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Conserved domains on  [gi|21885347|gb|AAL59753|]
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dihydropteroate synthase type II [Vibrio cholerae]

Protein Classification

dihydropteroate synthase( domain architecture ID 10091421)

dihydropteroate synthase catalyzes the formation of 7,8-dihydropteroate from para-aminobenzoic acid and 6-hydroxymethyl-7,8-dihydropterin-pyrophosphate, a key step in the folate biosynthetic pathway; similar to Neisseria meningitidis dihydropteroate synthase FolP

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DHPS cd00739
DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional ...
7-262 2.47e-96

DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional homodimer, catalyzes the condensation of p-aminobenzoic acid (pABA) in the de novo biosynthesis of folate, which is an essential cofactor in both nucleic acid and protein biosynthesis. Prokaryotes (and some lower eukaryotes) must synthesize folate de novo, while higher eukaryotes are able to utilize dietary folate and therefore lack DHPS. Sulfonamide drugs, which are substrate analogs of pABA, target DHPS.


:

Pssm-ID: 238380  Cd Length: 257  Bit Score: 283.34  E-value: 2.47e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347   7 IFGIVNITSDSFSDGGRYLAPDAAIAQARKLMAEGADVIDLGPASSNPDAAPVSSDTEIARIAPVLDALKAD-GIPVSLD 85
Cdd:cd00739   3 IMGILNVTPDSFSDGGRFLSLDKAVAHAEKMIAEGADIIDIGGESTRPGADPVSVEEELERVIPVLEALRGElDVLISVD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347  86 SYQPATQAYALSRGVAYLNDIRGFP-DAAFYPQLAKSSAKLVVMHSVQDGQADRREAPAGDIMDHIAAFFDARIAALTGA 164
Cdd:cd00739  83 TFRAEVARAALEAGADIINDVSGGSdDPAMLEVAAEYGAPLVLMHMRGTPKTMQENPYYEDVVDEVLSFLEARLEAAESA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347 165 GIKRNRLVLDPGMGFFLGaaPETSLSVLARFDELRlRFDLPVLLSVSRKSFLRALTGRGPGDVGAATLAAELAAAAGGAD 244
Cdd:cd00739 163 GVARNRIILDPGIGFGKT--PEHNLELLRRLDELK-QLGLPVLVGASRKSFIGALLGREPKDRDWGTLALSALAAANGAD 239
                       250
                ....*....|....*...
gi 21885347 245 FIRTHEPRPLRDGLAVLA 262
Cdd:cd00739 240 IVRVHDVKATRDALKVAD 257
 
Name Accession Description Interval E-value
DHPS cd00739
DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional ...
7-262 2.47e-96

DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional homodimer, catalyzes the condensation of p-aminobenzoic acid (pABA) in the de novo biosynthesis of folate, which is an essential cofactor in both nucleic acid and protein biosynthesis. Prokaryotes (and some lower eukaryotes) must synthesize folate de novo, while higher eukaryotes are able to utilize dietary folate and therefore lack DHPS. Sulfonamide drugs, which are substrate analogs of pABA, target DHPS.


Pssm-ID: 238380  Cd Length: 257  Bit Score: 283.34  E-value: 2.47e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347   7 IFGIVNITSDSFSDGGRYLAPDAAIAQARKLMAEGADVIDLGPASSNPDAAPVSSDTEIARIAPVLDALKAD-GIPVSLD 85
Cdd:cd00739   3 IMGILNVTPDSFSDGGRFLSLDKAVAHAEKMIAEGADIIDIGGESTRPGADPVSVEEELERVIPVLEALRGElDVLISVD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347  86 SYQPATQAYALSRGVAYLNDIRGFP-DAAFYPQLAKSSAKLVVMHSVQDGQADRREAPAGDIMDHIAAFFDARIAALTGA 164
Cdd:cd00739  83 TFRAEVARAALEAGADIINDVSGGSdDPAMLEVAAEYGAPLVLMHMRGTPKTMQENPYYEDVVDEVLSFLEARLEAAESA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347 165 GIKRNRLVLDPGMGFFLGaaPETSLSVLARFDELRlRFDLPVLLSVSRKSFLRALTGRGPGDVGAATLAAELAAAAGGAD 244
Cdd:cd00739 163 GVARNRIILDPGIGFGKT--PEHNLELLRRLDELK-QLGLPVLVGASRKSFIGALLGREPKDRDWGTLALSALAAANGAD 239
                       250
                ....*....|....*...
gi 21885347 245 FIRTHEPRPLRDGLAVLA 262
Cdd:cd00739 240 IVRVHDVKATRDALKVAD 257
FolP COG0294
Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part ...
7-268 9.91e-82

