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Conserved domains on  [gi|222418558|ref|NP_001138450|]
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bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial isoform 2 [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 ...
51-344 6.76e-145

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


:

Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 410.56  E-value: 6.76e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  51 AIIISGTEMAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDV 130
Cdd:COG0190    3 AQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 131 TDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:COG0190   82 IDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLhtdgEHErpggDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:COG0190  162 VVVGRSNIVGKPLALLL----LRR----NATVTVCHSRTK--DLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGI 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 222418558 291 NYVHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:COG0190  232 NRVED-----GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280
 
Name Accession Description Interval E-value
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
51-344 6.76e-145

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


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 410.56  E-value: 6.76e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  51 AIIISGTEMAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDV 130
Cdd:COG0190    3 AQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 131 TDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:COG0190   82 IDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLhtdgEHErpggDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:COG0190  162 VVVGRSNIVGKPLALLL----LRR----NATVTVCHSRTK--DLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGI 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 222418558 291 NYVHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:COG0190  232 NRVED-----GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280
PRK14190 PRK14190
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
51-344 1.27e-122

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


Pssm-ID: 184560 [Multi-domain]  Cd Length: 284  Bit Score: 354.32  E-value: 1.27e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  51 AIIISGTEMAKHIQKEIQRGVESwvsLGNRR--PHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELL 128
Cdd:PRK14190   3 AVIIDGKEVAKEKREQLKEEVVK---LKEQGivPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 129 DVTDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGK 208
Cdd:PRK14190  80 ALIDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 209 NVVVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDV 288
Cdd:PRK14190 160 HVVVVGRSNIVGKPVGQLLLNE--------NATVTYCHSKTK--NLAELTKQADILIVAVGKPKLITADMVKEGAVVIDV 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 222418558 289 GINYVHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:PRK14190 230 GVNRLEN-----GKLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKR 280
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
164-343 5.35e-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: 254.02  E-value: 5.35e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 164 PEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHtdgeherpGGDATVT 243
Cdd:cd01080    1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLL--------NRNATVT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 244 IAHRYTPKeqLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDPvtGKTKLVGDVDFEAVKKKAGFITPVP 323
Cdd:cd01080   73 VCHSKTKN--LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDK--SGGKLVGDVDFESAKEKASAITPVP 148
                        170       180
                 ....*....|....*....|
gi 222418558 324 GGVGPMTVAMLLKNTLLAAK 343
Cdd:cd01080  149 GGVGPMTVAMLMKNTVEAAK 168
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
172-344 9.11e-81

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


Pssm-ID: 427036  Cd Length: 160  Bit Score: 243.14  E-value: 9.11e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  172 HIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTPk 251
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA--------NATVTVCHSKTK- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  252 eQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVhdpvtGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTV 331
Cdd:pfam02882  72 -DLAEITREADIVVVAVGKPELIKADWIKPGAVVIDVGINRV-----GNGKLVGDVDFENVKEKASAITPVPGGVGPMTV 145
                         170
                  ....*....|...
gi 222418558  332 AMLLKNTLLAAKK 344
Cdd:pfam02882 146 AMLLQNTVEAAKR 158
 
Name Accession Description Interval E-value
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
51-344 6.76e-145

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


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 410.56  E-value: 6.76e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  51 AIIISGTEMAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDV 130
Cdd:COG0190    3 AQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 131 TDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:COG0190   82 IDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLhtdgEHErpggDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:COG0190  162 VVVGRSNIVGKPLALLL----LRR----NATVTVCHSRTK--DLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGI 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 222418558 291 NYVHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:COG0190  232 NRVED-----GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280
PRK14190 PRK14190
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
51-344 1.27e-122

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


Pssm-ID: 184560 [Multi-domain]  Cd Length: 284  Bit Score: 354.32  E-value: 1.27e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  51 AIIISGTEMAKHIQKEIQRGVESwvsLGNRR--PHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELL 128
Cdd:PRK14190   3 AVIIDGKEVAKEKREQLKEEVVK---LKEQGivPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 129 DVTDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGK 208
Cdd:PRK14190  80 ALIDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 209 NVVVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDV 288
Cdd:PRK14190 160 HVVVVGRSNIVGKPVGQLLLNE--------NATVTYCHSKTK--NLAELTKQADILIVAVGKPKLITADMVKEGAVVIDV 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 222418558 289 GINYVHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:PRK14190 230 GVNRLEN-----GKLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKR 280
PRK10792 PRK10792
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
51-344 2.63e-110

