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Conserved domains on  [gi|1461091156|emb|SYT59714|]
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Dhfr1 [Klebsiella pneumoniae]

Protein Classification

dihydrofolate reductase family protein( domain architecture ID 106942)

dihydrofolate reductase family protein; similar to Lacticaseibacillus rhamnosus dihydrofolate reductase which reduces dihydrofolic acid to tetrahydrofolic acid, using NADPH as electron donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DHFR super family cl17279
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ...
 2-81 3.97e-18

Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with NADPH as a cofactor. This is an essential step in the biosynthesis of deoxythymidine phosphate since 5,6,7,8-tetrahydrofolate is required to regenerate 5,10-methylenetetrahydrofolate which is then utilized by thymidylate synthase. Inhibition of DHFR interrupts thymidilate synthesis and DNA replication, inhibitors of DHFR (such as Methotrexate) are used in cancer chemotherapy. 5,6,7,8-tetrahydrofolate also is involved in glycine, serine, and threonine metabolism and aminoacyl-tRNA biosynthesis.


The actual alignment was detected with superfamily member cd00209:

Pssm-ID: 473077 [Multi-domain]  Cd Length: 158  Bit Score: 73.33  E-value: 3.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461091156   2 VFSSIQDALINLEEITDHVIVSGGGEIYKSLISKVDTLHISTVDIERDGDIVFPEI-PDTFKLVFEQDF--ESNINYCYQ 78
Cdd:cd00209    76 VVHSLEEALELAENTVEEIFVIGGAEIYKQALPYADRLYLTRIHAEFEGDTFFPEIdESEWELVSEEEVfeEDGYSYTFE 155


                  ...
gi 1461091156  79 IWQ 81
Cdd:cd00209   156 TYE 158
 
Name Accession Description Interval E-value
DHFR cd00209
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ...
 2-81 3.97e-18

Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with NADPH as a cofactor. This is an essential step in the biosynthesis of deoxythymidine phosphate since 5,6,7,8-tetrahydrofolate is required to regenerate 5,10-methylenetetrahydrofolate which is then utilized by thymidylate synthase. Inhibition of DHFR interrupts thymidilate synthesis and DNA replication, inhibitors of DHFR (such as Methotrexate) are used in cancer chemotherapy. 5,6,7,8-tetrahydrofolate also is involved in glycine, serine, and threonine metabolism and aminoacyl-tRNA biosynthesis.


Pssm-ID: 238127 [Multi-domain]  Cd Length: 158  Bit Score: 73.33  E-value: 3.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461091156   2 VFSSIQDALINLEEITDHVIVSGGGEIYKSLISKVDTLHISTVDIERDGDIVFPEI-PDTFKLVFEQDF--ESNINYCYQ 78
Cdd:cd00209    76 VVHSLEEALELAENTVEEIFVIGGAEIYKQALPYADRLYLTRIHAEFEGDTFFPEIdESEWELVSEEEVfeEDGYSYTFE 155


                  ...
gi 1461091156  79 IWQ 81
Cdd:cd00209   156 TYE 158
DHFR_1 pfam00186
Dihydrofolate reductase;
2-82 1.00e-16

Dihydrofolate reductase;


Pssm-ID: 425512 [Multi-domain]  Cd Length: 159  Bit Score: 69.49  E-value: 1.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461091156   2 VFSSIQDALiNLEEITDHVIVSGGGEIYKSLISKVDTLHISTVDIERDGDIVFPEI-PDTFKLVFEQDFESN----INYC 76
Cdd:pfam00186  75 VVHSLEEAL-ALAAEAEEIFIIGGAEIYAQALPLADRLYITEIDAEFDGDTFFPEIdPSEWQLVSREEHEADeknpYPYT 153


                  ....*.
gi 1461091156  77 YQIWQK 82
Cdd:pfam00186 154 FVTYER 159
folA PRK10769
type 3 dihydrofolate reductase;
4-82 1.84e-09

type 3 dihydrofolate reductase;


Pssm-ID: 182714 [Multi-domain]  Cd Length: 159  Bit Score: 50.89  E-value: 1.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461091156   4 SSIQDALINLEEItDHVIVSGGGEIYKSLISKVDTLHISTVDIERDGDIVFPEI-PDTFKLVF----EQDFESNINYCYQ 78
Cdd:PRK10769   76 KSVDEALAAAGDV-PEIMVIGGGRVYEQFLPKAQRLYLTHIDAEVEGDTHFPDYePDEWESVFsefhDADEQNSHSYCFE 154


                  ....
gi 1461091156  79 IWQK 82
Cdd:PRK10769  155 ILER 158
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
 2-67 4.19e-07

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


Pssm-ID: 440032 [Multi-domain]  Cd Length: 168  Bit Score: 44.46  E-value: 4.19e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1461091156   2 VFSSIQDALINLEEITD-HVIVSGGGEIYKSLISK--VDTLHISTVDIE-RDGDIVFPEI--PDTFKLVFEQ 67
Cdd:COG0262    87 VSGDLEEALAALKAAGGkDIWVIGGGELYRQLLPAglVDELYLTVVPVVlGEGDRLFPELdaPSRLELVESE 158
dihyfolred_HdrA_Halo NF041386
dihydrofolate reductase HdrA;
4-70 7.21e-04

dihydrofolate reductase HdrA;


