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Conserved domains on  [gi|550766432|ref|WP_022649792|]
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MULTISPECIES: methylenetetrahydrofolate reductase [Enterobacter]

Protein Classification

methylenetetrahydrofolate reductase( domain architecture ID 10793259)

methylenetetrahydrofolate reductase catalyzes NADH-dependent reduction of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate using FAD as a cofactor

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
metF PRK09432
methylenetetrahydrofolate reductase;
1-296 0e+00

methylenetetrahydrofolate reductase;


:

Pssm-ID: 181852  Cd Length: 296  Bit Score: 700.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432   1 MSFFHANQREALNQSLAEVNGQINVSFEFFPPRTSEMEQTLWSSIDRLSSLKPKFVSVTYGANSGERDRTHSIIKGIKDR 80
Cdd:PRK09432   1 MSFFHANQRDALNQSLAELQGQINVSFEFFPPRTSEMEQTLWNSIDRLSSLKPKFVSVTYGANSGERDRTHSIIKGIKKR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432  81 TGLEAAPHLTCIDATPDELRAIAQDYWNNGIRHIVALRGDLPPGSGKPDMYATDLVALLKDVADFDISVAAYPEVHPEAK 160
Cdd:PRK09432  81 TGLEAAPHLTCIDATPDELRTIAKDYWNNGIRHIVALRGDLPPGSGKPEMYASDLVTLLKSVADFDISVAAYPEVHPEAK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432 161 SAQADLLNLKRKVDAGANRAITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKFADMTNVRIPLWMSKMYE 240
Cdd:PRK09432 161 SAQADLINLKRKVDAGANRAITQFFFDVESYLRFRDRCVSAGIDVEIVPGILPVSNFKQLKKFADMTNVRIPAWMAKMFD 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 550766432 241 GLDDDPETRKLVGANIAMDMVKILSREGVKDFHFYTLNRAEMSYAICHTLGVRPAL 296
Cdd:PRK09432 241 GLDDDAETRKLVGASIAMDMVKILSREGVKDFHFYTLNRAELTYAICHTLGVRPGL 296
 
Name Accession Description Interval E-value
metF PRK09432
methylenetetrahydrofolate reductase;
1-296 0e+00

methylenetetrahydrofolate reductase;


Pssm-ID: 181852  Cd Length: 296  Bit Score: 700.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432   1 MSFFHANQREALNQSLAEVNGQINVSFEFFPPRTSEMEQTLWSSIDRLSSLKPKFVSVTYGANSGERDRTHSIIKGIKDR 80
Cdd:PRK09432   1 MSFFHANQRDALNQSLAELQGQINVSFEFFPPRTSEMEQTLWNSIDRLSSLKPKFVSVTYGANSGERDRTHSIIKGIKKR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432  81 TGLEAAPHLTCIDATPDELRAIAQDYWNNGIRHIVALRGDLPPGSGKPDMYATDLVALLKDVADFDISVAAYPEVHPEAK 160
Cdd:PRK09432  81 TGLEAAPHLTCIDATPDELRTIAKDYWNNGIRHIVALRGDLPPGSGKPEMYASDLVTLLKSVADFDISVAAYPEVHPEAK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432 161 SAQADLLNLKRKVDAGANRAITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKFADMTNVRIPLWMSKMYE 240
Cdd:PRK09432 161 SAQADLINLKRKVDAGANRAITQFFFDVESYLRFRDRCVSAGIDVEIVPGILPVSNFKQLKKFADMTNVRIPAWMAKMFD 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 550766432 241 GLDDDPETRKLVGANIAMDMVKILSREGVKDFHFYTLNRAEMSYAICHTLGVRPAL 296
Cdd:PRK09432 241 GLDDDAETRKLVGASIAMDMVKILSREGVKDFHFYTLNRAELTYAICHTLGVRPGL 296
fadh2 TIGR00676
5,10-methylenetetrahydrofolate reductase, prokaryotic form; The enzyme activities ...
25-291 2.06e-155

