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Conserved domains on  [gi|347588368|gb|AEP12898|]
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pyridoxal phosphate synthase yaaD subunit [Chloracidobacterium thermophilum B]

Protein Classification

pyridoxal 5'-phosphate synthase subunit PdxS( domain architecture ID 10785092)

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
PdxS COG0214
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ...
 10-298 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: 560.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368  10 RLKTGLAEMLKGGVIMDVVNVEQARIAEEAGAVAVMALERVPADIRRDGGVARMSNPRMIRQIMEAVSIPVMAKVRIGHT 89
Cdd:COG0214    7 RVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAKVRIGHF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368  90 AEAQVLEALGVDFIDESEVLTPADPYHHVNKFAFRVPFVCGATNLGEALRRIGEGAAMIRSKGEAGTGNIIEAVRHLREI 169
Cdd:COG0214   87 VEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAVRHMRTI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368 170 RRDIRLLTVLDEDELMAEAKRLQAPYELVRYVAQHGKLPVPLFAAGGVATPADAALCMQLGAETVFVGSGVFKSNDPARF 249
Cdd:COG0214  167 NSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSEDPEKR 246

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 347588368 250 ARAIVKAVTFYQDPAKVLEACEEIedGQPMRGLAIETLPAEQVLAARGW 298
Cdd:COG0214  247 ARAIVEATTHYDDPEVLAEVSEGL--GEAMKGIDISTLPEEERLQERGW 293
 
Name Accession Description Interval E-value
PdxS COG0214
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ...
 10-298 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: 560.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368  10 RLKTGLAEMLKGGVIMDVVNVEQARIAEEAGAVAVMALERVPADIRRDGGVARMSNPRMIRQIMEAVSIPVMAKVRIGHT 89
Cdd:COG0214    7 RVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAKVRIGHF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368  90 AEAQVLEALGVDFIDESEVLTPADPYHHVNKFAFRVPFVCGATNLGEALRRIGEGAAMIRSKGEAGTGNIIEAVRHLREI 169
Cdd:COG0214   87 VEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAVRHMRTI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368 170 RRDIRLLTVLDEDELMAEAKRLQAPYELVRYVAQHGKLPVPLFAAGGVATPADAALCMQLGAETVFVGSGVFKSNDPARF 249
Cdd:COG0214  167 NSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSEDPEKR 246

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 347588368 250 ARAIVKAVTFYQDPAKVLEACEEIedGQPMRGLAIETLPAEQVLAARGW 298
Cdd:COG0214  247 ARAIVEATTHYDDPEVLAEVSEGL--GEAMKGIDISTLPEEERLQERGW 293
PRK04180 PRK04180
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
10-298 0e+00

pyridoxal 5'-phosphate synthase lyase subunit PdxS;


Pssm-ID: 179769  Cd Length: 293  Bit Score: 551.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368  10 RLKTGLAEMLKGGVIMDVVNVEQARIAEEAGAVAVMALERVPADIRRDGGVARMSNPRMIRQIMEAVSIPVMAKVRIGHT 89
Cdd:PRK04180   7 RVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKARIGHF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368  90 AEAQVLEALGVDFIDESEVLTPADPYHHVNKFAFRVPFVCGATNLGEALRRIGEGAAMIRSKGEAGTGNIIEAVRHLREI 169
Cdd:PRK04180  87 VEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMRQI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368 170 RRDIRLLTVLDEDELMAEAKRLQAPYELVRYVAQHGKLPVPLFAAGGVATPADAALCMQLGAETVFVGSGVFKSNDPARF 249
Cdd:PRK04180 167 NGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSGDPEKR 246