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 236760 [Multi-domain]  Cd Length: 285  Bit Score: 323.02  E-value: 2.63e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  51 AIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDV 130
Cdd:PRK10792   3 AKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELLAL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 131 TDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:PRK10792  83 IDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGLNA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLHTDGeherpggdATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK10792 163 VVVGASNIVGRPMSLELLLAG--------CTVTVCHRFTK--NLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGI 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 222418558 291 NYVHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:PRK10792 233 NRLED-----GKLVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEE 281
PRK14186 PRK14186
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
51-344 1.09e-104

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237636 [Multi-domain]  Cd Length: 297  Bit Score: 308.92  E-value: 1.09e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  51 AIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDV 130
Cdd:PRK14186   2 ALILDGKALAAEIEQRLQAQIESNLPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 131 TDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:PRK14186  82 IAQLNQDERVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKKA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLHTdgeherpgGDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14186 162 VVVGRSILVGKPLALMLLA--------ANATVTIAHSRTQ--DLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGI 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 222418558 291 NYVHDPvTGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:PRK14186 232 HRLPSS-DGKTRLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSWQK 284
PRK14191 PRK14191
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
53-344 1.57e-99

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172679 [Multi-domain]  Cd Length: 285  Bit Score: 295.52  E-value: 1.57e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  53 IISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTD 132
Cdd:PRK14191   3 LLDGKALSYKIEKDLKNKIQILTAQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLIK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 133 QLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVV 212
Cdd:PRK14191  83 DLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVVI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 213 AGRSKNVGMPIAMLLHTDGeherpggdATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINY 292
Cdd:PRK14191 163 IGASNIVGKPLAMLMLNAG--------ASVSVCHILT--KDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINR 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 222418558 293 VHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:PRK14191 233 LND-----GRLVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEK 279
PRK14189 PRK14189
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
51-344 2.13e-99

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 184559 [Multi-domain]  Cd Length: 285  Bit Score: 295.06  E-value: 2.13e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  51 AIIISGTEMAKHIQKEIQRGVESWVSLGNRrPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDV 130
Cdd:PRK14189   3 AQLIDGNALSKQLRAEAAQRAAALTARGHQ-PGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 131 TDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:PRK14189  82 IDELNRDPKIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGAHA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLHTDGeherpggdATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14189 162 VVIGRSNIVGKPMAMLLLQAG--------ATVTICHSKTR--DLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGM 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 222418558 291 NYVHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:PRK14189 232 NRDDA-----GKLCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAER 280
PRK14188 PRK14188
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
50-345 1.04e-98

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184558 [Multi-domain]  Cd Length: 296  Bit Score: 293.79  E-value: 1.04e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  50 EAIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLD 129
Cdd:PRK14188   1 MATIIDGKAFAADVRATVAAEVARLKAAHGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 130 VTDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKN 209
Cdd:PRK14188  81 LIARLNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 210 VVVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVG 289
Cdd:PRK14188 161 AVVIGRSNLVGKPMAQLLLAA--------NATVTIAHSRT--RDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVG 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 222418558 290 INYVHDP--VTGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKI 345
Cdd:PRK14188 231 INRIPAPekGEGKTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACRA 288
PRK14176 PRK14176
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
49-346 2.91e-94

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


Pssm-ID: 184553 [Multi-domain]  Cd Length: 287  Bit Score: 282.08  E-value: 2.91e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  49 HEAIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELL 128
Cdd:PRK14176   6 YESRIIDGKALAKKIEAEVRSGVERLKSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 129 DVTDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGK 208
Cdd:PRK14176  86 ELIDSLNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGK 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 209 NVVVAGRSKNVGMPIA-MLLHTdgeherpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVID 287
Cdd:PRK14176 166 NAVIVGHSNVVGKPMAaMLLNR---------NATVSVCHVFT--DDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFD 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 222418558 288 VGINYVHDpvtgktKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKII 346
Cdd:PRK14176 235 VGITKEED------KVYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEKSL 287
PRK14179 PRK14179
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
51-344 7.83e-92

