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Conserved domains on  [gi|463284648|gb|EMJ54710|]
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tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain protein [Leptospira interrogans serovar Valbuzzi str. Duyster]

Protein Classification

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase( domain architecture ID 11487135)

bifunctional 5,10-methylenetetrahydrofolate dehydrogenase/ 5,10-methenyltetrahydrofolate cyclohydrolase reversibly catalyzes oxidation of 5,10-methylene-THF to 5,10-methenyl-THF and hydrolysis of 5,10-methenyl-THF to 10-formyl-THF

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK14177 PRK14177
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 1-284 0e+00

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


:

Pssm-ID: 172665 [Multi-domain]  Cd Length: 284  Bit Score: 603.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   1 MNPVLLDGKKLSEKIKEEIRSAIEERKTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELL 80
Cdd:PRK14177   1 MSPILLDGKKLSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  81 DVIDKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGK 160
Cdd:PRK14177  81 GVIDKLNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 161 NAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNPGNIGDI 240
Cdd:PRK14177 161 NAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYNPGNVGDI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 463284648 241 EISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKEHFTPPVK 284
Cdd:PRK14177 241 EISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFKEHFTPPVE 284
 
Name Accession Description Interval E-value
PRK14177 PRK14177
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 1-284 0e+00

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172665 [Multi-domain]  Cd Length: 284  Bit Score: 603.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   1 MNPVLLDGKKLSEKIKEEIRSAIEERKTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELL 80
Cdd:PRK14177   1 MSPILLDGKKLSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  81 DVIDKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGK 160
Cdd:PRK14177  81 GVIDKLNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 161 NAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNPGNIGDI 240
Cdd:PRK14177 161 NAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYNPGNVGDI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 463284648 241 EISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKEHFTPPVK 284
Cdd:PRK14177 241 EISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFKEHFTPPVE 284
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
 1-278 3.99e-155

5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 433.67  E-value: 3.99e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   1 MNPVLLDGKKLSEKIKEEIRSAIEERKTKNfRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELL 80
Cdd:COG0190    1 MMAQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  81 DVIDKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGK 160
Cdd:COG0190   80 ALIDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 161 NAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNP---GNI 237
Cdd:COG0190  160 HAVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRvedGKL 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 463284648 238 -GDIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKEH 278
Cdd:COG0190  240 vGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQ 281
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
124-279 3.09e-81

Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;


Pssm-ID: 427036  Cd Length: 160  Bit Score: 241.99  E-value: 3.09e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  124 TTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGKNAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNA 203
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITREA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  204 DIIIGAVGKPEFIKADWISNGAILLDAGYNPGN----IGDIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKEHF 279
Cdd:pfam02882  81 DIVVVAVGKPELIKADWIKPGAVVIDVGINRVGngklVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNTVEAAKRQL 160
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
 117-276 2.80e-76

NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding domain of the Methylene-Tetrahydrofolate Dehydrogenase/cyclohydrolase (m-THF DH/cyclohydrolase) bifunctional enzyme. Tetrahydrofolate is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofucntional DH, as well as bifunctional m-THF m-THF DHm-THF DHDH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains the bifunctional DH/cyclohydrolase. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains.


Pssm-ID: 133448  Cd Length: 168  Bit Score: 229.75  E-value: 2.80e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 117 HKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGKNAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNL 196
Cdd:cd01080    2 EKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKTKNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 197 PDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNPGN-------IGDIEISKAKDRSSFYTPVPGGVGPMTIAVLLL 269
Cdd:cd01080   82 KEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPdksggklVGDVDFESAKEKASAITPVPGGVGPMTVAMLMK 161


                 ....*..
gi 463284648 270 QTLYSAK 276
Cdd:cd01080  162 NTVEAAK 168
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
149-245 2.00e-04

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 40.90  E-value: 2.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   149 LLKEYGIDVAGKNAVVVGRSPIlGKPMAMLLTEMNATVTLCHS-------------KTQNLPDIVRNADIIIGAVGKPEF 215
Cdd:smart00997  13 ILRATNVLLAGKNVVVAGYGDV-GKGVAARLRGLGARVIVTEIdpiraleaamdgfEVMKMEEAAKRADIFVTATGNKDV 91

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 463284648   216 IKADWI---SNGAILldagynpGNIG--DIEISKA 245
Cdd:smart00997  92 ITREHFramKDGAIL-------ANAGhfDVEIDVA 119
 
Name Accession Description Interval E-value
PRK14177 PRK14177
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 1-284 0e+00

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172665 [Multi-domain]  Cd Length: 284  Bit Score: 603.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   1 MNPVLLDGKKLSEKIKEEIRSAIEERKTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELL 80
Cdd:PRK14177   1 MSPILLDGKKLSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  81 DVIDKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGK 160
Cdd:PRK14177  81 GVIDKLNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 161 NAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNPGNIGDI 240
Cdd:PRK14177 161 NAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYNPGNVGDI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 463284648 241 EISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKEHFTPPVK 284
Cdd:PRK14177 241 EISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFKEHFTPPVE 284
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
 1-278 3.99e-155

