd:PRK04180   83 IGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRH 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255 164 MRKVNAQIRKVAAMSEDELMTEAKNLGAPYELLVQIKKDGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSDN 243
Cdd:PRK04180  163 MRQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSGD 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1672633255 244 PAKFAKAIVEATTHFTDYRLIAELSKELGTAMKGIEISNLLPEERMQERGW 294
Cdd:PRK04180  243 PEKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDELPPEERLQERGW 293
PdxS COG0214
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ...
 4-294 0e+00

Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5'-phosphate synthase subunit PdxS is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 439984  Cd Length: 293  Bit Score: 589.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255   4 KGTERVKRGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPRIVEEVQNAVTIPVMAKAR 83
Cdd:COG0214     3 TGTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAKVR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255  84 IGHIVEARVLEALGVDYIDESEVLTPADEEFHLNKNEYTVPFVCGCRDLGEATRRIAEGASMLRTKGEPGTGNIVEAVRH 163
Cdd:COG0214    83 IGHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAVRH 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255 164 MRKVNAQIRKVAAMSEDELMTEAKNLGAPYELLVQIKKDGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSDN 243
Cdd:COG0214   163 MRTINSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSED 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1672633255 244 PAKFAKAIVEATTHFTDYRLIAELSKELGTAMKGIEISNLLPEERMQERGW 294
Cdd:COG0214   243 PEKRARAIVEATTHYDDPEVLAEVSEGLGEAMKGIDISTLPEEERLQERGW 293
pdxS cd04727
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ...
 11-293 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: 542.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255  11 RGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPRIVEEVQNAVTIPVMAKARIGHIVEA 90
Cdd:cd04727     1 RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255  91 RVLEALGVDYIDESEVLTPADEEFHLNKNEYTVPFVCGCRDLGEATRRIAEGASMLRTKGEPGTGNIVEAVRHMRKVNAQ 170
Cdd:cd04727    81 QILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255 171 IRKVAAMSEDELMTEAKNLGAPYELLVQIKKDGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSDNPAKFAKA 250
Cdd:cd04727   161 IRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARA 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1672633255 251 IVEATTHFTDYRLIAELSKELGTAMKGIEISNLLPEERMQERG 293
Cdd:cd04727   241 IVEAVTHYDDPEILAEVSEGLGEAMVGIDIASLKEEERMQERG 283
TIGR00343 TIGR00343
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a ...
 9-294 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: 513.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255   9 VKRGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPRIVEEVQNAVTIPVMAKARIGHIV 88
Cdd:TIGR00343   1 LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255  89 EARVLEALGVDYIDESEVLTPADEEFHLNKNEYTVPFVCGCRDLGEATRRIAEGASMLRTKGEPGTGNIVEAVRHMRKVN 168
Cdd:TIGR00343  81 EAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255 169 AQIRKVAAMS-EDELMTEAKNLGAPYELLVQIKKDGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSDNPAKF 247
Cdd:TIGR00343 161 EEIRQIQNMLeEEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1672633255 248 AKAIVEATTHFTDYRLIAELSKELGTAMKGIEISNLLPEERMQERGW 294
Cdd:TIGR00343 241 AKAIVEATTHYDNPEKLAEVSKDLGEAMKGISISSISEAERLQERGW 287
SOR_SNZ pfam01680
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ...
 6-211 8.64e-149

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: 8.64e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255   6 TERVKRGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPRIVEEVQNAVTIPVMAKARIG 85
Cdd:pfam01680   1 TFRVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255  86 HIVEARVLEALGVDYIDESEVLTPADEEFHLNKNEYTVPFVCGCRDLGEATRRIAEGASMLRTKGEPGTGNIVEAVRHMR 165
Cdd:pfam01680  81 HFVEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1672633255 166 KVNAQIRKVAAMSEDELMTEAKNLGAPYELLVQIKKDGKLPVVNFA 211
Cdd:pfam01680 161 TINGEIRRLQNMDEEELYAFAKELGAPYELVKEVAELGRLPVVNFA 206
 
Name Accession Description Interval E-value
PRK04180 PRK04180
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
4-294 0e+00

pyridoxal 5'-phosphate synthase lyase subunit PdxS;


