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Conserved domains on  [gi|62243412|ref|NP_001004346|]
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bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial isoform 1 [Homo sapiens]

Protein Classification

bifunctional 5,10-methylenetetrahydrofolate dehydrogenase/5,10-methenyltetrahydrofolate cyclohydrolase( domain architecture ID 11415140)

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
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
2-286 1.49e-140

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


:

Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 397.08  E-value: 1.49e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   2 AKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPR 81
Cdd:COG0190  12 AAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLALIDELNADPS 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  82 VSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNV 161
Cdd:COG0190  91 VHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHAVVVGRSNIV 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412 162 GMPIAMLLhtdgeHERpggDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDpvtg 241
Cdd:COG0190 171 GKPLALLL-----LRR---NATVTVCHSRTK--DLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVED---- 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 62243412 242 kTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 286
Cdd:COG0190 237 -GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280
 
Name Accession Description Interval E-value
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
2-286 1.49e-140

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


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 397.08  E-value: 1.49e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   2 AKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPR 81
Cdd:COG0190  12 AAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLALIDELNADPS 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  82 VSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNV 161
Cdd:COG0190  91 VHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHAVVVGRSNIV 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412 162 GMPIAMLLhtdgeHERpggDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDpvtg 241
Cdd:COG0190 171 GKPLALLL-----LRR---NATVTVCHSRTK--DLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVED---- 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 62243412 242 kTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 286
Cdd:COG0190 237 -GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280
PRK14190 PRK14190
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
24-286 1.59e-117

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


Pssm-ID: 184560 [Multi-domain]  Cd Length: 284  Bit Score: 338.91  E-value: 1.59e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   24 PHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDERTICNG 103
Cdd:PRK14190  33 PGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLALIDRLNADPRINGILVQLPLPKHIDEKAVIER 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  104 IAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTDgeherpggDAT 183
Cdd:PRK14190 113 ISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGKHVVVVGRSNIVGKPVGQLLLNE--------NAT 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  184 VTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDpvtgkTKLVGDVDFEAVKKKAGFITP 263
Cdd:PRK14190 185 VTYCHSKTK--NLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRLEN-----GKLCGDVDFDNVKEKASYITP 257
                        250       260
                 ....*....|....*....|...
gi 62243412  264 VPGGVGPMTVAMLLKNTLLAAKK 286
Cdd:PRK14190 258 VPGGVGPMTITMLMHNTVELAKR 280
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
106-285 6.14e-85

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: 251.71  E-value: 6.14e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412 106 PEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHtdgeherpGGDATVT 185
Cdd:cd01080   1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLL--------NRNATVT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412 186 IAHRYTPKeqLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDPvtGKTKLVGDVDFEAVKKKAGFITPVP 265
Cdd:cd01080  73 VCHSKTKN--LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDK--SGGKLVGDVDFESAKEKASAITPVP 148
                       170       180
                ....*....|....*....|
gi 62243412 266 GGVGPMTVAMLLKNTLLAAK 285
Cdd:cd01080 149 GGVGPMTVAMLMKNTVEAAK 168
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
114-286 4.16e-81

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


Pssm-ID: 427036  Cd Length: 160  Bit Score: 241.60  E-value: 4.16e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   114 HIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTPk 193
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA--------NATVTVCHSKTK- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   194 eQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVhdpvtGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTV 273
Cdd:pfam02882  72 -DLAEITREADIVVVAVGKPELIKADWIKPGAVVIDVGINRV-----GNGKLVGDVDFENVKEKASAITPVPGGVGPMTV 145
                         170
                  ....*....|...
gi 62243412   274 AMLLKNTLLAAKK 286
Cdd:pfam02882 146 AMLLQNTVEAAKR 158
 
Name Accession Description Interval E-value
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
2-286 1.49e-140

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


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 397.08  E-value: 1.49e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   2 AKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPR 81
Cdd:COG0190  12 AAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLALIDELNADPS 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  82 VSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNV 161
Cdd:COG0190  91 VHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHAVVVGRSNIV 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412 162 GMPIAMLLhtdgeHERpggDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDpvtg 241
Cdd:COG0190 171 GKPLALLL-----LRR---NATVTVCHSRTK--DLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVED---- 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 62243412 242 kTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 286
Cdd:COG0190 237 -GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280
PRK14190 PRK14190
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
24-286 1.59e-117

