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Conserved domains on  [gi|336019394|gb|EGN49119|]
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5-formyltetrahydrofolate cyclo-ligase [Lachnospiraceae bacterium 1_1_57FAA]

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];
1-182 4.12e-61

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


:

Pssm-ID: 439982 [Multi-domain]  Cd Length: 186  Bit Score: 188.06  E-value: 4.12e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019394   1 METKRDIRKMMTALRAAMSEKERAEAGRIIAARLFSSKVYEDAGTVCCYASFGSEVPTEEIIEESLRRGKCAAVPKVTGK 80
Cdd:COG0212    2 AMDKKALRKELLARRRALSPEERAEASAAIAERLLALLEFRRAKTIALYLPIRGEVDTRPLIEALLARGKRVALPVVVPD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019394  81 -QKMKFALIHSMADLKAGFHGIPEPESWCREIPKcgSKL-LVIVPGVVFDRAGNRIgygggyyDSYLK--QADCIKVGVA 156
Cdd:COG0212   82 gRPLEFRRWTPGDPLEPGRFGIPEPVGDAPEVAP--EEIdLVLVPLLAFDRRGYRLgygggyyDRTLArlRPRPLTIGLA 159
                        170       180
                 ....*....|....*....|....*.
gi 336019394 157 FDFQCVEQIVPEVHDVPVDYIITEKE 182
Cdd:COG0212  160 FDCQLVDELPVEPHDVPLDAIVTEKG 185
 
Name Accession Description Interval E-value
FAU1 COG0212
5-formyltetrahydrofolate cyclo-ligase [Coenzyme transport and metabolism];
1-182 4.12e-61

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


Pssm-ID: 439982 [Multi-domain]  Cd Length: 186  Bit Score: 188.06  E-value: 4.12e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019394   1 METKRDIRKMMTALRAAMSEKERAEAGRIIAARLFSSKVYEDAGTVCCYASFGSEVPTEEIIEESLRRGKCAAVPKVTGK 80
Cdd:COG0212    2 AMDKKALRKELLARRRALSPEERAEASAAIAERLLALLEFRRAKTIALYLPIRGEVDTRPLIEALLARGKRVALPVVVPD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019394  81 -QKMKFALIHSMADLKAGFHGIPEPESWCREIPKcgSKL-LVIVPGVVFDRAGNRIgygggyyDSYLK--QADCIKVGVA 156
Cdd:COG0212   82 gRPLEFRRWTPGDPLEPGRFGIPEPVGDAPEVAP--EEIdLVLVPLLAFDRRGYRLgygggyyDRTLArlRPRPLTIGLA 159
                        170       180
                 ....*....|....*....|....*.
gi 336019394 157 FDFQCVEQIVPEVHDVPVDYIITEKE 182
Cdd:COG0212  160 FDCQLVDELPVEPHDVPLDAIVTEKG 185
MTHFS_bact TIGR02727
5,10-methenyltetrahydrofolate synthetase; This enzyme, 5,10-methenyltetrahydrofolate ...
4-180 1.35e-49

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: 158.59  E-value: 1.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019394    4 KRDIRKMMTALRAAMSEKERAEAGRIIAARLFSSKVYEDAGTVCCYASFGSEVPTEEIIEESLRRGKCAAVPKVTGKQK- 82
Cdd:TIGR02727   1 KKELRKKLLEARKALSSEERKAASSAIAKRLLALIEWKNAKTIALYLPLRGEVDTRPLIEQLLKEGKRVALPKVDPDGKe 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019394   83 MKFALIHSMAD-LKAGFHGIPEPESWCREIPKCGSKLLVIVPGVVFDRAGNRIGYGGGYYDSYLKQADCIKVGVAFDFQC 161
Cdd:TIGR02727  81 MLFFRIWSPEQlLTKGPFGILEPVGDLEEPVPPDEIDLIIVPGVAFDRRGYRLGYGGGYYDRFLARLKGITIGLAFDFQL 160
                         170
                  ....*....|....*....
gi 336019394  162 VEQIVPEVHDVPVDYIITE 180
Cdd:TIGR02727 161 VDELPREPHDVPVDAIITE 179
5-FTHF_cyc-lig pfam01812
5-formyltetrahydrofolate cyclo-ligase family; 5-formyltetrahydrofolate cyclo-ligase or ...
4-180 5.45e-39