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 237634 [Multi-domain]  Cd Length: 284  Bit Score: 275.86  E-value: 7.83e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  51 AIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDV 130
Cdd:PRK14179   2 TEIIDGKALAQKMQAELAEKVAKLKEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 131 TDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:PRK14179  82 IERYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14179 162 VVIGRSNIVGKPMAQLLLDK--------NATVTLTHSRT--RNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGM 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 222418558 291 NYVHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:PRK14179 232 NRDEN-----GKLIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALR 280
PRK14184 PRK14184
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
52-344 2.15e-90

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


Pssm-ID: 237635 [Multi-domain]  Cd Length: 286  Bit Score: 272.42  E-value: 2.15e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  52 IIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVT 131
Cdd:PRK14184   2 LLLDGKATAATIREELKTEVAALTARHGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 132 DQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVV 211
Cdd:PRK14184  82 AELNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 212 VAGRSKNVGMPIAMLLHTDGeherPGGDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGIN 291
Cdd:PRK14184 162 VVGRSNIVGKPLALMLGAPG----KFANATVTVCHSRTP--DLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGIN 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 222418558 292 YVHDpvtgktKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:PRK14184 236 RTDD------GLVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQSWKE 282
PRK14185 PRK14185
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
53-347 4.77e-90

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184556 [Multi-domain]  Cd Length: 293  Bit Score: 271.70  E-value: 4.77e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  53 IISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTD 132
Cdd:PRK14185   3 LIDGKAISAQIKQEIAAEVAEIVAKGGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKVR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 133 QLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVV 212
Cdd:PRK14185  83 ELNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCVV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 213 AGRSKNVGMPIAMLLHTDGEherpGGDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINY 292
Cdd:PRK14185 163 LGRSNIVGKPMAQLMMQKAY----PGDCTVTVCHSRSK--NLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTR 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 222418558 293 VHDPVTGKT-KLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKIIY 347
Cdd:PRK14185 237 VPDATRKSGfKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKKAIY 292
PRK14174 PRK14174
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
52-339 1.26e-89

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


Pssm-ID: 172662 [Multi-domain]  Cd Length: 295  Bit Score: 270.54  E-value: 1.26e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  52 IIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVT 131
Cdd:PRK14174   2 LIIDGKKVSLDLKNELKTRVEAYRAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 132 DQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQ--HSLIPATASAVWEIIKRTGIQTFGKN 209
Cdd:PRK14174  82 EDLNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGHldKCFVSCTPYGILELLGRYNIETKGKH 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 210 VVVAGRSKNVGMPIAMLLHtdgeHERPGGDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVG 289
Cdd:PRK14174 162 CVVVGRSNIVGKPMANLML----QKLKESNCTVTICHSATK--DIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVG 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 222418558 290 INYVHDPVTGK-TKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTL 339
Cdd:PRK14174 236 INRIEDPSTKSgYRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTL 286
PRK14167 PRK14167
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
53-342 1.96e-89

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


Pssm-ID: 184549 [Multi-domain]  Cd Length: 297  Bit Score: 270.11  E-value: 1.96e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  53 IISGTEMAKHIQKEIQRGVESWVSLGNRrPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTD 132
Cdd:PRK14167   4 IIDGNAVAAQIRDDLTDAIETLEDAGVT-PGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTID 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 133 QLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVV 212
Cdd:PRK14167  83 ELNADEDVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADVVV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 213 AGRSKNVGMPIAMLLHTDGeherPGGDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINY 292
Cdd:PRK14167 163 VGRSDIVGKPMANLLIQKA----DGGNATVTVCHSRT--DDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINR 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 222418558 293 VHDPVTGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAA 342
Cdd:PRK14167 237 VDADTEKGYELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAA 286
PLN02516 PLN02516
methylenetetrahydrofolate dehydrogenase (NADP+)
49-346 3.05e-89

methylenetetrahydrofolate dehydrogenase (NADP+)


