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Conserved domains on  [gi|997304480|emb|CXU39754|]
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Pyridoxine biosynthesis glutamine amidotransferase%2C synthase subunit [Staphylococcus aureus]

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;
6-295 0e+00

pyridoxal 5'-phosphate synthase lyase subunit PdxS;


:

Pssm-ID: 179769  Cd Length: 293  Bit Score: 590.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480   6 GSDRVKRGMAEMQKGGVIMDVVNAEQARIAEEAGAVAVMALERVPSDIRAAGGVARMANPKIVEEVMNAVSIPVMAKARI 85
Cdd:PRK04180   4 GTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKARI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480  86 GHITEARVLEAMGVDYIDESEVLTPADEEYHLRKDQFTVPFVCGCRNLGEAARRIGEGAAMLRTKGEPGTGNIVEAVRHM 165
Cdd:PRK04180  84 GHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHM 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480 166 RQVNSEVSRLTVMNDDEIMTFAKDIGAPYEILKQIKDNGRLPVVNFAAGGVATPQDAALMMELGADGVFVGSGIFKSEDP 245
Cdd:PRK04180 164 RQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSGDP 243

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 997304480 246 EKFAKAIVQATTHYQDYELIGRLASELGTAMKGLDINQLSLEERMQERGW 295
Cdd:PRK04180 244 EKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDELPPEERLQERGW 293
 
Name Accession Description Interval E-value
PRK04180 PRK04180
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
6-295 0e+00

pyridoxal 5'-phosphate synthase lyase subunit PdxS;


Pssm-ID: 179769  Cd Length: 293  Bit Score: 590.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480   6 GSDRVKRGMAEMQKGGVIMDVVNAEQARIAEEAGAVAVMALERVPSDIRAAGGVARMANPKIVEEVMNAVSIPVMAKARI 85
Cdd:PRK04180   4 GTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKARI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480  86 GHITEARVLEAMGVDYIDESEVLTPADEEYHLRKDQFTVPFVCGCRNLGEAARRIGEGAAMLRTKGEPGTGNIVEAVRHM 165
Cdd:PRK04180  84 GHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHM 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480 166 RQVNSEVSRLTVMNDDEIMTFAKDIGAPYEILKQIKDNGRLPVVNFAAGGVATPQDAALMMELGADGVFVGSGIFKSEDP 245
Cdd:PRK04180 164 RQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSGDP 243

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 997304480 246 EKFAKAIVQATTHYQDYELIGRLASELGTAMKGLDINQLSLEERMQERGW 295
Cdd:PRK04180 244 EKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDELPPEERLQERGW 293
PdxS COG0214
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ...
 6-295 0e+00

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


Pssm-ID: 439984  Cd Length: 293  Bit Score: 581.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480   6 GSDRVKRGMAEMQKGGVIMDVVNAEQARIAEEAGAVAVMALERVPSDIRAAGGVARMANPKIVEEVMNAVSIPVMAKARI 85
Cdd:COG0214    4 GTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAKVRI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480  86 GHITEARVLEAMGVDYIDESEVLTPADEEYHLRKDQFTVPFVCGCRNLGEAARRIGEGAAMLRTKGEPGTGNIVEAVRHM 165
Cdd:COG0214   84 GHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAVRHM 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480 166 RQVNSEVSRLTVMNDDEIMTFAKDIGAPYEILKQIKDNGRLPVVNFAAGGVATPQDAALMMELGADGVFVGSGIFKSEDP 245
Cdd:COG0214  164 RTINSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSEDP 243

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 997304480 246 EKFAKAIVQATTHYQDYELIGRLASELGTAMKGLDINQLSLEERMQERGW 295
Cdd:COG0214  244 EKRARAIVEATTHYDDPEVLAEVSEGLGEAMKGIDISTLPEEERLQERGW 293
pdxS cd04727
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ...
 12-294 0e+00

PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in deoxyxylulose 5-phosphate (DXP)-independent pathway for de novo biosynthesis of PLP, present in some eubacteria, in archaea, fungi, plants, plasmodia, and some metazoa. Together with PdxT, PdxS forms the PLP synthase, a heteromeric glutamine amidotransferase (GATase), whereby PdxT produces ammonia from glutamine and PdxS combines ammonia with five- and three-carbon phosphosugars to form PLP. PLP is the biologically active form of vitamin B6, an essential cofactor in many biochemical processes. PdxS subunits form two hexameric rings.