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


Pssm-ID: 184560 [Multi-domain]  Cd Length: 284  Bit Score: 338.91  E-value: 1.59e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   24 PHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDERTICNG 103
Cdd:PRK14190  33 PGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLALIDRLNADPRINGILVQLPLPKHIDEKAVIER 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  104 IAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTDgeherpggDAT 183
Cdd:PRK14190 113 ISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGKHVVVVGRSNIVGKPVGQLLLNE--------NAT 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  184 VTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDpvtgkTKLVGDVDFEAVKKKAGFITP 263
Cdd:PRK14190 185 VTYCHSKTK--NLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRLEN-----GKLCGDVDFDNVKEKASYITP 257
                        250       260
                 ....*....|....*....|...
gi 62243412  264 VPGGVGPMTVAMLLKNTLLAAKK 286
Cdd:PRK14190 258 VPGGVGPMTITMLMHNTVELAKR 280
PRK10792 PRK10792
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
2-286 2.82e-106

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 236760 [Multi-domain]  Cd Length: 285  Bit Score: 310.31  E-value: 2.82e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    2 AKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPR 81
Cdd:PRK10792  12 AQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELLALIDELNADPT 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   82 VSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNV 161
Cdd:PRK10792  92 IDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGLNAVVVGASNIV 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  162 GMPIAMLLHTDGeherpggdATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDpvtg 241
Cdd:PRK10792 172 GRPMSLELLLAG--------CTVTVCHRFTK--NLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLED---- 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 62243412  242 kTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 286
Cdd:PRK10792 238 -GKLVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEE 281
PRK14186 PRK14186
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-286 4.85e-104

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237636 [Multi-domain]  Cd Length: 297  Bit Score: 305.06  E-value: 4.85e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    1 MAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14186  10 LAAEIEQRLQAQIESNLPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEALIAQLNQDE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14186  90 RVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKKAVVVGRSIL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  161 VGMPIAMLLHTdgeherpgGDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDPvT 240
Cdd:PRK14186 170 VGKPLALMLLA--------ANATVTIAHSRTQ--DLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHRLPSS-D 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 62243412  241 GKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 286
Cdd:PRK14186 239 GKTRLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSWQK 284
PRK14189 PRK14189
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
1-286 7.62e-98

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 184559 [Multi-domain]  Cd Length: 285  Bit Score: 288.89  E-value: 7.62e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    1 MAKHIQKEIQRGVESWVSLGNRrPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14189  11 LSKQLRAEAAQRAAALTARGHQ-PGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLARIDELNRDP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14189  90 KIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGAHAVVIGRSNI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  161 VGMPIAMLLHTDGeherpggdATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDpvt 240
Cdd:PRK14189 170 VGKPMAMLLLQAG--------ATVTICHSKTR--DLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMNRDDA--- 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 62243412  241 gkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 286
Cdd:PRK14189 237 --GKLCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAER 280
PRK14188 PRK14188
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
2-287 1.31e-97

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184558 [Multi-domain]  Cd Length: 296  Bit Score: 288.78  E-value: 1.31e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    2 AKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPR 81
Cdd:PRK14188  11 AADVRATVAAEVARLKAAHGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLALIARLNADPA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   82 VSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNV 161
Cdd:PRK14188  91 IHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLNAVVIGRSNLV 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  162 GMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDP--V 239
Cdd:PRK14188 171 GKPMAQLLLAA--------NATVTIAHSRT--RDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIPAPekG 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 62243412  240 TGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKI 287
Cdd:PRK14188 241 EGKTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACRA 288
PRK14191 PRK14191
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
5-286 3.74e-97

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172679 [Multi-domain]  Cd Length: 285  Bit Score: 287.05  E-value: 3.74e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    5 IQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSG 84
Cdd:PRK14191  13 IEKDLKNKIQILTAQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLIKDLNTDQNIDG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   85 ILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMP 164
Cdd:PRK14191  93 ILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVVIIGASNIVGKP 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  165 IAMLLHTDGeherpggdATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDpvtgkTK 244
Cdd:PRK14191 173 LAMLMLNAG--------ASVSVCHILT--KDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLND-----GR 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 62243412  245 LVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 286
Cdd:PRK14191 238 LVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEK 279
PRK14176 PRK14176
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
1-288 2.15e-91