Pssm-ID: 178131 [Multi-domain]  Cd Length: 299  Bit Score: 269.84  E-value: 3.05e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  49 HEAIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELL 128
Cdd:PLN02516   7 HVAQIIDGKAIAKAIRSEIAEEVAQLSEKHGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 129 DVTDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLD--QHSLIPATASAVWEIIKRTGIQTF 206
Cdd:PLN02516  87 SKVHELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMKgrEPLFLPCTPKGCLELLSRSGIPIK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 207 GKNVVVAGRSKNVGMPIAMLLHTdgeherpgGDATVTIAHRYTPKEQLKIHTqlADIIIVAAGIPKLITSDMVKEGAAVI 286
Cdd:PLN02516 167 GKKAVVVGRSNIVGLPVSLLLLK--------ADATVTVVHSRTPDPESIVRE--ADIVIAAAGQAMMIKGDWIKPGAAVI 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 222418558 287 DVGINYVHDPvTGKT--KLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKII 346
Cdd:PLN02516 237 DVGTNAVSDP-SKKSgyRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKRVF 297
PRK14183 PRK14183
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
53-343 4.79e-88

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


Pssm-ID: 184555 [Multi-domain]  Cd Length: 281  Bit Score: 266.31  E-value: 4.79e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  53 IISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTD 132
Cdd:PRK14183   3 ILDGKALSDKIKENVKKEVDELKLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETIA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 133 QLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVV 212
Cdd:PRK14183  83 MMNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVCV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 213 AGRSKNVGMPIAMLLHTDGeherpggdATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINY 292
Cdd:PRK14183 163 VGASNIVGKPMAALLLNAN--------ATVDICHIFT--KDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINR 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 222418558 293 VHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAK 343
Cdd:PRK14183 233 TED-----GRLVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAK 278
PRK14168 PRK14168
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
51-343 2.25e-87

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237633 [Multi-domain]  Cd Length: 297  Bit Score: 265.20  E-value: 2.25e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  51 AIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDV 130
Cdd:PRK14168   3 AKIIKGTEIREEILEEIRGEVAELKEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLAL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 131 TDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCL--DQHSLIPATASAVWEIIKRTGIQTFGK 208
Cdd:PRK14168  83 IDKYNNDDSIHGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIggDEVKFLPCTPAGIQEMLVRSGVETSGA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 209 NVVVAGRSKNVGMPIAMLLHTDGeherPGGDATVTIAHryTPKEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDV 288
Cdd:PRK14168 163 EVVVVGRSNIVGKPIANMMTQKG----PGANATVTIVH--TRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDV 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 222418558 289 GINYV-HDPVTGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAK 343
Cdd:PRK14168 237 GVNRVgTNESTGKAILSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAK 292
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
164-343 5.35e-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: 254.02  E-value: 5.35e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 164 PEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHtdgeherpGGDATVT 243
Cdd:cd01080    1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLL--------NRNATVT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 244 IAHRYTPKeqLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDPvtGKTKLVGDVDFEAVKKKAGFITPVP 323
Cdd:cd01080   73 VCHSKTKN--LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDK--SGGKLVGDVDFESAKEKASAITPVP 148
                        170       180
                 ....*....|....*....|
gi 222418558 324 GGVGPMTVAMLLKNTLLAAK 343
Cdd:cd01080  149 GGVGPMTVAMLMKNTVEAAK 168
PLN02616 PLN02616
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
2-345 1.15e-84

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 215332 [Multi-domain]  Cd Length: 364  Bit Score: 260.32  E-value: 1.15e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558   2 TVPVRGFSLLRGRLG----RAPALGRSTapSVRAPGEPGSAFRGfrSSGVRHEAIIISGTEMAKHIQKEIQRGVESWVSL 77
Cdd:PLN02616  24 STPFNGTFLLRRCVGplrvRTTASGRGC--CINSSSSPSPVINA--DTGSEGGAKVIDGKAVAKKIRDEITIEVSRMKES 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  78 GNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDERT 157
Cdd:PLN02616 100 IGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKFISGFNNDPSVHGILVQLPLPSHMDEQN 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 158 ICNGIAPEKDVDGFHIINIGRLCLDQHS--LIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTDgeher 235
Cdd:PLN02616 180 ILNAVSIEKDVDGFHPLNIGRLAMRGREplFVPCTPKGCIELLHRYNVEIKGKRAVVIGRSNIVGMPAALLLQRE----- 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 236 pggDATVTIAHRYT--PKEQlkihTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDPVTGKT-KLVGDVDFEAV 312
Cdd:PLN02616 255 ---DATVSIVHSRTknPEEI----TREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPVEDASSPRGyRLVGDVCYEEA 327
                        330       340       350
                 ....*....|....*....|....*....|...
gi 222418558 313 KKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKI 345
Cdd:PLN02616 328 CKVASAVTPVPGGVGPMTIAMLLSNTLTSAKRI 360
PRK14175 PRK14175
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
51-343 7.01e-84