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


Pssm-ID: 440063  Cd Length: 274  Bit Score: 246.89  E-value: 9.91e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347   7 IFGIVNITSDSFSDGGRYLAPDAAIAQARKLMAEGADVIDLGPASSNPDAAPVSSDTEIARIAPVLDALKAD-GIPVSLD 85
Cdd:COG0294  14 VMGILNVTPDSFSDGGRYNDPDAALAHAEEMVEEGADIIDIGGESTRPGAEPVSAEEELARVVPVIEALRAEfDVPISVD 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347  86 SYQPATQAYALSRGVAYLNDIRGF-PDAAFYPQLAKSSAKLVVMHSVQDGQADRREAPAGDIMDHIAAFFDARIAALTGA 164
Cdd:COG0294  94 TYKAEVARAALEAGADIINDVSGLrFDPEMAEVAAEYGVPVVLMHMRGTPQTMQRNPHYDDVVAEVRDFLEERIEAAEAA 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347 165 GIKRNRLVLDPGMGFflGAAPETSLSVLARFDELRlRFDLPVLLSVSRKSFLRALTGRGPGDVGAATLAAELAAAAGGAD 244
Cdd:COG0294 174 GIARERIILDPGIGF--GKTLEHNLELLRRLDELR-ALGYPVLVGVSRKSFIGALLGRPPEERLAGTLAAAALAAARGAD 250
                       250       260
                ....*....|....*....|....
gi 21885347 245 FIRTHEPRPLRDGLAVLAALKETA 268
Cdd:COG0294 251 IVRVHDVAETVDALKVADAIRRAR 274
Pterin_bind pfam00809
Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt ...
8-249 2.82e-80

Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt a TIM barrel fold. The family includes dihydropteroate synthase EC:2.5.1.15 as well as a group methyltransferase enzymes including methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) that catalyzes a key step in the Wood-Ljungdahl pathway of carbon dioxide fixation. It transfers the N5-methyl group from methyltetrahydrofolate (CH3-H4folate) to a cob(I)amide centre in another protein, the corrinoid iron-sulfur protein. MeTr is a member of a family of proteins that includes methionine synthase and methanogenic enzymes that activate the methyl group of methyltetra-hydromethano(or -sarcino)pterin.


Pssm-ID: 395651 [Multi-domain]  Cd Length: 243  Bit Score: 242.19  E-value: 2.82e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347     8 FGIVNITSDSFSDGGRYLAPDAAIAQARKLMAEGADVIDLGPASSNPDAAPVSSDTEIARIAPVLDALKAD-GIPVSLDS 86
Cdd:pfam00809   1 MGILNVTPDSFSDGGRFLDLDKALAHARRMVEEGADIIDIGGESTRPGAERVDGEEEMERVLPVLAALRDEaDVPISVDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347    87 YQPATQAYALSRGVAYLNDIRGFP-DAAFYPQLAKSSAKLVVMHSVQDGQADRREAP-AGDIMDHIAAFFDARIAALTGA 164
Cdd:pfam00809  81 TKAEVAEAALKAGADIINDISGGDgDPEMAELAAEYGAAVVVMHMDGTPKTMQENEQqYEDVVEEVERFLRARVAAAEEA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347   165 GIKRNRLVLDPGMGFflGAAPETSLSVLARFDELRLRFDLPVLLSVSRKSFLRALTGRGPGDVGAATLAAELAAAAGGAD 244
Cdd:pfam00809 161 GVPPEDIILDPGIGF--GKTEEHNLELLRTLDELRVILGVPVLLGVSRKSFIGRGLPLGGEERDAGTAAFLALAIAAGAD 238

