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Conserved domains on  [gi|635780956|gb|KDF62378|]
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hypothetical protein AF40_01156 [Enterobacter roggenkampii MGH 54]

Protein Classification

dihydrofolate reductase family protein( domain architecture ID 10000815)

dihydrofolate reductase (DHFR) family protein similar to DHFR that is involved in the biosynthesis of deoxythymidine phosphate, catalyzing the reduction of 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with NADPH as a cofactor

CATH:  3.40.430.10
EC:  1.5.1.3
Gene Ontology:  GO:0046654|GO:0004146|GO:0050661
PubMed:  8593164

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
6-174 5.04e-41

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: 135.75  E-value: 5.04e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780956   6 VFIATSLDGYIARHNDDIDWLLQrdDPNEDHGYTAFIADKDWIVMGRGSYEKVRTFetWPY----DRPVLVLSRQLADTP 81
Cdd:COG0262    5 LIVAVSLDGVIGGPDGDLPWLFP--DPEDLAHFKELTAGADAVLMGRKTYESIAGY--WPTrplpGRPKIVLSRTLDEAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780956  82 VPDalrgkVQFSSRTPKVVLDDLARQNARRVYL-DGGQVIQSFLREGLVADMVITTVPVLLGSGKSLFGALPGDIDLTLV 160
Cdd:COG0262   81 WEG-----VTVVSGDLEEALAALKAAGGKDIWViGGGELYRQLLPAGLVDELYLTVVPVVLGEGDRLFPELDAPSRLELV 155
                        170
                 ....*....|....
gi 635780956 161 SSRSfPSGLVQSHY 174
Cdd:COG0262  156 ESEA-DSGFVHLTY 168
 
Name Accession Description Interval E-value
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
6-174 5.04e-41

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: 135.75  E-value: 5.04e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780956   6 VFIATSLDGYIARHNDDIDWLLQrdDPNEDHGYTAFIADKDWIVMGRGSYEKVRTFetWPY----DRPVLVLSRQLADTP 81
Cdd:COG0262    5 LIVAVSLDGVIGGPDGDLPWLFP--DPEDLAHFKELTAGADAVLMGRKTYESIAGY--WPTrplpGRPKIVLSRTLDEAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780956  82 VPDalrgkVQFSSRTPKVVLDDLARQNARRVYL-DGGQVIQSFLREGLVADMVITTVPVLLGSGKSLFGALPGDIDLTLV 160
Cdd:COG0262   81 WEG-----VTVVSGDLEEALAALKAAGGKDIWViGGGELYRQLLPAGLVDELYLTVVPVVLGEGDRLFPELDAPSRLELV 155
                        170
                 ....*....|....
gi 635780956 161 SSRSfPSGLVQSHY 174
Cdd:COG0262  156 ESEA-DSGFVHLTY 168
RibD_C pfam01872
RibD C-terminal domain; The function of this domain is not known, but it is thought to be ...
6-170 1.69e-14

RibD C-terminal domain; The function of this domain is not known, but it is thought to be involved in riboflavin biosynthesis. This domain is found in the C terminus of RibD/RibG, in combination with pfam00383, as well as in isolation in some archaebacterial proteins. This family appears to be related to pfam00186.


Pssm-ID: 396444  Cd Length: 196  Bit Score: 68.18  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780956    6 VFIATSLDGYIARHNDDIDWLLQRDDPNEDHGYTAfiaDKDWIVMGRGSYEK------VRTFETWPYDR--PVLVLSRQL 77
Cdd:pfam01872   5 LKFAISLDGKIAAAGGSSQWITGEEARADVHQLRA---EADAILVGRGTVRAdnpsltVRWVKGRAAERqpPRVVVDSTL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780956   78 ADTPVPDALRG------------------KVQFSSRTPKVVLDDLARQNARRVYLDGG-QVIQSFLREGLVADMVITTVP 138
Cdd:pfam01872  82 RVPLDARVLNDdaptlvattepadkekveKLKVLRVDLKELLRELKERGIRSLLVEGGaTLAGSLLRAGLVDELRLYIAP 161
                         170       180       190
                  ....*....|....*....|....*....|....
gi 635780956  139 VLLGS-GKSLFGALPGD-IDLTLVSSRSFPSGLV 170
Cdd:pfam01872 162 KLLGGgGRTLFGGEGFLaLKLKLVSSEAIGNGVV 195
 