5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 433.67  E-value: 3.99e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   1 MNPVLLDGKKLSEKIKEEIRSAIEERKTKNfRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELL 80
Cdd:COG0190    1 MMAQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  81 DVIDKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGK 160
Cdd:COG0190   80 ALIDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 161 NAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNP---GNI 237
Cdd:COG0190  160 HAVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRvedGKL 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 463284648 238 -GDIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKEH 278
Cdd:COG0190  240 vGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQ 281
PRK14192 PRK14192
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 1-277 2.86e-135

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184561 [Multi-domain]  Cd Length: 283  Bit Score: 383.81  E-value: 2.86e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   1 MNPVLLDGKKLSEKIKEEIRSAIEERKTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELL 80
Cdd:PRK14192   1 MMALVLDGKALAKQIEEELSVRVEALKAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  81 DVIDKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGK 160
Cdd:PRK14192  81 AKIEELNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 161 NAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNP---GNI 237
Cdd:PRK14192 161 HAVVVGRSAILGKPMAMMLLNANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFHPrdgGGV 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 463284648 238 GDIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKE 277
Cdd:PRK14192 241 GDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEK 280
PRK10792 PRK10792
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 1-278 1.60e-112

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 236760 [Multi-domain]  Cd Length: 285  Bit Score: 326.10  E-value: 1.60e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   1 MNPVLLDGKKLSEKIKEEIRSAIEERKTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELL 80
Cdd:PRK10792   1 MTAKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  81 DVIDKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGK 160
Cdd:PRK10792  81 ALIDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 161 NAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYN---PGNI 237
Cdd:PRK10792 161 NAVVVGASNIVGRPMSLELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINrleDGKL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 463284648 238 -GDIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKEH 278
Cdd:PRK10792 241 vGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEEY 282
PRK14190 PRK14190
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 1-277 3.54e-112

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 184560 [Multi-domain]  Cd Length: 284  Bit Score: 325.04  E-value: 3.54e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   1 MNPVLLDGKKLSEKIKEEIRSAIEERKTKNFrIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELL 80
Cdd:PRK14190   1 MMAVIIDGKEVAKEKREQLKEEVVKLKEQGI-VPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  81 DVIDKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGK 160
Cdd:PRK14190  80 ALIDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 161 NAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNPGN---- 236
Cdd:PRK14190 160 HVVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRLEngkl 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 463284648 237 IGDIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKE 277
Cdd:PRK14190 240 CGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKR 280
PRK14191 PRK14191
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 4-276 1.16e-110

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172679 [Multi-domain]  Cd Length: 285  Bit Score: 321.33  E-value: 1.16e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   4 VLLDGKKLSEKIKEEIRSAIEERKTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVI 83
Cdd:PRK14191   2 VLLDGKALSYKIEKDLKNKIQILTAQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  84 DKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGKNAV 163
Cdd:PRK14191  82 KDLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 164 VVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNPGN----IGD 239
Cdd:PRK14191 162 IIGASNIVGKPLAMLMLNAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLNdgrlVGD 241

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 463284648 240 IEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAK 276
Cdd:PRK14191 242 VDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAE 278
PRK14186 PRK14186
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 5-279 3.65e-104

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237636 [Multi-domain]  Cd Length: 297  Bit Score: 305.06  E-value: 3.65e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   5 LLDGKKLSEKIKEEIRSAIEERKTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVID 84
Cdd:PRK14186   4 ILDGKALAAEIEQRLQAQIESNLPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEALIA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  85 KLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGKNAVV 164
Cdd:PRK14186  84 QLNQDERVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKKAVV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 165 VGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYN--------PGN 236
Cdd:PRK14186 164 VGRSILVGKPLALMLLAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHrlpssdgkTRL 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 463284648 237 IGDIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKEHF 279
Cdd:PRK14186 244 CGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSWQKRH 286
PRK14188 PRK14188
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 5-276 1.20e-103

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184558 [Multi-domain]  Cd Length: 296  Bit Score: 303.80  E-value: 1.20e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   5 LLDGKKLSEKIKEEIRSAIEERKTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVID 84
Cdd:PRK14188   4 IIDGKAFAADVRATVAAEVARLKAAHGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLALIA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  85 KLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGKNAVV 164
Cdd:PRK14188  84 RLNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLNAVV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 165 VGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYN--------PGN 236
Cdd:PRK14188 164 IGRSNLVGKPMAQLLLAANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINripapekgEGK 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 463284648 237 ---IGDIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAK 276
Cdd:PRK14188 244 trlVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAAC 286
PRK14189 PRK14189
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
1-275 8.08e-101