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 347588368 250 ARAIVKAVTFYQDPAKVLEACEEIedGQPMRGLAIETLPAEQVLAARGW 298
Cdd:PRK04180 247 ARAIVEATTHYDDPEVLAEVSKGL--GEAMVGIDIDELPPEERLQERGW 293
pdxS cd04727
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ...
 13-297 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: 502.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368  13 TGLAEMLKGGVIMDVVNVEQARIAEEAGAVAVMALERVPADIRRDGGVARMSNPRMIRQIMEAVSIPVMAKVRIGHTAEA 92
Cdd:cd04727    1 RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368  93 QVLEALGVDFIDESEVLTPADPYHHVNKFAFRVPFVCGATNLGEALRRIGEGAAMIRSKGEAGTGNIIEAVRHLREIRRD 172
Cdd:cd04727   81 QILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368 173 IRLLTVLDEDELMAEAKRLQAPYELVRYVAQHGKLPVPLFAAGGVATPADAALCMQLGAETVFVGSGVFKSNDPARFARA 252
Cdd:cd04727  161 IRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARA 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 347588368 253 IVKAVTFYQDPAKVLEACEEIedGQPMRGLAIETLPAEQVLAARG 297
Cdd:cd04727  241 IVEAVTHYDDPEILAEVSEGL--GEAMVGIDIASLKEEERMQERG 283
TIGR00343 TIGR00343
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a ...
 11-298 8.96e-158

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: 441.52  E-value: 8.96e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368   11 LKTGLAEMLKGGVIMDVVNVEQARIAEEAGAVAVMALERVPADIRRDGGVARMSNPRMIRQIMEAVSIPVMAKVRIGHTA 90
Cdd:TIGR00343   1 LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368   91 EAQVLEALGVDFIDESEVLTPADPYHHVNKFAFRVPFVCGATNLGEALRRIGEGAAMIRSKGEAGTGNIIEAVRHLREIR 170
Cdd:TIGR00343  81 EAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368  171 RDIR-LLTVLDEDELMAEAKRLQAPYELVRYVAQHGKLPVPLFAAGGVATPADAALCMQLGAETVFVGSGVFKSNDPARF 249
Cdd:TIGR00343 161 EEIRqIQNMLEEEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 347588368  250 ARAIVKAVTFYQDPAKVLEACEEIedGQPMRGLAIETLPAEQVLAARGW 298
Cdd:TIGR00343 241 AKAIVEATTHYDNPEKLAEVSKDL--GEAMKGISISSISEAERLQERGW 287
SOR_SNZ pfam01680
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ...
 10-213 2.01e-146

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: 409.18  E-value: 2.01e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368   10 RLKTGLAEMLKGGVIMDVVNVEQARIAEEAGAVAVMALERVPADIRRDGGVARMSNPRMIRQIMEAVSIPVMAKVRIGHT 89
Cdd:pfam01680   3 RVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIGHF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368   90 AEAQVLEALGVDFIDESEVLTPADPYHHVNKFAFRVPFVCGATNLGEALRRIGEGAAMIRSKGEAGTGNIIEAVRHLREI 169
Cdd:pfam01680  83 VEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMRTI 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 347588368  170 RRDIRLLTVLDEDELMAEAKRLQAPYELVRYVAQHGKLPVPLFA 213
Cdd:pfam01680 163 NGEIRRLQNMDEEELYAFAKELGAPYELVKEVAELGRLPVVNFA 206
 
Name Accession Description Interval E-value
PdxS COG0214
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ...
 10-298 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: 560.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368  10 RLKTGLAEMLKGGVIMDVVNVEQARIAEEAGAVAVMALERVPADIRRDGGVARMSNPRMIRQIMEAVSIPVMAKVRIGHT 89
Cdd:COG0214    7 RVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAKVRIGHF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368  90 AEAQVLEALGVDFIDESEVLTPADPYHHVNKFAFRVPFVCGATNLGEALRRIGEGAAMIRSKGEAGTGNIIEAVRHLREI 169
Cdd:COG0214   87 VEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAVRHMRTI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368 170 RRDIRLLTVLDEDELMAEAKRLQAPYELVRYVAQHGKLPVPLFAAGGVATPADAALCMQLGAETVFVGSGVFKSNDPARF 249
Cdd:COG0214  167 NSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSEDPEKR 246