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: 131.66  E-value: 5.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019394    4 KRDIRKMMTALRAAMSEKERAEAGRIIAARLFSSKVYEDAGTVCCYASFGSEVPTEEIIEESLRRGKCAAVPKV---TGK 80
Cdd:pfam01812   1 KQELRKQLLARRRALSEEERAAQSEALHQRLISLPEYQKAKRVAAYVSVGGEIDTRELIDLLLEEGKRVLLPVPrpgSGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019394   81 QKM-KFALIHSMADLKAGFHGIPEP-ESWCREIPkcGSKL-LVIVPGVVFDRAGNRIGYGGGYYDSYLK-----QADCIK 152
Cdd:pfam01812  81 LDMvRFTPYYPEDSLPRGAWGLKEPvEEELRELA--LGQLdLVLVPGVAFDRQGYRLGRGGGYYDRYLArlqghGAKPYT 158
                         170       180
                  ....*....|....*....|....*...
gi 336019394  153 VGVAFDFQCVEQIVPEVHDVPVDYIITE 180
Cdd:pfam01812 159 VGLAFDEQLVERLPVEPHDVPVDEVVTE 186
PLN02812 PLN02812
5-formyltetrahydrofolate cyclo-ligase
2-184 2.46e-20

5-formyltetrahydrofolate cyclo-ligase


Pssm-ID: 178408  Cd Length: 211  Bit Score: 84.31  E-value: 2.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019394   2 ETKRDIRKmmtALRAaMSEKERAEAGRIIAARLFSSKVYEDAGTVCCYASFGS--EVPTEEIIEESLRRGKCAA-VPKVT 78
Cdd:PLN02812   9 ALRKEVRR---ALKA-LSPEQRAQEDAAIQSRLLELPWFKSSKRLCAYVSCAKlrEVDTSKILSEILQNPDKRLyVPRVE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019394  79 GKQ-KMKFALIHSMA-DLKAGFHGIPEPESWCREIPKCGSKL-------LVIVPGVVFDRAGNRIGYGGGYYDSYLKQAD 149
Cdd:PLN02812  85 DKNsNMRMLHITDMAdDLVANSMNILEPTPVDADGNPREDVLqapepldLLLLPGLAFDRSGRRLGRGGGYYDTFLSKYQ 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 336019394 150 CIK----------VGVAFDFQCVEQ-IVP-EVHDVPVDYIITEKEMI 184
Cdd:PLN02812 165 ELAkekgwkqpllVALSYSPQILDEgSVPvDETDVLVDALVTPSGVI 211
 
Name Accession Description Interval E-value
FAU1 COG0212
5-formyltetrahydrofolate cyclo-ligase [Coenzyme transport and metabolism];
1-182 4.12e-61

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


Pssm-ID: 439982 [Multi-domain]  Cd Length: 186  Bit Score: 188.06  E-value: 4.12e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019394   1 METKRDIRKMMTALRAAMSEKERAEAGRIIAARLFSSKVYEDAGTVCCYASFGSEVPTEEIIEESLRRGKCAAVPKVTGK 80
Cdd:COG0212    2 AMDKKALRKELLARRRALSPEERAEASAAIAERLLALLEFRRAKTIALYLPIRGEVDTRPLIEALLARGKRVALPVVVPD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019394  81 -QKMKFALIHSMADLKAGFHGIPEPESWCREIPKcgSKL-LVIVPGVVFDRAGNRIgygggyyDSYLK--QADCIKVGVA 156
Cdd:COG0212   82 gRPLEFRRWTPGDPLEPGRFGIPEPVGDAPEVAP--EEIdLVLVPLLAFDRRGYRLgygggyyDRTLArlRPRPLTIGLA 159
                        170       180
                 ....*....|....*....|....*.
gi 336019394 157 FDFQCVEQIVPEVHDVPVDYIITEKE 182
Cdd:COG0212  160 FDCQLVDELPVEPHDVPLDAIVTEKG 185
MTHFS_bact TIGR02727
5,10-methenyltetrahydrofolate synthetase; This enzyme, 5,10-methenyltetrahydrofolate ...
4-180 1.35e-49

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: 158.59  E-value: 1.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019394    4 KRDIRKMMTALRAAMSEKERAEAGRIIAARLFSSKVYEDAGTVCCYASFGSEVPTEEIIEESLRRGKCAAVPKVTGKQK- 82
Cdd:TIGR02727   1 KKELRKKLLEARKALSSEERKAASSAIAKRLLALIEWKNAKTIALYLPLRGEVDTRPLIEQLLKEGKRVALPKVDPDGKe 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019394   83 MKFALIHSMAD-LKAGFHGIPEPESWCREIPKCGSKLLVIVPGVVFDRAGNRIGYGGGYYDSYLKQADCIKVGVAFDFQC 161
Cdd:TIGR02727  81 MLFFRIWSPEQlLTKGPFGILEPVGDLEEPVPPDEIDLIIVPGVAFDRRGYRLGYGGGYYDRFLARLKGITIGLAFDFQL 160
                         170
                  ....*....|....*....
gi 336019394  162 VEQIVPEVHDVPVDYIITE 180
Cdd:TIGR02727 161 VDELPREPHDVPVDAIITE 179
5-FTHF_cyc-lig pfam01812
5-formyltetrahydrofolate cyclo-ligase family; 5-formyltetrahydrofolate cyclo-ligase or ...
4-180 5.45e-39