5,10-methylenetetrahydrofolate reductase, prokaryotic form; The enzyme activities methylenetetrahydrofolate reductase (EC 1.5.1.20) and 5,10-methylenetetrahydrofolate reductase (FADH) (EC 1.7.99.5) differ in that 1.5.1.20 (assigned in many eukaryotes) is defined to use NADP+ as an acceptor, while 1.7.99.5 (assigned in many bacteria) is flexible with respect to the acceptor; both convert 5-methyltetrahydrofolate to 5,10-methylenetetrahydrofolate. From a larger set of proteins assigned as 1.5.1.20 and 1.7.99.5, this model describes the subset of proteins found in bacteria, and currently designated 1.7.99.5. This protein is an FAD-containing flavoprotein. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273212  Cd Length: 272  Bit Score: 434.75  E-value: 2.06e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432   25 VSFEFFPPRTSEMEQTLWSSIDRLSSLKPKFVSVTYGANSGERDRTHSIIKGIKDRTGLEAAPHLTCIDATPDELRAIAQ 104
Cdd:TIGR00676   1 FSFEFFPPKTDEGEENLWETVDRLSPLDPDFVSVTYGAGGSTRDRTVRIVRRIKKETGIPTVPHLTCIGATREEIREILR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432  105 DYWNNGIRHIVALRGDLPPGSGKPD----MYATDLVALLKDV-ADFDISVAAYPEVHPEAKSAQADLLNLKRKVDAGANR 179
Cdd:TIGR00676  81 EYRELGIRHILALRGDPPKGEGTPTpggfNYASELVEFIRNEfGDFDIGVAAYPEKHPEAPNLEEDIENLKRKVDAGADY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432  180 AITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKFADMTNVRIPLWMSKMYEGLDDDPETRKLVGANIAMD 259
Cdd:TIGR00676 161 AITQLFFDNDDYYRFVDRCRAAGIDVPIIPGIMPITNFKQLLRFAERCGAEIPAWLVKRLEKYDDDPEEVRAVGIEYATD 240
                         250       260       270
                  ....*....|....*....|....*....|..
gi 550766432  260 MVKILSREGVKDFHFYTLNRAEMSYAICHTLG 291
Cdd:TIGR00676 241 QCEDLIAEGVPGIHFYTLNRADATLEICENLG 272
MetF COG0685
5,10-methylenetetrahydrofolate reductase [Amino acid transport and metabolism];
20-293 2.97e-149

5,10-methylenetetrahydrofolate reductase [Amino acid transport and metabolism];


Pssm-ID: 440449  Cd Length: 284  Bit Score: 419.58  E-value: 2.97e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432  20 NGQINVSFEFFPPRTSEMEQTLWSSIDRLSSLKPKFVSVTYGANSGERDRTHSIIKGIKDRTGLEAAPHLTCIDATPDEL 99
Cdd:COG0685    9 AGKPVVSFEFFPPKTAEGEEKLWETAEELAPLDPDFVSVTYGAGGSTRDRTLAIAARIQQETGLEPVAHLTCVGRNREEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432 100 RAIAQDYWNNGIRHIVALRGDLPPGSGKP--DMYATDLVALLKDV-ADFDISVAAYPEVHPEAKSAQADLLNLKRKVDAG 176
Cdd:COG0685   89 ESILLGLAALGIRNILALRGDPPKGDGHPggFLYASELVALIREMnGDFCIGVAAYPEKHPEAPSLEADLDRLKKKVDAG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432 177 ANRAITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKFADMTNVRIPLWMSKMYEGLDDDpETRKLVGANI 256
Cdd:COG0685  169 ADFAITQLFFDNDAYFRFVDRARAAGIDVPIIPGIMPITSFKQLARFAELCGAEIPDWLLKRLEKAGDD-EAVRAVGIEI 247
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 550766432 257 AMDMVKILSREGVKDFHFYTLNRAEMSYAICHTLGVR 293
Cdd:COG0685  248 ATEQCEELLAEGVPGLHFYTLNRAEATLEILERLGLL 284
MTHFR pfam02219
Methylenetetrahydrofolate reductase; This family includes the 5,10-methylenetetrahydrofolate ...
12-291 2.51e-142

Methylenetetrahydrofolate reductase; This family includes the 5,10-methylenetetrahydrofolate reductase EC:1.7.99.5 from bacteria and methylenetetrahydrofolate reductase EC: 1.5.1.20 from eukaryotes. The structure for this domain is known to be a TIM barrel.