Pssm-ID: 179769  Cd Length: 293  Bit Score: 599.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255   4 KGTERVKRGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPRIVEEVQNAVTIPVMAKAR 83
Cdd:PRK04180    3 TGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKAR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255  84 IGHIVEARVLEALGVDYIDESEVLTPADEEFHLNKNEYTVPFVCGCRDLGEATRRIAEGASMLRTKGEPGTGNIVEAVRH 163
Cdd:PRK04180   83 IGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRH 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255 164 MRKVNAQIRKVAAMSEDELMTEAKNLGAPYELLVQIKKDGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSDN 243
Cdd:PRK04180  163 MRQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSGD 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1672633255 244 PAKFAKAIVEATTHFTDYRLIAELSKELGTAMKGIEISNLLPEERMQERGW 294
Cdd:PRK04180  243 PEKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDELPPEERLQERGW 293
PdxS COG0214
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ...
 4-294 0e+00

Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5'-phosphate synthase subunit PdxS is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 439984  Cd Length: 293  Bit Score: 589.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255   4 KGTERVKRGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPRIVEEVQNAVTIPVMAKAR 83
Cdd:COG0214     3 TGTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAKVR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255  84 IGHIVEARVLEALGVDYIDESEVLTPADEEFHLNKNEYTVPFVCGCRDLGEATRRIAEGASMLRTKGEPGTGNIVEAVRH 163
Cdd:COG0214    83 IGHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAVRH 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255 164 MRKVNAQIRKVAAMSEDELMTEAKNLGAPYELLVQIKKDGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSDN 243
Cdd:COG0214   163 MRTINSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSED 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1672633255 244 PAKFAKAIVEATTHFTDYRLIAELSKELGTAMKGIEISNLLPEERMQERGW 294
Cdd:COG0214   243 PEKRARAIVEATTHYDDPEVLAEVSEGLGEAMKGIDISTLPEEERLQERGW 293
pdxS cd04727
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ...
 11-293 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: 542.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255  11 RGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPRIVEEVQNAVTIPVMAKARIGHIVEA 90
Cdd:cd04727     1 RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255  91 RVLEALGVDYIDESEVLTPADEEFHLNKNEYTVPFVCGCRDLGEATRRIAEGASMLRTKGEPGTGNIVEAVRHMRKVNAQ 170
Cdd:cd04727    81 QILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255 171 IRKVAAMSEDELMTEAKNLGAPYELLVQIKKDGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSDNPAKFAKA 250
Cdd:cd04727   161 IRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARA 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1672633255 251 IVEATTHFTDYRLIAELSKELGTAMKGIEISNLLPEERMQERG 293
Cdd:cd04727   241 IVEAVTHYDDPEILAEVSEGLGEAMVGIDIASLKEEERMQERG 283
TIGR00343 TIGR00343
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a ...
 9-294 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: 513.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255   9 VKRGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPRIVEEVQNAVTIPVMAKARIGHIV 88
Cdd:TIGR00343   1 LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255  89 EARVLEALGVDYIDESEVLTPADEEFHLNKNEYTVPFVCGCRDLGEATRRIAEGASMLRTKGEPGTGNIVEAVRHMRKVN 168
Cdd:TIGR00343  81 EAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255 169 AQIRKVAAMS-EDELMTEAKNLGAPYELLVQIKKDGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSDNPAKF 247
Cdd:TIGR00343 161 EEIRQIQNMLeEEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1672633255 248 AKAIVEATTHFTDYRLIAELSKELGTAMKGIEISNLLPEERMQERGW 294
Cdd:TIGR00343 241 AKAIVEATTHYDNPEKLAEVSKDLGEAMKGISISSISEAERLQERGW 287
SOR_SNZ pfam01680
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ...
 6-211 8.64e-149

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: 8.64e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255   6 TERVKRGMAEMQKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPRIVEEVQNAVTIPVMAKARIG 85
Cdd:pfam01680   1 TFRVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255  86 HIVEARVLEALGVDYIDESEVLTPADEEFHLNKNEYTVPFVCGCRDLGEATRRIAEGASMLRTKGEPGTGNIVEAVRHMR 165
Cdd:pfam01680  81 HFVEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1672633255 166 KVNAQIRKVAAMSEDELMTEAKNLGAPYELLVQIKKDGKLPVVNFA 211
Cdd:pfam01680 161 TINGEIRRLQNMDEEELYAFAKELGAPYELVKEVAELGRLPVVNFA 206
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 28-236 6.47e-10