                  ....*
gi 21885347   245 FIRTH 249
Cdd:pfam00809 239 IVRVH 243
DHPS TIGR01496
dihydropteroate synthase; This model represents dihydropteroate synthase, the enzyme that ...
6-264 1.37e-79

dihydropteroate synthase; This model represents dihydropteroate synthase, the enzyme that catalyzes the second to last step in folic acid biosynthesis. The gene is usually designated folP (folic acid biosynthsis) or sul (sulfanilamide resistance). This model represents one branch of the family of pterin-binding enzymes (pfam00809) and of a cluster of dihydropteroate synthase and related enzymes (COG0294). Other members of pfam00809 and COG0294 are represented by model TIGR00284. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]


Pssm-ID: 273657  Cd Length: 257  Bit Score: 240.62  E-value: 1.37e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347     6 IIFGIVNITSDSFSDGGRYLAPDAAIAQARKLMAEGADVIDLGPASSNPDAAPVSSDTEIARIAPVLDALK-ADGIPVSL 84
Cdd:TIGR01496   1 QIMGIVNVTPDSFSDGGRFLSVDKAVAHAERMLEEGADIIDVGGESTRPGADRVSPEEELNRVVPVIKALRdQPDVPISV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347    85 DSYQPATQAYALSRGVAYLNDIRGFPDAAFYPQLAKSSAKLVVMHSVQDGQADRREAPAGDIMDHIAAFFDARIAALTGA 164
Cdd:TIGR01496  81 DTYRAEVARAALEAGADIINDVSGGQDPAMLEVAAEYGVPLVLMHMRGTPRTMQENPHYEDVVEEVLRFLEARAEELVAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347   165 GIKRNRLVLDPGMGFFLgaAPETSLSVLARFDELRlRFDLPVLLSVSRKSFLRALTGRGPGDVGAATLAAELAAAAGGAD 244
Cdd:TIGR01496 161 GVAAERIILDPGIGFGK--TPEHNLELLKHLEEFV-ALGYPLLVGASRKSFIGALLGTPPEERLEGTLAASAYAVQKGAD 237
                         250       260
                  ....*....|....*....|
gi 21885347   245 FIRTHEPRPLRDGLAVLAAL 264
Cdd:TIGR01496 238 IVRVHDVKETRDALKVLEAL 257
PRK13753 PRK13753
dihydropteroate synthase; Provisional
5-258 3.23e-72

dihydropteroate synthase; Provisional


Pssm-ID: 184303  Cd Length: 279  Bit Score: 223.04  E-value: 3.23e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347    5 LIIFGIVNITSDSFSDGGRYLAPDAAIAQARKLMAEGADVIDLGPASSNPDAAPVSSDTEIARIAPVLDALKADGIPVSL 84
Cdd:PRK13753   2 VTVFGILNLTEDSFFDESRRLDPAGAVTAAIEMLRVGSDVVDVGPAASHPDARPVSPADEIRRIAPLLDALSDQMHRVSI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347   85 DSYQPATQAYALSRGVAYLNDIRGFPDAAFYPQLAKSSAKLVVMHSVQ-DGQADRR-EAPAGDIMDHIAAFFDARIAALT 162
Cdd:PRK13753  82 DSFQPETQRYALKRGVGYLNDIQGFPDPALYPDIAEADCRLVVMHSAQrDGIATRTgHLRPEDALDEIVRFFEARVSALR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347  163 GAGIKRNRLVLDPGMGFFLGAAPETSLSVLARFDELRLRFDLPVLLSVSRKSFLRALTGRGPGDVGAATLAAELAAAAGG 242
Cdd:PRK13753 162 RSGVAADRLILDPGMGFFLSPAPETSLHVLSNLQKLKSALGLPLLVSVSRKSFLGATVGLPVKDLGPASLAAELHAIGNG 241
                        250
                 ....*....|....*.
gi 21885347  243 ADFIRTHEPRPLRDGL 258
Cdd:PRK13753 242 ADYVRTHAPGDLRSAI 257
 
Name Accession Description Interval E-value
DHPS cd00739
DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional ...
7-262 2.47e-96

DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional homodimer, catalyzes the condensation of p-aminobenzoic acid (pABA) in the de novo biosynthesis of folate, which is an essential cofactor in both nucleic acid and protein biosynthesis. Prokaryotes (and some lower eukaryotes) must synthesize folate de novo, while higher eukaryotes are able to utilize dietary folate and therefore lack DHPS. Sulfonamide drugs, which are substrate analogs of pABA, target DHPS.