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


Pssm-ID: 184553 [Multi-domain]  Cd Length: 287  Bit Score: 272.83  E-value: 2.15e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    1 MAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14176  16 LAKKIEAEVRSGVERLKSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELIDSLNKRK 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14176  96 DVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGKNAVIVGHSNV 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  161 VGMPIA-MLLHTdgeherpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDpv 239
Cdd:PRK14176 176 VGKPMAaMLLNR---------NATVSVCHVFT--DDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITKEED-- 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 62243412  240 tgktKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKII 288
Cdd:PRK14176 243 ----KVYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEKSL 287
PRK14184 PRK14184
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
2-286 1.16e-89

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


Pssm-ID: 237635 [Multi-domain]  Cd Length: 286  Bit Score: 268.18  E-value: 1.16e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    2 AKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPR 81
Cdd:PRK14184  10 AATIREELKTEVAALTARHGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLIAELNARPD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   82 VSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNV 161
Cdd:PRK14184  90 IDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAVVVGRSNIV 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  162 GMPIAMLLHTDGeherPGGDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDpvtg 241
Cdd:PRK14184 170 GKPLALMLGAPG----KFANATVTVCHSRTP--DLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRTDD---- 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 62243412  242 ktKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 286
Cdd:PRK14184 240 --GLVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQSWKE 282
PRK14179 PRK14179
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
1-286 3.42e-89

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 237634 [Multi-domain]  Cd Length: 284  Bit Score: 267.00  E-value: 3.42e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    1 MAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14179  10 LAQKMQAELAEKVAKLKEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDLIERYNQDP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14179  90 TWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHAVVIGRSNI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  161 VGMPIAMLLHTDgeherpggDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDpvt 240
Cdd:PRK14179 170 VGKPMAQLLLDK--------NATVTLTHSRTR--NLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMNRDEN--- 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 62243412  241 gkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 286
Cdd:PRK14179 237 --GKLIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALR 280
PRK14185 PRK14185
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-289 5.75e-89

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184556 [Multi-domain]  Cd Length: 293  Bit Score: 266.69  E-value: 5.75e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    1 MAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14185   9 ISAQIKQEIAAEVAEIVAKGGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKVRELNQDD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14185  89 DVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCVVLGRSNI 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  161 VGMPIAMLLHTDGEherpGGDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDPVT 240
Cdd:PRK14185 169 VGKPMAQLMMQKAY----PGDCTVTVCHSRSK--NLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTRVPDATR 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 62243412  241 GKT-KLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKIIY 289
Cdd:PRK14185 243 KSGfKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKKAIY 292
PRK14174 PRK14174
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
5-281 3.86e-87

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


Pssm-ID: 172662 [Multi-domain]  Cd Length: 295  Bit Score: 262.06  E-value: 3.86e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    5 IQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSG 84
Cdd:PRK14174  13 LKNELKTRVEAYRAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKIEDLNNDPDVHG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   85 ILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQ--HSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVG 162
Cdd:PRK14174  93 ILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGHldKCFVSCTPYGILELLGRYNIETKGKHCVVVGRSNIVG 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  163 MPIAMLLHtdgeHERPGGDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDPVTGK 242
Cdd:PRK14174 173 KPMANLML----QKLKESNCTVTICHSATK--DIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRIEDPSTKS 246
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 62243412  243 -TKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTL 281
Cdd:PRK14174 247 gYRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTL 286
PLN02516 PLN02516
methylenetetrahydrofolate dehydrogenase (NADP+)
1-288 1.38e-86

methylenetetrahydrofolate dehydrogenase (NADP+)


Pssm-ID: 178131 [Multi-domain]  Cd Length: 299  Bit Score: 260.98  E-value: 1.38e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    1 MAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PLN02516  17 IAKAIRSEIAEEVAQLSEKHGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISKVHELNANP 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLD--QHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRS 158
Cdd:PLN02516  97 DVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMKgrEPLFLPCTPKGCLELLSRSGIPIKGKKAVVVGRS 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  159 KNVGMPIAMLLHTdgeherpgGDATVTIAHRYTPKEQLKIHTqlADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDP 238
Cdd:PLN02516 177 NIVGLPVSLLLLK--------ADATVTVVHSRTPDPESIVRE--ADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVSDP 246
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 62243412  239 vTGKT--KLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKII 288
Cdd:PLN02516 247 -SKKSgyRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKRVF 297
PRK14167 PRK14167
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
1-284 1.57e-86