Pssm-ID: 240078  Cd Length: 283  Bit Score: 531.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480  12 RGMAEMQKGGVIMDVVNAEQARIAEEAGAVAVMALERVPSDIRAAGGVARMANPKIVEEVMNAVSIPVMAKARIGHITEA 91
Cdd:cd04727    1 RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480  92 RVLEAMGVDYIDESEVLTPADEEYHLRKDQFTVPFVCGCRNLGEAARRIGEGAAMLRTKGEPGTGNIVEAVRHMRQVNSE 171
Cdd:cd04727   81 QILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480 172 VSRLTVMNDDEIMTFAKDIGAPYEILKQIKDNGRLPVVNFAAGGVATPQDAALMMELGADGVFVGSGIFKSEDPEKFAKA 251
Cdd:cd04727  161 IRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARA 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 997304480 252 IVQATTHYQDYELIGRLASELGTAMKGLDINQLSLEERMQERG 294
Cdd:cd04727  241 IVEAVTHYDDPEILAEVSEGLGEAMVGIDIASLKEEERMQERG 283
TIGR00343 TIGR00343
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a ...
 10-295 5.75e-175

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: 484.66  E-value: 5.75e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480   10 VKRGMAEMQKGGVIMDVVNAEQARIAEEAGAVAVMALERVPSDIRAAGGVARMANPKIVEEVMNAVSIPVMAKARIGHIT 89
Cdd:TIGR00343   1 LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480   90 EARVLEAMGVDYIDESEVLTPADEEYHLRKDQFTVPFVCGCRNLGEAARRIGEGAAMLRTKGEPGTGNIVEAVRHMRQVN 169
Cdd:TIGR00343  81 EAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480  170 SEVSRLTVMN-DDEIMTFAKDIGAPYEILKQIKDNGRLPVVNFAAGGVATPQDAALMMELGADGVFVGSGIFKSEDPEKF 248
Cdd:TIGR00343 161 EEIRQIQNMLeEEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 997304480  249 AKAIVQATTHYQDYELIGRLASELGTAMKGLDINQLSLEERMQERGW 295
Cdd:TIGR00343 241 AKAIVEATTHYDNPEKLAEVSKDLGEAMKGISISSISEAERLQERGW 287
SOR_SNZ pfam01680
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ...
 7-212 3.78e-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: 416.11  E-value: 3.78e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480    7 SDRVKRGMAEMQKGGVIMDVVNAEQARIAEEAGAVAVMALERVPSDIRAAGGVARMANPKIVEEVMNAVSIPVMAKARIG 86
Cdd:pfam01680   1 TFRVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480   87 HITEARVLEAMGVDYIDESEVLTPADEEYHLRKDQFTVPFVCGCRNLGEAARRIGEGAAMLRTKGEPGTGNIVEAVRHMR 166
Cdd:pfam01680  81 HFVEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 997304480  167 QVNSEVSRLTVMNDDEIMTFAKDIGAPYEILKQIKDNGRLPVVNFA 212
Cdd:pfam01680 161 TINGEIRRLQNMDEEELYAFAKELGAPYELVKEVAELGRLPVVNFA 206
 
Name Accession Description Interval E-value
PRK04180 PRK04180
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
6-295 0e+00

pyridoxal 5'-phosphate synthase lyase subunit PdxS;


Pssm-ID: 179769  Cd Length: 293  Bit Score: 590.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480   6 GSDRVKRGMAEMQKGGVIMDVVNAEQARIAEEAGAVAVMALERVPSDIRAAGGVARMANPKIVEEVMNAVSIPVMAKARI 85
Cdd:PRK04180   4 GTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKARI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480  86 GHITEARVLEAMGVDYIDESEVLTPADEEYHLRKDQFTVPFVCGCRNLGEAARRIGEGAAMLRTKGEPGTGNIVEAVRHM 165
Cdd:PRK04180  84 GHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHM 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480 166 RQVNSEVSRLTVMNDDEIMTFAKDIGAPYEILKQIKDNGRLPVVNFAAGGVATPQDAALMMELGADGVFVGSGIFKSEDP 245
Cdd:PRK04180 164 RQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSGDP 243

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 997304480 246 EKFAKAIVQATTHYQDYELIGRLASELGTAMKGLDINQLSLEERMQERGW 295
Cdd:PRK04180 244 EKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDELPPEERLQERGW 293
PdxS COG0214
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ...
 6-295 0e+00

