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Conserved domains on  [gi|500174479|ref|WP_011848904|]
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pyridoxal 5'-phosphate synthase lyase subunit PdxS [Pyrobaculum calidifontis]

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;
40-336 0e+00

pyridoxal 5'-phosphate synthase lyase subunit PdxS;


:

Pssm-ID: 179769  Cd Length: 293  Bit Score: 523.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479  40 LAVGTPLVKLGFIAMLRRGVIMDVTNVEQAQVAEEAGAVGVMVLDKLPYDVRKAGGVARMADLKIIEEVMDAITIPVSAK 119
Cdd:PRK04180   1 LETGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479 120 VRIGHFYEAVLLEQIGVDLIDESEVLTPVDEQHHINKWLFKTPFVNGARELCEALRRISEGASMIRSKGEAGTGNVAEAV 199
Cdd:PRK04180  81 ARIGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479 200 KHFKAIYGAVRDLTAHRDDEeyLRDYARRCQVPLEVVKLTADMGRVPVITFAAGGIATPADAAFMMWLGADGVFVGSGIF 279
Cdd:PRK04180 161 RHMRQINGEIRRLTSMSEDE--LYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIF 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 500174479 280 KSQDPERRAEAIVLATAYWDDPEAVAEAQKMVSEkaSMMGIDIRALKPEELLQTRGV 336
Cdd:PRK04180 239 KSGDPEKRARAIVEATTHYDDPEVLAEVSKGLGE--AMVGIDIDELPPEERLQERGW 293
 
Name Accession Description Interval E-value
PRK04180 PRK04180
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
40-336 0e+00

pyridoxal 5'-phosphate synthase lyase subunit PdxS;


Pssm-ID: 179769  Cd Length: 293  Bit Score: 523.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479  40 LAVGTPLVKLGFIAMLRRGVIMDVTNVEQAQVAEEAGAVGVMVLDKLPYDVRKAGGVARMADLKIIEEVMDAITIPVSAK 119
Cdd:PRK04180   1 LETGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479 120 VRIGHFYEAVLLEQIGVDLIDESEVLTPVDEQHHINKWLFKTPFVNGARELCEALRRISEGASMIRSKGEAGTGNVAEAV 199
Cdd:PRK04180  81 ARIGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479 200 KHFKAIYGAVRDLTAHRDDEeyLRDYARRCQVPLEVVKLTADMGRVPVITFAAGGIATPADAAFMMWLGADGVFVGSGIF 279
Cdd:PRK04180 161 RHMRQINGEIRRLTSMSEDE--LYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIF 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 500174479 280 KSQDPERRAEAIVLATAYWDDPEAVAEAQKMVSEkaSMMGIDIRALKPEELLQTRGV 336
Cdd:PRK04180 239 KSGDPEKRARAIVEATTHYDDPEVLAEVSKGLGE--AMVGIDIDELPPEERLQERGW 293
PdxS COG0214
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ...
 40-336 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: 516.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479  40 LAVGTPLVKLGFIAMLRRGVIMDVTNVEQAQVAEEAGAVGVMVLDKLPYDVRKAGGVARMADLKIIEEVMDAITIPVSAK 119
Cdd:COG0214    1 LETGTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479 120 VRIGHFYEAVLLEQIGVDLIDESEVLTPVDEQHHINKWLFKTPFVNGARELCEALRRISEGASMIRSKGEAGTGNVAEAV 199
Cdd:COG0214   81 VRIGHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479 200 KHFKAIYGAVRDLTAHRDDEeyLRDYARRCQVPLEVVKLTADMGRVPVITFAAGGIATPADAAFMMWLGADGVFVGSGIF 279
Cdd:COG0214  161 RHMRTINSEIRRLQGMDEEE--LMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIF 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 500174479 280 KSQDPERRAEAIVLATAYWDDPEAVAEAQKMVSEkaSMMGIDIRALKPEELLQTRGV 336
Cdd:COG0214  239 KSEDPEKRARAIVEATTHYDDPEVLAEVSEGLGE--AMKGIDISTLPEEERLQERGW 293
pdxS cd04727
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ...
 50-335 1.01e-173