Pssm-ID: 396687  Cd Length: 287  Bit Score: 402.08  E-value: 2.51e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432   12 LNQSLAEvnGQINVSFEFFPPRTSEMEQTLWSSIDRLSSLKPKFVSVTYGANSGERDRTHSIIKGIKDRTGLEAAPHLTC 91
Cdd:pfam02219   2 IRQILAE--GKFFISFEFFPPKTENGERNLWERIDRMSAVGPLFVSVTWGAGGSTRDRTSSIASVIQQDTGLEACMHLTC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432   92 IDATPDELRAIAQDYWNNGIRHIVALRGDLPPGSGKPD------MYATDLVALLK-DVAD-FDISVAAYPEVHPEAKSAQ 163
Cdd:pfam02219  80 TDMSKEELDDALEDAKALGIRNILALRGDPPKGTDDWErpeggfKYALDLVRLIRqEYGDyFDIGVAAYPEGHPEAKSWQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432  164 ADLLNLKRKVDAGANRAITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKFADMTNVRIPLWMSKMYEGLD 243
Cdd:pfam02219 160 ADLKYLKEKVDAGADFIITQLFFDVDNFLRFVDRVRAAGIDIPIIPGIMPITSYKSLKRIAKLSGVSIPQELIDRLEPIK 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 550766432  244 DDPETRKLVGANIAMDMVKILSREGVKDFHFYTLNRAEMSYAICHTLG 291
Cdd:pfam02219 240 DDDEAVKSIGIELAVEMCKKLLAEGVPGLHFYTLNREEATLEILENLG 287
MTHFR cd00537
Methylenetetrahydrofolate reductase (MTHFR). 5,10-Methylenetetrahydrofolate is reduced to ...
25-290 4.23e-124

Methylenetetrahydrofolate reductase (MTHFR). 5,10-Methylenetetrahydrofolate is reduced to 5-methyltetrahydrofolate by methylenetetrahydrofolate reductase, a cytoplasmic, NAD(P)-dependent enzyme. 5-methyltetrahydrofolate is utilized by methionine synthase to convert homocysteine to methionine. The enzymatic mechanism is a ping-pong bi-bi mechanism, in which NAD(P)+ release precedes the binding of methylenetetrahydrofolate and the acceptor is free FAD. The family includes the 5,10-methylenetetrahydrofolate reductase EC:1.7.99.5 from prokaryotes and methylenetetrahydrofolate reductase EC: 1.5.1.20 from eukaryotes. The bacterial enzyme is a homotetramer and NADH is the preferred reductant while the eukaryotic enzyme is a homodimer and NADPH is the preferred reductant. In humans, there are several clinically significant mutations in MTHFR that result in hyperhomocysteinemia, which is a risk factor for the development of cardiovascular disease.


Pssm-ID: 238299  Cd Length: 274  Bit Score: 355.39  E-value: 4.23e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432  25 VSFEFFPPRTSEMEQTLWSSIDRLSSLKPKFVSVTYGANSGERDRTHSIIKGIKDRTGLEAAPHLTCIDATPDELRAIAQ 104
Cdd:cd00537    1 ISFEFFPPKTADGEENLEAAADLLGALDPDFVSVTDGAGGSTRDMTLLAAARILQEGGIEPIPHLTCRDRNRIELQSILL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432 105 DYWNNGIRHIVALRGDLPPGSGKP------DMYATDLVALLKDV--ADFDISVAAYPEVHPEAKSAQADLLNLKRKVDAG 176
Cdd:cd00537   81 GAHALGIRNILALRGDPPKGGDQPgakpvgFVYAVDLVELIRKEngGGFSIGVAAYPEGHPEAPSLEEDIKRLKRKVDAG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432 177 ANRAITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKFADMTNVRIPLWMSKMYEGLDDDPETRKLVGANI 256
Cdd:cd00537  161 ADFIITQLFFDNDAFLRFVDRCRAAGITVPIIPGIMPLTSYKQAKRFAKLCGVEIPDWLLERLEKLKDDAEAVRAEGIEI 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 550766432 257 AMDMVKILSREGVKDFHFYTLNRAEMSYAICHTL 290
Cdd:cd00537  241 AAELCDELLEHGVPGIHFYTLNREEATAEILENL 274
 