Pssm-ID: 238380  Cd Length: 257  Bit Score: 283.34  E-value: 2.47e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347   7 IFGIVNITSDSFSDGGRYLAPDAAIAQARKLMAEGADVIDLGPASSNPDAAPVSSDTEIARIAPVLDALKAD-GIPVSLD 85
Cdd:cd00739   3 IMGILNVTPDSFSDGGRFLSLDKAVAHAEKMIAEGADIIDIGGESTRPGADPVSVEEELERVIPVLEALRGElDVLISVD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347  86 SYQPATQAYALSRGVAYLNDIRGFP-DAAFYPQLAKSSAKLVVMHSVQDGQADRREAPAGDIMDHIAAFFDARIAALTGA 164
Cdd:cd00739  83 TFRAEVARAALEAGADIINDVSGGSdDPAMLEVAAEYGAPLVLMHMRGTPKTMQENPYYEDVVDEVLSFLEARLEAAESA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347 165 GIKRNRLVLDPGMGFFLGaaPETSLSVLARFDELRlRFDLPVLLSVSRKSFLRALTGRGPGDVGAATLAAELAAAAGGAD 244
Cdd:cd00739 163 GVARNRIILDPGIGFGKT--PEHNLELLRRLDELK-QLGLPVLVGASRKSFIGALLGREPKDRDWGTLALSALAAANGAD 239
                       250
                ....*....|....*...
gi 21885347 245 FIRTHEPRPLRDGLAVLA 262
Cdd:cd00739 240 IVRVHDVKATRDALKVAD 257
Pterin_binding cd00423
Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and ...
7-262 4.57e-82

Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and cobalamin-dependent methyltransferases such as methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) and methionine synthase (MetH). DHPS, a functional homodimer, catalyzes the condensation of p-aminobenzoic acid (pABA) in the de novo biosynthesis of folate, which is an essential cofactor in both nucleic acid and protein biosynthesis. Prokaryotes (and some lower eukaryotes) must synthesize folate de novo, while higher eukaryotes are able to utilize dietary folate and therefore lack DHPS. Sulfonamide drugs, which are substrate analogs of pABA, target DHPS. Cobalamin-dependent methyltransferases catalyze the transfer of a methyl group via a methyl- cob(III)amide intermediate. These include MeTr, a functional heterodimer, and the folate binding domain of MetH.


Pssm-ID: 238242 [Multi-domain]  Cd Length: 258  Bit Score: 247.19  E-value: 4.57e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347   7 IFGIVNITSDSFSDGGRYLAPDAAIAQARKLMAEGADVIDLGPASSNPDAAPVSSDTEIARIAPVLDALKAD-GIPVSLD 85
Cdd:cd00423   3 IMGILNVTPDSFSDGGKFLSLDKALEHARRMVEEGADIIDIGGESTRPGAEPVSVEEELERVIPVLRALAGEpDVPISVD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347  86 SYQPATQAYALSRGVAYLNDIRGFP-DAAFYPQLAKSSAKLVVMHSVQDGQADRREAPAGDIMDHIAAFFDARIAALTGA 164
Cdd:cd00423  83 TFNAEVAEAALKAGADIINDVSGGRgDPEMAPLAAEYGAPVVLMHMDGTPQTMQNNPYYADVVDEVVEFLEERVEAATEA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347 165 GIKRNRLVLDPGMGFflGAAPETSLSVLARFDELRLRFDLPVLLSVSRKSFLRALTGRGPGDVGAATLAAELAAAAGGAD 244
Cdd:cd00423 163 GIPPEDIILDPGIGF--GKTEEHNLELLRRLDAFRELPGLPLLLGVSRKSFLGDLLSVGPKDRLAGTAAFLAAAILNGAD 240
                       250
                ....*....|....*...
gi 21885347 245 FIRTHEPRPLRDGLAVLA 262
Cdd:cd00423 241 IVRVHDVKELRDAIKVAE 258
FolP COG0294
Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part ...
7-268 9.91e-82