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: 483.29  E-value: 1.01e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479  50 GFIAMLRRGVIMDVTNVEQAQVAEEAGAVGVMVLDKLPYDVRKAGGVARMADLKIIEEVMDAITIPVSAKVRIGHFYEAV 129
Cdd:cd04727    2 GFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEAQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479 130 LLEQIGVDLIDESEVLTPVDEQHHINKWLFKTPFVNGARELCEALRRISEGASMIRSKGEAGTGNVAEAVKHFKAIYGAV 209
Cdd:cd04727   82 ILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGEI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479 210 RDLTAHRDDEeyLRDYARRCQVPLEVVKLTADMGRVPVITFAAGGIATPADAAFMMWLGADGVFVGSGIFKSQDPERRAE 289
Cdd:cd04727  162 RKLQSMSEEE--LYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRAR 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 500174479 290 AIVLATAYWDDPEAVAEAQKmvSEKASMMGIDIRALKPEELLQTRG 335
Cdd:cd04727  240 AIVEAVTHYDDPEILAEVSE--GLGEAMVGIDIASLKEEERMQERG 283
SOR_SNZ pfam01680
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ...
 44-251 2.39e-122

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: 349.86  E-value: 2.39e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479   44 TPLVKLGFIAMLRRGVIMDVTNVEQAQVAEEAGAVGVMVLDKLPYDVRKAGGVARMADLKIIEEVMDAITIPVSAKVRIG 123
Cdd:pfam01680   1 TFRVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479  124 HFYEAVLLEQIGVDLIDESEVLTPVDEQHHINKWLFKTPFVNGARELCEALRRISEGASMIRSKGEAGTGNVAEAVKHFK 203
Cdd:pfam01680  81 HFVEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 500174479  204 AIYGAVRDLTAHRDDEeyLRDYARRCQVPLEVVKLTADMGRVPVITFA 251
Cdd:pfam01680 161 TINGEIRRLQNMDEEE--LYAFAKELGAPYELVKEVAELGRLPVVNFA 206
 
Name Accession Description Interval E-value
PRK04180 PRK04180
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
40-336 0e+00

pyridoxal 5'-phosphate synthase lyase subunit PdxS;


Pssm-ID: 179769  Cd Length: 293  Bit Score: 523.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479  40 LAVGTPLVKLGFIAMLRRGVIMDVTNVEQAQVAEEAGAVGVMVLDKLPYDVRKAGGVARMADLKIIEEVMDAITIPVSAK 119
Cdd:PRK04180   1 LETGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479 120 VRIGHFYEAVLLEQIGVDLIDESEVLTPVDEQHHINKWLFKTPFVNGARELCEALRRISEGASMIRSKGEAGTGNVAEAV 199
Cdd:PRK04180  81 ARIGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479 200 KHFKAIYGAVRDLTAHRDDEeyLRDYARRCQVPLEVVKLTADMGRVPVITFAAGGIATPADAAFMMWLGADGVFVGSGIF 279
Cdd:PRK04180 161 RHMRQINGEIRRLTSMSEDE--LYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIF 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 500174479 280 KSQDPERRAEAIVLATAYWDDPEAVAEAQKMVSEkaSMMGIDIRALKPEELLQTRGV 336
Cdd:PRK04180 239 KSGDPEKRARAIVEATTHYDDPEVLAEVSKGLGE--AMVGIDIDELPPEERLQERGW 293
PdxS COG0214
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ...
 40-336 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: 516.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479  40 LAVGTPLVKLGFIAMLRRGVIMDVTNVEQAQVAEEAGAVGVMVLDKLPYDVRKAGGVARMADLKIIEEVMDAITIPVSAK 119
Cdd:COG0214    1 LETGTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479 120 VRIGHFYEAVLLEQIGVDLIDESEVLTPVDEQHHINKWLFKTPFVNGARELCEALRRISEGASMIRSKGEAGTGNVAEAV 199
Cdd:COG0214   81 VRIGHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479 200 KHFKAIYGAVRDLTAHRDDEeyLRDYARRCQVPLEVVKLTADMGRVPVITFAAGGIATPADAAFMMWLGADGVFVGSGIF 279
Cdd:COG0214  161 RHMRTINSEIRRLQGMDEEE--LMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIF 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 500174479 280 KSQDPERRAEAIVLATAYWDDPEAVAEAQKMVSEkaSMMGIDIRALKPEELLQTRGV 336
Cdd:COG0214  239 KSEDPEKRARAIVEATTHYDDPEVLAEVSEGLGE--AMKGIDISTLPEEERLQERGW 293
pdxS cd04727
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ...
 50-335 1.01e-173