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


Pssm-ID: 439984  Cd Length: 293  Bit Score: 581.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480   6 GSDRVKRGMAEMQKGGVIMDVVNAEQARIAEEAGAVAVMALERVPSDIRAAGGVARMANPKIVEEVMNAVSIPVMAKARI 85
Cdd:COG0214    4 GTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAKVRI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480  86 GHITEARVLEAMGVDYIDESEVLTPADEEYHLRKDQFTVPFVCGCRNLGEAARRIGEGAAMLRTKGEPGTGNIVEAVRHM 165
Cdd:COG0214   84 GHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAVRHM 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480 166 RQVNSEVSRLTVMNDDEIMTFAKDIGAPYEILKQIKDNGRLPVVNFAAGGVATPQDAALMMELGADGVFVGSGIFKSEDP 245
Cdd:COG0214  164 RTINSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSEDP 243

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 997304480 246 EKFAKAIVQATTHYQDYELIGRLASELGTAMKGLDINQLSLEERMQERGW 295
Cdd:COG0214  244 EKRARAIVEATTHYDDPEVLAEVSEGLGEAMKGIDISTLPEEERLQERGW 293
pdxS cd04727
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ...
 12-294 0e+00

PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in deoxyxylulose 5-phosphate (DXP)-independent pathway for de novo biosynthesis of PLP, present in some eubacteria, in archaea, fungi, plants, plasmodia, and some metazoa. Together with PdxT, PdxS forms the PLP synthase, a heteromeric glutamine amidotransferase (GATase), whereby PdxT produces ammonia from glutamine and PdxS combines ammonia with five- and three-carbon phosphosugars to form PLP. PLP is the biologically active form of vitamin B6, an essential cofactor in many biochemical processes. PdxS subunits form two hexameric rings.


Pssm-ID: 240078  Cd Length: 283  Bit Score: 531.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480  12 RGMAEMQKGGVIMDVVNAEQARIAEEAGAVAVMALERVPSDIRAAGGVARMANPKIVEEVMNAVSIPVMAKARIGHITEA 91
Cdd:cd04727    1 RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480  92 RVLEAMGVDYIDESEVLTPADEEYHLRKDQFTVPFVCGCRNLGEAARRIGEGAAMLRTKGEPGTGNIVEAVRHMRQVNSE 171
Cdd:cd04727   81 QILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480 172 VSRLTVMNDDEIMTFAKDIGAPYEILKQIKDNGRLPVVNFAAGGVATPQDAALMMELGADGVFVGSGIFKSEDPEKFAKA 251
Cdd:cd04727  161 IRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARA 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 997304480 252 IVQATTHYQDYELIGRLASELGTAMKGLDINQLSLEERMQERG 294
Cdd:cd04727  241 IVEAVTHYDDPEILAEVSEGLGEAMVGIDIASLKEEERMQERG 283
TIGR00343 TIGR00343
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a ...
 10-295 5.75e-175