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184552 [Multi-domain]  Cd Length: 286  Bit Score: 255.61  E-value: 7.01e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  51 AIIISGTEMAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDV 130
Cdd:PRK14175   3 AKILDGKQIAKDYRQGLQDQVEALKEKG-FTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLNE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 131 TDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:PRK14175  82 LNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGKNA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLHTdgeherpgGDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGi 290
Cdd:PRK14175 162 VVIGRSHIVGQPVSKLLLQ--------KNASVTILHSRS--KDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVG- 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 222418558 291 nyvhDPVTGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAK 343
Cdd:PRK14175 231 ----NTPDENGKLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEK 279
PRK14193 PRK14193
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
51-344 8.12e-84

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


Pssm-ID: 237637 [Multi-domain]  Cd Length: 284  Bit Score: 255.32  E-value: 8.12e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  51 AIIISGTEMAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICS---ELilkPKDVSQEEL 127
Cdd:PRK14193   3 AIILDGKATADEIKADLAERVAALKEKG-ITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSirrDL---PADATQEEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 128 LDVTDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFG 207
Cdd:PRK14193  79 NAVIDELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 208 KNVVVAGRSKNVGMPIAMLLhtdgehERPGGDATVTIAHryTPKEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVID 287
Cdd:PRK14193 159 AHVVVIGRGVTVGRPIGLLL------TRRSENATVTLCH--TGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLD 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 222418558 288 VGINYVhdpvtGKTKLVGDVDfEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:PRK14193 231 VGVSRA-----GDGKLVGDVH-PDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAER 281
PRK14166 PRK14166
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
53-343 1.59e-83

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


Pssm-ID: 172654 [Multi-domain]  Cd Length: 282  Bit Score: 254.57  E-value: 1.59e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  53 IISGTEMAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTD 132
Cdd:PRK14166   3 LLDGKALSAKIKEELKEKNQFLKSKG-IESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALIN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 133 QLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHS-LIPATASAVWEIIKRTGIQTFGKNVV 211
Cdd:PRK14166  82 TLNHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGLESgFLPCTPLGVMKLLKAYEIDLEGKDAV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 212 VAGRSKNVGMPIAMLLHTDGeherpggdATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGIN 291
Cdd:PRK14166 162 IIGASNIVGRPMATMLLNAG--------ATVSVCHIKT--KDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGIN 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 222418558 292 YVHdpvtgKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAK 343
Cdd:PRK14166 232 RLE-----SGKIVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAK 278
PRK14173 PRK14173
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
51-342 4.03e-82

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


Pssm-ID: 184551 [Multi-domain]  Cd Length: 287  Bit Score: 251.29  E-value: 4.03e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  51 AIIISGTEMAKHIQKEIQRGVESWVSlgnrRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDV 130
Cdd:PRK14173   3 ARELSGPPAAEAVYAELRARLAKLPF----VPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 131 TDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:PRK14173  79 IARLNADPEVDGILVQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGKEV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLHtdgeherpGGDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14173 159 VVVGRSNIVGKPLAALLL--------REDATVTLAHSKTQ--DLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGI 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 222418558 291 NYVHDPvTGKTKLVGDVDFEaVKKKAGFITPVPGGVGPMTVAMLLKNTLLAA 342
Cdd:PRK14173 229 NRVGGN-GGRDILTGDVHPE-VAEVAGALTPVPGGVGPMTVAMLMANTVIAA 278
PRK14170 PRK14170
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
53-345 1.95e-81