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 347588368 250 ARAIVKAVTFYQDPAKVLEACEEIedGQPMRGLAIETLPAEQVLAARGW 298
Cdd:COG0214  247 ARAIVEATTHYDDPEVLAEVSEGL--GEAMKGIDISTLPEEERLQERGW 293
PRK04180 PRK04180
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
10-298 0e+00

pyridoxal 5'-phosphate synthase lyase subunit PdxS;


Pssm-ID: 179769  Cd Length: 293  Bit Score: 551.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368  10 RLKTGLAEMLKGGVIMDVVNVEQARIAEEAGAVAVMALERVPADIRRDGGVARMSNPRMIRQIMEAVSIPVMAKVRIGHT 89
Cdd:PRK04180   7 RVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKARIGHF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368  90 AEAQVLEALGVDFIDESEVLTPADPYHHVNKFAFRVPFVCGATNLGEALRRIGEGAAMIRSKGEAGTGNIIEAVRHLREI 169
Cdd:PRK04180  87 VEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMRQI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368 170 RRDIRLLTVLDEDELMAEAKRLQAPYELVRYVAQHGKLPVPLFAAGGVATPADAALCMQLGAETVFVGSGVFKSNDPARF 249
Cdd:PRK04180 167 NGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSGDPEKR 246

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 347588368 250 ARAIVKAVTFYQDPAKVLEACEEIedGQPMRGLAIETLPAEQVLAARGW 298
Cdd:PRK04180 247 ARAIVEATTHYDDPEVLAEVSKGL--GEAMVGIDIDELPPEERLQERGW 293
pdxS cd04727
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ...
 13-297 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: 502.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368  13 TGLAEMLKGGVIMDVVNVEQARIAEEAGAVAVMALERVPADIRRDGGVARMSNPRMIRQIMEAVSIPVMAKVRIGHTAEA 92
Cdd:cd04727    1 RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368  93 QVLEALGVDFIDESEVLTPADPYHHVNKFAFRVPFVCGATNLGEALRRIGEGAAMIRSKGEAGTGNIIEAVRHLREIRRD 172
Cdd:cd04727   81 QILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368 173 IRLLTVLDEDELMAEAKRLQAPYELVRYVAQHGKLPVPLFAAGGVATPADAALCMQLGAETVFVGSGVFKSNDPARFARA 252
Cdd:cd04727  161 IRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARA 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 347588368 253 IVKAVTFYQDPAKVLEACEEIedGQPMRGLAIETLPAEQVLAARG 297
Cdd:cd04727  241 IVEAVTHYDDPEILAEVSEGL--GEAMVGIDIASLKEEERMQERG 283
TIGR00343 TIGR00343
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a ...
 11-298 8.96e-158

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: 441.52  E-value: 8.96e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368   11 LKTGLAEMLKGGVIMDVVNVEQARIAEEAGAVAVMALERVPADIRRDGGVARMSNPRMIRQIMEAVSIPVMAKVRIGHTA 90
Cdd:TIGR00343   1 LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368   91 EAQVLEALGVDFIDESEVLTPADPYHHVNKFAFRVPFVCGATNLGEALRRIGEGAAMIRSKGEAGTGNIIEAVRHLREIR 170
Cdd:TIGR00343  81 EAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368  171 RDIR-LLTVLDEDELMAEAKRLQAPYELVRYVAQHGKLPVPLFAAGGVATPADAALCMQLGAETVFVGSGVFKSNDPARF 249
Cdd:TIGR00343 161 EEIRqIQNMLEEEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 347588368  250 ARAIVKAVTFYQDPAKVLEACEEIedGQPMRGLAIETLPAEQVLAARGW 298
Cdd:TIGR00343 241 AKAIVEATTHYDNPEKLAEVSKDL--GEAMKGISISSISEAERLQERGW 287
SOR_SNZ pfam01680
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ...
 10-213 2.01e-146