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 184559 [Multi-domain]  Cd Length: 285  Bit Score: 296.21  E-value: 8.08e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   1 MNPVLLDGKKLSEKIKEEIR---SAIEERKTKnfriPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTK 77
Cdd:PRK14189   1 MTAQLIDGNALSKQLRAEAAqraAALTARGHQ----PGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  78 ELLDVIDKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDV 157
Cdd:PRK14189  77 ELLARIDELNRDPKIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 158 AGKNAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNPGN- 236
Cdd:PRK14189 157 RGAHAVVIGRSNIVGKPMAMLLLQAGATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMNRDDa 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 463284648 237 ---IGDIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSA 275
Cdd:PRK14189 237 gklCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAA 278
PRK14184 PRK14184
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 5-278 2.58e-98

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 237635 [Multi-domain]  Cd Length: 286  Bit Score: 290.14  E-value: 2.58e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   5 LLDGKKLSEKIKEEIRSAIEERKTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVID 84
Cdd:PRK14184   3 LLDGKATAATIREELKTEVAALTARHGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLIA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  85 KLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGKNAVV 164
Cdd:PRK14184  83 ELNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAVV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 165 VGRSPILGKPMAMLLTEM----NATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYN---PGNI 237
Cdd:PRK14184 163 VGRSNIVGKPLALMLGAPgkfaNATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINrtdDGLV 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 463284648 238 GDIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKEH 278
Cdd:PRK14184 243 GDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQSWKER 283
PRK14172 PRK14172
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 5-269 2.65e-92

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 172660 [Multi-domain]  Cd Length: 278  Bit Score: 274.35  E-value: 2.65e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   5 LLDGKKLSEKIKEEIRSAIEERKTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVID 84
Cdd:PRK14172   4 IINGKEVALKIKEEIKNFVEERKENGLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEIE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  85 KLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGKNAVV 164
Cdd:PRK14172  84 ELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVVV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 165 VGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNPGN---IGDIE 241
Cdd:PRK14172 164 IGRSNIVGKPVAQLLLNENATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSVNgkiTGDVN 243

                        250       260
                 ....*....|....*....|....*...
gi 463284648 242 ISKAKDRSSFYTPVPGGVGPMTIAVLLL 269
Cdd:PRK14172 244 FDKVIDKASYITPVPGGVGSLTTTLLIK 271
PRK14174 PRK14174
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 4-274 1.13e-91

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 172662 [Multi-domain]  Cd Length: 295  Bit Score: 273.62  E-value: 1.13e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   4 VLLDGKKLSEKIKEEIRSAIEERKTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVI 83
Cdd:PRK14174   2 LIIDGKKVSLDLKNELKTRVEAYRAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  84 DKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGV--ETYLPCTPYGMVLLLKEYGIDVAGKN 161
Cdd:PRK14174  82 EDLNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGHldKCFVSCTPYGILELLGRYNIETKGKH 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 162 AVVVGRSPILGKPMAML----LTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYN---- 233
Cdd:PRK14174 162 CVVVGRSNIVGKPMANLmlqkLKESNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINried 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 463284648 234 PGN------IGDIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYS 274
Cdd:PRK14174 242 PSTksgyrlVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTLQS 288
PRK14179 PRK14179
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
5-276 6.58e-91

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 237634 [Multi-domain]  Cd Length: 284  Bit Score: 271.24  E-value: 6.58e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   5 LLDGKKLSEKIKEEIRSAIEERKTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVID 84
Cdd:PRK14179   4 IIDGKALAQKMQAELAEKVAKLKEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDLIE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  85 KLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGKNAVV 164
Cdd:PRK14179  84 RYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHAVV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 165 VGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNPGN----IGDI 240
Cdd:PRK14179 164 IGRSNIVGKPMAQLLLDKNATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMNRDEngklIGDV 243

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 463284648 241 EISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAK 276
Cdd:PRK14179 244 DFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAAL 279
PRK14176 PRK14176
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 2-277 1.06e-90

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 184553 [Multi-domain]  Cd Length: 287  Bit Score: 270.52  E-value: 1.06e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   2 NPVLLDGKKLSEKIKEEIRSAIEERKTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLD 81
Cdd:PRK14176   7 ESRIIDGKALAKKIEAEVRSGVERLKSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  82 VIDKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGKN 161
Cdd:PRK14176  87 LIDSLNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGKN 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 162 AVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNP---GNIG 238
Cdd:PRK14176 167 AVIVGHSNVVGKPMAAMLLNRNATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITKeedKVYG 246

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 463284648 239 DIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKE 277
Cdd:PRK14176 247 DVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEK 285
PRK14178 PRK14178
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 4-276 3.50e-90