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172658 [Multi-domain]  Cd Length: 284  Bit Score: 249.61  E-value: 1.95e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  53 IISGTEMAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTD 132
Cdd:PRK14170   4 IIDGKKLAKEIQEKVTREVAELVKEG-KKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSVVE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 133 QLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVV 212
Cdd:PRK14170  83 ELNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRAVV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 213 AGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINY 292
Cdd:PRK14170 163 IGRSNIVGKPVAQLLLNE--------NATVTIAHSRT--KDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDR 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 222418558 293 VHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKI 345
Cdd:PRK14170 233 DEN-----NKLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKRI 280
PRK14187 PRK14187
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
50-342 4.91e-81

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172675 [Multi-domain]  Cd Length: 294  Bit Score: 248.59  E-value: 4.91e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  50 EAIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLD 129
Cdd:PRK14187   1 ETNIIDGKKIANDITEILATCIDDLKRQHNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 130 VTDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQ--HSLIPATASAVWEIIKRTGIQTFG 207
Cdd:PRK14187  81 KINELNNDDSVHGILVQLPVPNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQkkNCLIPCTPKGCLYLIKTITRNLSG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 208 KNVVVAGRSKNVGMPIAMLLHtdgeherpGGDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVID 287
Cdd:PRK14187 161 SDAVVIGRSNIVGKPMACLLL--------GENCTVTTVHSAT--RDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVID 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 222418558 288 VGINYVHdpVTGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAA 342
Cdd:PRK14187 231 VGINSIE--EGGVKKFVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAA 283
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
172-344 9.11e-81

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


Pssm-ID: 427036  Cd Length: 160  Bit Score: 243.14  E-value: 9.11e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  172 HIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTPk 251
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA--------NATVTVCHSKTK- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  252 eQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVhdpvtGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTV 331
Cdd:pfam02882  72 -DLAEITREADIVVVAVGKPELIKADWIKPGAVVIDVGINRV-----GNGKLVGDVDFENVKEKASAITPVPGGVGPMTV 145
                         170
                  ....*....|...
gi 222418558  332 AMLLKNTLLAAKK 344
Cdd:pfam02882 146 AMLLQNTVEAAKR 158
PRK14172 PRK14172
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
52-337 1.22e-79

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


Pssm-ID: 172660 [Multi-domain]  Cd Length: 278  Bit Score: 244.69  E-value: 1.22e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  52 IIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVT 131
Cdd:PRK14172   3 QIINGKEVALKIKEEIKNFVEERKENGLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 132 DQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVV 211
Cdd:PRK14172  83 EELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 212 VAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGIN 291
Cdd:PRK14172 163 VIGRSNIVGKPVAQLLLNE--------NATVTICHSKT--KNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTS 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 222418558 292 YVHDpvtgktKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKN 337
Cdd:PRK14172 233 SVNG------KITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKN 272
PRK14171 PRK14171
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
53-347 5.97e-78

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172659 [Multi-domain]  Cd Length: 288  Bit Score: 240.63  E-value: 5.97e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  53 IISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTD 132
Cdd:PRK14171   4 IIDGKALANEILADLKLEIQELKSQTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKIN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 133 QLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRL--CLDQhSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:PRK14171  84 ELNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLhsGISQ-GFIPCTALGCLAVIKKYEPNLTGKNV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14171 163 VIIGRSNIVGKPLSALLLKE--------NCSVTICHSKT--HNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGI 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 222418558 291 NYVhdpvtGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKIIY 347
Cdd:PRK14171 233 NRI-----SGNKIIGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKAFKDSLY 284
PLN02897 PLN02897
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
49-345 2.05e-77

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 178485 [Multi-domain]  Cd Length: 345  Bit Score: 241.02  E-value: 2.05e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  49 HEAIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELL 128
Cdd:PLN02897  54 QKTVVIDGNVIAEEIRTKIASEVRKMKKAVGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQIL 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 129 DVTDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHS--LIPATASAVWEIIKRTGIQTF 206
Cdd:PLN02897 134 SALRKFNEDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREplFVSCTPKGCVELLIRSGVEIA 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 207 GKNVVVAGRSKNVGMPIAMLLHtdgEHerpggDATVTIAHRYTPK-EQLkihTQLADIIIVAAGIPKLITSDMVKEGAAV 285
Cdd:PLN02897 214 GKNAVVIGRSNIVGLPMSLLLQ---RH-----DATVSTVHAFTKDpEQI---TRKADIVIAAAGIPNLVRGSWLKPGAVV 282
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 222418558 286 IDVGINYVHDPVTG-KTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKI 345
Cdd:PLN02897 283 IDVGTTPVEDSSCEfGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKRI 343
PRK14180 PRK14180
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
52-345 1.12e-76