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: 409.18  E-value: 2.01e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368   10 RLKTGLAEMLKGGVIMDVVNVEQARIAEEAGAVAVMALERVPADIRRDGGVARMSNPRMIRQIMEAVSIPVMAKVRIGHT 89
Cdd:pfam01680   3 RVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIGHF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368   90 AEAQVLEALGVDFIDESEVLTPADPYHHVNKFAFRVPFVCGATNLGEALRRIGEGAAMIRSKGEAGTGNIIEAVRHLREI 169
Cdd:pfam01680  83 VEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMRTI 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 347588368  170 RRDIRLLTVLDEDELMAEAKRLQAPYELVRYVAQHGKLPVPLFA 213
Cdd:pfam01680 163 NGEIRRLQNMDEEELYAFAKELGAPYELVKEVAELGRLPVVNFA 206
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 30-238 4.06e-07

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: 49.51  E-value: 4.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368  30 VEQARIAEEAGAVAVMALERVPADIRRDGGvarmsNPRMIRQIMEAVSIPVMAKVRIGHTAEAQ-----VLEALGVD--F 102
Cdd:cd04722   15 VELAKAAAEAGADAIIVGTRSSDPEEAETD-----DKEVLKEVAAETDLPLGVQLAINDAAAAVdiaaaAARAAGADgvE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368 103 IDESEVLTPADPYHHVNKFAFRVP-----FVCGATNLGEALRRIGEGAAMIRSKGEAGTGNIIEAVRHLREIRRDIRLlt 177
Cdd:cd04722   90 IHGAVGYLAREDLELIRELREAVPdvkvvVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKR-- 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 347588368 178 vldedelmaeakrlqapyelvryvaqhgKLPVPLFAAGGVATPADAALCMQLGAETVFVGS 238
Cdd:cd04722  168 ----------------------------GSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
ThiG pfam05690
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ...
 191-257 5.62e-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: 46.47  E-value: 5.62e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 347588368  191 LQAPYELvRYVAQHGKLPVPLFAagGVATPADAALCMQLGAETVFVGSGVFKSNDPARFARAIVKAV 257
Cdd:pfam05690 161 LLNPYNL-KIIIEEADVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFKLAV 224
ThiG cd04728
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ...
 209-257 8.49e-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: 45.94  E-value: 8.49e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 347588368 209 VPLFAAGGVATPADAALCMQLGAETVFVGSGVFKSNDPARFARAIVKAV 257
Cdd:cd04728  176 VPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFKLAV 224
PRK11840 PRK11840
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
 191-257 3.63e-05

bifunctional sulfur carrier protein/thiazole synthase protein; Provisional


Pssm-ID: 236998 [Multi-domain]  Cd Length: 326  Bit Score: 44.74  E-value: 3.63e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 347588368 191 LQAPYElVRYVAQHGKLPVPLFAagGVATPADAALCMQLGAETVFVGSGVFKSNDPARFARAIVKAV 257
Cdd:PRK11840 235 IQNPYT-IRLIVEGATVPVLVDA--GVGTASDAAVAMELGCDGVLMNTAIAEAKNPVLMARAMKLAV 298
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 30-103 3.77e-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: 3.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368  30 VEQARIAEEAGAVAVmalervpaDI----------RRDGGVARMSNP----RMIRQIMEAVSIPVMAKVRIGHTAE---- 91
Cdd:cd02801   70 AEAAKIVEELGADGI--------DLnmgcpspkvtKGGAGAALLKDPelvaEIVRAVREAVPIPVTVKIRLGWDDEeetl 141

                         90
                 ....*....|....
gi 347588368  92 --AQVLEALGVDFI 103
Cdd:cd02801  142 elAKALEDAGASAL 155
thiG PRK00208
thiazole synthase; Reviewed
 209-257 5.59e-05

thiazole synthase; Reviewed


Pssm-ID: 234687  Cd Length: 250  Bit Score: 43.51  E-value: 5.59e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 347588368 209 VPLFAAGGVATPADAALCMQLGAETVFVGSGVFKSNDPARFARAIVKAV 257
Cdd:PRK00208 176 VPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFKLAV 224
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 194-257 5.71e-05

