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Conserved domains on  [gi|1573864424|gb|RZD53862|]
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MAG: dihydropteroate synthase [Methanobacteriota archaeon]

Protein Classification

dihydropteroate synthase( domain architecture ID 11416730)

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

CATH:  3.20.20.20
EC:  2.5.1.15
PubMed:  19899766|22383850
SCOP:  4003341

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FolP COG0294
Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part ...
12-280 4.58e-125

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


:

Pssm-ID: 440063  Cd Length: 274  Bit Score: 357.06  E-value: 4.58e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  12 DDGRPRLMGIVNVTPDSFHAASRVASLEAAITTALDMWDAGADWVDVGGESTRPGAQPVPINEEISRVIPVIEALRnKRP 91
Cdd:COG0294     8 DLSRPLVMGILNVTPDSFSDGGRYNDPDAALAHAEEMVEEGADIIDIGGESTRPGAEPVSAEEELARVVPVIEALR-AEF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  92 HGLISIDTRHPSVATEALAAGANMVNDVSGLR-DPEMFNLVLESKCAVCIMHMLGEPGNMQSNPQYDNVVNEVSESLLST 170
Cdd:COG0294    87 DVPISVDTYKAEVARAALEAGADIINDVSGLRfDPEMAEVAAEYGVPVVLMHMRGTPQTMQRNPHYDDVVAEVRDFLEER 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424 171 ARRLIANGHSSELISLDSGIGFGKTLEQNLALLEKSEPFRGeEEFSLLWGVSRKSLFKDLLSREsSDQRLSGTLGVAAHA 250
Cdd:COG0294   167 IEAAEAAGIARERIILDPGIGFGKTLEHNLELLRRLDELRA-LGYPVLVGVSRKSFIGALLGRP-PEERLAGTLAAAALA 244
                         250       260       270
                  ....*....|....*....|....*....|
gi 1573864424 251 MSQGVDILRVHDVPEHHDLVTVLSELRNQQ 280
Cdd:COG0294   245 AARGADIVRVHDVAETVDALKVADAIRRAR 274
 
Name Accession Description Interval E-value
FolP COG0294
Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part ...
12-280 4.58e-125

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


Pssm-ID: 440063  Cd Length: 274  Bit Score: 357.06  E-value: 4.58e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  12 DDGRPRLMGIVNVTPDSFHAASRVASLEAAITTALDMWDAGADWVDVGGESTRPGAQPVPINEEISRVIPVIEALRnKRP 91
Cdd:COG0294     8 DLSRPLVMGILNVTPDSFSDGGRYNDPDAALAHAEEMVEEGADIIDIGGESTRPGAEPVSAEEELARVVPVIEALR-AEF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  92 HGLISIDTRHPSVATEALAAGANMVNDVSGLR-DPEMFNLVLESKCAVCIMHMLGEPGNMQSNPQYDNVVNEVSESLLST 170
Cdd:COG0294    87 DVPISVDTYKAEVARAALEAGADIINDVSGLRfDPEMAEVAAEYGVPVVLMHMRGTPQTMQRNPHYDDVVAEVRDFLEER 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424 171 ARRLIANGHSSELISLDSGIGFGKTLEQNLALLEKSEPFRGeEEFSLLWGVSRKSLFKDLLSREsSDQRLSGTLGVAAHA 250
Cdd:COG0294   167 IEAAEAAGIARERIILDPGIGFGKTLEHNLELLRRLDELRA-LGYPVLVGVSRKSFIGALLGRP-PEERLAGTLAAAALA 244
                         250       260       270
                  ....*....|....*....|....*....|
gi 1573864424 251 MSQGVDILRVHDVPEHHDLVTVLSELRNQQ 280
Cdd:COG0294   245 AARGADIVRVHDVAETVDALKVADAIRRAR 274
DHPS TIGR01496
dihydropteroate synthase; This model represents dihydropteroate synthase, the enzyme that ...
19-276 2.74e-99