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


Pssm-ID: 184549 [Multi-domain]  Cd Length: 297  Bit Score: 260.48  E-value: 1.57e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    1 MAKHIQKEIQRGVESWVSLGNRrPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14167  10 VAAQIRDDLTDAIETLEDAGVT-PGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTIDELNADE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14167  89 DVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADVVVVGRSDI 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  161 VGMPIAMLLHTDGeherPGGDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDPVT 240
Cdd:PRK14167 169 VGKPMANLLIQKA----DGGNATVTVCHSRT--DDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINRVDADTE 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 62243412  241 GKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAA 284
Cdd:PRK14167 243 KGYELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAA 286
PRK14183 PRK14183
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
1-285 3.46e-85

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


Pssm-ID: 184555 [Multi-domain]  Cd Length: 281  Bit Score: 256.68  E-value: 3.46e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    1 MAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14183   9 LSDKIKENVKKEVDELKLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETIAMMNNNP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14183  89 NIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVCVVGASNI 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  161 VGMPIAMLLHTDGeherpggdATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDpvt 240
Cdd:PRK14183 169 VGKPMAALLLNAN--------ATVDICHIFT--KDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINRTED--- 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 62243412  241 gkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAK 285
Cdd:PRK14183 236 --GRLVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAK 278
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
106-285 6.14e-85

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: 251.71  E-value: 6.14e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412 106 PEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHtdgeherpGGDATVT 185
Cdd:cd01080   1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLL--------NRNATVT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412 186 IAHRYTPKeqLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDPvtGKTKLVGDVDFEAVKKKAGFITPVP 265
Cdd:cd01080  73 VCHSKTKN--LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDK--SGGKLVGDVDFESAKEKASAITPVP 148
                       170       180
                ....*....|....*....|
gi 62243412 266 GGVGPMTVAMLLKNTLLAAK 285
Cdd:cd01080 149 GGVGPMTVAMLMKNTVEAAK 168
PRK14173 PRK14173
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
23-284 6.37e-84

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


Pssm-ID: 184551 [Multi-domain]  Cd Length: 287  Bit Score: 253.60  E-value: 6.37e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   23 RPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDERTICN 102
Cdd:PRK14173  29 VPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLELIARLNADPEVDGILVQLPLPPHIDFQRVLE 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  103 GIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHtdgeherpGGDA 182
Cdd:PRK14173 109 AIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGKEVVVVGRSNIVGKPLAALLL--------REDA 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  183 TVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDPvTGKTKLVGDVDFEaVKKKAGFIT 262
Cdd:PRK14173 181 TVTLAHSKTQ--DLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINRVGGN-GGRDILTGDVHPE-VAEVAGALT 256
                        250       260
                 ....*....|....*....|..
gi 62243412  263 PVPGGVGPMTVAMLLKNTLLAA 284
Cdd:PRK14173 257 PVPGGVGPMTVAMLMANTVIAA 278
PRK14168 PRK14168
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
3-285 1.53e-83

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237633 [Multi-domain]  Cd Length: 297  Bit Score: 252.87  E-value: 1.53e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    3 KHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRV 82
Cdd:PRK14168  13 EEILEEIRGEVAELKEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLALIDKYNNDDSI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   83 SGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCL--DQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14168  93 HGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIggDEVKFLPCTPAGIQEMLVRSGVETSGAEVVVVGRSNI 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  161 VGMPIAMLLHTDGeherPGGDATVTIAHryTPKEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYV-HDPV 239
Cdd:PRK14168 173 VGKPIANMMTQKG----PGANATVTIVH--TRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVNRVgTNES 246
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 62243412  240 TGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAK 285
Cdd:PRK14168 247 TGKAILSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAK 292
PRK14193 PRK14193
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
22-286 2.35e-83