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172666 [Multi-domain]  Cd Length: 279  Bit Score: 269.02  E-value: 3.50e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   4 VLLDGKKLSEKIKEEIRSAIEERKTKnfriPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVI 83
Cdd:PRK14178   1 MILDGKAVSEKRLELLKEEIIESGLY----PRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  84 DKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGKNAV 163
Cdd:PRK14178  77 RRLNEDPDINGILVQLPLPKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 164 VVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNPGN---IGDI 240
Cdd:PRK14178 157 VVGRSIDVGRPMAALLLNADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQVNgklCGDV 236

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 463284648 241 EISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAK 276
Cdd:PRK14178 237 DFDAVKEIAGAITPVPGGVGPMTIATLMENTFDAAK 272
PRK14166 PRK14166
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 5-276 6.82e-90

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 172654 [Multi-domain]  Cd Length: 282  Bit Score: 268.43  E-value: 6.82e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   5 LLDGKKLSEKIKEEIRSAIEERKTKNFRiPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVID 84
Cdd:PRK14166   3 LLDGKALSAKIKEELKEKNQFLKSKGIE-SCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALIN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  85 KLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVET-YLPCTPYGMVLLLKEYGIDVAGKNAV 163
Cdd:PRK14166  82 TLNHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGLESgFLPCTPLGVMKLLKAYEIDLEGKDAV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 164 VVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYN---PGNI-GD 239
Cdd:PRK14166 162 IIGASNIVGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINrleSGKIvGD 241

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 463284648 240 IEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAK 276
Cdd:PRK14166 242 VDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAK 278
PRK14169 PRK14169
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 5-277 9.13e-89

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184550 [Multi-domain]  Cd Length: 282  Bit Score: 265.66  E-value: 9.13e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   5 LLDGKKLSEKIKEEIRSAIEERKTKNFrIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVID 84
Cdd:PRK14169   3 RLDGRAVSKKILADLKQTVAKLAQQDV-TPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAKVA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  85 KLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGKNAVV 164
Cdd:PRK14169  82 ELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRVVI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 165 VGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNPGN----IGDI 240
Cdd:PRK14169 162 VGRSNIVGRPLAGLMVNHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRGAdgklLGDV 241

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 463284648 241 EISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKE 277
Cdd:PRK14169 242 DEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKR 278
PRK14193 PRK14193
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 1-268 4.49e-88

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 237637 [Multi-domain]  Cd Length: 284  Bit Score: 263.80  E-value: 4.49e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   1 MNPVLLDGKKLSEKIKEEIRSAIEERKTKNfRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELL 80
Cdd:PRK14193   1 MTAIILDGKATADEIKADLAERVAALKEKG-ITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  81 DVIDKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGK 160
Cdd:PRK14193  80 AVIDELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 161 NAVVVGRSPILGKPMAMLLT--EMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNPGN-- 236
Cdd:PRK14193 160 HVVVIGRGVTVGRPIGLLLTrrSENATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSRAGdg 239

                        250       260       270
                 ....*....|....*....|....*....|....
gi 463284648 237 --IGDIEiSKAKDRSSFYTPVPGGVGPMTIAVLL 268
Cdd:PRK14193 240 klVGDVH-PDVWEVAGAVSPNPGGVGPMTRAFLL 272
PLN02616 PLN02616
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
 4-276 4.55e-87

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 215332 [Multi-domain]  Cd Length: 364  Bit Score: 264.17  E-value: 4.55e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   4 VLLDGKKLSEKIKEEIRSAIEERKTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVI 83
Cdd:PLN02616  74 KVIDGKAVAKKIRDEITIEVSRMKESIGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKFI 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  84 DKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSM-GVET-YLPCTPYGMVLLLKEYGIDVAGKN 161
Cdd:PLN02616 154 SGFNNDPSVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMrGREPlFVPCTPKGCIELLHRYNVEIKGKR 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 162 AVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNPGN----- 236
Cdd:PLN02616 234 AVVIGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPVEdassp 313

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 463284648 237 -----IGDIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAK 276
Cdd:PLN02616 314 rgyrlVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAK 358
PRK14183 PRK14183
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 5-278 1.75e-86

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 184555 [Multi-domain]  Cd Length: 281  Bit Score: 259.76  E-value: 1.75e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   5 LLDGKKLSEKIKEEIRSAIEERKTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVID 84
Cdd:PRK14183   3 ILDGKALSDKIKENVKKEVDELKLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETIA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  85 KLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGKNAVV 164
Cdd:PRK14183  83 MMNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVCV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 165 VGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNPGN----IGDI 240
Cdd:PRK14183 163 VGASNIVGKPMAALLLNANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINRTEdgrlVGDV 242

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 463284648 241 EISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKEH 278
Cdd:PRK14183 243 DFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKNR 280
PRK14167 PRK14167
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 5-277 5.39e-86