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


Pssm-ID: 440063  Cd Length: 274  Bit Score: 246.89  E-value: 9.91e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347   7 IFGIVNITSDSFSDGGRYLAPDAAIAQARKLMAEGADVIDLGPASSNPDAAPVSSDTEIARIAPVLDALKAD-GIPVSLD 85
Cdd:COG0294  14 VMGILNVTPDSFSDGGRYNDPDAALAHAEEMVEEGADIIDIGGESTRPGAEPVSAEEELARVVPVIEALRAEfDVPISVD 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347  86 SYQPATQAYALSRGVAYLNDIRGF-PDAAFYPQLAKSSAKLVVMHSVQDGQADRREAPAGDIMDHIAAFFDARIAALTGA 164
Cdd:COG0294  94 TYKAEVARAALEAGADIINDVSGLrFDPEMAEVAAEYGVPVVLMHMRGTPQTMQRNPHYDDVVAEVRDFLEERIEAAEAA 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347 165 GIKRNRLVLDPGMGFflGAAPETSLSVLARFDELRlRFDLPVLLSVSRKSFLRALTGRGPGDVGAATLAAELAAAAGGAD 244
Cdd:COG0294 174 GIARERIILDPGIGF--GKTLEHNLELLRRLDELR-ALGYPVLVGVSRKSFIGALLGRPPEERLAGTLAAAALAAARGAD 250
                       250       260
                ....*....|....*....|....
gi 21885347 245 FIRTHEPRPLRDGLAVLAALKETA 268
Cdd:COG0294 251 IVRVHDVAETVDALKVADAIRRAR 274
Pterin_bind pfam00809
Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt ...
8-249 2.82e-80

Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt a TIM barrel fold. The family includes dihydropteroate synthase EC:2.5.1.15 as well as a group methyltransferase enzymes including methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) that catalyzes a key step in the Wood-Ljungdahl pathway of carbon dioxide fixation. It transfers the N5-methyl group from methyltetrahydrofolate (CH3-H4folate) to a cob(I)amide centre in another protein, the corrinoid iron-sulfur protein. MeTr is a member of a family of proteins that includes methionine synthase and methanogenic enzymes that activate the methyl group of methyltetra-hydromethano(or -sarcino)pterin.


Pssm-ID: 395651 [Multi-domain]  Cd Length: 243  Bit Score: 242.19  E-value: 2.82e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347     8 FGIVNITSDSFSDGGRYLAPDAAIAQARKLMAEGADVIDLGPASSNPDAAPVSSDTEIARIAPVLDALKAD-GIPVSLDS 86
Cdd:pfam00809   1 MGILNVTPDSFSDGGRFLDLDKALAHARRMVEEGADIIDIGGESTRPGAERVDGEEEMERVLPVLAALRDEaDVPISVDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347    87 YQPATQAYALSRGVAYLNDIRGFP-DAAFYPQLAKSSAKLVVMHSVQDGQADRREAP-AGDIMDHIAAFFDARIAALTGA 164
Cdd:pfam00809  81 TKAEVAEAALKAGADIINDISGGDgDPEMAELAAEYGAAVVVMHMDGTPKTMQENEQqYEDVVEEVERFLRARVAAAEEA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347   165 GIKRNRLVLDPGMGFflGAAPETSLSVLARFDELRLRFDLPVLLSVSRKSFLRALTGRGPGDVGAATLAAELAAAAGGAD 244
Cdd:pfam00809 161 GVPPEDIILDPGIGF--GKTEEHNLELLRTLDELRVILGVPVLLGVSRKSFIGRGLPLGGEERDAGTAAFLALAIAAGAD 238

                  ....*
gi 21885347   245 FIRTH 249
Cdd:pfam00809 239 IVRVH 243
DHPS TIGR01496
dihydropteroate synthase; This model represents dihydropteroate synthase, the enzyme that ...
6-264 1.37e-79

dihydropteroate synthase; This model represents dihydropteroate synthase, the enzyme that catalyzes the second to last step in folic acid biosynthesis. The gene is usually designated folP (folic acid biosynthsis) or sul (sulfanilamide resistance). This model represents one branch of the family of pterin-binding enzymes (pfam00809) and of a cluster of dihydropteroate synthase and related enzymes (COG0294). Other members of pfam00809 and COG0294 are represented by model TIGR00284. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]