Name Accession Description Interval E-value
metF PRK09432
methylenetetrahydrofolate reductase;
1-296 0e+00

methylenetetrahydrofolate reductase;


Pssm-ID: 181852  Cd Length: 296  Bit Score: 700.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432   1 MSFFHANQREALNQSLAEVNGQINVSFEFFPPRTSEMEQTLWSSIDRLSSLKPKFVSVTYGANSGERDRTHSIIKGIKDR 80
Cdd:PRK09432   1 MSFFHANQRDALNQSLAELQGQINVSFEFFPPRTSEMEQTLWNSIDRLSSLKPKFVSVTYGANSGERDRTHSIIKGIKKR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432  81 TGLEAAPHLTCIDATPDELRAIAQDYWNNGIRHIVALRGDLPPGSGKPDMYATDLVALLKDVADFDISVAAYPEVHPEAK 160
Cdd:PRK09432  81 TGLEAAPHLTCIDATPDELRTIAKDYWNNGIRHIVALRGDLPPGSGKPEMYASDLVTLLKSVADFDISVAAYPEVHPEAK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432 161 SAQADLLNLKRKVDAGANRAITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKFADMTNVRIPLWMSKMYE 240
Cdd:PRK09432 161 SAQADLINLKRKVDAGANRAITQFFFDVESYLRFRDRCVSAGIDVEIVPGILPVSNFKQLKKFADMTNVRIPAWMAKMFD 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 550766432 241 GLDDDPETRKLVGANIAMDMVKILSREGVKDFHFYTLNRAEMSYAICHTLGVRPAL 296
Cdd:PRK09432 241 GLDDDAETRKLVGASIAMDMVKILSREGVKDFHFYTLNRAELTYAICHTLGVRPGL 296
fadh2 TIGR00676
5,10-methylenetetrahydrofolate reductase, prokaryotic form; The enzyme activities ...
25-291 2.06e-155

5,10-methylenetetrahydrofolate reductase, prokaryotic form; The enzyme activities methylenetetrahydrofolate reductase (EC 1.5.1.20) and 5,10-methylenetetrahydrofolate reductase (FADH) (EC 1.7.99.5) differ in that 1.5.1.20 (assigned in many eukaryotes) is defined to use NADP+ as an acceptor, while 1.7.99.5 (assigned in many bacteria) is flexible with respect to the acceptor; both convert 5-methyltetrahydrofolate to 5,10-methylenetetrahydrofolate. From a larger set of proteins assigned as 1.5.1.20 and 1.7.99.5, this model describes the subset of proteins found in bacteria, and currently designated 1.7.99.5. This protein is an FAD-containing flavoprotein. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273212  Cd Length: 272  Bit Score: 434.75  E-value: 2.06e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432   25 VSFEFFPPRTSEMEQTLWSSIDRLSSLKPKFVSVTYGANSGERDRTHSIIKGIKDRTGLEAAPHLTCIDATPDELRAIAQ 104
Cdd:TIGR00676   1 FSFEFFPPKTDEGEENLWETVDRLSPLDPDFVSVTYGAGGSTRDRTVRIVRRIKKETGIPTVPHLTCIGATREEIREILR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432  105 DYWNNGIRHIVALRGDLPPGSGKPD----MYATDLVALLKDV-ADFDISVAAYPEVHPEAKSAQADLLNLKRKVDAGANR 179
Cdd:TIGR00676  81 EYRELGIRHILALRGDPPKGEGTPTpggfNYASELVEFIRNEfGDFDIGVAAYPEKHPEAPNLEEDIENLKRKVDAGADY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432  180 AITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKFADMTNVRIPLWMSKMYEGLDDDPETRKLVGANIAMD 259
Cdd:TIGR00676 161 AITQLFFDNDDYYRFVDRCRAAGIDVPIIPGIMPITNFKQLLRFAERCGAEIPAWLVKRLEKYDDDPEEVRAVGIEYATD 240
                         250       260       270
                  ....*....|....*....|....*....|..
gi 550766432  260 MVKILSREGVKDFHFYTLNRAEMSYAICHTLG 291
Cdd:TIGR00676 241 QCEDLIAEGVPGIHFYTLNRADATLEICENLG 272
MetF COG0685
5,10-methylenetetrahydrofolate reductase [Amino acid transport and metabolism];
20-293 2.97e-149