Name Accession Description Interval E-value
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
6-174 5.04e-41

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: 135.75  E-value: 5.04e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780956   6 VFIATSLDGYIARHNDDIDWLLQrdDPNEDHGYTAFIADKDWIVMGRGSYEKVRTFetWPY----DRPVLVLSRQLADTP 81
Cdd:COG0262    5 LIVAVSLDGVIGGPDGDLPWLFP--DPEDLAHFKELTAGADAVLMGRKTYESIAGY--WPTrplpGRPKIVLSRTLDEAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780956  82 VPDalrgkVQFSSRTPKVVLDDLARQNARRVYL-DGGQVIQSFLREGLVADMVITTVPVLLGSGKSLFGALPGDIDLTLV 160
Cdd:COG0262   81 WEG-----VTVVSGDLEEALAALKAAGGKDIWViGGGELYRQLLPAGLVDELYLTVVPVVLGEGDRLFPELDAPSRLELV 155
                        170
                 ....*....|....
gi 635780956 161 SSRSfPSGLVQSHY 174
Cdd:COG0262  156 ESEA-DSGFVHLTY 168
RibD_C pfam01872
RibD C-terminal domain; The function of this domain is not known, but it is thought to be ...
6-170 1.69e-14

RibD C-terminal domain; The function of this domain is not known, but it is thought to be involved in riboflavin biosynthesis. This domain is found in the C terminus of RibD/RibG, in combination with pfam00383, as well as in isolation in some archaebacterial proteins. This family appears to be related to pfam00186.


Pssm-ID: 396444  Cd Length: 196  Bit Score: 68.18  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780956    6 VFIATSLDGYIARHNDDIDWLLQRDDPNEDHGYTAfiaDKDWIVMGRGSYEK------VRTFETWPYDR--PVLVLSRQL 77
Cdd:pfam01872   5 LKFAISLDGKIAAAGGSSQWITGEEARADVHQLRA---EADAILVGRGTVRAdnpsltVRWVKGRAAERqpPRVVVDSTL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780956   78 ADTPVPDALRG------------------KVQFSSRTPKVVLDDLARQNARRVYLDGG-QVIQSFLREGLVADMVITTVP 138
Cdd:pfam01872  82 RVPLDARVLNDdaptlvattepadkekveKLKVLRVDLKELLRELKERGIRSLLVEGGaTLAGSLLRAGLVDELRLYIAP 161
                         170       180       190
                  ....*....|....*....|....*....|....
gi 635780956  139 VLLGS-GKSLFGALPGD-IDLTLVSSRSFPSGLV 170
Cdd:pfam01872 162 KLLGGgGRTLFGGEGFLaLKLKLVSSEAIGNGVV 195
RibD COG1985
Pyrimidine reductase, riboflavin biosynthesis [Coenzyme transport and metabolism]; Pyrimidine ...
67-176 7.76e-10

Pyrimidine reductase, riboflavin biosynthesis [Coenzyme transport and metabolism]; Pyrimidine reductase, riboflavin biosynthesis is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 441588  Cd Length: 217  Bit Score: 55.55  E-value: 7.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780956  67 DRPVLVLSRQLADTPVPDALRGK----VQFSSR---TPKVVLDDLARQNARRVYLDGG-QVIQSFLREGLVADMVITTVP 138
Cdd:COG1985   93 AAPTLVLTTEAADAERRAALEAAgaevIVLPGDgrvDLAALLAALAERGIRSVLVEGGpTLAGSFLAAGLVDELILYIAP 172
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 635780956 139 VLLGS-GKSLFGALPGD-----IDLTLVSSRSFPSGLVqSHYRV 176
Cdd:COG1985  173 KLLGGdGPTLVGGPGLEtladaPRLRLVSVRRLGDDLL-LRYRP 215
 
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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