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 57.60  E-value: 6.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255  28 AEQAKIAEEAGAVAVMALERVPADIRAAGgvarmADPRIVEEVQNAVTIPVMAKARIGHIVE-----ARVLEALGVDYID 102
Cdd:cd04722    15 VELAKAAAEAGADAIIVGTRSSDPEEAET-----DDKEVLKEVAAETDLPLGVQLAINDAAAavdiaAAAARAAGADGVE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255 103 ESEVLTPADEEFHLNKNE-----YTVPFVCGCRDLGEATRRIAE--GASMLRTKGEPGTGNIVEAVrhmrkvnaqirkva 175
Cdd:cd04722    90 IHGAVGYLAREDLELIRElreavPDVKVVVKLSPTGELAAAAAEeaGVDEVGLGNGGGGGGGRDAV-------------- 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1672633255 176 amsedelmteaknlgaPYELLVQIKKDGKLPVVNFAAGGVATPADAALMMQLGADGVFVGS 236
Cdd:cd04722   156 ----------------PIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
thiG CHL00162
thiamin biosynthesis protein G; Validated
 199-251 1.47e-06

thiamin biosynthesis protein G; Validated


Pssm-ID: 214380  Cd Length: 267  Bit Score: 48.55  E-value: 1.47e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1672633255 199 IKKDGKLPVVNFAagGVATPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAI 251
Cdd:CHL00162  184 IIENAKIPVIIDA--GIGTPSEASQAMELGASGVLLNTAVAQAKNPEQMAKAM 234
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 194-253 1.87e-06

Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.


Pssm-ID: 238317 [Multi-domain]  Cd Length: 196  Bit Score: 47.51  E-value: 1.87e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255 194 ELLVQIKKDGKLPVVnfAAGGVaTPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAIVE 253
Cdd:cd00564   140 ELLREIAELVEIPVV--AIGGI-TPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 28-248 3.13e-06

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


Pssm-ID: 439812 [Multi-domain]  Cd Length: 310  Bit Score: 47.78  E-value: 3.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255  28 AEQAKIAEEAGAVAVmalervpaDI----------RAAGGVARMADP----RIVEEVQNAVTIPVMAKARIGhivearvl 93
Cdd:COG0042    77 AEAARIAEELGADEI--------DInmgcpvkkvtKGGAGAALLRDPelvaEIVKAVVEAVDVPVTVKIRLG-------- 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255  94 ealgvdyIDESevltpadeefHLNkneytvpfvcgCRDLGeatrRIAE--GASML----RTKGEpgtgniveavrhMRKV 167
Cdd:COG0042   141 -------WDDD----------DEN-----------ALEFA----RIAEdaGAAALtvhgRTREQ------------RYKG 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255 168 NAQirkvaamsedelmteaknlgapYELLVQIKKDGKLPVVnfAAGGVATPADAALMMQL-GADGVFVGSGIFKsdNPAK 246
Cdd:COG0042   177 PAD----------------------WDAIARVKEAVSIPVI--GNGDIFSPEDAKRMLEEtGCDGVMIGRGALG--NPWL 230


                  ..
gi 1672633255 247 FA 248
Cdd:COG0042   231 FR 232
ThiG cd04728
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ...
 194-254 7.97e-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: 46.33  E-value: 7.97e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1672633255 194 ELLVQIKKDGKLPVVNFAagGVATPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAI---VEA 254
Cdd:cd04728   165 YNLRIIIERADVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFklaVEA 226
ThiG pfam05690
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ...
 194-254 9.70e-06

Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole biosynthesis protein G sequences. ThiG, together with ThiF and ThiH, is proposed to be involved in the synthesis of 4-methyl-5-(b-hydroxyethyl)thiazole (THZ) which is an intermediate in the thiazole production pathway. This family also includes triosephosphate isomerase and pyridoxal 5'-phosphate synthase subunit PdxS.


Pssm-ID: 428589  Cd Length: 247  Bit Score: 46.09  E-value: 9.70e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1672633255 194 ELLVQIKKDGKLPVVNFAagGVATPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAI---VEA 254
Cdd:pfam05690 165 YNLKIIIEEADVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFklaVEA 226
thiG PRK00208
thiazole synthase; Reviewed
 204-254 1.09e-05

thiazole synthase; Reviewed


Pssm-ID: 234687  Cd Length: 250  Bit Score: 45.82  E-value: 1.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1672633255 204 KLPVVNFAagGVATPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAI---VEA 254
Cdd:PRK00208  175 DVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFklaVEA 226
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 191-255 1.82e-05

2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.