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 184549 [Multi-domain]  Cd Length: 297  Bit Score: 258.94  E-value: 5.39e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   5 LLDGKKLSEKIKEEIRSAIEERKTKNFRiPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVID 84
Cdd:PRK14167   4 IIDGNAVAAQIRDDLTDAIETLEDAGVT-PGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  85 KLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGKNAVV 164
Cdd:PRK14167  83 ELNADEDVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADVVV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 165 VGRSPILGKPMAMLLTEM----NATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNPGN---- 236
Cdd:PRK14167 163 VGRSDIVGKPMANLLIQKadggNATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINRVDadte 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 463284648 237 -----IGDIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKE 277
Cdd:PRK14167 243 kgyelVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAASL 288
PRK14173 PRK14173
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 1-275 8.28e-83

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 184551 [Multi-domain]  Cd Length: 287  Bit Score: 250.52  E-value: 8.28e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   1 MNPVLLDGKKLSEKIKEEIRSAIEerkTKNFRiPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELL 80
Cdd:PRK14173   1 MAARELSGPPAAEAVYAELRARLA---KLPFV-PHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  81 DVIDKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGK 160
Cdd:PRK14173  77 ELIARLNADPEVDGILVQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 161 NAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYN--PGN-- 236
Cdd:PRK14173 157 EVVVVGRSNIVGKPLAALLLREDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINrvGGNgg 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 463284648 237 ----IGDIEISKAkDRSSFYTPVPGGVGPMTIAVLLLQTLYSA 275
Cdd:PRK14173 237 rdilTGDVHPEVA-EVAGALTPVPGGVGPMTVAMLMANTVIAA 278
PRK14175 PRK14175
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 1-276 1.12e-82

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184552 [Multi-domain]  Cd Length: 286  Bit Score: 250.22  E-value: 1.12e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   1 MNPVLLDGKKLSEKIKEEIRSAIEERKTKNFrIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELL 80
Cdd:PRK14175   1 MVAKILDGKQIAKDYRQGLQDQVEALKEKGF-TPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  81 DVIDKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGK 160
Cdd:PRK14175  80 NELNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 161 NAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNP---GNI 237
Cdd:PRK14175 160 NAVVIGRSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVGNTPdenGKL 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 463284648 238 -GDIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAK 276
Cdd:PRK14175 240 kGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEK 279
PLN02516 PLN02516
methylenetetrahydrofolate dehydrogenase (NADP+)
 5-279 1.93e-82

methylenetetrahydrofolate dehydrogenase (NADP+)


Pssm-ID: 178131 [Multi-domain]  Cd Length: 299  Bit Score: 250.19  E-value: 1.93e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   5 LLDGKKLSEKIKEEIRSAIEERKTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVID 84
Cdd:PLN02516  11 IIDGKAIAKAIRSEIAEEVAQLSEKHGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISKVH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  85 KLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSM-GVE-TYLPCTPYGMVLLLKEYGIDVAGKNA 162
Cdd:PLN02516  91 ELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMkGREpLFLPCTPKGCLELLSRSGIPIKGKKA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 163 VVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNPGN------ 236
Cdd:PLN02516 171 VVVGRSNIVGLPVSLLLLKADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVSdpskks 250

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 463284648 237 ----IGDIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKEHF 279
Cdd:PLN02516 251 gyrlVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKRVF 297
PRK14185 PRK14185
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 5-277 4.40e-82

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184556 [Multi-domain]  Cd Length: 293  Bit Score: 248.98  E-value: 4.40e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   5 LLDGKKLSEKIKEEIRSAIEERKTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVID 84
Cdd:PRK14185   3 LIDGKAISAQIKQEIAAEVAEIVAKGGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKVR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  85 KLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGKNAVV 164
Cdd:PRK14185  83 ELNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCVV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 165 VGRSPILGKPMAMLLTEM----NATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYN--PGNI- 237
Cdd:PRK14185 163 LGRSNIVGKPMAQLMMQKaypgDCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTrvPDATr 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 463284648 238 -------GDIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKE 277
Cdd:PRK14185 243 ksgfkltGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKK 289
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
124-279 3.09e-81

Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;


Pssm-ID: 427036  Cd Length: 160  Bit Score: 241.99  E-value: 3.09e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  124 TTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGKNAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNA 203
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITREA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  204 DIIIGAVGKPEFIKADWISNGAILLDAGYNPGN----IGDIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKEHF 279
Cdd:pfam02882  81 DIVVVAVGKPELIKADWIKPGAVVIDVGINRVGngklVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNTVEAAKRQL 160
PRK14194 PRK14194
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 1-276 1.34e-79