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


Pssm-ID: 237637 [Multi-domain]  Cd Length: 284  Bit Score: 251.86  E-value: 2.35e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   22 RRPHLSIILVGDNPASHTYVRNKIRAASAVGICS---ELilkPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDER 98
Cdd:PRK14193  31 ITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSirrDL---PADATQEELNAVIDELNADPACTGYIVQLPLPKHLDEN 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   99 TICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLhtdgehERP 178
Cdd:PRK14193 108 AVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGAHVVVIGRGVTVGRPIGLLL------TRR 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  179 GGDATVTIAHryTPKEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVhdpvtGKTKLVGDVDfEAVKKKA 258
Cdd:PRK14193 182 SENATVTLCH--TGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSRA-----GDGKLVGDVH-PDVWEVA 253
                        250       260
                 ....*....|....*....|....*...
gi 62243412  259 GFITPVPGGVGPMTVAMLLKNTLLAAKK 286
Cdd:PRK14193 254 GAVSPNPGGVGPMTRAFLLTNVVERAER 281
PLN02616 PLN02616
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
1-287 1.04e-82

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 215332 [Multi-domain]  Cd Length: 364  Bit Score: 253.39  E-value: 1.04e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    1 MAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PLN02616  81 VAKKIRDEITIEVSRMKESIGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKFISGFNNDP 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHS--LIPATASAVWEIIKRTGIQTFGKNVVVAGRS 158
Cdd:PLN02616 161 SVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMRGREplFVPCTPKGCIELLHRYNVEIKGKRAVVIGRS 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  159 KNVGMPIAMLLHTDgeherpggDATVTIAHRYT--PKEQlkihTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVH 236
Cdd:PLN02616 241 NIVGMPAALLLQRE--------DATVSIVHSRTknPEEI----TREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPVE 308
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 62243412  237 DPVTGKT-KLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKI 287
Cdd:PLN02616 309 DASSPRGyRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKRI 360
PRK14166 PRK14166
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
24-285 2.03e-81

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


Pssm-ID: 172654 [Multi-domain]  Cd Length: 282  Bit Score: 247.25  E-value: 2.03e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   24 PHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDERTICNG 103
Cdd:PRK14166  31 SCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALINTLNHDDSVHGILVQLPLPDHICKDLILES 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  104 IAPEKDVDGFHIINIGRLCLDQHS-LIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTDGeherpggdA 182
Cdd:PRK14166 111 IISSKDVDGFHPINVGYLNLGLESgFLPCTPLGVMKLLKAYEIDLEGKDAVIIGASNIVGRPMATMLLNAG--------A 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  183 TVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHdpvtgKTKLVGDVDFEAVKKKAGFIT 262
Cdd:PRK14166 183 TVSVCHIKT--KDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLE-----SGKIVGDVDFEEVSKKSSYIT 255
                        250       260
                 ....*....|....*....|...
gi 62243412  263 PVPGGVGPMTVAMLLKNTLLAAK 285
Cdd:PRK14166 256 PVPGGVGPMTIAMLLENTVKSAK 278
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
114-286 4.16e-81

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


Pssm-ID: 427036  Cd Length: 160  Bit Score: 241.60  E-value: 4.16e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   114 HIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTPk 193
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA--------NATVTVCHSKTK- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   194 eQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVhdpvtGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTV 273
Cdd:pfam02882  72 -DLAEITREADIVVVAVGKPELIKADWIKPGAVVIDVGINRV-----GNGKLVGDVDFENVKEKASAITPVPGGVGPMTV 145
                         170
                  ....*....|...
gi 62243412   274 AMLLKNTLLAAKK 286
Cdd:pfam02882 146 AMLLQNTVEAAKR 158
PRK14175 PRK14175
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
3-285 4.23e-81

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184552 [Multi-domain]  Cd Length: 286  Bit Score: 246.37  E-value: 4.23e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    3 KHIQKEIQRGVESWVSLGNRR---PHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMD 79
Cdd:PRK14175   9 KQIAKDYRQGLQDQVEALKEKgftPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLNELNRLNND 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   80 PRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSK 159
Cdd:PRK14175  89 DSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGKNAVVIGRSH 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  160 NVGMPIAMLLHTdgeherpgGDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGinyvhDPV 239
Cdd:PRK14175 169 IVGQPVSKLLLQ--------KNASVTILHSRS--KDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVG-----NTP 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 62243412  240 TGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAK 285
Cdd:PRK14175 234 DENGKLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEK 279
PRK14170 PRK14170
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-287 4.84e-79