Pssm-ID: 240081 [Multi-domain]  Cd Length: 236  Bit Score: 45.17  E-value: 1.82e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1672633255 191 APYELLVQIKKDGKLPVVnfAAGGVATPADAALMMQLGADGVFVGSgIF----KSDNPAKFAKAIVEAT 255
Cdd:cd04730   143 GTFALVPEVRDAVDIPVI--AAGGIADGRGIAAALALGADGVQMGT-RFlateESGASPAYKQALLAAT 208
PRK11840 PRK11840
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
 199-254 2.06e-05

bifunctional sulfur carrier protein/thiazole synthase protein; Provisional


Pssm-ID: 236998 [Multi-domain]  Cd Length: 326  Bit Score: 45.51  E-value: 2.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1672633255 199 IKKDGKLPVVNFAagGVATPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAI---VEA 254
Cdd:PRK11840  244 IVEGATVPVLVDA--GVGTASDAAVAMELGCDGVLMNTAIAEAKNPVLMARAMklaVEA 300
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 28-249 4.15e-05

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: 44.02  E-value: 4.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255  28 AEQAKIAEEAGAVAVmalervpaDI----------RAAGGVARMADP----RIVEEVQNAVTIPVMAKARIGHivearvl 93
Cdd:cd02801    70 AEAAKIVEELGADGI--------DLnmgcpspkvtKGGAGAALLKDPelvaEIVRAVREAVPIPVTVKIRLGW------- 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255  94 ealgvdyidesevltpadeefhlNKNEYTVPFVCGCRDlgeatrriaEGASMLrtkgepgtgnIVeavrHMRKVnAQIRK 173
Cdd:cd02801   135 -----------------------DDEEETLELAKALED---------AGASAL----------TV----HGRTR-EQRYS 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1672633255 174 VAAmseDelmteaknlgapYELLVQIKKDGKLPVvnFAAGGVATPADAALMMQL-GADGVFVGSGIFKsdNPAKFAK 249
Cdd:cd02801   168 GPA---D------------WDYIAEIKEAVSIPV--IANGDIFSLEDALRCLEQtGVDGVMIGRGALG--NPWLFRE 225
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
193-238 6.33e-05

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


Pssm-ID: 234907  Cd Length: 221  Bit Score: 43.21  E-value: 6.33e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1672633255 193 YELLVQIKKDGKLPVVnfAAGGVATPADAALMMQLGADGVFVGSGI 238
Cdd:PRK01130  162 FALLKELLKAVGCPVI--AEGRINTPEQAKKALELGAHAVVVGGAI 205
IGPS cd00331
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ...
 211-251 6.96e-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: 43.22  E-value: 6.96e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1672633255 211 AAGGVATPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAI 251
Cdd:cd00331   177 SESGISTPEDVKRLAEAGADAVLIGESLMRAPDPGAALREL 217
thiE PRK00043
thiamine phosphate synthase;
194-255 1.06e-04

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 42.48  E-value: 1.06e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1672633255 194 ELLVQIKKDGK-LPVVnfAAGGVaTPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAIVEAT 255
Cdd:PRK00043  149 EGLREIRAAVGdIPIV--AIGGI-TPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAF 208
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 193-238 1.25e-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: 42.18  E-value: 1.25e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1672633255 193 YELLVQIKKDGKLPVVnfAAGGVATPADAALMMQLGADGVFVGSGI 238
Cdd:cd04729   166 FELLKELRKALGIPVI--AEGRINSPEQAAKALELGADAVVVGSAI 209
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 185-251 2.48e-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: 41.41  E-value: 2.48e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1672633255 185 EAKNLGAPYELLVQIKKDGKLPVVnfAAGGVaTPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAI 251
Cdd:cd04726   139 QAAGGWWPEDDLKKVKKLLGVKVA--VAGGI-TPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
Dus pfam01207
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ...
 28-248 2.76e-04