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: 484.66  E-value: 5.75e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480   10 VKRGMAEMQKGGVIMDVVNAEQARIAEEAGAVAVMALERVPSDIRAAGGVARMANPKIVEEVMNAVSIPVMAKARIGHIT 89
Cdd:TIGR00343   1 LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480   90 EARVLEAMGVDYIDESEVLTPADEEYHLRKDQFTVPFVCGCRNLGEAARRIGEGAAMLRTKGEPGTGNIVEAVRHMRQVN 169
Cdd:TIGR00343  81 EAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480  170 SEVSRLTVMN-DDEIMTFAKDIGAPYEILKQIKDNGRLPVVNFAAGGVATPQDAALMMELGADGVFVGSGIFKSEDPEKF 248
Cdd:TIGR00343 161 EEIRQIQNMLeEEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 997304480  249 AKAIVQATTHYQDYELIGRLASELGTAMKGLDINQLSLEERMQERGW 295
Cdd:TIGR00343 241 AKAIVEATTHYDNPEKLAEVSKDLGEAMKGISISSISEAERLQERGW 287
SOR_SNZ pfam01680
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ...
 7-212 3.78e-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: 416.11  E-value: 3.78e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480    7 SDRVKRGMAEMQKGGVIMDVVNAEQARIAEEAGAVAVMALERVPSDIRAAGGVARMANPKIVEEVMNAVSIPVMAKARIG 86
Cdd:pfam01680   1 TFRVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480   87 HITEARVLEAMGVDYIDESEVLTPADEEYHLRKDQFTVPFVCGCRNLGEAARRIGEGAAMLRTKGEPGTGNIVEAVRHMR 166
Cdd:pfam01680  81 HFVEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 997304480  167 QVNSEVSRLTVMNDDEIMTFAKDIGAPYEILKQIKDNGRLPVVNFA 212
Cdd:pfam01680 161 TINGEIRRLQNMDEEELYAFAKELGAPYELVKEVAELGRLPVVNFA 206
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 29-237 2.25e-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: 61.83  E-value: 2.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480  29 AEQARIAEEAGAVAVMALERVPSDIRAAGgvarmANPKIVEEVMNAVSIPVMAKARIGHITE-----ARVLEAMGVDYID 103
Cdd:cd04722   15 VELAKAAAEAGADAIIVGTRSSDPEEAET-----DDKEVLKEVAAETDLPLGVQLAINDAAAavdiaAAAARAAGADGVE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480 104 ESEVLTPADEEYH-----LRKDQFTVPFVCGCRNLGEAARR--IGEGAAMLRTKGEPGTGNIVEAVRHMRQVNSEVsrlt 176
Cdd:cd04722   90 IHGAVGYLAREDLelireLREAVPDVKVVVKLSPTGELAAAaaEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILA---- 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 997304480 177 vmnddeimtfakdigapyeilkqikdNGRLPVVNFAAGGVATPQDAALMMELGADGVFVGS 237
Cdd:cd04722  166 --------------------------KRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
thiG CHL00162
thiamin biosynthesis protein G; Validated
 183-269 2.99e-09

thiamin biosynthesis protein G; Validated


Pssm-ID: 214380  Cd Length: 267  Bit Score: 56.64  E-value: 2.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480 183 IMTFAKDIGAPYEI-----LKQIKDNGRLPVVNFAagGVATPQDAALMMELGADGVFVGSGIFKSEDPEKFAKAI---VQ 254
Cdd:CHL00162 162 VMPLGSPIGSGQGLqnllnLQIIIENAKIPVIIDA--GIGTPSEASQAMELGASGVLLNTAVAQAKNPEQMAKAMklaVQ 239

                         90
                 ....*....|....*
gi 997304480 255 AtthyqdyeliGRLA 269
Cdd:CHL00162 240 A----------GRLA 244
ThiG pfam05690
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ...
 195-273 3.80e-08

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: 53.02  E-value: 3.80e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 997304480  195 EILKQIKDNGRLPVVNFAagGVATPQDAALMMELGADGVFVGSGIFKSEDPEKFAKAIVQATThyqdyelIGRLASELG 273
Cdd:pfam05690 165 YNLKIIIEEADVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFKLAVE-------AGRLAYLAG 234
PRK11840 PRK11840
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
 183-269 6.42e-08

bifunctional sulfur carrier protein/thiazole synthase protein; Provisional


Pssm-ID: 236998 [Multi-domain]  Cd Length: 326  Bit Score: 52.83  E-value: 6.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480 183 IMTFAKDIGA------PYEILKqIKDNGRLPVVNFAagGVATPQDAALMMELGADGVFVGSGIFKSEDPEKFAKAIVQAT 256
Cdd:PRK11840 222 VMPLGAPIGSglgiqnPYTIRL-IVEGATVPVLVDA--GVGTASDAAVAMELGCDGVLMNTAIAEAKNPVLMARAMKLAV 298

                         90
                 ....*....|...
gi 997304480 257 THYQDYELIGRLA 269
Cdd:PRK11840 299 EAGRLAYLAGRMP 311
ThiG cd04728
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ...
 197-273 1.19e-07

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


Pssm-ID: 240079  Cd Length: 248  Bit Score: 51.72  E-value: 1.19e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 997304480 197 LKQIKDNGRLPVVNFAagGVATPQDAALMMELGADGVFVGSGIFKSEDPEKFAKAIVQATThyqdyelIGRLASELG 273
Cdd:cd04728  167 LRIIIERADVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFKLAVE-------AGRLAYLAG 234
thiG PRK00208
thiazole synthase; Reviewed
 197-273 1.26e-07

thiazole synthase; Reviewed


Pssm-ID: 234687  Cd Length: 250  Bit Score: 51.60  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480 197 LKQIKDNGRLPVVNFAagGVATPQDAALMMELGADGVFVGSGIFKSEDPEKFAKAI---VQAtthyqdyeliGRLASELG 273
Cdd:PRK00208 167 LRIIIEQADVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFklaVEA----------GRLAYLAG 234
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 195-254 1.73e-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: 50.59  E-value: 1.73e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480 195 EILKQIKDNGRLPVVnfAAGGVaTPQDAALMMELGADGVFVGSGIFKSEDPEKFAKAIVQ 254
Cdd:cd00564  140 ELLREIAELVEIPVV--AIGGI-TPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 29-240 2.05e-07

