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Conserved domains on  [gi|1933262282|gb|QPD68801|]
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dihydrofolate reductase (plasmid) [Enterobacter hormaechei]

Protein Classification

dihydrofolate reductase( domain architecture ID 10082841)

dihydrofolate reductase (DHFR) is involved in the biosynthesis of deoxythymidine phosphate; it reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with NADPH as a cofactor

CATH:  3.40.430.10
EC:  1.5.1.3
SCOP:  4000755

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DHFR cd00209
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ...
1-156 1.04e-54

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: 169.63  E-value: 1.04e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933262282   1 MKMIAAVGRNYEIGIGNELPWRCPTDLKLFKQLTKNATVVMGRKTMESL-KRPLPERHNLVLTRSRGY--IPNGFYPAGI 77
Cdd:cd00209     1 ISLIVAVDENGVIGKDNKLPWHLPEDLKHFKKTTTGNPVIMGRKTFESIpRRPLPGRTNIVLSRQLDYqdAEGVEVVHSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933262282  78 DDVLRL----PDPVWVIGGGQIYSLFMPHVEEIWLSHIGVDVPGaDAFFPAPMMRSLgfvpVETAYTQRANEDEPGFLQI 153
Cdd:cd00209    81 EEALELaentVEEIFVIGGAEIYKQALPYADRLYLTRIHAEFEG-DTFFPEIDESEW----ELVSEEEVFEEDGYSYTFE 155

                  ...
gi 1933262282 154 VYR 156
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 ...
1-156 1.04e-54

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: 169.63  E-value: 1.04e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933262282   1 MKMIAAVGRNYEIGIGNELPWRCPTDLKLFKQLTKNATVVMGRKTMESL-KRPLPERHNLVLTRSRGY--IPNGFYPAGI 77
Cdd:cd00209     1 ISLIVAVDENGVIGKDNKLPWHLPEDLKHFKKTTTGNPVIMGRKTFESIpRRPLPGRTNIVLSRQLDYqdAEGVEVVHSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933262282  78 DDVLRL----PDPVWVIGGGQIYSLFMPHVEEIWLSHIGVDVPGaDAFFPAPMMRSLgfvpVETAYTQRANEDEPGFLQI 153
Cdd:cd00209    81 EEALELaentVEEIFVIGGAEIYKQALPYADRLYLTRIHAEFEG-DTFFPEIDESEW----ELVSEEEVFEEDGYSYTFE 155

                  ...
gi 1933262282 154 VYR 156
Cdd:cd00209   156 TYE 158
DHFR_1 pfam00186
Dihydrofolate reductase;
3-124 2.55e-47

Dihydrofolate reductase;


Pssm-ID: 425512 [Multi-domain]  Cd Length: 159  Bit Score: 150.77  E-value: 2.55e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933262282   3 MIAAVGRNYEIGIGNELPWRCPTDLKLFKQLTKNATVVMGRKTMESLKRPLPERHNLVLTRSRGYIPNGFYPAG-IDDVL 81
Cdd:pfam00186   4 LIAAMDENGVIGKDNDLPWHLPADLKHFKKLTTGKPVIMGRKTFESIGRPLPGRKNIVLTRNPDYKVDGVEVVHsLEEAL 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1933262282  82 RL---PDPVWVIGGGQIYSLFMPHVEEIWLSHIGVDVPGaDAFFPA 124
Cdd:pfam00186  84 ALaaeAEEIFIIGGAEIYAQALPLADRLYITEIDAEFDG-DTFFPE 128
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
3-155 4.82e-30

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: 106.86  E-value: 4.82e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933262282   3 MIAAVGRNYEIG-IGNELPW--RCPTDLKLFKQLTKNA-TVVMGRKTMESL-----KRPLPERHNLVLTRSRGYIPNG-- 71
Cdd:COG0262     5 LIVAVSLDGVIGgPDGDLPWlfPDPEDLAHFKELTAGAdAVLMGRKTYESIagywpTRPLPGRPKIVLSRTLDEADWEgv 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933262282  72 -FYPAGIDDVLRL-----PDPVWVIGGGQIYSLFMPH--VEEIWLSHIGVDVPGADAFFPApmmrslgfVPVETAYTQRA 143
Cdd:COG0262    85 tVVSGDLEEALAAlkaagGKDIWVIGGGELYRQLLPAglVDELYLTVVPVVLGEGDRLFPE--------LDAPSRLELVE 156
                         170
                  ....*....|..
gi 1933262282 144 NEDEPGFLQIVY 155
Cdd:COG0262   157 SEADSGFVHLTY 168
folA PRK10769
type 3 dihydrofolate reductase;
3-123 4.90e-29

type 3 dihydrofolate reductase;