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: 483.29  E-value: 1.01e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479  50 GFIAMLRRGVIMDVTNVEQAQVAEEAGAVGVMVLDKLPYDVRKAGGVARMADLKIIEEVMDAITIPVSAKVRIGHFYEAV 129
Cdd:cd04727    2 GFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEAQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479 130 LLEQIGVDLIDESEVLTPVDEQHHINKWLFKTPFVNGARELCEALRRISEGASMIRSKGEAGTGNVAEAVKHFKAIYGAV 209
Cdd:cd04727   82 ILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGEI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479 210 RDLTAHRDDEeyLRDYARRCQVPLEVVKLTADMGRVPVITFAAGGIATPADAAFMMWLGADGVFVGSGIFKSQDPERRAE 289
Cdd:cd04727  162 RKLQSMSEEE--LYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRAR 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 500174479 290 AIVLATAYWDDPEAVAEAQKmvSEKASMMGIDIRALKPEELLQTRG 335
Cdd:cd04727  240 AIVEAVTHYDDPEILAEVSE--GLGEAMVGIDIASLKEEERMQERG 283
SOR_SNZ pfam01680
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ...
 44-251 2.39e-122

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: 349.86  E-value: 2.39e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479   44 TPLVKLGFIAMLRRGVIMDVTNVEQAQVAEEAGAVGVMVLDKLPYDVRKAGGVARMADLKIIEEVMDAITIPVSAKVRIG 123
Cdd:pfam01680   1 TFRVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479  124 HFYEAVLLEQIGVDLIDESEVLTPVDEQHHINKWLFKTPFVNGARELCEALRRISEGASMIRSKGEAGTGNVAEAVKHFK 203
Cdd:pfam01680  81 HFVEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 500174479  204 AIYGAVRDLTAHRDDEeyLRDYARRCQVPLEVVKLTADMGRVPVITFA 251
Cdd:pfam01680 161 TINGEIRRLQNMDEEE--LYAFAKELGAPYELVKEVAELGRLPVVNFA 206
thiG CHL00162
thiamin biosynthesis protein G; Validated
 244-294 7.58e-09

thiamin biosynthesis protein G; Validated


Pssm-ID: 214380  Cd Length: 267  Bit Score: 55.87  E-value: 7.58e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 500174479 244 RVPVITFAagGIATPADAAFMMWLGADGVFVGSGIFKSQDPERRAEAIVLA 294
Cdd:CHL00162 189 KIPVIIDA--GIGTPSEASQAMELGASGVLLNTAVAQAKNPEQMAKAMKLA 237
thiG PRK00208
thiazole synthase; Reviewed
 244-294 1.73e-06

thiazole synthase; Reviewed


Pssm-ID: 234687  Cd Length: 250  Bit Score: 48.52  E-value: 1.73e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 500174479 244 RVPVITFAagGIATPADAAFMMWLGADGVFVGSGIFKSQDPERRAEAIVLA 294
Cdd:PRK00208 175 DVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFKLA 223
ThiG cd04728
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ...
 244-295 3.13e-06

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


Pssm-ID: 240079  Cd Length: 248  Bit Score: 47.87  E-value: 3.13e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 500174479 244 RVPVITFAagGIATPADAAFMMWLGADGVFVGSGIFKSQDPERRAEAIVLAT 295
Cdd:cd04728  175 DVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFKLAV 224
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 66-276 3.47e-06

