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Conserved domains on  [gi|568940988|ref|XP_006505760|]
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bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial isoform X2 [Mus musculus]

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 ...
18-311 9.48e-156

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


:

Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 437.52  E-value: 9.48e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  18 AVVISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:COG0190    3 AQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:COG0190   82 IDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLhtdgAHErpggDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:COG0190  162 VVVGRSNIVGKPLALLL----LRR----NATVTVCHSRTK--DLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGI 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568940988 258 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 311
Cdd:COG0190  232 NRVED-----GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280
 
Name Accession Description Interval E-value
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
18-311 9.48e-156

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


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 437.52  E-value: 9.48e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  18 AVVISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:COG0190    3 AQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:COG0190   82 IDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLhtdgAHErpggDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:COG0190  162 VVVGRSNIVGKPLALLL----LRR----NATVTVCHSRTK--DLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGI 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568940988 258 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 311
Cdd:COG0190  232 NRVED-----GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280
PRK14190 PRK14190
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
18-311 8.04e-128

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


Pssm-ID: 184560 [Multi-domain]  Cd Length: 284  Bit Score: 366.64  E-value: 8.04e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  18 AVVISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK14190   3 AVIIDGKEVAKEKREQLKEEVVKLKEQG-IVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14190  82 IDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGKHV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14190 162 VVVGRSNIVGKPVGQLLLNE--------NATVTYCHSKTK--NLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGV 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568940988 258 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 311
Cdd:PRK14190 232 NRLEN-----GKLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKR 280
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
131-310 3.86e-87

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: 259.02  E-value: 3.86e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 131 PDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHtdgaherpGGDATVT 210
Cdd:cd01080    1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLL--------NRNATVT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 211 ISHRYTPKeqLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVQDPvtAKPKLVGDVDFEGVKKKAGYITPVP 290
Cdd:cd01080   73 VCHSKTKN--LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDK--SGGKLVGDVDFESAKEKASAITPVP 148
                        170       180
                 ....*....|....*....|
gi 568940988 291 GGVGPMTVAMLMKNTIIAAK 310
Cdd:cd01080  149 GGVGPMTVAMLMKNTVEAAK 168
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
139-311 5.47e-83

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


Pssm-ID: 427036  Cd Length: 160  Bit Score: 248.15  E-value: 5.47e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  139 HVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTPk 218
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA--------NATVTVCHSKTK- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  219 eQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVQdpvtaKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTV 298
Cdd:pfam02882  72 -DLAEITREADIVVVAVGKPELIKADWIKPGAVVIDVGINRVG-----NGKLVGDVDFENVKEKASAITPVPGGVGPMTV 145
                         170
                  ....*....|...
gi 568940988  299 AMLMKNTIIAAKK 311
Cdd:pfam02882 146 AMLLQNTVEAAKR 158
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
219-257 2.84e-03

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 37.49  E-value: 2.84e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 568940988   219 EQLKKHTILADIVISAAGIPN-----LITADMI---KEGAAVIDVGI 257
Cdd:smart01002  75 ELLEEAVKEADLVIGAVLIPGakapkLVTREMVksmKPGSVIVDVAA 121
 
Name Accession Description Interval E-value
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
18-311 9.48e-156

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


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 437.52  E-value: 9.48e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  18 AVVISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:COG0190    3 AQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:COG0190   82 IDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLhtdgAHErpggDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:COG0190  162 VVVGRSNIVGKPLALLL----LRR----NATVTVCHSRTK--DLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGI 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568940988 258 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 311
Cdd:COG0190  232 NRVED-----GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280
PRK14190 PRK14190
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
18-311 8.04e-128

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


Pssm-ID: 184560 [Multi-domain]  Cd Length: 284  Bit Score: 366.64  E-value: 8.04e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  18 AVVISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK14190   3 AVIIDGKEVAKEKREQLKEEVVKLKEQG-IVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14190  82 IDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGKHV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14190 162 VVVGRSNIVGKPVGQLLLNE--------NATVTYCHSKTK--NLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGV 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568940988 258 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 311
Cdd:PRK14190 232 NRLEN-----GKLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKR 280
PRK10792 PRK10792
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
18-311 1.10e-120

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 236760 [Multi-domain]  Cd Length: 285  Bit Score: 348.44  E-value: 1.10e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  18 AVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK10792   3 AKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELLAL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK10792  83 IDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGLNA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLHTDGaherpggdATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK10792 163 VVVGASNIVGRPMSLELLLAG--------CTVTVCHRFTK--NLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGI 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568940988 258 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 311
Cdd:PRK10792 233 NRLED-----GKLVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEE 281
PRK14189 PRK14189
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
18-315 3.51e-111