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: 41.93  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255  28 AEQAKIAEEAGAVAVMALERVPAD--IRAAGGVARMADP----RIVEEVQNAVTIPVMAKARIGhivearvlealgvdyI 101
Cdd:pfam01207  69 AEAAKLVEDRGADGIDINMGCPSKkvTRGGGGAALLRNPdlvaQIVKAVVKAVGIPVTVKIRIG---------------W 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255 102 DESevltpadeefHLNKNEYtVPFVCGCrdlgeatrriaeGASMLrtkgepgtgniveaVRHMRkvnaqirkvaamsede 181
Cdd:pfam01207 134 DDS----------HENAVEI-AKIVEDA------------GAQAL--------------TVHGR---------------- 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255 182 lmTEAKNLGAP--YELLVQIKKDGKLPVvnFAAGGVATPADA-ALMMQLGADGVFVGSGIFKsdNPAKFA 248
Cdd:pfam01207 161 --TRAQNYEGTadWDAIKQVKQAVSIPV--IANGDITDPEDAqRCLAYTGADGVMIGRGALG--NPWLFA 224
PRK07695 PRK07695
thiazole tautomerase TenI;
194-254 3.50e-04

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 40.77  E-value: 3.50e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1672633255 194 ELLVQIKKDGKLPVVnfAAGGVaTPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAIVEA 254
Cdd:PRK07695  139 EELSDIARALSIPVI--AIGGI-TPENTRDVLAAGVSGIAVMSGIFSSANPYSKAKRYAES 196
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 192-254 5.85e-04

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


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 41.16  E-value: 5.85e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1672633255 192 PYELLVQIKKDGKLPVVnfAAGGVaTPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAIVEA 254
Cdd:PRK07028  150 PLELLKEVSEEVSIPIA--VAGGL-DAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIREA 209
trpC PRK00278
indole-3-glycerol phosphate synthase TrpC;
214-254 8.62e-04

indole-3-glycerol phosphate synthase TrpC;


Pssm-ID: 234710  Cd Length: 260  Bit Score: 40.14  E-value: 8.62e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1672633255 214 GVATPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAIVEA 254
Cdd:PRK00278  219 GIFTPEDLKRLAKAGADAVLVGESLMRADDPGAALRELLGA 259
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 192-236 1.27e-03

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


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 39.71  E-value: 1.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1672633255 192 PYELLVQIKKDGKLPVVnfAAGGVATPADAALMMQLGADGVFVGS 236
Cdd:COG2070   146 TFALVPEVRDAVDIPVI--AAGGIADGRGIAAALALGADGVQMGT 188
PRK07565 PRK07565
dihydroorotate dehydrogenase-like protein;
31-99 2.74e-03

dihydroorotate dehydrogenase-like protein;


Pssm-ID: 236051  Cd Length: 334  Bit Score: 38.69  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672633255  31 AKIAEEAGAVAvmaLE----RVPADIRAAGGV--ARMADprIVEEVQNAVTIPVMAK-----ARIGHIveARVLEALGVD 99
Cdd:PRK07565  120 ARQIEQAGADA---LElniyYLPTDPDISGAEveQRYLD--ILRAVKSAVSIPVAVKlspyfSNLANM--AKRLDAAGAD 192
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 213-251 6.31e-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: 37.07  E-value: 6.31e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1672633255 213 GGVaTPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAI 251
Cdd:cd00429   173 GGI-NLETIPLLAEAGADVLVAGSALFGSDDYAEAIKEL 210
DHOD_like cd04739
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ...
 31-99 6.58e-03

Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. This subgroup has the conserved FMN binding site, but lacks some catalytic residues and may therefore be inactive.


Pssm-ID: 240090  Cd Length: 325  Bit Score: 37.59  E-value: 6.58e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1672633255  31 AKIAEEAGAVAV-MALERVPADIRAAGGVARMADPRIVEEVQNAVTIPVMAK-----ARIGHIveARVLEALGVD 99
Cdd:cd04739   118 ARQIEEAGADALeLNIYALPTDPDISGAEVEQRYLDILRAVKSAVTIPVAVKlspffSALAHM--AKQLDAAGAD 190
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 204-240 7.93e-03

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


Pssm-ID: 184165  Cd Length: 241  Bit Score: 37.19  E-value: 7.93e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1672633255 204 KLPVVnfAAGGVATPADAALMMQLGADGVFVGSGIFK 240
Cdd:PRK13585  193 DIPVI--ASGGVTTLDDLRALKEAGAAGVVVGSALYK 227
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
 200-237 8.27e-03

IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.


Pssm-ID: 238223 [Multi-domain]  Cd Length: 325  Bit Score: 37.11  E-value: 8.27e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1672633255 200 KKDGKLPVVnfaAGGVATPADAALMMQLGADGVFVGSG 237
Cdd:cd00381   131 KKYPNVDVI---AGNVVTAEAARDLIDAGADGVKVGIG 165
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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