5,10-methylenetetrahydrofolate reductase [Amino acid transport and metabolism];


Pssm-ID: 440449  Cd Length: 284  Bit Score: 419.58  E-value: 2.97e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432  20 NGQINVSFEFFPPRTSEMEQTLWSSIDRLSSLKPKFVSVTYGANSGERDRTHSIIKGIKDRTGLEAAPHLTCIDATPDEL 99
Cdd:COG0685    9 AGKPVVSFEFFPPKTAEGEEKLWETAEELAPLDPDFVSVTYGAGGSTRDRTLAIAARIQQETGLEPVAHLTCVGRNREEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432 100 RAIAQDYWNNGIRHIVALRGDLPPGSGKP--DMYATDLVALLKDV-ADFDISVAAYPEVHPEAKSAQADLLNLKRKVDAG 176
Cdd:COG0685   89 ESILLGLAALGIRNILALRGDPPKGDGHPggFLYASELVALIREMnGDFCIGVAAYPEKHPEAPSLEADLDRLKKKVDAG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432 177 ANRAITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKFADMTNVRIPLWMSKMYEGLDDDpETRKLVGANI 256
Cdd:COG0685  169 ADFAITQLFFDNDAYFRFVDRARAAGIDVPIIPGIMPITSFKQLARFAELCGAEIPDWLLKRLEKAGDD-EAVRAVGIEI 247
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 550766432 257 AMDMVKILSREGVKDFHFYTLNRAEMSYAICHTLGVR 293
Cdd:COG0685  248 ATEQCEELLAEGVPGLHFYTLNRAEATLEILERLGLL 284
MTHFR pfam02219
Methylenetetrahydrofolate reductase; This family includes the 5,10-methylenetetrahydrofolate ...
12-291 2.51e-142

Methylenetetrahydrofolate reductase; This family includes the 5,10-methylenetetrahydrofolate reductase EC:1.7.99.5 from bacteria and methylenetetrahydrofolate reductase EC: 1.5.1.20 from eukaryotes. The structure for this domain is known to be a TIM barrel.


Pssm-ID: 396687  Cd Length: 287  Bit Score: 402.08  E-value: 2.51e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432   12 LNQSLAEvnGQINVSFEFFPPRTSEMEQTLWSSIDRLSSLKPKFVSVTYGANSGERDRTHSIIKGIKDRTGLEAAPHLTC 91
Cdd:pfam02219   2 IRQILAE--GKFFISFEFFPPKTENGERNLWERIDRMSAVGPLFVSVTWGAGGSTRDRTSSIASVIQQDTGLEACMHLTC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432   92 IDATPDELRAIAQDYWNNGIRHIVALRGDLPPGSGKPD------MYATDLVALLK-DVAD-FDISVAAYPEVHPEAKSAQ 163
Cdd:pfam02219  80 TDMSKEELDDALEDAKALGIRNILALRGDPPKGTDDWErpeggfKYALDLVRLIRqEYGDyFDIGVAAYPEGHPEAKSWQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432  164 ADLLNLKRKVDAGANRAITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKFADMTNVRIPLWMSKMYEGLD 243
Cdd:pfam02219 160 ADLKYLKEKVDAGADFIITQLFFDVDNFLRFVDRVRAAGIDIPIIPGIMPITSYKSLKRIAKLSGVSIPQELIDRLEPIK 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 550766432  244 DDPETRKLVGANIAMDMVKILSREGVKDFHFYTLNRAEMSYAICHTLG 291
Cdd:pfam02219 240 DDDEAVKSIGIELAVEMCKKLLAEGVPGLHFYTLNREEATLEILENLG 287
MTHFR cd00537
Methylenetetrahydrofolate reductase (MTHFR). 5,10-Methylenetetrahydrofolate is reduced to ...
25-290 4.23e-124