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 184559 [Multi-domain]  Cd Length: 285  Bit Score: 324.33  E-value: 3.51e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  18 AVVISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK14189   3 AQLIDGNALSKQLRAEAAQRAAALTARG-HQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14189  82 IDELNRDPKIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGAHA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLHTDGaherpggdATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14189 162 VVIGRSNIVGKPMAMLLLQAG--------ATVTICHSKTR--DLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGM 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568940988 258 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRP 315
Cdd:PRK14189 232 NRDDA-----GKLCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAERAAAA 284
PRK14186 PRK14186
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
18-311 1.27e-110

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237636 [Multi-domain]  Cd Length: 297  Bit Score: 323.55  E-value: 1.27e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  18 AVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK14186   2 ALILDGKALAAEIEQRLQAQIESNLPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14186  82 IAQLNQDERVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKKA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14186 162 VVVGRSILVGKPLALMLLA--------ANATVTIAHSRTQ--DLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGI 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568940988 258 NRVQDPvTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 311
Cdd:PRK14186 232 HRLPSS-DGKTRLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSWQK 284
PRK14191 PRK14191
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
19-314 1.34e-106

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172679 [Multi-domain]  Cd Length: 285  Bit Score: 312.86  E-value: 1.34e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  19 VVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSI 98
Cdd:PRK14191   2 VLLDGKALSYKIEKDLKNKIQILTAQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  99 RKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVV 178
Cdd:PRK14191  82 KDLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 179 VAGRSKNVGMPIAMLLHTDGaherpggdATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGIN 258
Cdd:PRK14191 162 IIGASNIVGKPLAMLMLNAG--------ASVSVCHILT--KDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGIN 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568940988 259 RVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 314
Cdd:PRK14191 232 RLND-----GRLVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEKRQR 282
PRK14188 PRK14188
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
17-311 9.81e-104

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184558 [Multi-domain]  Cd Length: 296  Bit Score: 306.11  E-value: 9.81e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  17 EAVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLN 96
Cdd:PRK14188   1 MATIIDGKAFAADVRATVAAEVARLKAAHGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  97 SIRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKN 176
Cdd:PRK14188  81 LIARLNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 177 VVVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVG 256
Cdd:PRK14188 161 AVVIGRSNLVGKPMAQLLLAA--------NATVTIAHSRT--RDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVG 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568940988 257 INRVQDPVTA--KPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 311
Cdd:PRK14188 231 INRIPAPEKGegKTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACR 287
PRK14185 PRK14185
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
20-313 3.84e-102

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184556 [Multi-domain]  Cd Length: 293  Bit Score: 301.75  E-value: 3.84e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  20 VISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 99
Cdd:PRK14185   3 LIDGKAISAQIKQEIAAEVAEIVAKGGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKVR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 100 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVV 179
Cdd:PRK14185  83 ELNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCVV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 180 AGRSKNVGMPIAMLLHTDGAherpGGDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINR 259
Cdd:PRK14185 163 LGRSNIVGKPMAQLMMQKAY----PGDCTVTVCHSRSK--NLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTR 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568940988 260 VQDPVTAKP-KLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVL 313
Cdd:PRK14185 237 VPDATRKSGfKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKKAI 291
PRK14184 PRK14184
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
20-311 7.56e-100

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


Pssm-ID: 237635 [Multi-domain]  Cd Length: 286  Bit Score: 295.92  E-value: 7.56e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  20 VISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 99
Cdd:PRK14184   3 LLDGKATAATIREELKTEVAALTARHGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLIA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 100 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVV 179
Cdd:PRK14184  83 ELNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAVV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 180 AGRSKNVGMPIAMLLHTDGaherPGGDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINR 259
Cdd:PRK14184 163 VGRSNIVGKPLALMLGAPG----KFANATVTVCHSRTP--DLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINR 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568940988 260 VQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 311
Cdd:PRK14184 237 TDD------GLVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQSWKE 282
PRK14174 PRK14174
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
19-306 9.47e-100

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


Pssm-ID: 172662 [Multi-domain]  Cd Length: 295  Bit Score: 295.96  E-value: 9.47e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  19 VVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSI 98
Cdd:PRK14174   2 LIIDGKKVSLDLKNELKTRVEAYRAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  99 RKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYS--MLPATPWGVWEIIKRTGIPTLGKN 176
Cdd:PRK14174  82 EDLNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGHLDkcFVSCTPYGILELLGRYNIETKGKH 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 177 VVVAGRSKNVGMPIAMLLhtdgAHERPGGDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVG 256
Cdd:PRK14174 162 CVVVGRSNIVGKPMANLM----LQKLKESNCTVTICHSATK--DIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVG 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568940988 257 INRVQDPVT-AKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTI 306
Cdd:PRK14174 236 INRIEDPSTkSGYRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTL 286
PRK14183 PRK14183
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
20-310 2.15e-98