Pssm-ID: 182714 [Multi-domain]  Cd Length: 159  Bit Score: 104.05  E-value: 4.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933262282   3 MIAAVGRNYEIGIGNELPWRCPTDLKLFKQLTKNATVVMGRKTMESLKRPLPERHNLVLTRSRGYIPNGFYPAGIDDVLR 82
Cdd:PRK10769    4 LIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIVISSQPGTDDRVTWVKSVDEALA 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1933262282  83 LP---DPVWVIGGGQIYSLFMPHVEEIWLSHIGVDVPGaDAFFP 123
Cdd:PRK10769   84 AAgdvPEIMVIGGGRVYEQFLPKAQRLYLTHIDAEVEG-DTHFP 126
dihyfolred_HdrA_Halo NF041386
dihydrofolate reductase HdrA;
4-124 7.86e-25

dihydrofolate reductase HdrA;


Pssm-ID: 469277 [Multi-domain]  Cd Length: 158  Bit Score: 93.48  E-value: 7.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933262282   4 IAAVGRNYEIGIGNELPWRC-PTDLKLFKQLTKNATVVMGRKTMESLKRPLPERHNLVLTRS-RGY-IPNGFYPAGIDDV 80
Cdd:NF041386    6 VAAVAENGVIGRDGELPWPSiPADKRQYRERVADDPVILGRRTFESMRDDLPGSAQIVLSRSeREFdVETAHHAGGVDEA 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1933262282  81 LRLP-----DPVWVIGGGQIYSLFMPHVEEIWLSHigvdVPGA---DAFFPA 124
Cdd:NF041386   86 IEIAeslgaERAYVLGGAAIYELFQPHVDRMVLSR----VPGEyegDAYYPE 133
trim_DfrL NF041668
trimethoprim-resistant dihydrofolate reductase DfrL;
10-71 1.31e-06

trimethoprim-resistant dihydrofolate reductase DfrL;


Pssm-ID: 469550 [Multi-domain]  Cd Length: 176  Bit Score: 45.80  E-value: 1.31e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1933262282  10 NYEIGIGNELPWRCPTDLKLFKQLTKNATVVMGRKTMESL-KRPLPERHNLVLTRSRGYIPNG 71
Cdd:NF041668   10 CGEIGKPGDLFVNAEDDMGHFGNSGDDDVNLMGDKKHEKIpTMDDKNRIGIKLTENIPVRADG 72
 
Name Accession Description Interval E-value
DHFR cd00209
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ...
1-156 1.04e-54

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: 169.63  E-value: 1.04e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933262282   1 MKMIAAVGRNYEIGIGNELPWRCPTDLKLFKQLTKNATVVMGRKTMESL-KRPLPERHNLVLTRSRGY--IPNGFYPAGI 77
Cdd:cd00209     1 ISLIVAVDENGVIGKDNKLPWHLPEDLKHFKKTTTGNPVIMGRKTFESIpRRPLPGRTNIVLSRQLDYqdAEGVEVVHSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933262282  78 DDVLRL----PDPVWVIGGGQIYSLFMPHVEEIWLSHIGVDVPGaDAFFPAPMMRSLgfvpVETAYTQRANEDEPGFLQI 153
Cdd:cd00209    81 EEALELaentVEEIFVIGGAEIYKQALPYADRLYLTRIHAEFEG-DTFFPEIDESEW----ELVSEEEVFEEDGYSYTFE 155

                  ...
gi 1933262282 154 VYR 156
Cdd:cd00209   156 TYE 158
DHFR_1 pfam00186
Dihydrofolate reductase;
3-124 2.55e-47

Dihydrofolate reductase;


Pssm-ID: 425512 [Multi-domain]  Cd Length: 159  Bit Score: 150.77  E-value: 2.55e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933262282   3 MIAAVGRNYEIGIGNELPWRCPTDLKLFKQLTKNATVVMGRKTMESLKRPLPERHNLVLTRSRGYIPNGFYPAG-IDDVL 81
Cdd:pfam00186   4 LIAAMDENGVIGKDNDLPWHLPADLKHFKKLTTGKPVIMGRKTFESIGRPLPGRKNIVLTRNPDYKVDGVEVVHsLEEAL 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1933262282  82 RL---PDPVWVIGGGQIYSLFMPHVEEIWLSHIGVDVPGaDAFFPA 124
Cdd:pfam00186  84 ALaaeAEEIFIIGGAEIYAQALPLADRLYITEIDAEFDG-DTFFPE 128
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
3-155 4.82e-30

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: 106.86  E-value: 4.82e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933262282   3 MIAAVGRNYEIG-IGNELPW--RCPTDLKLFKQLTKNA-TVVMGRKTMESL-----KRPLPERHNLVLTRSRGYIPNG-- 71
Cdd:COG0262     5 LIVAVSLDGVIGgPDGDLPWlfPDPEDLAHFKELTAGAdAVLMGRKTYESIagywpTRPLPGRPKIVLSRTLDEADWEgv 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933262282  72 -FYPAGIDDVLRL-----PDPVWVIGGGQIYSLFMPH--VEEIWLSHIGVDVPGADAFFPApmmrslgfVPVETAYTQRA 143
Cdd:COG0262    85 tVVSGDLEEALAAlkaagGKDIWVIGGGELYRQLLPAglVDELYLTVVPVVLGEGDRLFPE--------LDAPSRLELVE 156
                         170
                  ....*....|..
gi 1933262282 144 NEDEPGFLQIVY 155
Cdd:COG0262   157 SEADSGFVHLTY 168
folA PRK10769
type 3 dihydrofolate reductase;
3-123 4.90e-29

type 3 dihydrofolate reductase;