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172658 [Multi-domain]  Cd Length: 284  Bit Score: 241.13  E-value: 4.84e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    1 MAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14170  10 LAKEIQEKVTREVAELVKEG-KKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSVVEELNEDK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14170  89 TIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRAVVIGRSNI 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  161 VGMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDpvt 240
Cdd:PRK14170 169 VGKPVAQLLLNE--------NATVTIAHSRT--KDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDRDEN--- 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 62243412  241 gkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKI 287
Cdd:PRK14170 236 --NKLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKRI 280
PRK14187 PRK14187
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
24-284 1.24e-77

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172675 [Multi-domain]  Cd Length: 294  Bit Score: 237.80  E-value: 1.24e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   24 PHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDERTICNG 103
Cdd:PRK14187  33 PCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKINELNNDDSVHGILVQLPVPNHIDKNLIINT 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  104 IAPEKDVDGFHIINIGRLCLDQ--HSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHtdgeherpGGD 181
Cdd:PRK14187 113 IDPEKDVDGFHNENVGRLFTGQkkNCLIPCTPKGCLYLIKTITRNLSGSDAVVIGRSNIVGKPMACLLL--------GEN 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  182 ATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHdpVTGKTKLVGDVDFEAVKKKAGFI 261
Cdd:PRK14187 185 CTVTTVHSAT--RDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSIE--EGGVKKFVGDVDFAEVKKKASAI 260
                        250       260
                 ....*....|....*....|...
gi 62243412  262 TPVPGGVGPMTVAMLLKNTLLAA 284
Cdd:PRK14187 261 TPVPGGVGPMTIAFLMVNTVIAA 283
PLN02897 PLN02897
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
3-287 2.53e-77

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 178485 [Multi-domain]  Cd Length: 345  Bit Score: 238.71  E-value: 2.53e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    3 KHIQKEIQRGVESWV-----SLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLN 77
Cdd:PLN02897  62 NVIAEEIRTKIASEVrkmkkAVG-KVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILSALRKFN 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   78 MDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHS--LIPATASAVWEIIKRTGIQTFGKNVVVA 155
Cdd:PLN02897 141 EDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREplFVSCTPKGCVELLIRSGVEIAGKNAVVI 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  156 GRSKNVGMPIAMLLHtdgEHerpggDATVTIAHRYTpKEQLKIhTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYV 235
Cdd:PLN02897 221 GRSNIVGLPMSLLLQ---RH-----DATVSTVHAFT-KDPEQI-TRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPV 290
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 62243412  236 HDPVTG-KTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKI 287
Cdd:PLN02897 291 EDSSCEfGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKRI 343
PRK14178 PRK14178
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
24-285 2.92e-77

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172666 [Multi-domain]  Cd Length: 279  Bit Score: 236.28  E-value: 2.92e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   24 PHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDERTICNG 103
Cdd:PRK14178  27 PRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIRRLNEDPDINGILVQLPLPKGVDTERVIAA 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  104 IAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTdgeherpgGDAT 183
Cdd:PRK14178 107 ILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAVVVGRSIDVGRPMAALLLN--------ADAT 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  184 VTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDpvtgktKLVGDVDFEAVKKKAGFITP 263
Cdd:PRK14178 179 VTICHSKT--ENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQVNG------KLCGDVDFDAVKEIAGAITP 250
                        250       260
                 ....*....|....*....|..
gi 62243412  264 VPGGVGPMTVAMLLKNTLLAAK 285
Cdd:PRK14178 251 VPGGVGPMTIATLMENTFDAAK 272
PRK14169 PRK14169
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-286 2.11e-76

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184550 [Multi-domain]  Cd Length: 282  Bit Score: 234.45  E-value: 2.11e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    1 MAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14169   9 VSKKILADLKQTVAKLAQQD-VTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAKVAELNHDP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14169  88 DVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRVVIVGRSNI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  161 VGMPIAMLLhtdgeherPGGDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDpvt 240
Cdd:PRK14169 168 VGRPLAGLM--------VNHDATVTIAHSKT--RNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRGAD--- 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 62243412  241 gkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 286
Cdd:PRK14169 235 --GKLLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKR 278
PRK14171 PRK14171
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-289 1.07e-74