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: 291.08  E-value: 2.74e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  19 MGIVNVTPDSFHAASRVASLEAAITTALDMWDAGADWVDVGGESTRPGAQPVPINEEISRVIPVIEALRnKRPHGLISID 98
Cdd:TIGR01496   3 MGIVNVTPDSFSDGGRFLSVDKAVAHAERMLEEGADIIDVGGESTRPGADRVSPEEELNRVVPVIKALR-DQPDVPISVD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  99 TRHPSVATEALAAGANMVNDVSGLRDPEMFNLVLESKCAVCIMHMLGEPGNMQSNPQYDNVVNEVSESLLSTARRLIANG 178
Cdd:TIGR01496  82 TYRAEVARAALEAGADIINDVSGGQDPAMLEVAAEYGVPLVLMHMRGTPRTMQENPHYEDVVEEVLRFLEARAEELVAAG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424 179 HSSELISLDSGIGFGKTLEQNLALLEKSEPFRgEEEFSLLWGVSRKSlFKDLLSRESSDQRLSGTLGVAAHAMSQGVDIL 258
Cdd:TIGR01496 162 VAAERIILDPGIGFGKTPEHNLELLKHLEEFV-ALGYPLLVGASRKS-FIGALLGTPPEERLEGTLAASAYAVQKGADIV 239
                         250
                  ....*....|....*...
gi 1573864424 259 RVHDVPEHHDLVTVLSEL 276
Cdd:TIGR01496 240 RVHDVKETRDALKVLEAL 257
DHPS cd00739
DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional ...
16-273 2.54e-98

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: 288.74  E-value: 2.54e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  16 PRLMGIVNVTPDSFHAASRVASLEAAITTALDMWDAGADWVDVGGESTRPGAQPVPINEEISRVIPVIEALRnKRPHGLI 95
Cdd:cd00739     1 TQIMGILNVTPDSFSDGGRFLSLDKAVAHAEKMIAEGADIIDIGGESTRPGADPVSVEEELERVIPVLEALR-GELDVLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  96 SIDTRHPSVATEALAAGANMVNDVSGLR-DPEMFNLVLESKCAVCIMHMLGEPGNMQSNPQYDNVVNEVSESLLSTARRL 174
Cdd:cd00739    80 SVDTFRAEVARAALEAGADIINDVSGGSdDPAMLEVAAEYGAPLVLMHMRGTPKTMQENPYYEDVVDEVLSFLEARLEAA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424 175 IANGHSSELISLDSGIGFGKTLEQNLALLEKSEPFRgEEEFSLLWGVSRKSLFKDLLSRESSDqRLSGTLGVAAHAMSQG 254
Cdd:cd00739   160 ESAGVARNRIILDPGIGFGKTPEHNLELLRRLDELK-QLGLPVLVGASRKSFIGALLGREPKD-RDWGTLALSALAAANG 237
                         250
                  ....*....|....*....
gi 1573864424 255 VDILRVHDVPEHHDLVTVL 273
Cdd:cd00739   238 ADIVRVHDVKATRDALKVA 256
Pterin_bind pfam00809
Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt ...
19-261 1.62e-79

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: 240.65  E-value: 1.62e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  19 MGIVNVTPDSFHAASRVASLEAAITTALDMWDAGADWVDVGGESTRPGAQPVPINEEISRVIPVIEALRnKRPHGLISID 98
Cdd:pfam00809   1 MGILNVTPDSFSDGGRFLDLDKALAHARRMVEEGADIIDIGGESTRPGAERVDGEEEMERVLPVLAALR-DEADVPISVD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  99 TRHPSVATEALAAGANMVNDVSGLR-DPEMFNLVLESKCAVCIMHMLGEPGNMQSNP-QYDNVVNEVSESLLSTARRLIA 176
Cdd:pfam00809  80 TTKAEVAEAALKAGADIINDISGGDgDPEMAELAAEYGAAVVVMHMDGTPKTMQENEqQYEDVVEEVERFLRARVAAAEE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424 177 NGHSSELISLDSGIGFGKTLEQNLALLEKSEPFRGEEEFSLLWGVSRKSLFKDLLSRESSDqRLSGTLGVAAHAMSQGVD 256
Cdd:pfam00809 160 AGVPPEDIILDPGIGFGKTEEHNLELLRTLDELRVILGVPVLLGVSRKSFIGRGLPLGGEE-RDAGTAAFLALAIAAGAD 238