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: 51.25  E-value: 2.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480  29 AEQARIAEEAGAVAVmalervpsDI----------RAAGGVARMANP----KIVEEVMNAVSIPVMAKARIGhitearvl 94
Cdd:COG0042   77 AEAARIAEELGADEI--------DInmgcpvkkvtKGGAGAALLRDPelvaEIVKAVVEAVDVPVTVKIRLG-------- 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480  95 eamgvdyIDESEvltpadeeyhlrkdqftvpfvcgcRNLGEAARRI-GEGAAML----RTKGEpgtgniveavrhmrqvn 169
Cdd:COG0042  141 -------WDDDD------------------------ENALEFARIAeDAGAAALtvhgRTREQ----------------- 172

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 997304480 170 sevsrltvmnddeimtfaKDIG-APYEILKQIKDNGRLPVVnfAAGGVATPQDAALMMEL-GADGVFVGSGIF 240
Cdd:COG0042  173 ------------------RYKGpADWDAIARVKEAVSIPVI--GNGDIFSPEDAKRMLEEtGCDGVMIGRGAL 225
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 195-255 3.66e-07

Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440121 [Multi-domain]  Cd Length: 206  Bit Score: 49.80  E-value: 3.66e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 997304480 195 EILKQIKDNGRLPVVnfAAGGVaTPQDAALMMELGADGVFVGSGIFKSEDPEKFAKAIVQA 255
Cdd:COG0352  145 EGLAWWAELVEIPVV--AIGGI-TPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAA 202
Dus pfam01207
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ...
 29-238 3.78e-07

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: 50.40  E-value: 3.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480   29 AEQARIAEEAGAVAVMALERVPSD--IRAAGGVARMANP----KIVEEVMNAVSIPVMAKARIGhitearvleamgvdyI 102
Cdd:pfam01207  69 AEAAKLVEDRGADGIDINMGCPSKkvTRGGGGAALLRNPdlvaQIVKAVVKAVGIPVTVKIRIG---------------W 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480  103 DESevltpadeeyhlrkdqftvpfvcgCRNLGEAARRI-GEGAAML----RTKGEPGTGNiveavrhmrqvnsevsrltv 177
Cdd:pfam01207 134 DDS------------------------HENAVEIAKIVeDAGAQALtvhgRTRAQNYEGT-------------------- 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 997304480  178 mnddeimtfakdigAPYEILKQIKDNGRLPVvnFAAGGVATPQDA-ALMMELGADGVFVGSG 238
Cdd:pfam01207 170 --------------ADWDAIKQVKQAVSIPV--IANGDITDPEDAqRCLAYTGADGVMIGRG 215
IGPS cd00331
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ...
 19-252 8.85e-07

Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, catalyzing the ring closure reaction of 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate (CdRP) to indole-3-glycerol phosphate (IGP), accompanied by the release of carbon dioxide and water. IGPS is active as a separate monomer in most organisms, but is also found fused to other enzymes as part of a bifunctional or multifunctional enzyme involved in tryptophan biosynthesis.


Pssm-ID: 238203  Cd Length: 217  Bit Score: 48.61  E-value: 8.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480  19 KGGVIMDVVNAEQARIAEEAGAVAVMALervpSDIRAAGGvarmaNPKIVEEVMNAVSIPVMAKARIGH---ITEARVLE 95
Cdd:cd00331   24 KGLIREDFDPVEIAKAYEKAGAAAISVL----TEPKYFQG-----SLEDLRAVREAVSLPVLRKDFIIDpyqIYEARAAG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480  96 AMGVDYIdeSEVLTPAD-EEYHLRkdqftvpfvcgCRNLG-----------EAARRIGEGAAMLrtkgepgtgniveavr 163
Cdd:cd00331   95 ADAVLLI--VAALDDEQlKELYEL-----------ARELGmevlvevhdeeELERALALGAKII---------------- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480 164 hmrQVNsevsrltvmNDDeIMTFAKDIGAPYEILKQIKDNgRLPVvnfAAGGVATPQDAALMMELGADGVFVGSGIFKSE 243
Cdd:cd00331  146 ---GIN---------NRD-LKTFEVDLNTTERLAPLIPKD-VILV---SESGISTPEDVKRLAEAGADAVLIGESLMRAP 208