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172659 [Multi-domain]  Cd Length: 288  Bit Score: 230.23  E-value: 1.07e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    1 MAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14171  10 LANEILADLKLEIQELKSQTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKINELNLDN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRL--CLDQhSLIPATASAVWEIIKRTGIQTFGKNVVVAGRS 158
Cdd:PRK14171  90 EISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLhsGISQ-GFIPCTALGCLAVIKKYEPNLTGKNVVIIGRS 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  159 KNVGMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVhdp 238
Cdd:PRK14171 169 NIVGKPLSALLLKE--------NCSVTICHSKT--HNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRI--- 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 62243412  239 vtGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKIIY 289
Cdd:PRK14171 236 --SGNKIIGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKAFKDSLY 284
PRK14172 PRK14172
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
1-279 1.27e-74

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


Pssm-ID: 172660 [Multi-domain]  Cd Length: 278  Bit Score: 229.67  E-value: 1.27e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    1 MAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14172  10 VALKIKEEIKNFVEERKENGLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEIEELNKDN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14172  90 NVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVVVIGRSNI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  161 VGMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDpvt 240
Cdd:PRK14172 170 VGKPVAQLLLNE--------NATVTICHSKT--KNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSVNG--- 236
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 62243412  241 gktKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKN 279
Cdd:PRK14172 237 ---KITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKN 272
PRK14194 PRK14194
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
23-285 2.19e-74

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172682 [Multi-domain]  Cd Length: 301  Bit Score: 229.73  E-value: 2.19e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   23 RPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDERTICN 102
Cdd:PRK14194  33 EPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLLALIAELNADPSVNGILLQLPLPAHIDEARVLQ 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  103 GIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTdgeherpgGDA 182
Cdd:PRK14194 113 AINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGKHAVVIGRSNIVGKPMAALLLQ--------AHC 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  183 TVTIAHryTPKEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDpvTGKTKLVGDVDFEAVKKKAGFIT 262
Cdd:PRK14194 185 SVTVVH--SRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINRIDD--DGRSRLVGDVDFDSALPVVSAIT 260
                        250       260
                 ....*....|....*....|...
gi 62243412  263 PVPGGVGPMTVAMLLKNTLLAAK 285
Cdd:PRK14194 261 PVPGGVGPMTIAFLMKNTVTAAR 283
PRK14180 PRK14180
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
24-287 3.07e-74

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


Pssm-ID: 172668 [Multi-domain]  Cd Length: 282  Bit Score: 228.76  E-value: 3.07e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   24 PHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDERTICNG 103
Cdd:PRK14180  32 PKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELIDQLNNDSSVHAILVQLPLPAHINKNNVIYS 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  104 IAPEKDVDGFHIINIGRLCL-DQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTdgeherpgGDA 182
Cdd:PRK14180 112 IKPEKDVDGFHPTNVGRLQLrDKKCLESCTPKGIMTMLREYGIKTEGAYAVVVGASNVVGKPVSQLLLN--------AKA 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  183 TVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVhdpvtgKTKLVGDVDFEAVKKKAGFIT 262
Cdd:PRK14180 184 TVTTCHRFT--TDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHV------DGKIVGDVDFAAVKDKVAAIT 255
                        250       260
                 ....*....|....*....|....*
gi 62243412  263 PVPGGVGPMTVAMLLKNTLLAAKKI 287
Cdd:PRK14180 256 PVPGGVGPMTITELLYNTFQCAQEL 280
PRK14177 PRK14177
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-285 5.77e-73

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172665 [Multi-domain]  Cd Length: 284  Bit Score: 225.62  E-value: 5.77e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    1 MAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14177  11 LSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLGVIDKLNLDP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14177  91 NVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGKNAVVVGRSPI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  161 VGMPIAMLLHTdgeherpgGDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHdpvt 240
Cdd:PRK14177 171 LGKPMAMLLTE--------MNATVTLCHSKT--QNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYNPGN---- 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 62243412  241 gktklVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAK 285
Cdd:PRK14177 237 -----VGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFK 276
PRK14181 PRK14181
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
17-280 2.78e-70