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


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 44.24  E-value: 5.71e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 347588368 194 PYELVRYVAQhgKLPVPLFAAGGVaTPADAALCMQLGAETVFVGSGVFKSNDPARFARAIVKAV 257
Cdd:PRK07028 150 PLELLKEVSE--EVSIPIAVAGGL-DAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIREAI 210
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 186-253 1.25e-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: 42.18  E-value: 1.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 347588368 186 AEAKRLQAPYELVRYVAQHGKLPVPlfAAGGVaTPADAALCMQLGAETVFVGSGVFKSNDPARFARAI 253
Cdd:cd04726  138 AQAAGGWWPEDDLKKVKKLLGVKVA--VAGGI-TPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 196-255 1.30e-04

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: 42.12  E-value: 1.30e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368 196 ELVRYVAQHGKLPVplFAAGGVaTPADAALCMQLGAETVFVGSGVFKSNDPARFARAIVK 255
Cdd:cd00564  140 ELLREIAELVEIPV--VAIGGI-TPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
thiG CHL00162
thiamin biosynthesis protein G; Validated
 209-257 2.25e-04

thiamin biosynthesis protein G; Validated


Pssm-ID: 214380  Cd Length: 267  Bit Score: 42.00  E-value: 2.25e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 347588368 209 VPLFAAGGVATPADAALCMQLGAETVFVGSGVFKSNDPARFARAIVKAV 257
Cdd:CHL00162 190 IPVIIDAGIGTPSEASQAMELGASGVLLNTAVAQAKNPEQMAKAMKLAV 238
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
195-238 3.26e-04

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


Pssm-ID: 234907  Cd Length: 221  Bit Score: 41.29  E-value: 3.26e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 347588368 195 YELVRYVAQHGKlpVPLFAAGGVATPADAALCMQLGAETVFVGS 238
Cdd:PRK01130 162 FALLKELLKAVG--CPVIAEGRINTPEQAKKALELGAHAVVVGG 203
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 196-241 4.89e-04

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: 40.83  E-value: 4.89e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 347588368 196 ELVRYVAQHGKLPVPLFAAGGVATPADAALCMQLGAETVFVGSGVF 241
Cdd:COG0167  224 RMVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALF 269
PRK11840 PRK11840
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
 32-101 5.02e-04

bifunctional sulfur carrier protein/thiazole synthase protein; Provisional


Pssm-ID: 236998 [Multi-domain]  Cd Length: 326  Bit Score: 41.27  E-value: 5.02e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368  32 QARIAEEAGAVAVMALervPADIrrdGGVARMSNPRMIRQIMEAVSIPVMAKVRIGHTAEAQVLEALGVD 101
Cdd:PRK11840 210 AAKRLEDAGAVAVMPL---GAPI---GSGLGIQNPYTIRLIVEGATVPVLVDAGVGTASDAAVAMELGCD 273
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 195-238 5.14e-04

N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.


Pssm-ID: 240080 [Multi-domain]  Cd Length: 219  Bit Score: 40.64  E-value: 5.14e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 347588368 195 YELVRYVAQHGKlpVPLFAAGGVATPADAALCMQLGAETVFVGS 238
Cdd:cd04729  166 FELLKELRKALG--IPVIAEGRINSPEQAAKALELGADAVVVGS 207
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 191-238 8.03e-04

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


Pssm-ID: 240081 [Multi-domain]  Cd Length: 236  Bit Score: 40.16  E-value: 8.03e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 347588368 191 LQAPYELVRYVAQHgkLPVPLFAAGGVATPADAALCMQLGAETVFVGS 238
Cdd:cd04730  141 DIGTFALVPEVRDA--VDIPVIAAGGIADGRGIAAALALGADGVQMGT 186
PRK07565 PRK07565
dihydroorotate dehydrogenase-like protein;
30-101 1.27e-03

dihydroorotate dehydrogenase-like protein;


