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Conserved domains on  [gi|161077430|ref|NP_001097432|]
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methenyltetrahydrofolate synthetase, isoform A [Drosophila melanogaster]

Protein Classification

5-formyltetrahydrofolate cyclo-ligase( domain architecture ID 10000709)

5-formyltetrahydrofolate cyclo-ligase catalyzes the irreversible conversion of 5-formyltetrahydrofolate (5-FTHF) to 5,10-methenyltetrahydrofolate, part of the folate metabolism

CATH:  3.40.50.10420
EC:  6.3.3.2
Gene Ontology:  GO:0005524|GO:0030272
PubMed:  8034591

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FAU1 COG0212
5-formyltetrahydrofolate cyclo-ligase [Coenzyme transport and metabolism];
10-201 3.40e-51

5-formyltetrahydrofolate cyclo-ligase [Coenzyme transport and metabolism];


:

Pssm-ID: 439982 [Multi-domain]  Cd Length: 186  Bit Score: 163.40  E-value: 3.40e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077430  10 KVALRKRMKDALKGIDAEAIARQSQAVTAKVLQSEIFRQAQRVSIYLSTASELDTTALLSEMFRLEKMVFVP--TYEGSR 87
Cdd:COG0212    5 KKALRKELLARRRALSPEERAEASAAIAERLLALLEFRRAKTIALYLPIRGEVDTRPLIEALLARGKRVALPvvVPDGRP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077430  88 MKMVRLRGMEEYESlplTKWNIKQPDFKEAREDAmtngHGIDLFIVPGVAFTRCGARMGHGMGYYDKFLKQHaekypHKK 167
Cdd:COG0212   85 LEFRRWTPGDPLEP---GRFGIPEPVGDAPEVAP----EEIDLVLVPLLAFDRRGYRLGYGGGYYDRTLARL-----RPR 152
                        170       180       190
                 ....*....|....*....|....*....|....
gi 161077430 168 ISLMALSLNEQIVsnEELPMESHDVRLHSVITEN 201
Cdd:COG0212  153 PLTIGLAFDCQLV--DELPVEPHDVPLDAIVTEK 184
 
Name Accession Description Interval E-value
FAU1 COG0212
5-formyltetrahydrofolate cyclo-ligase [Coenzyme transport and metabolism];
10-201 3.40e-51

5-formyltetrahydrofolate cyclo-ligase [Coenzyme transport and metabolism];


Pssm-ID: 439982 [Multi-domain]  Cd Length: 186  Bit Score: 163.40  E-value: 3.40e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077430  10 KVALRKRMKDALKGIDAEAIARQSQAVTAKVLQSEIFRQAQRVSIYLSTASELDTTALLSEMFRLEKMVFVP--TYEGSR 87
Cdd:COG0212    5 KKALRKELLARRRALSPEERAEASAAIAERLLALLEFRRAKTIALYLPIRGEVDTRPLIEALLARGKRVALPvvVPDGRP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077430  88 MKMVRLRGMEEYESlplTKWNIKQPDFKEAREDAmtngHGIDLFIVPGVAFTRCGARMGHGMGYYDKFLKQHaekypHKK 167
Cdd:COG0212   85 LEFRRWTPGDPLEP---GRFGIPEPVGDAPEVAP----EEIDLVLVPLLAFDRRGYRLGYGGGYYDRTLARL-----RPR 152
                        170       180       190
                 ....*....|....*....|....*....|....
gi 161077430 168 ISLMALSLNEQIVsnEELPMESHDVRLHSVITEN 201
Cdd:COG0212  153 PLTIGLAFDCQLV--DELPVEPHDVPLDAIVTEK 184
PLN02812 PLN02812
5-formyltetrahydrofolate cyclo-ligase
10-201 1.73e-50