Pssm-ID: 273657  Cd Length: 257  Bit Score: 240.62  E-value: 1.37e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347     6 IIFGIVNITSDSFSDGGRYLAPDAAIAQARKLMAEGADVIDLGPASSNPDAAPVSSDTEIARIAPVLDALK-ADGIPVSL 84
Cdd:TIGR01496   1 QIMGIVNVTPDSFSDGGRFLSVDKAVAHAERMLEEGADIIDVGGESTRPGADRVSPEEELNRVVPVIKALRdQPDVPISV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347    85 DSYQPATQAYALSRGVAYLNDIRGFPDAAFYPQLAKSSAKLVVMHSVQDGQADRREAPAGDIMDHIAAFFDARIAALTGA 164
Cdd:TIGR01496  81 DTYRAEVARAALEAGADIINDVSGGQDPAMLEVAAEYGVPLVLMHMRGTPRTMQENPHYEDVVEEVLRFLEARAEELVAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347   165 GIKRNRLVLDPGMGFFLgaAPETSLSVLARFDELRlRFDLPVLLSVSRKSFLRALTGRGPGDVGAATLAAELAAAAGGAD 244
Cdd:TIGR01496 161 GVAAERIILDPGIGFGK--TPEHNLELLKHLEEFV-ALGYPLLVGASRKSFIGALLGTPPEERLEGTLAASAYAVQKGAD 237
                         250       260
                  ....*....|....*....|
gi 21885347   245 FIRTHEPRPLRDGLAVLAAL 264
Cdd:TIGR01496 238 IVRVHDVKETRDALKVLEAL 257
PRK13753 PRK13753
dihydropteroate synthase; Provisional
5-258 3.23e-72

dihydropteroate synthase; Provisional


Pssm-ID: 184303  Cd Length: 279  Bit Score: 223.04  E-value: 3.23e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347    5 LIIFGIVNITSDSFSDGGRYLAPDAAIAQARKLMAEGADVIDLGPASSNPDAAPVSSDTEIARIAPVLDALKADGIPVSL 84
Cdd:PRK13753   2 VTVFGILNLTEDSFFDESRRLDPAGAVTAAIEMLRVGSDVVDVGPAASHPDARPVSPADEIRRIAPLLDALSDQMHRVSI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347   85 DSYQPATQAYALSRGVAYLNDIRGFPDAAFYPQLAKSSAKLVVMHSVQ-DGQADRR-EAPAGDIMDHIAAFFDARIAALT 162
Cdd:PRK13753  82 DSFQPETQRYALKRGVGYLNDIQGFPDPALYPDIAEADCRLVVMHSAQrDGIATRTgHLRPEDALDEIVRFFEARVSALR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347  163 GAGIKRNRLVLDPGMGFFLGAAPETSLSVLARFDELRLRFDLPVLLSVSRKSFLRALTGRGPGDVGAATLAAELAAAAGG 242
Cdd:PRK13753 162 RSGVAADRLILDPGMGFFLSPAPETSLHVLSNLQKLKSALGLPLLVSVSRKSFLGATVGLPVKDLGPASLAAELHAIGNG 241
                        250
                 ....*....|....*.
gi 21885347  243 ADFIRTHEPRPLRDGL 258
Cdd:PRK13753 242 ADYVRTHAPGDLRSAI 257
folP PRK11613
dihydropteroate synthase; Provisional
7-226 4.22e-39

dihydropteroate synthase; Provisional


Pssm-ID: 183230  Cd Length: 282  Bit Score: 137.58  E-value: 4.22e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347    7 IFGIVNITSDSFSDGGRYLAPDAAIAQARKLMAEGADVIDLGPASSNPDAAPVSSDTEIARIAPVLDAL-KADGIPVSLD 85
Cdd:PRK11613  17 VMGILNVTPDSFSDGGTHNSLIDAVKHANLMINAGATIIDVGGESTRPGAAEVSVEEELDRVIPVVEAIaQRFEVWISVD 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21885347   86 SYQPATQAYALSRGVAYLNDIRGFPDAAFYPQLAKSSAKLVVMHsVQDGQADRREAPA-GDIMDHIAAFFDARIAALTGA 164
Cdd:PRK11613  97 TSKPEVIRESAKAGAHIINDIRSLSEPGALEAAAETGLPVCLMH-MQGNPKTMQEAPKyDDVFAEVNRYFIEQIARCEAA 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21885347  165 GIKRNRLVLDPGMGFflGAAPETSLSVLARFDELRlRFDLPVLLSVSRKSFLRALTGRGPGD 226
Cdd:PRK11613 176 GIAKEKLLLDPGFGF--GKNLSHNYQLLARLAEFH-HFNLPLLVGMSRKSMIGQLLNVGPSE 234
 
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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