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: 131.66  E-value: 5.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019394    4 KRDIRKMMTALRAAMSEKERAEAGRIIAARLFSSKVYEDAGTVCCYASFGSEVPTEEIIEESLRRGKCAAVPKV---TGK 80
Cdd:pfam01812   1 KQELRKQLLARRRALSEEERAAQSEALHQRLISLPEYQKAKRVAAYVSVGGEIDTRELIDLLLEEGKRVLLPVPrpgSGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019394   81 QKM-KFALIHSMADLKAGFHGIPEP-ESWCREIPkcGSKL-LVIVPGVVFDRAGNRIGYGGGYYDSYLK-----QADCIK 152
Cdd:pfam01812  81 LDMvRFTPYYPEDSLPRGAWGLKEPvEEELRELA--LGQLdLVLVPGVAFDRQGYRLGRGGGYYDRYLArlqghGAKPYT 158
                         170       180
                  ....*....|....*....|....*...
gi 336019394  153 VGVAFDFQCVEQIVPEVHDVPVDYIITE 180
Cdd:pfam01812 159 VGLAFDEQLVERLPVEPHDVPVDEVVTE 186
PLN02812 PLN02812
5-formyltetrahydrofolate cyclo-ligase
2-184 2.46e-20

5-formyltetrahydrofolate cyclo-ligase


Pssm-ID: 178408  Cd Length: 211  Bit Score: 84.31  E-value: 2.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019394   2 ETKRDIRKmmtALRAaMSEKERAEAGRIIAARLFSSKVYEDAGTVCCYASFGS--EVPTEEIIEESLRRGKCAA-VPKVT 78
Cdd:PLN02812   9 ALRKEVRR---ALKA-LSPEQRAQEDAAIQSRLLELPWFKSSKRLCAYVSCAKlrEVDTSKILSEILQNPDKRLyVPRVE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019394  79 GKQ-KMKFALIHSMA-DLKAGFHGIPEPESWCREIPKCGSKL-------LVIVPGVVFDRAGNRIGYGGGYYDSYLKQAD 149
Cdd:PLN02812  85 DKNsNMRMLHITDMAdDLVANSMNILEPTPVDADGNPREDVLqapepldLLLLPGLAFDRSGRRLGRGGGYYDTFLSKYQ 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 336019394 150 CIK----------VGVAFDFQCVEQ-IVP-EVHDVPVDYIITEKEMI 184
Cdd:PLN02812 165 ELAkekgwkqpllVALSYSPQILDEgSVPvDETDVLVDALVTPSGVI 211
PRK10333 PRK10333
5-formyltetrahydrofolate cyclo-ligase family protein; Provisional
10-179 1.51e-10

5-formyltetrahydrofolate cyclo-ligase family protein; Provisional


Pssm-ID: 182385  Cd Length: 182  Bit Score: 57.63  E-value: 1.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019394  10 MMTALRAAMSEKERAEAGRIIAARLFSSKVYEDAGTVCCYASFGSEVPTEEIIEESLRRGKCAAVPKVT--GKQKMKFAL 87
Cdd:PRK10333   1 MIRQRRRALTPEQQQEMGQQAATRMMTYPPVVMAHTVAVFLSFDGELDTQPLIEQLWRAGKRVYLPVLHpfSAGNLLFLN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019394  88 IHSMADLKAGFHGIPEPESWCREIPKCGSKLLVIVPGVVFDRAGNRIGYGGGYYDSYLK---QADCIKVGVAFDFQCVEQ 164
Cdd:PRK10333  81 YHPQSELVMNRLKIHEPKLDVRDVLPLSRLDVLITPLVAFDEYGQRLGMGGGFYDRTLQnwqHYKTQPVGYAHDCQLVEK 160
                        170
                 ....*....|....*
gi 336019394 165 IVPEVHDVPVDYIIT 179
Cdd:PRK10333 161 LPVEEWDIPLPAVVT 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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