5-formyltetrahydrofolate cyclo-ligase


Pssm-ID: 178408  Cd Length: 211  Bit Score: 162.12  E-value: 1.73e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077430  10 KVALRKRMKDALKGIDAEAIARQSQAVTAKVLQSEIFRQAQRVSIYLSTAS--ELDTTALLSEMFRLE-KMVFVPTYEG- 85
Cdd:PLN02812   7 KKALRKEVRRALKALSPEQRAQEDAAIQSRLLELPWFKSSKRLCAYVSCAKlrEVDTSKILSEILQNPdKRLYVPRVEDk 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077430  86 -SRMKMVRLRGMeeYESLPLTKWNIKQP----DFKEAREDAMTNGHGIDLFIVPGVAFTRCGARMGHGMGYYDKFLKQHA 160
Cdd:PLN02812  87 nSNMRMLHITDM--ADDLVANSMNILEPtpvdADGNPREDVLQAPEPLDLLLLPGLAFDRSGRRLGRGGGYYDTFLSKYQ 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 161077430 161 E-------KYPhkkiSLMALSLNEQIVSNEELPMESHDVRLHSVITEN 201
Cdd:PLN02812 165 ElakekgwKQP----LLVALSYSPQILDEGSVPVDETDVLVDALVTPS 208
5-FTHF_cyc-lig pfam01812
5-formyltetrahydrofolate cyclo-ligase family; 5-formyltetrahydrofolate cyclo-ligase or ...
10-200 2.80e-48

5-formyltetrahydrofolate cyclo-ligase family; 5-formyltetrahydrofolate cyclo-ligase or methenyl-THF synthetase EC:6.3.3.2 catalyzes the interchange of 5-formyltetrahydrofolate (5-FTHF) to 5-10-methenyltetrahydrofolate, this requires ATP and Mg2+. 5-FTHF is used in chemotherapy where it is clinically known as Leucovorin.


Pssm-ID: 396398 [Multi-domain]  Cd Length: 186  Bit Score: 155.93  E-value: 2.80e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077430   10 KVALRKRMKDALKGIDAEAIARQSQAVTAKVLQSEIFRQAQRVSIYLSTASELDTTALLSEMFRLEKMVFVPTY--EGSR 87
Cdd:pfam01812   1 KQELRKQLLARRRALSEEERAAQSEALHQRLISLPEYQKAKRVAAYVSVGGEIDTRELIDLLLEEGKRVLLPVPrpGSGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077430   88 MKMVRLRGMEEYESLPLTKWNIKQPDFKEAREDAMTnghGIDLFIVPGVAFTRCGARMGHGMGYYDKFLKQHAEKYPHKK 167
Cdd:pfam01812  81 LDMVRFTPYYPEDSLPRGAWGLKEPVEEELRELALG---QLDLVLVPGVAFDRQGYRLGRGGGYYDRYLARLQGHGAKPY 157
                         170       180       190
                  ....*....|....*....|....*....|...
gi 161077430  168 isLMALSLNEQIVsnEELPMESHDVRLHSVITE 200
Cdd:pfam01812 158 --TVGLAFDEQLV--ERLPVEPHDVPVDEVVTE 186
MTHFS_bact TIGR02727
5,10-methenyltetrahydrofolate synthetase; This enzyme, 5,10-methenyltetrahydrofolate ...
10-200 1.97e-42

5,10-methenyltetrahydrofolate synthetase; This enzyme, 5,10-methenyltetrahydrofolate synthetase, is also called 5-formyltetrahydrofolate cycloligase. Function of bacterial proteins in this family was inferred originally from the known activity of eukaryotic homologs. Recently, activity was shown explicitly for the member from Mycoplasma pneumonia. Members of this family from alpha- and gamma-proteobacteria, designated ygfA, are often found in an operon with 6S structural RNA, and show a similar pattern of high expression during stationary phase. The function may be to deplete folate to slow 1-carbon biosynthetic metabolism. [Central intermediary metabolism, One-carbon metabolism]


Pssm-ID: 274270 [Multi-domain]  Cd Length: 179  Bit Score: 140.49  E-value: 1.97e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077430   10 KVALRKRMKDALKGIDAEAIARQSQAVTAKVLQSEIFRQAQRVSIYLSTASELDTTALLSEMFRLEKMVFVP--TYEGSR 87
Cdd:TIGR02727   1 KKELRKKLLEARKALSSEERKAASSAIAKRLLALIEWKNAKTIALYLPLRGEVDTRPLIEQLLKEGKRVALPkvDPDGKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077430   88 MkMVRLRGMEEyESLPLTKWNIKQPDFKEAREDamtNGHGIDLFIVPGVAFTRCGARMGHGMGYYDKFLKQHaeKYPhkK 167
Cdd:TIGR02727  81 M-LFFRIWSPE-QLLTKGPFGILEPVGDLEEPV---PPDEIDLIIVPGVAFDRRGYRLGYGGGYYDRFLARL--KGI--T 151
                         170       180       190
                  ....*....|....*....|....*....|...
gi 161077430  168 ISlmaLSLNEQIVsnEELPMESHDVRLHSVITE 200
Cdd:TIGR02727 152 IG---LAFDFQLV--DELPREPHDVPVDAIITE 179
 