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172682 [Multi-domain]  Cd Length: 301  Bit Score: 242.83  E-value: 1.34e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   1 MNPVLLDGKKLSEKIKEEIRSAIEERKTKNFRiPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELL 80
Cdd:PRK14194   2 MSAKLIDGKAAAARVLAQVREDVRTLKAAGIE-PALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  81 DVIDKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGK 160
Cdd:PRK14194  81 ALIAELNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 161 NAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNPGN---- 236
Cdd:PRK14194 161 HAVVIGRSNIVGKPMAALLLQAHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINRIDddgr 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 463284648 237 ---IGDIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAK 276
Cdd:PRK14194 241 srlVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAAR 283
PRK14182 PRK14182
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 5-276 6.83e-78

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 172670 [Multi-domain]  Cd Length: 282  Bit Score: 238.00  E-value: 6.83e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   5 LLDGKKLSEKIKEEIRSAIEERKTKNFRiPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVID 84
Cdd:PRK14182   3 LIDGKQIAAKVKGEVATEVRALAARGVQ-TGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  85 KLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVE-TYLPCTPYGMVLLLKEYGIDVAGKNAV 163
Cdd:PRK14182  82 RLNADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAgVPRPCTPAGVMRMLDEARVDPKGKRAL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 164 VVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNPGN----IGD 239
Cdd:PRK14182 162 VVGRSNIVGKPMAMMLLERHATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLAdgklVGD 241

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 463284648 240 IEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAK 276
Cdd:PRK14182 242 VEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAK 278
PLN02897 PLN02897
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
 4-279 1.86e-76

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 178485 [Multi-domain]  Cd Length: 345  Bit Score: 236.39  E-value: 1.86e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   4 VLLDGKKLSEKIKEEIRSAIEERKTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVI 83
Cdd:PLN02897  57 VVIDGNVIAEEIRTKIASEVRKMKKAVGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILSAL 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  84 DKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSM-GVET-YLPCTPYGMVLLLKEYGIDVAGKN 161
Cdd:PLN02897 137 RKFNEDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMrGREPlFVSCTPKGCVELLIRSGVEIAGKN 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 162 AVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNPGN----- 236
Cdd:PLN02897 217 AVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPVEdssce 296

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 463284648 237 -----IGDIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKEHF 279
Cdd:PLN02897 297 fgyrlVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKRIF 344
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
 117-276 2.80e-76

NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding domain of the Methylene-Tetrahydrofolate Dehydrogenase/cyclohydrolase (m-THF DH/cyclohydrolase) bifunctional enzyme. Tetrahydrofolate is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofucntional DH, as well as bifunctional m-THF m-THF DHm-THF DHDH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains the bifunctional DH/cyclohydrolase. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains.


Pssm-ID: 133448  Cd Length: 168  Bit Score: 229.75  E-value: 2.80e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 117 HKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGKNAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNL 196
Cdd:cd01080    2 EKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKTKNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 197 PDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNPGN-------IGDIEISKAKDRSSFYTPVPGGVGPMTIAVLLL 269
Cdd:cd01080   82 KEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPdksggklVGDVDFESAKEKASAITPVPGGVGPMTVAMLMK 161


                 ....*..
gi 463284648 270 QTLYSAK 276
Cdd:cd01080  162 NTVEAAK 168
PRK14171 PRK14171
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 5-280 3.58e-76

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172659 [Multi-domain]  Cd Length: 288  Bit Score: 233.70  E-value: 3.58e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   5 LLDGKKLSEKIKEEIRSAIEERKTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVID 84
Cdd:PRK14171   4 IIDGKALANEILADLKLEIQELKSQTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKIN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  85 KLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGV-ETYLPCTPYGMVLLLKEYGIDVAGKNAV 163
Cdd:PRK14171  84 ELNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSGIsQGFIPCTALGCLAVIKKYEPNLTGKNVV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 164 VVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYN--PGN--IGD 239
Cdd:PRK14171 164 IIGRSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINriSGNkiIGD 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 463284648 240 IEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKEHFT 280
Cdd:PRK14171 244 VDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKAFKDSLY 284
PRK14187 PRK14187
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 4-275 4.98e-76

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172675 [Multi-domain]  Cd Length: 294  Bit Score: 233.57  E-value: 4.98e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   4 VLLDGKKLSEKIKEEIRSAIEERKTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVI 83
Cdd:PRK14187   3 NIIDGKKIANDITEILATCIDDLKRQHNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  84 DKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMG--VETYLPCTPYGMVLLLKEYGIDVAGKN 161
Cdd:PRK14187  83 NELNNDDSVHGILVQLPVPNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGqkKNCLIPCTPKGCLYLIKTITRNLSGSD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 162 AVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNPGN----- 236
Cdd:PRK14187 163 AVVIGRSNIVGKPMACLLLGENCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSIEeggvk 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 463284648 237 --IGDIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSA 275
Cdd:PRK14187 243 kfVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAA 283
PRK14180 PRK14180
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 4-277 5.72e-76