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: 47.20  E-value: 3.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479  66 VEQAQVAEEAGAVGVMVLDKLPYDVRkaggvARMADLKIIEEVMDAITIPVSAKVRIGHFYEAV-----LLEQIGVDLID 140
Cdd:cd04722   15 VELAKAAAEAGADAIIVGTRSSDPEE-----AETDDKEVLKEVAAETDLPLGVQLAINDAAAAVdiaaaAARAAGADGVE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479 141 ESEVLTPVDEqhhinkwlfktpfvnGARELCEALRRISEGASMIRSKGEAGTGNVAEAVKHFKAIYGAVRdltahRDDEE 220
Cdd:cd04722   90 IHGAVGYLAR---------------EDLELIRELREAVPDVKVVVKLSPTGELAAAAAEEAGVDEVGLGN-----GGGGG 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 500174479 221 YLRDYARRCQVPLEVVKLtadmgRVPVITFAAGGIATPADAAFMMWLGADGVFVGS 276
Cdd:cd04722  150 GGRDAVPIADLLLILAKR-----GSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
ThiG pfam05690
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ...
 244-295 3.73e-06

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


Pssm-ID: 428589  Cd Length: 247  Bit Score: 47.63  E-value: 3.73e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 500174479  244 RVPVITFAagGIATPADAAFMMWLGADGVFVGSGIFKSQDPERRAEAIVLAT 295
Cdd:pfam05690 175 DVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFKLAV 224
PRK11840 PRK11840
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
 236-294 6.82e-06

bifunctional sulfur carrier protein/thiazole synthase protein; Provisional


Pssm-ID: 236998 [Multi-domain]  Cd Length: 326  Bit Score: 47.05  E-value: 6.82e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 500174479 236 VKLTADMGRVPVITFAagGIATPADAAFMMWLGADGVFVGSGIFKSQDPERRAEAIVLA 294
Cdd:PRK11840 241 IRLIVEGATVPVLVDA--GVGTASDAAVAMELGCDGVLMNTAIAEAKNPVLMARAMKLA 297
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 232-276 7.37e-06

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


Pssm-ID: 240081 [Multi-domain]  Cd Length: 236  Bit Score: 46.32  E-value: 7.37e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 500174479 232 PLEVVKLTADMGRVPVItfAAGGIATPADAAFMMWLGADGVFVGS 276
Cdd:cd04730  144 TFALVPEVRDAVDIPVI--AAGGIADGRGIAAALALGADGVQMGT 186
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 231-291 9.32e-05

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: 42.89  E-value: 9.32e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500174479 231 VPLEVVKLTADMGRVPVItfAAGGIaTPADAAFMMWLGADGVFVGSGIFKSQDPERRAEAI 291
Cdd:cd00564  137 LGLELLREIAELVEIPVV--AIGGI-TPENAAEVLAAGADGVAVISAITGADDPAAAAREL 194
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 66-279 1.50e-04

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


Pssm-ID: 439812 [Multi-domain]  Cd Length: 310  Bit Score: 42.77  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479  66 VEQAQVAEEAGAVGV---------MVldklpydVRKAGGVARMADL----KIIEEVMDAITIPVSAKVRIGhfyeavlle 132
Cdd:COG0042   77 AEAARIAEELGADEIdinmgcpvkKV-------TKGGAGAALLRDPelvaEIVKAVVEAVDVPVTVKIRLG--------- 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479 133 qigvdlidesevltpVDEQHHInkwlfktpfvngARELCEALRriSEGASMI---------RSKGEAgtgnvaeavkHFK 203
Cdd:COG0042  141 ---------------WDDDDEN------------ALEFARIAE--DAGAAALtvhgrtreqRYKGPA----------DWD 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500174479 204 AIYGAVRDLtahrddeeylrdyarrcqvplevvkltadmgRVPVItfAAGGIATPADAAFMM-WLGADGVFVGSGIF 279
Cdd:COG0042  182 AIARVKEAV-------------------------------SIPVI--GNGDIFSPEDAKRMLeETGCDGVMIGRGAL 225
IGPS cd00331
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ...
 247-291 3.61e-04

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: 41.30  E-value: 3.61e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 500174479 247 VITFAAGGIATPADAAFMMWLGADGVFVGSGIFKSQDPERRAEAI 291
Cdd:cd00331  173 VILVSESGISTPEDVKRLAEAGADAVLIGESLMRAPDPGAALREL 217
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 233-291 1.83e-03

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: 39.01  E-value: 1.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 500174479 233 LEVVKLTADMGRVPVitFAAGGIaTPADAAFMMWLGADGVFVGSGIFKSQDPERRAEAI 291
Cdd:COG0352  144 LEGLAWWAELVEIPV--VAIGGI-TPENAAEVLAAGADGVAVISAIWGAPDPAAAAREL 199
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
69-278 1.96e-03