Pssm-ID: 469277 [Multi-domain]  Cd Length: 158  Bit Score: 35.70  E-value: 7.21e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1461091156   4 SSIQDALINLEEI-TDHVIVSGGGEIYKSLISKVDTLHISTVDIERDGDIVFPEI-PDTFKLVFEQDFE 70
Cdd:NF041386   80 GGVDEAIEIAESLgAERAYVLGGAAIYELFQPHVDRMVLSRVPGEYEGDAYYPEWdEDEWELVEETEYD 148
 
Name Accession Description Interval E-value
DHFR cd00209
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ...
 2-81 3.97e-18

Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with NADPH as a cofactor. This is an essential step in the biosynthesis of deoxythymidine phosphate since 5,6,7,8-tetrahydrofolate is required to regenerate 5,10-methylenetetrahydrofolate which is then utilized by thymidylate synthase. Inhibition of DHFR interrupts thymidilate synthesis and DNA replication, inhibitors of DHFR (such as Methotrexate) are used in cancer chemotherapy. 5,6,7,8-tetrahydrofolate also is involved in glycine, serine, and threonine metabolism and aminoacyl-tRNA biosynthesis.


Pssm-ID: 238127 [Multi-domain]  Cd Length: 158  Bit Score: 73.33  E-value: 3.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461091156   2 VFSSIQDALINLEEITDHVIVSGGGEIYKSLISKVDTLHISTVDIERDGDIVFPEI-PDTFKLVFEQDF--ESNINYCYQ 78
Cdd:cd00209    76 VVHSLEEALELAENTVEEIFVIGGAEIYKQALPYADRLYLTRIHAEFEGDTFFPEIdESEWELVSEEEVfeEDGYSYTFE 155


                  ...
gi 1461091156  79 IWQ 81
Cdd:cd00209   156 TYE 158
DHFR_1 pfam00186
Dihydrofolate reductase;
2-82 1.00e-16

Dihydrofolate reductase;


Pssm-ID: 425512 [Multi-domain]  Cd Length: 159  Bit Score: 69.49  E-value: 1.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461091156   2 VFSSIQDALiNLEEITDHVIVSGGGEIYKSLISKVDTLHISTVDIERDGDIVFPEI-PDTFKLVFEQDFESN----INYC 76
Cdd:pfam00186  75 VVHSLEEAL-ALAAEAEEIFIIGGAEIYAQALPLADRLYITEIDAEFDGDTFFPEIdPSEWQLVSREEHEADeknpYPYT 153


                  ....*.
gi 1461091156  77 YQIWQK 82
Cdd:pfam00186 154 FVTYER 159
folA PRK10769
type 3 dihydrofolate reductase;
4-82 1.84e-09

type 3 dihydrofolate reductase;


Pssm-ID: 182714 [Multi-domain]  Cd Length: 159  Bit Score: 50.89  E-value: 1.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461091156   4 SSIQDALINLEEItDHVIVSGGGEIYKSLISKVDTLHISTVDIERDGDIVFPEI-PDTFKLVF----EQDFESNINYCYQ 78
Cdd:PRK10769   76 KSVDEALAAAGDV-PEIMVIGGGRVYEQFLPKAQRLYLTHIDAEVEGDTHFPDYePDEWESVFsefhDADEQNSHSYCFE 154


                  ....
gi 1461091156  79 IWQK 82
Cdd:PRK10769  155 ILER 158
PTZ00164 PTZ00164
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
 2-83 7.25e-09

bifunctional dihydrofolate reductase-thymidylate synthase; Provisional


Pssm-ID: 240299 [Multi-domain]  Cd Length: 514  Bit Score: 50.44  E-value: 7.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461091156   2 VFSSIQDALINLEEITDH--VIVSGGGEIYKSLIS--KVDTLHISTVDIERDGDIVFPEIPDTFKLVFE--QDFESN-IN 74
Cdd:PTZ00164  101 VFGSLEDALRLLAEDLSIekIFIIGGASVYREALSanLLDKIYLTRVNSEYECDVFFPKIPESFFIVAIvsQTFSTNgTS 180


                  ....*....
gi 1461091156  75 YCYQIWQKS 83
Cdd:PTZ00164  181 YDFVIYEKK 189
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
 2-67 4.19e-07

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


Pssm-ID: 440032 [Multi-domain]  Cd Length: 168  Bit Score: 44.46  E-value: 4.19e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1461091156   2 VFSSIQDALINLEEITD-HVIVSGGGEIYKSLISK--VDTLHISTVDIE-RDGDIVFPEI--PDTFKLVFEQ 67
Cdd:COG0262    87 VSGDLEEALAALKAAGGkDIWVIGGGELYRQLLPAglVDELYLTVVPVVlGEGDRLFPELdaPSRLELVESE 158
dihyfolred_HdrA_Halo NF041386
dihydrofolate reductase HdrA;
4-70 7.21e-04

dihydrofolate reductase HdrA;


Pssm-ID: 469277 [Multi-domain]  Cd Length: 158  Bit Score: 35.70  E-value: 7.21e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1461091156   4 SSIQDALINLEEI-TDHVIVSGGGEIYKSLISKVDTLHISTVDIERDGDIVFPEI-PDTFKLVFEQDFE 70
Cdd:NF041386   80 GGVDEAIEIAESLgAERAYVLGGAAIYELFQPHVDRMVLSRVPGEYEGDAYYPEWdEDEWELVEETEYD 148
 
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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