                 ....*....
gi 997304480 244 DPEKFAKAI 252
Cdd:cd00331  209 DPGAALREL 217
IGPS pfam00218
Indole-3-glycerol phosphate synthase;
10-251 1.89e-06

Indole-3-glycerol phosphate synthase;


Pssm-ID: 395163  Cd Length: 252  Bit Score: 48.06  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480   10 VKRgmAEMQKGGVIMDVVNAEQARIAEEAGAVAVMALERVP------SDIRAaggvarmanpkiveeVMNAVSIPVMAKA 83
Cdd:pfam00218  53 VKK--ASPSKGLIREDFDPAEIARVYEAAGASAISVLTDPKyfqgsiEYLRA---------------VRQAVSLPVLRKD 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480   84 RI---GHITEARVLEAMGVDYIdeSEVLTpaDEEYHlrkdqftvpfvcgcrNLGEAARRIGegaaMlrtkgEPgtgnIVE 160
Cdd:pfam00218 116 FIideYQIDEARLAGADAILLI--VAVLD--DELLE---------------ELYAYARSLG----M-----EV----LVE 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480  161 avrhmrqVNSEV---------SRLTVMNDDEIMTFAKDIGAPYEILKQIKDNgrlpVVNFAAGGVATPQDAALMMELGAD 231
Cdd:pfam00218 164 -------VHNEEeleralalgAKIIGVNNRNLKTFEVDLNTTRRLAPLIPAD----VLLVAESGIYTPADVRELKEHGAN 232

                         250       260
                  ....*....|....*....|
gi 997304480  232 GVFVGSGIFKSEDPEKFAKA 251
Cdd:pfam00218 233 AFLVGESLMRQEDVRAAIRE 252
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 192-237 3.04e-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: 3.04e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 997304480 192 APYEILKQIKDNGRLPVVnfAAGGVATPQDAALMMELGADGVFVGS 237
Cdd:cd04730  143 GTFALVPEVRDAVDIPVI--AAGGIADGRGIAAALALGADGVQMGT 186
thiE PRK00043
thiamine phosphate synthase;
195-259 6.39e-06

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 45.94  E-value: 6.39e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 997304480 195 EILKQIKD-NGRLPVVnfAAGGVaTPQDAALMMELGADGVFVGSGIFKSEDPEKFAKAIVQATTHY 259
Cdd:PRK00043 149 EGLREIRAaVGDIPIV--AIGGI-TPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAA 211
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 193-255 1.23e-05

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


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 46.17  E-value: 1.23e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 997304480 193 PYEILKQIKDNGRLPVVnfAAGGVaTPQDAALMMELGADGVFVGSGIFKSEDPEKFAKAIVQA 255
Cdd:PRK07028 150 PLELLKEVSEEVSIPIA--VAGGL-DAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIREA 209
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 79-240 1.63e-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: 45.18  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480  79 VMAKArighiteARVLEAMGVDYIDesevltpadeeyhlrkdqftvpFVCGCrnlgeAARRI---GEGAAMLRTKGEpgT 155
Cdd:cd02801   68 TLAEA-------AKIVEELGADGID----------------------LNMGC-----PSPKVtkgGAGAALLKDPEL--V 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480 156 GNIVEAVRhmRQVNSEVS---RLTVMNDDEIMTFAKDI---GA----------------P--YEILKQIKDNGRLPVvnF 211
Cdd:cd02801  112 AEIVRAVR--EAVPIPVTvkiRLGWDDEEETLELAKALedaGAsaltvhgrtreqrysgPadWDYIAEIKEAVSIPV--I 187

                        170       180       190
                 ....*....|....*....|....*....|
gi 997304480 212 AAGGVATPQDAALMMEL-GADGVFVGSGIF 240
Cdd:cd02801  188 ANGDIFSLEDALRCLEQtGVDGVMIGRGAL 217
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 194-239 3.10e-05

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: 44.10  E-value: 3.10e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 997304480 194 YEILKQIKDNGRLPVVnfAAGGVATPQDAALMMELGADGVFVGSGI 239
Cdd:cd04729  166 FELLKELRKALGIPVI--AEGRINSPEQAAKALELGADAVVVGSAI 209
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
194-239 3.21e-05