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


Pssm-ID: 172668 [Multi-domain]  Cd Length: 282  Bit Score: 237.24  E-value: 1.12e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  52 IIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVT 131
Cdd:PRK14180   2 ILIDGKSLSKDLKERLATQVQEYKHHTAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 132 DQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCL-DQHSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:PRK14180  82 DQLNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLQLrDKKCLESCTPKGIMTMLREYGIKTEGAYA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLHTdgeherpgGDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14180 162 VVVGASNVVGKPVSQLLLN--------AKATVTTCHRFT--TDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGI 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 222418558 291 NYVhdpvtgKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKI 345
Cdd:PRK14180 232 NHV------DGKIVGDVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQEL 280
PRK14169 PRK14169
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
51-344 1.68e-76

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184550 [Multi-domain]  Cd Length: 282  Bit Score: 236.77  E-value: 1.68e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  51 AIIISGTEMAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDV 130
Cdd:PRK14169   1 ATRLDGRAVSKKILADLKQTVAKLAQQD-VTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 131 TDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:PRK14169  80 VAELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLhtdgeherPGGDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14169 160 VIVGRSNIVGRPLAGLM--------VNHDATVTIAHSKT--RNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGI 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 222418558 291 NYVHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:PRK14169 230 SRGAD-----GKLLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKR 278
PRK14178 PRK14178
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
82-343 4.22e-76

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172666 [Multi-domain]  Cd Length: 279  Bit Score: 235.51  E-value: 4.22e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  82 PHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDERTICNG 161
Cdd:PRK14178  27 PRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIRRLNEDPDINGILVQLPLPKGVDTERVIAA 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 162 IAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTdgeherpgGDAT 241
Cdd:PRK14178 107 ILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAVVVGRSIDVGRPMAALLLN--------ADAT 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 242 VTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDpvtgktKLVGDVDFEAVKKKAGFITP 321
Cdd:PRK14178 179 VTICHSKT--ENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQVNG------KLCGDVDFDAVKEIAGAITP 250
                        250       260
                 ....*....|....*....|..
gi 222418558 322 VPGGVGPMTVAMLLKNTLLAAK 343
Cdd:PRK14178 251 VPGGVGPMTIATLMENTFDAAK 272
PRK14177 PRK14177
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
50-343 2.88e-74

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172665 [Multi-domain]  Cd Length: 284  Bit Score: 231.02  E-value: 2.88e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  50 EAIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLD 129
Cdd:PRK14177   2 SPILLDGKKLSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 130 VTDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKN 209
Cdd:PRK14177  82 VIDKLNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGKN 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 210 VVVAGRSKNVGMPIAMLLHTdgeherpgGDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVG 289
Cdd:PRK14177 162 AVVVGRSPILGKPMAMLLTE--------MNATVTLCHSKT--QNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAG 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 222418558 290 INYVHdpvtgktklVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAK 343
Cdd:PRK14177 232 YNPGN---------VGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFK 276
PRK14194 PRK14194
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
53-343 1.41e-73

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172682 [Multi-domain]  Cd Length: 301  Bit Score: 229.73  E-value: 1.41e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  53 IISGTEMAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTD 132
Cdd:PRK14194   6 LIDGKAAAARVLAQVREDVRTLKAAG-IEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLLALIA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 133 QLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVV 212
Cdd:PRK14194  85 ELNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGKHAVV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 213 AGRSKNVGMPIAMLLHTdgeherpgGDATVTIAHryTPKEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINY 292
Cdd:PRK14194 165 IGRSNIVGKPMAALLLQ--------AHCSVTVVH--SRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINR 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 222418558 293 VHDpvTGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAK 343
Cdd:PRK14194 235 IDD--DGRSRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAAR 283
PRK14181 PRK14181
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
52-338 3.82e-71