                  ....*
gi 1573864424 257 ILRVH 261
Cdd:pfam00809 239 IVRVH 243
folP PRK11613
dihydropteroate synthase; Provisional
12-265 5.65e-72

dihydropteroate synthase; Provisional


Pssm-ID: 183230  Cd Length: 282  Bit Score: 222.70  E-value: 5.65e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  12 DDGRPRLMGIVNVTPDSFHAASRVASLEAAITTALDMWDAGADWVDVGGESTRPGAQPVPINEEISRVIPVIEALRnKRP 91
Cdd:PRK11613   11 DLSHPHVMGILNVTPDSFSDGGTHNSLIDAVKHANLMINAGATIIDVGGESTRPGAAEVSVEEELDRVIPVVEAIA-QRF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  92 HGLISIDTRHPSVATEALAAGANMVNDVSGLRDPEMFNLVLESKCAVCIMHMLGEPGNMQSNPQYDNVVNEVSESLLSTA 171
Cdd:PRK11613   90 EVWISVDTSKPEVIRESAKAGAHIINDIRSLSEPGALEAAAETGLPVCLMHMQGNPKTMQEAPKYDDVFAEVNRYFIEQI 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424 172 RRLIANGHSSELISLDSGIGFGKTLEQNLALLEKSEPFRgEEEFSLLWGVSRKSLFKDLLSrESSDQRLSGTLGVAAHAM 251
Cdd:PRK11613  170 ARCEAAGIAKEKLLLDPGFGFGKNLSHNYQLLARLAEFH-HFNLPLLVGMSRKSMIGQLLN-VGPSERLSGSLACAVIAA 247
                         250
                  ....*....|....
gi 1573864424 252 SQGVDILRVHDVPE 265
Cdd:PRK11613  248 MQGAQIIRVHDVKE 261
 
Name Accession Description Interval E-value
FolP COG0294
Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part ...
12-280 4.58e-125

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


Pssm-ID: 440063  Cd Length: 274  Bit Score: 357.06  E-value: 4.58e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  12 DDGRPRLMGIVNVTPDSFHAASRVASLEAAITTALDMWDAGADWVDVGGESTRPGAQPVPINEEISRVIPVIEALRnKRP 91
Cdd:COG0294     8 DLSRPLVMGILNVTPDSFSDGGRYNDPDAALAHAEEMVEEGADIIDIGGESTRPGAEPVSAEEELARVVPVIEALR-AEF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  92 HGLISIDTRHPSVATEALAAGANMVNDVSGLR-DPEMFNLVLESKCAVCIMHMLGEPGNMQSNPQYDNVVNEVSESLLST 170
Cdd:COG0294    87 DVPISVDTYKAEVARAALEAGADIINDVSGLRfDPEMAEVAAEYGVPVVLMHMRGTPQTMQRNPHYDDVVAEVRDFLEER 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424 171 ARRLIANGHSSELISLDSGIGFGKTLEQNLALLEKSEPFRGeEEFSLLWGVSRKSLFKDLLSREsSDQRLSGTLGVAAHA 250
Cdd:COG0294   167 IEAAEAAGIARERIILDPGIGFGKTLEHNLELLRRLDELRA-LGYPVLVGVSRKSFIGALLGRP-PEERLAGTLAAAALA 244
                         250       260       270
                  ....*....|....*....|....*....|
gi 1573864424 251 MSQGVDILRVHDVPEHHDLVTVLSELRNQQ 280
Cdd:COG0294   245 AARGADIVRVHDVAETVDALKVADAIRRAR 274
DHPS TIGR01496
dihydropteroate synthase; This model represents dihydropteroate synthase, the enzyme that ...
19-276 2.74e-99

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: 291.08  E-value: 2.74e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  19 MGIVNVTPDSFHAASRVASLEAAITTALDMWDAGADWVDVGGESTRPGAQPVPINEEISRVIPVIEALRnKRPHGLISID 98
Cdd:TIGR01496   3 MGIVNVTPDSFSDGGRFLSVDKAVAHAERMLEEGADIIDVGGESTRPGADRVSPEEELNRVVPVIKALR-DQPDVPISVD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  99 TRHPSVATEALAAGANMVNDVSGLRDPEMFNLVLESKCAVCIMHMLGEPGNMQSNPQYDNVVNEVSESLLSTARRLIANG 178
Cdd:TIGR01496  82 TYRAEVARAALEAGADIINDVSGGQDPAMLEVAAEYGVPLVLMHMRGTPRTMQENPHYEDVVEEVLRFLEARAEELVAAG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424 179 HSSELISLDSGIGFGKTLEQNLALLEKSEPFRgEEEFSLLWGVSRKSlFKDLLSRESSDQRLSGTLGVAAHAMSQGVDIL 258
Cdd:TIGR01496 162 VAAERIILDPGIGFGKTPEHNLELLKHLEEFV-ALGYPLLVGASRKS-FIGALLGTPPEERLEGTLAASAYAVQKGADIV 239
                         250
                  ....*....|....*...
gi 1573864424 259 RVHDVPEHHDLVTVLSEL 276
Cdd:TIGR01496 240 RVHDVKETRDALKVLEAL 257
DHPS cd00739
DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional ...
16-273 2.54e-98