Pssm-ID: 182714 [Multi-domain]  Cd Length: 159  Bit Score: 104.05  E-value: 4.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933262282   3 MIAAVGRNYEIGIGNELPWRCPTDLKLFKQLTKNATVVMGRKTMESLKRPLPERHNLVLTRSRGYIPNGFYPAGIDDVLR 82
Cdd:PRK10769    4 LIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIVISSQPGTDDRVTWVKSVDEALA 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1933262282  83 LP---DPVWVIGGGQIYSLFMPHVEEIWLSHIGVDVPGaDAFFP 123
Cdd:PRK10769   84 AAgdvPEIMVIGGGRVYEQFLPKAQRLYLTHIDAEVEG-DTHFP 126
dihyfolred_HdrA_Halo NF041386
dihydrofolate reductase HdrA;
4-124 7.86e-25

dihydrofolate reductase HdrA;


Pssm-ID: 469277 [Multi-domain]  Cd Length: 158  Bit Score: 93.48  E-value: 7.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933262282   4 IAAVGRNYEIGIGNELPWRC-PTDLKLFKQLTKNATVVMGRKTMESLKRPLPERHNLVLTRS-RGY-IPNGFYPAGIDDV 80
Cdd:NF041386    6 VAAVAENGVIGRDGELPWPSiPADKRQYRERVADDPVILGRRTFESMRDDLPGSAQIVLSRSeREFdVETAHHAGGVDEA 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1933262282  81 LRLP-----DPVWVIGGGQIYSLFMPHVEEIWLSHigvdVPGA---DAFFPA 124
Cdd:NF041386   86 IEIAeslgaERAYVLGGAAIYELFQPHVDRMVLSR----VPGEyegDAYYPE 133
PTZ00164 PTZ00164
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
2-125 4.18e-22

bifunctional dihydrofolate reductase-thymidylate synthase; Provisional


Pssm-ID: 240299 [Multi-domain]  Cd Length: 514  Bit Score: 91.27  E-value: 4.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933262282   2 KMIAAVGRNYEIGIGNELPWRCPTDLKLFKQLT--------------KNAtVVMGRKTMESLK---RPLPERHNLVLTRS 64
Cdd:PTZ00164   11 SIVVAVTLKRGIGIGNSLPWHIPEDMKFFSKITtyvreekyekspkkQNA-VIMGRKTWESIPkkfRPLKNRINVVLSRT 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1933262282  65 ---RGYIPNGFYPAGIDDVLRL---PDP---VWVIGGGQIYSLFMPH--VEEIWLSHIGVDVPGaDAFFPAP 125
Cdd:PTZ00164   90 lteEEADPGVLVFGSLEDALRLlaeDLSiekIFIIGGASVYREALSAnlLDKIYLTRVNSEYEC-DVFFPKI 160
scpA PRK00478
segregation and condensation protein ScpA;
1-122 9.68e-09

segregation and condensation protein ScpA;


Pssm-ID: 234776 [Multi-domain]  Cd Length: 505  Bit Score: 53.01  E-value: 9.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933262282   1 MKMIAAVGRNYEIGIGNELPWRCPTDLKLFKQLTKNATVVMGRKTMESLKRPLPERHNLVLTR---------SRGYIPNG 71
Cdd:PRK00478    2 IKLIWCEDLNFGIAKNNQIPWKIDEELNHFHQTTTNHTIVMGYNTFQAMNKILANQANIVISKkhqrelknnNELFVFND 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1933262282  72 FYPAGIDDVLRlpdPVWVIGGGQIYSLFMPHVEEIWLSHIGVDVpGADAFF 122
Cdd:PRK00478   82 LKKLLIDFSNV---DLFIIGGKKTIEQFIKYADQLIISKLNADY-KCDLFV 128
trim_DfrL NF041668
trimethoprim-resistant dihydrofolate reductase DfrL;
10-71 1.31e-06

trimethoprim-resistant dihydrofolate reductase DfrL;


Pssm-ID: 469550 [Multi-domain]  Cd Length: 176  Bit Score: 45.80  E-value: 1.31e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1933262282  10 NYEIGIGNELPWRCPTDLKLFKQLTKNATVVMGRKTMESL-KRPLPERHNLVLTRSRGYIPNG 71
Cdd:NF041668   10 CGEIGKPGDLFVNAEDDMGHFGNSGDDDVNLMGDKKHEKIpTMDDKNRIGIKLTENIPVRADG 72
 
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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