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


Pssm-ID: 234907  Cd Length: 221  Bit Score: 43.98  E-value: 3.21e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 997304480 194 YEILKQIKDNGRLPVVnfAAGGVATPQDAALMMELGADGVFVGSGI 239
Cdd:PRK01130 162 FALLKELLKAVGCPVI--AEGRINTPEQAKKALELGAHAVVVGGAI 205
PRK07695 PRK07695
thiazole tautomerase TenI;
195-251 3.66e-05

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 43.86  E-value: 3.66e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 997304480 195 EILKQIKDNGRLPVVnfAAGGVaTPQDAALMMELGADGVFVGSGIFKSEDPEKFAKA 251
Cdd:PRK07695 139 EELSDIARALSIPVI--AIGGI-TPENTRDVLAAGVSGIAVMSGIFSSANPYSKAKR 192
trpC PRK00278
indole-3-glycerol phosphate synthase TrpC;
185-255 8.21e-05

indole-3-glycerol phosphate synthase TrpC;


Pssm-ID: 234710  Cd Length: 260  Bit Score: 43.22  E-value: 8.21e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 997304480 185 TFAKDIGAPYEILKQIKDNgRLPVvnfAAGGVATPQDAALMMELGADGVFVGSGIFKSEDPEKFAKAIVQA 255
Cdd:PRK00278 193 TFEVDLETTERLAPLIPSD-RLVV---SESGIFTPEDLKRLAKAGADAVLVGESLMRADDPGAALRELLGA 259
trpA TIGR00262
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ...
 172-252 3.69e-04

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: 41.18  E-value: 3.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480  172 VSRLTVmnddeimTFAKDIGAP--YEILKQIKDNGRLPV-VNFaagGVATPQDAALMMELGADGVFVGSGIFK-----SE 243
Cdd:TIGR00262 170 VSRAGV-------TGARNRAASalNELVKRLKAYSAKPVlVGF---GISKPEQVKQAIDAGADGVIVGSAIVKiieenLN 239


                  ....*....
gi 997304480  244 DPEKFAKAI 252
Cdd:TIGR00262 240 TPEKMLQAL 248
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 193-237 3.86e-04

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


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 41.25  E-value: 3.86e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 997304480 193 PYEILKQIKDNGRLPVVnfAAGGVATPQDAALMMELGADGVFVGS 237
Cdd:COG2070  146 TFALVPEVRDAVDIPVI--AAGGIADGRGIAAALALGADGVQMGT 188
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 203-285 4.27e-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: 41.21  E-value: 4.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480 203 NGRLPVVnfAAGGVATPQDAALMMELGADGVFVGSGIFksedpekfakaivqatthYQDYELIGRLASELGTAMKGLDIN 282
Cdd:COG0167  234 GGDIPII--GVGGISTAEDALEFILAGASAVQVGTALF------------------YEGPGLVRRIIRGLEAYLEEKGFS 293


                 ...
gi 997304480 283 QLS 285
Cdd:COG0167  294 SIS 296
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 198-241 6.51e-04

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


Pssm-ID: 184165  Cd Length: 241  Bit Score: 40.28  E-value: 6.51e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 997304480 198 KQIKDNGRLPVVnfAAGGVATPQDAALMMELGADGVFVGSGIFK 241
Cdd:PRK13585 186 KELVDSVDIPVI--ASGGVTTLDDLRALKEAGAAGVVVGSALYK 227
thiE TIGR00693
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ...
 195-252 6.72e-04

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


Pssm-ID: 273222 [Multi-domain]  Cd Length: 196  Bit Score: 39.92  E-value: 6.72e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 997304480  195 EILKQIKDNG-RLPVVnfAAGGVaTPQDAALMMELGADGVFVGSGIFKSEDPEKFAKAI 252
Cdd:TIGR00693 141 ELLREIAATLiDIPIV--AIGGI-TLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 195-252 1.03e-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: 39.39  E-value: 1.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 997304480 195 EILKQIKDNGRLPVVNFAAGGVaTPQDAALMMELGADGVFVGSGIFKSEDPEKFAKAI 252
Cdd:cd00429  154 RKLRELIPENNLNLLIEVDGGI-NLETIPLLAEAGADVLVAGSALFGSDDYAEAIKEL 210
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
 196-239 1.20e-03