Name Accession Description Interval E-value
FAU1 COG0212
5-formyltetrahydrofolate cyclo-ligase [Coenzyme transport and metabolism];
10-201 3.40e-51

5-formyltetrahydrofolate cyclo-ligase [Coenzyme transport and metabolism];


Pssm-ID: 439982 [Multi-domain]  Cd Length: 186  Bit Score: 163.40  E-value: 3.40e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077430  10 KVALRKRMKDALKGIDAEAIARQSQAVTAKVLQSEIFRQAQRVSIYLSTASELDTTALLSEMFRLEKMVFVP--TYEGSR 87
Cdd:COG0212    5 KKALRKELLARRRALSPEERAEASAAIAERLLALLEFRRAKTIALYLPIRGEVDTRPLIEALLARGKRVALPvvVPDGRP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077430  88 MKMVRLRGMEEYESlplTKWNIKQPDFKEAREDAmtngHGIDLFIVPGVAFTRCGARMGHGMGYYDKFLKQHaekypHKK 167
Cdd:COG0212   85 LEFRRWTPGDPLEP---GRFGIPEPVGDAPEVAP----EEIDLVLVPLLAFDRRGYRLGYGGGYYDRTLARL-----RPR 152
                        170       180       190
                 ....*....|....*....|....*....|....
gi 161077430 168 ISLMALSLNEQIVsnEELPMESHDVRLHSVITEN 201
Cdd:COG0212  153 PLTIGLAFDCQLV--DELPVEPHDVPLDAIVTEK 184
PLN02812 PLN02812
5-formyltetrahydrofolate cyclo-ligase
10-201 1.73e-50

5-formyltetrahydrofolate cyclo-ligase


Pssm-ID: 178408  Cd Length: 211  Bit Score: 162.12  E-value: 1.73e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077430  10 KVALRKRMKDALKGIDAEAIARQSQAVTAKVLQSEIFRQAQRVSIYLSTAS--ELDTTALLSEMFRLE-KMVFVPTYEG- 85
Cdd:PLN02812   7 KKALRKEVRRALKALSPEQRAQEDAAIQSRLLELPWFKSSKRLCAYVSCAKlrEVDTSKILSEILQNPdKRLYVPRVEDk 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077430  86 -SRMKMVRLRGMeeYESLPLTKWNIKQP----DFKEAREDAMTNGHGIDLFIVPGVAFTRCGARMGHGMGYYDKFLKQHA 160
Cdd:PLN02812  87 nSNMRMLHITDM--ADDLVANSMNILEPtpvdADGNPREDVLQAPEPLDLLLLPGLAFDRSGRRLGRGGGYYDTFLSKYQ 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 161077430 161 E-------KYPhkkiSLMALSLNEQIVSNEELPMESHDVRLHSVITEN 201
Cdd:PLN02812 165 ElakekgwKQP----LLVALSYSPQILDEGSVPVDETDVLVDALVTPS 208
5-FTHF_cyc-lig pfam01812
5-formyltetrahydrofolate cyclo-ligase family; 5-formyltetrahydrofolate cyclo-ligase or ...
10-200 2.80e-48

5-formyltetrahydrofolate cyclo-ligase family; 5-formyltetrahydrofolate cyclo-ligase or methenyl-THF synthetase EC:6.3.3.2 catalyzes the interchange of 5-formyltetrahydrofolate (5-FTHF) to 5-10-methenyltetrahydrofolate, this requires ATP and Mg2+. 5-FTHF is used in chemotherapy where it is clinically known as Leucovorin.