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


Pssm-ID: 234907  Cd Length: 221  Bit Score: 38.98  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479  69 AQVAEEAGAVGVmvldklpydvrKAGGVARmadlkiIEEVMDAITIPVsakvrighfyeavlleqIGV---DLiDESEVl 145
Cdd:PRK01130  29 ALAAVQGGAVGI-----------RANGVED------IKAIRAVVDVPI-----------------IGIikrDY-PDSEV- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479 146 tpvdeqhhinkwlFKTPFVNGARELCEAlrriseGASMI--------RSKGEagtgNVAEAVKHFKAIYGA--------V 209
Cdd:PRK01130  73 -------------YITPTLKEVDALAAA------GADIIaldatlrpRPDGE----TLAELVKRIKEYPGQllmadcstL 129

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500174479 210 RD-LTAHRDDEEY----LRDY--ARRCQVP--LEVVKLTADMGRVPVItfAAGGIATPADAAFMMWLGADGVFVGSGI 278
Cdd:PRK01130 130 EEgLAAQKLGFDFigttLSGYteETKKPEEpdFALLKELLKAVGCPVI--AEGRINTPEQAKKALELGAHAVVVGGAI 205
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 232-276 1.96e-03

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


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 39.32  E-value: 1.96e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 500174479 232 PLEVVKLTADMGRVPVItfAAGGIATPADAAFMMWLGADGVFVGS 276
Cdd:COG2070  146 TFALVPEVRDAVDIPVI--AAGGIADGRGIAAALALGADGVQMGT 188
thiE PRK00043
thiamine phosphate synthase;
237-290 2.97e-03

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 38.24  E-value: 2.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 500174479 237 KLTADMGRVPVitFAAGGIaTPADAAFMMWLGADGVFVGSGIFKSQDPERRAEA 290
Cdd:PRK00043 153 EIRAAVGDIPI--VAIGGI-TPENAPEVLEAGADGVAVVSAITGAEDPEAAARA 203
PA cd00538
PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ...
 50-90 6.65e-03

PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases including, hSPPL2a and 2b which catalyze the intramembrane proteolysis of tumor necrosis factor alpha, ii) various proteins containing a C3H2C3 RING finger including, Arabidopsis ReMembR-H2 protein and various E3 ubiquitin ligases such as human GRAIL (gene related to anergy in lymphocytes), iii) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), iv) various plant vacuolar sorting receptors such as Pisum sativum BP-80, v) glutamate carboxypeptidase II (GCPII), vi) yeast aminopeptidase Y, vii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, viii) lactocepin (a cell envelope-associated protease from Lactobacillus paracasei subsp. paracasei NCDO 151), ix) various subtilisin-like proteases such as melon Cucumisin, and x) human TfR (transferrin receptor) 1 and 2.


Pssm-ID: 238300 [Multi-domain]  Cd Length: 126  Bit Score: 36.34  E-value: 6.65e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 500174479  50 GFIAMLRRGvimDVTNVEQAQVAEEAGAVGVMVLDKLPYDV 90
Cdd:cd00538   47 GKIVLVRRG---GCSFSEKVKNAQKAGAKAVIIYNNGDDPG 84
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 66-139 7.16e-03

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: 37.47  E-value: 7.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500174479  66 VEQAQVAEEAGAVGV---------MVldklpydVRKAGGVARMADL----KIIEEVMDAITIPVSAKVRIGHFYE----- 127
Cdd:cd02801   70 AEAAKIVEELGADGIdlnmgcpspKV-------TKGGAGAALLKDPelvaEIVRAVREAVPIPVTVKIRLGWDDEeetle 142

                         90
                 ....*....|...
gi 500174479 128 -AVLLEQIGVDLI 139
Cdd:cd02801  143 lAKALEDAGASAL 155
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 233-278 8.43e-03

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: 37.17  E-value: 8.43e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 500174479 233 LEVVKLTADMGRVPVItfAAGGIATPADAAFMMWLGADGVFVGSGI 278
Cdd:cd04729  166 FELLKELRKALGIPVI--AEGRINSPEQAAKALELGADAVVVGSAI 209
 
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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