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 172668 [Multi-domain]  Cd Length: 282  Bit Score: 233.00  E-value: 5.72e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   4 VLLDGKKLSEKIKEEIRSAIEERKTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVI 83
Cdd:PRK14180   2 ILIDGKSLSKDLKERLATQVQEYKHHTAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  84 DKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYL-PCTPYGMVLLLKEYGIDVAGKNA 162
Cdd:PRK14180  82 DQLNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLQLRDKKCLeSCTPKGIMTMLREYGIKTEGAYA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 163 VVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYNPGN---IGD 239
Cdd:PRK14180 162 VVVGASNVVGKPVSQLLLNAKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHVDgkiVGD 241

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 463284648 240 IEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKE 277
Cdd:PRK14180 242 VDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQE 279
PRK14170 PRK14170
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 5-276 1.00e-74

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172658 [Multi-domain]  Cd Length: 284  Bit Score: 229.96  E-value: 1.00e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   5 LLDGKKLSEKIKEEIRSAIEERkTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVID 84
Cdd:PRK14170   4 IIDGKKLAKEIQEKVTREVAEL-VKEGKKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSVVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  85 KLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVAGKNAVV 164
Cdd:PRK14170  83 ELNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRAVV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 165 VGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGY----NPGNIGDI 240
Cdd:PRK14170 163 IGRSNIVGKPVAQLLLNENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMdrdeNNKLCGDV 242

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 463284648 241 EISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAK 276
Cdd:PRK14170 243 DFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAK 278
PRK14168 PRK14168
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 1-278 6.61e-74

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237633 [Multi-domain]  Cd Length: 297  Bit Score: 228.22  E-value: 6.61e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   1 MNPVLLDGKKLSEKIKEEIRSAIEERKTKNFRIPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELL 80
Cdd:PRK14168   1 MSAKIIKGTEIREEILEEIRGEVAELKEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  81 DVIDKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMGVE--TYLPCTPYGMVLLLKEYGIDVA 158
Cdd:PRK14168  81 ALIDKYNNDDSIHGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIGGDevKFLPCTPAGIQEMLVRSGVETS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 159 GKNAVVVGRSPILGKPMAMLLTE----MNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYN- 233
Cdd:PRK14168 161 GAEVVVVGRSNIVGKPIANMMTQkgpgANATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVNr 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 463284648 234 ---------PGNIGDIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKEH 278
Cdd:PRK14168 241 vgtnestgkAILSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAKFH 294
PRK14181 PRK14181
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 4-278 1.03e-72

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172669 [Multi-domain]  Cd Length: 287  Bit Score: 224.74  E-value: 1.03e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   4 VLLDGKKLSEKIKEEIRSAIEERKTKnfriPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVI 83
Cdd:PRK14181   1 MLLKGAPAAEHILATIKENISASSTA----PGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648  84 DKLNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVDGVTTLSFGKLSMG-VETYLPCTPYGMVLLLKEYGIDVAGKNA 162
Cdd:PRK14181  77 HRLNNDPNIHGILVQLPLPKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGeTDGFIPCTPAGIIELLKYYEIPLHGRHV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 163 VVVGRSPILGKPMAMLLTE----MNATVTLCHSKTQNLPDIVRNADIIIGAVGKPEFIKADWISNGAILLDAGYN--PGN 236
Cdd:PRK14181 157 AIVGRSNIVGKPLAALLMQkhpdTNATVTLLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSrvPAA 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 463284648 237 -------IGDIEISKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAKEH 278
Cdd:PRK14181 237 npkgyilVGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNTWESYLRH 285
THF_DHG_CYH pfam00763
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
6-121 6.28e-56

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;


Pssm-ID: 459930 [Multi-domain]  Cd Length: 115  Bit Score: 175.67  E-value: 6.28e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648    6 LDGKKLSEKIKEEIRSAIEERKTKNFRiPKLATILVGNNPASETYVSMKVKACHSVGMGSEMIRLREQTTTKELLDVIDK 85
Cdd:pfam00763   1 IDGKAIAKKIREELKEEVAALKAGGRK-PGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDK 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 463284648   86 LNSDPNVDGILLQHPTPSGIDERAAFDRIALHKDVD 121
Cdd:pfam00763  80 LNADPSVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115
NAD_bind_m-THF_DH_Cyclohyd_like cd05212
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ...
 139-276 1.72e-29

NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NAD(P) binding domains of methylene-tetrahydrofolate dehydrogenase (m-THF DH) and m-THF DH/cyclohydrolase bifunctional enzymes (m-THF DH/cyclohydrolase). M-THF is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, mono-functional DH, as well as bifunctional DH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express a monofunctional DH. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133451  Cd Length: 140  Bit Score: 108.75  E-value: 1.72e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 139 LPCTPYGMVLLLKE-------YGIDVAGKNAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPDIVRNADIIIGAVG 211
Cdd:cd05212    1 GPCTPLFVSPVAKAvkellnkEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 463284648 212 KPEFIKADWISNGAILLDAGYNPgNIGDieisKAKDRSSFYTPVPGGVGPMTIAVLLLQTLYSAK 276
Cdd:cd05212   81 KPEKVPTEWIKPGATVINCSPTK-LSGD----DVKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140
NAD_bind_m-THF_DH cd01079
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ...
 116-278 4.48e-13

NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of methylene-tetrahydrofolate dehydrogenase (m-THF DH). M-THF is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. M-THF DH is a component of an unusual monofunctional enzyme; in eukaryotes, m-THF DH is typically found as part of a multifunctional protein. NADP-dependent m-THF DHs in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofunctional DH, as well as bifunctional DH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains only the monofunctional DHs from S. cerevisiae and certain bacteria. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133447 [Multi-domain]  Cd Length: 197  Bit Score: 66.30  E-value: 4.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 116 LHKDVDGVTTLSFGKLSMGV---------ETYLPCTPYGMVLLLK---------EYGIDVAGKNAVVVGRSPILGKPMAM 177
Cdd:cd01079    1 PHKDVEGLSHKYIFNLYHNIrfldpenrkKSILPCTPLAIVKILEflgiynkilPYGNRLYGKTITIINRSEVVGRPLAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 178 LLTEMNATV---------------------TLCHSKTQNLPDIVRNADIIIGAVGKPEF-IKADWISNGAILLDAGYNpG 235
Cdd:cd01079   81 LLANDGARVysvdingiqvftrgesirhekHHVTDEEAMTLDCLSQSDVVITGVPSPNYkVPTELLKDGAICINFASI-K 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 463284648 236 NIGDieisKAKDRSSFYTPVpggVGPMTIAVLL--LQTLYSAKEH 278
Cdd:cd01079  160 NFEP----SVKEKASIYVPS---IGKVTIAMLLrnLLRLYHNQHH 197
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
149-245 2.00e-04

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 40.90  E-value: 2.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648   149 LLKEYGIDVAGKNAVVVGRSPIlGKPMAMLLTEMNATVTLCHS-------------KTQNLPDIVRNADIIIGAVGKPEF 215
Cdd:smart00997  13 ILRATNVLLAGKNVVVAGYGDV-GKGVAARLRGLGARVIVTEIdpiraleaamdgfEVMKMEEAAKRADIFVTATGNKDV 91

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 463284648   216 IKADWI---SNGAILldagynpGNIG--DIEISKA 245
Cdd:smart00997  92 ITREHFramKDGAIL-------ANAGhfDVEIDVA 119
NAD_bind_amino_acid_DH cd05191
NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH) ...
 141-231 4.47e-04

NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and are found in glutamate, leucine, and phenylalanine DHs (DHs), methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133449 [Multi-domain]  Cd Length: 86  Bit Score: 38.51  E-value: 4.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 141 CTPYGMVLLLKE----YGIDVAGKNAVVVGRSPIlGKPMA-MLLTEMNATVTLCHSktqnlpdivrnaDIIIGAVGKPEF 215
Cdd:cd05191    1 ATAAGAVALLKAagkvTNKSLKGKTVVVLGAGEV-GKGIAkLLADEGGKKVVLCDR------------DILVTATPAGVP 67

                         90
                 ....*....|....*....
gi 463284648 216 IKAD---WISNGAILLDAG 231
Cdd:cd05191   68 VLEEataKINEGAVVIDLA 86
AroE COG0169
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ...
 144-234 5.16e-04

Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439939 [Multi-domain]  Cd Length: 270  Bit Score: 40.89  E-value: 5.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 144 YGMVLLLKEYGIDVAGKNAVVVG------------------------RSPilGKPMAmLLTEMNATVTlchsKTQNLPDI 199
Cdd:COG0169  106 IGFVRALREAGVDLAGKRVLVLGaggaaravaaalaeagaaeitivnRTP--ERAEA-LAARLGVRAV----PLDDLAAA 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 463284648 200 VRNADIII-----GAVGKPEF-IKADWISNGAILLDAGYNP 234
Cdd:COG0169  179 LAGADLVInatplGMAGGDALpLPASLLAPGAVVYDLVYNP 219
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 144-234 5.11e-03

NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133443 [Multi-domain]  Cd Length: 155  Bit Score: 36.87  E-value: 5.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 463284648 144 YGMVLLLKEYGIDVAGKNAVVVG-----RSPILGkpmamLLTEMNATVTLC---HSKTQ----------------NLPDI 199
Cdd:cd01065    4 LGFVRALEEAGIELKGKKVLILGaggaaRAVAYA-----LAELGAAKIVIVnrtLEKAKalaerfgelgiaiaylDLEEL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 463284648 200 VRNADIIIGAV------GKPEFIKADWISNGAILLDAGYNP 234
Cdd:cd01065   79 LAEADLIINTTpvgmkpGDELPLPPSLLKPGGVVYDVVYNP 119
 
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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