Methylenetetrahydrofolate reductase (MTHFR). 5,10-Methylenetetrahydrofolate is reduced to 5-methyltetrahydrofolate by methylenetetrahydrofolate reductase, a cytoplasmic, NAD(P)-dependent enzyme. 5-methyltetrahydrofolate is utilized by methionine synthase to convert homocysteine to methionine. The enzymatic mechanism is a ping-pong bi-bi mechanism, in which NAD(P)+ release precedes the binding of methylenetetrahydrofolate and the acceptor is free FAD. The family includes the 5,10-methylenetetrahydrofolate reductase EC:1.7.99.5 from prokaryotes and methylenetetrahydrofolate reductase EC: 1.5.1.20 from eukaryotes. The bacterial enzyme is a homotetramer and NADH is the preferred reductant while the eukaryotic enzyme is a homodimer and NADPH is the preferred reductant. In humans, there are several clinically significant mutations in MTHFR that result in hyperhomocysteinemia, which is a risk factor for the development of cardiovascular disease.


Pssm-ID: 238299  Cd Length: 274  Bit Score: 355.39  E-value: 4.23e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432  25 VSFEFFPPRTSEMEQTLWSSIDRLSSLKPKFVSVTYGANSGERDRTHSIIKGIKDRTGLEAAPHLTCIDATPDELRAIAQ 104
Cdd:cd00537    1 ISFEFFPPKTADGEENLEAAADLLGALDPDFVSVTDGAGGSTRDMTLLAAARILQEGGIEPIPHLTCRDRNRIELQSILL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432 105 DYWNNGIRHIVALRGDLPPGSGKP------DMYATDLVALLKDV--ADFDISVAAYPEVHPEAKSAQADLLNLKRKVDAG 176
Cdd:cd00537   81 GAHALGIRNILALRGDPPKGGDQPgakpvgFVYAVDLVELIRKEngGGFSIGVAAYPEGHPEAPSLEEDIKRLKRKVDAG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432 177 ANRAITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKFADMTNVRIPLWMSKMYEGLDDDPETRKLVGANI 256
Cdd:cd00537  161 ADFIITQLFFDNDAFLRFVDRCRAAGITVPIIPGIMPLTSYKQAKRFAKLCGVEIPDWLLERLEKLKDDAEAVRAEGIEI 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 550766432 257 AMDMVKILSREGVKDFHFYTLNRAEMSYAICHTL 290
Cdd:cd00537  241 AAELCDELLEHGVPGIHFYTLNREEATAEILENL 274
fadh2_euk TIGR00677
methylenetetrahydrofolate reductase, eukaryotic type; The enzyme activities ...
26-292 1.02e-71

methylenetetrahydrofolate reductase, eukaryotic type; The enzyme activities methylenetetrahydrofolate reductase (EC 1.5.1.20) and 5,10-methylenetetrahydrofolate reductase (FADH) (EC 1.7.99.5) differ in that 1.5.1.20 (assigned in many eukaryotes) is defined to use NADP+ as an acceptor, while 1.7.99.5 (assigned in many bacteria) is flexible with respect to the acceptor; both convert 5-methyltetrahydrofolate to 5,10-methylenetetrahydrofolate. From a larger set of proteins assigned as 1.5.1.20 and 1.7.99.5, this model describes the subset of proteins found in eukaryotes and designated 1.5.1.20. This protein is an FAD-containing flavoprotein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]