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: 288.74  E-value: 2.54e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  16 PRLMGIVNVTPDSFHAASRVASLEAAITTALDMWDAGADWVDVGGESTRPGAQPVPINEEISRVIPVIEALRnKRPHGLI 95
Cdd:cd00739     1 TQIMGILNVTPDSFSDGGRFLSLDKAVAHAEKMIAEGADIIDIGGESTRPGADPVSVEEELERVIPVLEALR-GELDVLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  96 SIDTRHPSVATEALAAGANMVNDVSGLR-DPEMFNLVLESKCAVCIMHMLGEPGNMQSNPQYDNVVNEVSESLLSTARRL 174
Cdd:cd00739    80 SVDTFRAEVARAALEAGADIINDVSGGSdDPAMLEVAAEYGAPLVLMHMRGTPKTMQENPYYEDVVDEVLSFLEARLEAA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424 175 IANGHSSELISLDSGIGFGKTLEQNLALLEKSEPFRgEEEFSLLWGVSRKSLFKDLLSRESSDqRLSGTLGVAAHAMSQG 254
Cdd:cd00739   160 ESAGVARNRIILDPGIGFGKTPEHNLELLRRLDELK-QLGLPVLVGASRKSFIGALLGREPKD-RDWGTLALSALAAANG 237
                         250
                  ....*....|....*....
gi 1573864424 255 VDILRVHDVPEHHDLVTVL 273
Cdd:cd00739   238 ADIVRVHDVKATRDALKVA 256
Pterin_binding cd00423
Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and ...
16-273 4.24e-86

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: 257.59  E-value: 4.24e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  16 PRLMGIVNVTPDSFHAASRVASLEAAITTALDMWDAGADWVDVGGESTRPGAQPVPINEEISRVIPVIEALRNkRPHGLI 95
Cdd:cd00423     1 TLIMGILNVTPDSFSDGGKFLSLDKALEHARRMVEEGADIIDIGGESTRPGAEPVSVEEELERVIPVLRALAG-EPDVPI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  96 SIDTRHPSVATEALAAGANMVNDVSGLR-DPEMFNLVLESKCAVCIMHMLGEPGNMQSNPQYDNVVNEVSESLLSTARRL 174
Cdd:cd00423    80 SVDTFNAEVAEAALKAGADIINDVSGGRgDPEMAPLAAEYGAPVVLMHMDGTPQTMQNNPYYADVVDEVVEFLEERVEAA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424 175 IANGHSSELISLDSGIGFGKTLEQNLALLEKSEPFRGEEEFSLLWGVSRKSLFKDLLSRESSDqRLSGTLGVAAHAMSQG 254
Cdd:cd00423   160 TEAGIPPEDIILDPGIGFGKTEEHNLELLRRLDAFRELPGLPLLLGVSRKSFLGDLLSVGPKD-RLAGTAAFLAAAILNG 238
                         250
                  ....*....|....*....
gi 1573864424 255 VDILRVHDVPEHHDLVTVL 273
Cdd:cd00423   239 ADIVRVHDVKELRDAIKVA 257
Pterin_bind pfam00809
Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt ...
19-261 1.62e-79