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172669 [Multi-domain]  Cd Length: 287  Bit Score: 218.96  E-value: 2.78e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   17 VSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVD 96
Cdd:PRK14181  20 ISASSTAPGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLIHRLNNDPNIHGILVQLPLPKHLD 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   97 ERTICNGIAPEKDVDGFHIINIGRLCLDQ-HSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHtdgeH 175
Cdd:PRK14181 100 AQAILQAISPDKDVDGLHPVNMGKLLLGEtDGFIPCTPAGIIELLKYYEIPLHGRHVAIVGRSNIVGKPLAALLM----Q 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  176 ERPGGDATVTIAHryTPKEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDPVTGKTKLVGDVDFEAVK 255
Cdd:PRK14181 176 KHPDTNATVTLLH--SQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRVPAANPKGYILVGDVDFNNVV 253
                        250       260
                 ....*....|....*....|....*
gi 62243412  256 KKAGFITPVPGGVGPMTVAMLLKNT 280
Cdd:PRK14181 254 PKCRAITPVPGGVGPMTVAMLMRNT 278
PRK14192 PRK14192
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-288 5.24e-66

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184561 [Multi-domain]  Cd Length: 283  Bit Score: 207.78  E-value: 5.24e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    1 MAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14192  11 LAKQIEEELSVRVEALKAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLAKIEELNANP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14192  91 DVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGKHAVVVGRSAI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  161 VGMPIAMLLHTdgeherpgGDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGInyvHDPVT 240
Cdd:PRK14192 171 LGKPMAMMLLN--------ANATVTICHSRT--QNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGF---HPRDG 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 62243412  241 GKtklVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKII 288
Cdd:PRK14192 238 GG---VGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKAL 282
PRK14182 PRK14182
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
1-286 5.21e-64

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


Pssm-ID: 172670 [Multi-domain]  Cd Length: 282  Bit Score: 202.56  E-value: 5.21e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412    1 MAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14182   9 IAAKVKGEVATEVRALAARG-VQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIARLNADP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412   81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLI-PATASAVWEIIKRTGIQTFGKNVVVAGRSK 159
Cdd:PRK14182  88 AVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGVPrPCTPAGVMRMLDEARVDPKGKRALVVGRSN 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412  160 NVGMPIAMLLhtdgeHERpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDpv 239
Cdd:PRK14182 168 IVGKPMAMML-----LER---HATVTIAHSRT--ADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLAD-- 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 62243412  240 tgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 286
Cdd:PRK14182 236 ---GKLVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKR 279
THF_DHG_CYH pfam00763
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
1-111 1.51e-50

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;


Pssm-ID: 459930 [Multi-domain]  Cd Length: 115  Bit Score: 162.19  E-value: 1.51e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412     1 MAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:pfam00763   6 IAKKIREELKEEVAALKAGG-RKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKLNADP 84
                          90       100       110
                  ....*....|....*....|....*....|.
gi 62243412    81 RVSGILVQLPLPDHVDERTICNGIAPEKDVD 111
Cdd:pfam00763  85 SVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115
NAD_bind_m-THF_DH_Cyclohyd_like cd05212
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ...
129-285 7.23e-23

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: 91.41  E-value: 7.23e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412 129 IPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTDGeherpggdATVTIAHRYTPKEQLKIHTqlADIIIV 208
Cdd:cd05212   8 VSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDG--------ATVYSCDWKTIQLQSKVHD--ADVVVV 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62243412 209 AAGIPKLITSDMVKEGAAVIDVGINYVHDpvtgktklvgdvdfEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAK 285
Cdd:cd05212  78 GSPKPEKVPTEWIKPGATVINCSPTKLSG--------------DDVKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140
NAD_bind_m-THF_DH cd01079
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ...
106-281 3.06e-10

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: 58.59  E-value: 3.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412 106 PEKDVDGFHIINIGRLC-----LD----QHSLIPATASAVWEIIKRTGI---------QTFGKNVVVAGRSKNVGMPIAM 167
Cdd:cd01079   1 PHKDVEGLSHKYIFNLYhnirfLDpenrKKSILPCTPLAIVKILEFLGIynkilpygnRLYGKTITIINRSEVVGRPLAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243412 168 LLHTDGE-------------HERPGGDATVTIAHRYTPKEQLKIhtQLADIIIVAAGIPKL-ITSDMVKEGAAVIDVGin 233
Cdd:cd01079  81 LLANDGArvysvdingiqvfTRGESIRHEKHHVTDEEAMTLDCL--SQSDVVITGVPSPNYkVPTELLKDGAICINFA-- 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 62243412 234 yvhdpvtgktklvGDVDFEA-VKKKAGFITPVpggVGPMTVAMLLKNTL 281
Cdd:cd01079 157 -------------SIKNFEPsVKEKASIYVPS---IGKVTIAMLLRNLL 189
 
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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