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172669 [Multi-domain]  Cd Length: 287  Bit Score: 223.20  E-value: 3.82e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  52 IIISGTEMAKHIQKEIQRGVESwvslGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVT 131
Cdd:PRK14181   1 MLLKGAPAAEHILATIKENISA----SSTAPGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 132 DQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQ-HSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:PRK14181  77 HRLNNDPNIHGILVQLPLPKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGEtDGFIPCTPAGIIELLKYYEIPLHGRHV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLHtdgeHERPGGDATVTIAHryTPKEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14181 157 AIVGRSNIVGKPLAALLM----QKHPDTNATVTLLH--SQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGT 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 222418558 291 NYVHDPVTGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNT 338
Cdd:PRK14181 231 SRVPAANPKGYILVGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNT 278
PRK14192 PRK14192
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
51-346 3.89e-67

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184561 [Multi-domain]  Cd Length: 283  Bit Score: 212.78  E-value: 3.89e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  51 AIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDV 130
Cdd:PRK14192   3 ALVLDGKALAKQIEEELSVRVEALKAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLAK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 131 TDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:PRK14192  83 IEELNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGKHA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLHTdgeherpgGDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14192 163 VVVGRSAILGKPMAMMLLN--------ANATVTICHSRT--QNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGF 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 222418558 291 nyvHDPVTGKtklVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKII 346
Cdd:PRK14192 233 ---HPRDGGG---VGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKAL 282
PRK14182 PRK14182
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
53-344 5.57e-64

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


Pssm-ID: 172670 [Multi-domain]  Cd Length: 282  Bit Score: 204.49  E-value: 5.57e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558  53 IISGTEMAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTD 132
Cdd:PRK14182   3 LIDGKQIAAKVKGEVATEVRALAARG-VQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 133 QLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLI-PATASAVWEIIKRTGIQTFGKNVV 211
Cdd:PRK14182  82 RLNADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGVPrPCTPAGVMRMLDEARVDPKGKRAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 212 VAGRSKNVGMPIAMLLhtdgeHERpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGIN 291
Cdd:PRK14182 162 VVGRSNIVGKPMAMML-----LER---HATVTIAHSRT--ADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMN 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 222418558 292 YVHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:PRK14182 232 RLAD-----GKLVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKR 279
THF_DHG_CYH pfam00763
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
54-169 7.41e-54

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;


Pssm-ID: 459930 [Multi-domain]  Cd Length: 115  Bit Score: 172.59  E-value: 7.41e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558   54 ISGTEMAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQ 133
Cdd:pfam00763   1 IDGKAIAKKIREELKEEVAALKAGG-RKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDK 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 222418558  134 LNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVD 169
Cdd:pfam00763  80 LNADPSVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115
NAD_bind_m-THF_DH_Cyclohyd_like cd05212
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ...
187-343 1.35e-22

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: 91.80  E-value: 1.35e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 187 IPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTDGeherpggdATVTIAHRYTPKEQLKIHTqlADIIIV 266
Cdd:cd05212    8 VSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDG--------ATVYSCDWKTIQLQSKVHD--ADVVVV 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 222418558 267 AAGIPKLITSDMVKEGAAVIDVGINYVHDpvtgktklvgdvdfEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAK 343
Cdd:cd05212   78 GSPKPEKVPTEWIKPGATVINCSPTKLSG--------------DDVKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140
NAD_bind_m-THF_DH cd01079
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ...
164-339 2.16e-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: 59.36  E-value: 2.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 164 PEKDVDGFHIINIGRLC-----LD----QHSLIPATASAVWEIIKRTGI---------QTFGKNVVVAGRSKNVGMPIAM 225
Cdd:cd01079    1 PHKDVEGLSHKYIFNLYhnirfLDpenrKKSILPCTPLAIVKILEFLGIynkilpygnRLYGKTITIINRSEVVGRPLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 226 LLHTDGE-------------HERPGGDATVTIAHRYTPKEQLKIhtQLADIIIVAAGIPKL-ITSDMVKEGAAVIDVGin 291
Cdd:cd01079   81 LLANDGArvysvdingiqvfTRGESIRHEKHHVTDEEAMTLDCL--SQSDVVITGVPSPNYkVPTELLKDGAICINFA-- 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 222418558 292 yvhdpvtgktklvGDVDFEA-VKKKAGFITPVpggVGPMTVAMLLKNTL 339
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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