Pssm-ID: 236051  Cd Length: 334  Bit Score: 39.85  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368  30 VEQARIAEEAGAVAvmaLE----RVPADIRRDGGVARMSNPRMIRQIMEAVSIPVMAKV-----RIGHTAEaqVLEALGV 100
Cdd:PRK07565 117 VDYARQIEQAGADA---LElniyYLPTDPDISGAEVEQRYLDILRAVKSAVSIPVAVKLspyfsNLANMAK--RLDAAGA 191


                 .
gi 347588368 101 D 101
Cdd:PRK07565 192 D 192
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 30-103 2.26e-03

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: 38.92  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368  30 VEQARIAEEAGAVAVmalervpaDI----------RRDGGVARMSNP----RMIRQIMEAVSIPVMAKVRIG-----HTA 90
Cdd:COG0042   77 AEAARIAEELGADEI--------DInmgcpvkkvtKGGAGAALLRDPelvaEIVKAVVEAVDVPVTVKIRLGwddddENA 148

                         90
                 ....*....|....*
gi 347588368  91 E--AQVLEALGVDFI 103
Cdd:COG0042  149 LefARIAEDAGAAAL 163
Dus pfam01207
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ...
 30-251 2.85e-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: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368   30 VEQARIAEEAGAVAVMALERVPAD--IRRDGGVARMSNPRMIRQIME----AVSIPVMAKVRIGhtaeaqvlealgvdfI 103
Cdd:pfam01207  69 AEAAKLVEDRGADGIDINMGCPSKkvTRGGGGAALLRNPDLVAQIVKavvkAVGIPVTVKIRIG---------------W 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347588368  104 DESEVLTPadpyhhvnKFAFRvpfVCGAtnlgealrrigeGAAMIRSKGEAgtgniieavrhlREIRRDIRlltvldede 183
Cdd:pfam01207 134 DDSHENAV--------EIAKI---VEDA------------GAQALTVHGRT------------RAQNYEGT--------- 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 347588368  184 lmaeakrlqAPYELVRYVAQhgKLPVPLFAAGGVATPADAALCM-QLGAETVFVGSGVFksNDPARFAR 251
Cdd:pfam01207 170 ---------ADWDAIKQVKQ--AVSIPVIANGDITDPEDAQRCLaYTGADGVMIGRGAL--GNPWLFAE 225
DHOD_like cd04739
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ...
 30-101 2.91e-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: 38.75  E-value: 2.91e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 347588368  30 VEQARIAEEAGAVAV-MALERVPADIRRDGGVARMSNPRMIRQIMEAVSIPVMAKV-----RIGHTAEAqvLEALGVD 101
Cdd:cd04739  115 VDYARQIEEAGADALeLNIYALPTDPDISGAEVEQRYLDILRAVKSAVTIPVAVKLspffsALAHMAKQ--LDAAGAD 190
PRK04169 PRK04169
heptaprenylglyceryl phosphate synthase;
196-257 3.17e-03

heptaprenylglyceryl phosphate synthase;


Pssm-ID: 235237  Cd Length: 232  Bit Score: 38.25  E-value: 3.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347588368 196 ELVRYVAQHGKLpVPLFAAGGVATPADAALCMQLGAETVFVGSGVFksNDPARFARAIVKAV 257
Cdd:PRK04169 173 EMVKAVKKALDI-TPLIYGGGIRSPEQARELMAAGADTIVVGNIIE--EDPKKTVKAIKKAI 231
DHOD_DHPD_FMN cd02810
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ...
 193-253 5.27e-03

Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. 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. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.


Pssm-ID: 239204 [Multi-domain]  Cd Length: 289  Bit Score: 37.72  E-value: 5.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 347588368 193 APYELVRYVAQHGKLPVPLFAAGGVATPADAALCMQLGAETVFVGSGVFKsNDPARFARAI 253
Cdd:cd02810  228 LALRWVARLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMW-DGPDVIRKIK 287
 
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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