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


Pssm-ID: 240086 [Multi-domain]  Cd Length: 353  Bit Score: 39.89  E-value: 1.20e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 997304480 196 ILKQIKD--NGRLPVVnfAAGGVATPQDAALMMELGADGVFVGSGI 239
Cdd:cd04735  273 IMELVKEriAGRLPLI--AVGSINTPDDALEALETGADLVAIGRGL 316
PRK04302 PRK04302
triosephosphate isomerase; Provisional
 211-247 1.58e-03

triosephosphate isomerase; Provisional


Pssm-ID: 235274  Cd Length: 223  Bit Score: 39.08  E-value: 1.58e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 997304480 211 FAAGGVATPQDAALMMELGADGVFVGSGIFKSEDPEK 247
Cdd:PRK04302 177 LCGAGISTGEDVKAALELGADGVLLASGVVKAKDPEA 213
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 197-255 1.60e-03

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


Pssm-ID: 439806  Cd Length: 218  Bit Score: 38.90  E-value: 1.60e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 997304480 197 LKQIKDNGRLPVVNFAAGGVaTPQDAALMMELGADGVFVGSGIFKSEDPEKFAKAIVQA 255
Cdd:COG0036  157 LRELIDERGLDILIEVDGGI-NAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREA 214
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
 195-239 2.61e-03

Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl)thiazole phosphate to yield thiamine phosphate. This Pfam family also includes the regulatory protein TENI, a protein from Bacillus subtilis that regulates the production of several extracellular enzymes by reducing alkaline protease production. While TenI shows high sequence similarity with thiamin phosphate synthase, the purified protein has no thiamin phosphate synthase activity. Instead, it is a thiazole tautomerase.


Pssm-ID: 426849 [Multi-domain]  Cd Length: 180  Bit Score: 37.91  E-value: 2.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 997304480  195 EILKQIKDNGRLPVVnfAAGGVaTPQDAALMMELGADGVFVGSGI 239
Cdd:pfam02581 139 EGLKAIAEAVEIPVV--AIGGI-TPENVPEVIEAGADGVAVVSAI 180
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 193-252 2.98e-03

3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates.


Pssm-ID: 240077 [Multi-domain]  Cd Length: 202  Bit Score: 37.95  E-value: 2.98e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480 193 PYEILKQIKDNGRLPVVnfAAGGVaTPQDAALMMELGADGVFVGSGIFKSEDPEKFAKAI 252
Cdd:cd04726  146 PEDDLKKVKKLLGVKVA--VAGGI-TPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
 195-238 4.25e-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: 38.27  E-value: 4.25e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 997304480 195 EILKQIKDN-GRLPVVnfaAGGVATPQDAALMMELGADGVFVGSG 238
Cdd:cd00381  124 EMIKFIKKKyPNVDVI---AGNVVTAEAARDLIDAGADGVKVGIG 165
TrpA COG0159
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ...
 195-277 6.53e-03

Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase alpha chain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439929  Cd Length: 262  Bit Score: 37.35  E-value: 6.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997304480 195 EILKQIKDNGRLPVvnfAAG-GVATPQDAALMMELgADGVFVGSgifksedpekfakAIVQATTHYQDYEL---IGRLAS 270
Cdd:COG0159  193 ELVARIRAHTDLPV---AVGfGISTPEQAAEVAAY-ADGVIVGS-------------ALVKLIEEGGDDEAleaLAAFVR 255


                 ....*..
gi 997304480 271 ELGTAMK 277
Cdd:COG0159  256 ELKAALR 262
PRK07565 PRK07565
dihydroorotate dehydrogenase-like protein;
32-100 8.36e-03

dihydroorotate dehydrogenase-like protein;


Pssm-ID: 236051  Cd Length: 334  Bit Score: 37.15  E-value: 8.36e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 997304480  32 ARIAEEAGAVAvmaLE----RVPSDIRAAGGVARMANPKIVEEVMNAVSIPVMAK-----ARIGHIteARVLEAMGVD 100
Cdd:PRK07565 120 ARQIEQAGADA---LElniyYLPTDPDISGAEVEQRYLDILRAVKSAVSIPVAVKlspyfSNLANM--AKRLDAAGAD 192
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 191-237 8.41e-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: 37.07  E-value: 8.41e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 997304480 191 GAPYEILKQIKDNGRLPVVnfAAGGVATPQDAALMMELGADGVFVGS 237
Cdd:cd04732  176 GPNFELYKELAAATGIPVI--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.
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