Pssm-ID: 396398 [Multi-domain]  Cd Length: 186  Bit Score: 155.93  E-value: 2.80e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077430   10 KVALRKRMKDALKGIDAEAIARQSQAVTAKVLQSEIFRQAQRVSIYLSTASELDTTALLSEMFRLEKMVFVPTY--EGSR 87
Cdd:pfam01812   1 KQELRKQLLARRRALSEEERAAQSEALHQRLISLPEYQKAKRVAAYVSVGGEIDTRELIDLLLEEGKRVLLPVPrpGSGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077430   88 MKMVRLRGMEEYESLPLTKWNIKQPDFKEAREDAMTnghGIDLFIVPGVAFTRCGARMGHGMGYYDKFLKQHAEKYPHKK 167
Cdd:pfam01812  81 LDMVRFTPYYPEDSLPRGAWGLKEPVEEELRELALG---QLDLVLVPGVAFDRQGYRLGRGGGYYDRYLARLQGHGAKPY 157
                         170       180       190
                  ....*....|....*....|....*....|...
gi 161077430  168 isLMALSLNEQIVsnEELPMESHDVRLHSVITE 200
Cdd:pfam01812 158 --TVGLAFDEQLV--ERLPVEPHDVPVDEVVTE 186
MTHFS_bact TIGR02727
5,10-methenyltetrahydrofolate synthetase; This enzyme, 5,10-methenyltetrahydrofolate ...
10-200 1.97e-42

5,10-methenyltetrahydrofolate synthetase; This enzyme, 5,10-methenyltetrahydrofolate synthetase, is also called 5-formyltetrahydrofolate cycloligase. Function of bacterial proteins in this family was inferred originally from the known activity of eukaryotic homologs. Recently, activity was shown explicitly for the member from Mycoplasma pneumonia. Members of this family from alpha- and gamma-proteobacteria, designated ygfA, are often found in an operon with 6S structural RNA, and show a similar pattern of high expression during stationary phase. The function may be to deplete folate to slow 1-carbon biosynthetic metabolism. [Central intermediary metabolism, One-carbon metabolism]


Pssm-ID: 274270 [Multi-domain]  Cd Length: 179  Bit Score: 140.49  E-value: 1.97e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077430   10 KVALRKRMKDALKGIDAEAIARQSQAVTAKVLQSEIFRQAQRVSIYLSTASELDTTALLSEMFRLEKMVFVP--TYEGSR 87
Cdd:TIGR02727   1 KKELRKKLLEARKALSSEERKAASSAIAKRLLALIEWKNAKTIALYLPLRGEVDTRPLIEQLLKEGKRVALPkvDPDGKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077430   88 MkMVRLRGMEEyESLPLTKWNIKQPDFKEAREDamtNGHGIDLFIVPGVAFTRCGARMGHGMGYYDKFLKQHaeKYPhkK 167
Cdd:TIGR02727  81 M-LFFRIWSPE-QLLTKGPFGILEPVGDLEEPV---PPDEIDLIIVPGVAFDRRGYRLGYGGGYYDRFLARL--KGI--T 151
                         170       180       190
                  ....*....|....*....|....*....|...
gi 161077430  168 ISlmaLSLNEQIVsnEELPMESHDVRLHSVITE 200
Cdd:TIGR02727 152 IG---LAFDFQLV--DELPREPHDVPVDAIITE 179
PRK10333 PRK10333
5-formyltetrahydrofolate cyclo-ligase family protein; Provisional
22-199 8.14e-13

5-formyltetrahydrofolate cyclo-ligase family protein; Provisional


Pssm-ID: 182385  Cd Length: 182  Bit Score: 63.80  E-value: 8.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077430  22 KGIDAEAIARQSQAVTAKVLQSEIFRQAQRVSIYLSTASELDTTALLSEMFRLEKMVFVPTYEGSRMKMVRLRGMEEYES 101
Cdd:PRK10333   7 RALTPEQQQEMGQQAATRMMTYPPVVMAHTVAVFLSFDGELDTQPLIEQLWRAGKRVYLPVLHPFSAGNLLFLNYHPQSE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077430 102 LPLTKWNIKQPdfKEAREDAMTNGHgIDLFIVPGVAFTRCGARMGHGMGYYDKFLkqhaEKYPHKKISLMALSLNEQIVs 181
Cdd:PRK10333  87 LVMNRLKIHEP--KLDVRDVLPLSR-LDVLITPLVAFDEYGQRLGMGGGFYDRTL----QNWQHYKTQPVGYAHDCQLV- 158
                        170
                 ....*....|....*...
gi 161077430 182 nEELPMESHDVRLHSVIT 199
Cdd:PRK10333 159 -EKLPVEEWDIPLPAVVT 175
 
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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