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: 240.65  E-value: 1.62e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  19 MGIVNVTPDSFHAASRVASLEAAITTALDMWDAGADWVDVGGESTRPGAQPVPINEEISRVIPVIEALRnKRPHGLISID 98
Cdd:pfam00809   1 MGILNVTPDSFSDGGRFLDLDKALAHARRMVEEGADIIDIGGESTRPGAERVDGEEEMERVLPVLAALR-DEADVPISVD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  99 TRHPSVATEALAAGANMVNDVSGLR-DPEMFNLVLESKCAVCIMHMLGEPGNMQSNP-QYDNVVNEVSESLLSTARRLIA 176
Cdd:pfam00809  80 TTKAEVAEAALKAGADIINDISGGDgDPEMAELAAEYGAAVVVMHMDGTPKTMQENEqQYEDVVEEVERFLRARVAAAEE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424 177 NGHSSELISLDSGIGFGKTLEQNLALLEKSEPFRGEEEFSLLWGVSRKSLFKDLLSRESSDqRLSGTLGVAAHAMSQGVD 256
Cdd:pfam00809 160 AGVPPEDIILDPGIGFGKTEEHNLELLRTLDELRVILGVPVLLGVSRKSFIGRGLPLGGEE-RDAGTAAFLALAIAAGAD 238

                  ....*
gi 1573864424 257 ILRVH 261
Cdd:pfam00809 239 IVRVH 243
folP PRK11613
dihydropteroate synthase; Provisional
12-265 5.65e-72

dihydropteroate synthase; Provisional


Pssm-ID: 183230  Cd Length: 282  Bit Score: 222.70  E-value: 5.65e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  12 DDGRPRLMGIVNVTPDSFHAASRVASLEAAITTALDMWDAGADWVDVGGESTRPGAQPVPINEEISRVIPVIEALRnKRP 91
Cdd:PRK11613   11 DLSHPHVMGILNVTPDSFSDGGTHNSLIDAVKHANLMINAGATIIDVGGESTRPGAAEVSVEEELDRVIPVVEAIA-QRF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  92 HGLISIDTRHPSVATEALAAGANMVNDVSGLRDPEMFNLVLESKCAVCIMHMLGEPGNMQSNPQYDNVVNEVSESLLSTA 171
Cdd:PRK11613   90 EVWISVDTSKPEVIRESAKAGAHIINDIRSLSEPGALEAAAETGLPVCLMHMQGNPKTMQEAPKYDDVFAEVNRYFIEQI 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424 172 RRLIANGHSSELISLDSGIGFGKTLEQNLALLEKSEPFRgEEEFSLLWGVSRKSLFKDLLSrESSDQRLSGTLGVAAHAM 251
Cdd:PRK11613  170 ARCEAAGIAKEKLLLDPGFGFGKNLSHNYQLLARLAEFH-HFNLPLLVGMSRKSMIGQLLN-VGPSERLSGSLACAVIAA 247
                         250
                  ....*....|....
gi 1573864424 252 SQGVDILRVHDVPE 265
Cdd:PRK11613  248 MQGAQIIRVHDVKE 261
PRK13753 PRK13753
dihydropteroate synthase; Provisional
15-261 2.86e-28

dihydropteroate synthase; Provisional


Pssm-ID: 184303  Cd Length: 279  Bit Score: 109.40  E-value: 2.86e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  15 RPRLMGIVNVTPDSFHAASRVASLEAAITTALDMWDAGADWVDVGGESTRPGAQPVPINEEISRVIPVIEALRNKRPHgl 94
Cdd:PRK13753    1 MVTVFGILNLTEDSFFDESRRLDPAGAVTAAIEMLRVGSDVVDVGPAASHPDARPVSPADEIRRIAPLLDALSDQMHR-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424  95 ISIDTRHPSVATEALAAGANMVNDVSGLRDPEMFNLVLESKCAVCIMH------MLGEPGNMQSNPQYDNVVnEVSESLL 168
Cdd:PRK13753   79 VSIDSFQPETQRYALKRGVGYLNDIQGFPDPALYPDIAEADCRLVVMHsaqrdgIATRTGHLRPEDALDEIV-RFFEARV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864424 169 STARRliaNGHSSELISLDSGIGF--GKTLEQNLALLEKSEPFRGEEEFSLLWGVSRKSLFKDLLSRESSDQRlSGTLGV 246
Cdd:PRK13753  158 SALRR---SGVAADRLILDPGMGFflSPAPETSLHVLSNLQKLKSALGLPLLVSVSRKSFLGATVGLPVKDLG-PASLAA 233
                         250
                  ....*....|....*
gi 1573864424 247 AAHAMSQGVDILRVH 261
Cdd:PRK13753  234 ELHAIGNGADYVRTH 248
 
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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