Pssm-ID: 129760  Cd Length: 281  Bit Score: 222.69  E-value: 1.02e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432   26 SFEFFPPRTSEMEQTLWSSIDRLSSLKPKFVSVTYGANSGERDRTHSIIKGIKDRTGLEAAPHLTCIDATPDELRAIAQD 105
Cdd:TIGR00677   3 SFEFFPPKTEEGVQNLYERMDRMVASGPLFIDITWGAGGTTAELTLTIASRAQNVVGVETCMHLTCTNMPIEMIDDALER 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432  106 YWNNGIRHIVALRGDLPPGSGK------PDMYATDLVALLK-DVAD-FDISVAAYPEVHPEAKSAQADLLNLKRKVDAGA 177
Cdd:TIGR00677  83 AYSNGIQNILALRGDPPHIGDDwtevegGFQYAVDLVKYIRsKYGDyFCIGVAGYPEGHPEAESVELDLKYLKEKVDAGA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432  178 NRAITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKFADMTNVRIPLWMSKMYEGLDDDPETRKLVGANIA 257
Cdd:TIGR00677 163 DFIITQLFYDVDNFLKFVNDCRAIGIDCPIVPGIMPINNYASFLRRAKWSKTKIPQEIMSRLEPIKDDDEAVRDYGIELI 242
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 550766432  258 MDMVKILSREGVKDFHFYTLNRAEMSYAICHTLGV 292
Cdd:TIGR00677 243 VEMCQKLLASGIKGLHFYTLNLEKAALMILERLGL 277
PLN02540 PLN02540
methylenetetrahydrofolate reductase
26-291 4.82e-61

methylenetetrahydrofolate reductase


Pssm-ID: 215296  Cd Length: 565  Bit Score: 203.04  E-value: 4.82e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432  26 SFEFFPPRTSEMEQTLWSSIDRLSSLKPKFVSVTYGANSGERDRTHSIIKGIKDRTGLEAAPHLTCIDATPDELRAIAQD 105
Cdd:PLN02540   2 SFEFFPPKTEEGVDNLFERMDRMVAHGPLFCDITWGAGGSTADLTLDIANRMQNMICVETMMHLTCTNMPVEKIDHALET 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432 106 YWNNGIRHIVALRGDLPPGSGKPDMY------ATDLVALLKDV-AD-FDISVAAYPEVHPEA---------KSAQADLLN 168
Cdd:PLN02540  82 IKSNGIQNILALRGDPPHGQDKFVQVeggfacALDLVKHIRSKyGDyFGITVAGYPEAHPDViggdglatpEAYQKDLAY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432 169 LKRKVDAGANRAITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKFADMTNVRIPLWMSKMYEGLDDDPET 248
Cdd:PLN02540 162 LKEKVDAGADLIITQLFYDTDIFLKFVNDCRQIGITCPIVPGIMPINNYKGFLRMTGFCKTKIPAEITAALEPIKDNDEA 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 550766432 249 RKLVGANIAMDMVKILSREGVKDFHFYTLNRAEMSYAICHTLG 291
Cdd:PLN02540 242 VKAYGIHLGTEMCKKILAHGIKGLHLYTLNLEKSALAILMNLG 284
PRK08645 PRK08645
bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; ...
58-283 1.22e-14

bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; Reviewed


Pssm-ID: 236321 [Multi-domain]  Cd Length: 612  Bit Score: 73.73  E-value: 1.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432  58 VTYGANSGERDRTHSIIKG--IKDRTGLEAAPHLTCID----ATPDELRAIAQdywnNGIRHIVALRGDlPPGSG-KPDm 130
Cdd:PRK08645 355 ITLADNPLARVRISNIALAslIKRELGIEPLVHITCRDrnliGLQSHLLGLHA----LGIRNVLAITGD-PAKVGdFPG- 428
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432 131 yAT--------DLVALLKDV--------------ADFDISVAAYPEV-HPEAKSAQadllnLKRKVDAGANRAITQFFFD 187
Cdd:PRK08645 429 -ATsvydlnsfGLIKLIKQLnegisysgkplgkkTNFSIGGAFNPNVrNLDKEVKR-----LEKKIEAGADYFITQPVYD 502
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766432 188 VESYLRFRDRcvSAGIDVEIIPGILPVSNFKQAkKFadMTN----VRIPLWMSKMYEGLDDDPETRKLvGANIAMDMV-K 262
Cdd:PRK08645 503 EELIEELLEA--TKHLGVPIFIGIMPLVSYRNA-EF--LHNevpgITLPEEIRERMRAVEDKEEAREE-GVAIARELIdA 576
                        250       260
                 ....*....|....*....|..
gi 550766432 263 ILSRegVKDFHFYT-LNRAEMS 283
Cdd:PRK08645 577 AREY--FNGIYLITpFLRYEMA 596
 
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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