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


Pssm-ID: 184555 [Multi-domain]  Cd Length: 281  Bit Score: 291.73  E-value: 2.15e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  20 VISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 99
Cdd:PRK14183   3 ILDGKALSDKIKENVKKEVDELKLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETIA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 100 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVV 179
Cdd:PRK14183  83 MMNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVCV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 180 AGRSKNVGMPIAMLLHTDGaherpggdATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINR 259
Cdd:PRK14183 163 VGASNIVGKPMAALLLNAN--------ATVDICHIFT--KDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINR 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568940988 260 VQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 310
Cdd:PRK14183 233 TED-----GRLVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAK 278
PRK14176 PRK14176
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
17-313 1.92e-97

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


Pssm-ID: 184553 [Multi-domain]  Cd Length: 287  Bit Score: 289.78  E-value: 1.92e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  17 EAVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLN 96
Cdd:PRK14176   7 ESRIIDGKALAKKIEAEVRSGVERLKSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  97 SIRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKN 176
Cdd:PRK14176  87 LIDSLNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGKN 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 177 VVVAGRSKNVGMPIA-MLLHTdgaherpggDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDV 255
Cdd:PRK14176 167 AVIVGHSNVVGKPMAaMLLNR---------NATVSVCHVFT--DDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDV 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568940988 256 GINRVQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVL 313
Cdd:PRK14176 236 GITKEED------KVYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEKSL 287
PRK14179 PRK14179
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
18-311 2.85e-95

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 237634 [Multi-domain]  Cd Length: 284  Bit Score: 283.95  E-value: 2.85e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  18 AVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK14179   2 TEIIDGKALAQKMQAELAEKVAKLKEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14179  82 IERYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14179 162 VVIGRSNIVGKPMAQLLLDK--------NATVTLTHSRTR--NLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGM 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568940988 258 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 311
Cdd:PRK14179 232 NRDEN-----GKLIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALR 280
PRK14168 PRK14168
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
18-310 1.23e-94

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237633 [Multi-domain]  Cd Length: 297  Bit Score: 282.92  E-value: 1.23e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  18 AVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK14168   3 AKIIKGTEIREEILEEIRGEVAELKEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLAL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCL--DQYSMLPATPWGVWEIIKRTGIPTLGK 175
Cdd:PRK14168  83 IDKYNNDDSIHGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIggDEVKFLPCTPAGIQEMLVRSGVETSGA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 176 NVVVAGRSKNVGMPIAMLLHTDGaherPGGDATVTISHryTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDV 255
Cdd:PRK14168 163 EVVVVGRSNIVGKPIANMMTQKG----PGANATVTIVH--TRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDV 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568940988 256 GINRV-QDPVTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 310
Cdd:PRK14168 237 GVNRVgTNESTGKAILSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAK 292
PRK14193 PRK14193
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
18-314 2.21e-93

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


Pssm-ID: 237637 [Multi-domain]  Cd Length: 284  Bit Score: 279.21  E-value: 2.21e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  18 AVVISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK14193   3 AIILDGKATADEIKADLAERVAALKEKG-ITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELNAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14193  82 IDELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGAHV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLhtdgahERPGGDATVTISHryTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14193 162 VVIGRGVTVGRPIGLLL------TRRSENATVTLCH--TGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGV 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568940988 258 NRVqdpvtAKPKLVGDVDfEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 314
Cdd:PRK14193 234 SRA-----GDGKLVGDVH-PDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAERRAG 284
PLN02516 PLN02516
methylenetetrahydrofolate dehydrogenase (NADP+)
18-313 2.56e-93

methylenetetrahydrofolate dehydrogenase (NADP+)


Pssm-ID: 178131 [Multi-domain]  Cd Length: 299  Bit Score: 279.47  E-value: 2.56e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  18 AVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PLN02516   9 AQIIDGKAIAKAIRSEIAEEVAQLSEKHGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLD--QYSMLPATPWGVWEIIKRTGIPTLGK 175
Cdd:PLN02516  89 VHELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMKgrEPLFLPCTPKGCLELLSRSGIPIKGK 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 176 NVVVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRYTPKEQlkkhTIL--ADIVISAAGIPNLITADMIKEGAAVI 253
Cdd:PLN02516 169 KAVVVGRSNIVGLPVSLLLLK--------ADATVTVVHSRTPDPE----SIVreADIVIAAAGQAMMIKGDWIKPGAAVI 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568940988 254 DVGINRVQDPVTAKP-KLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVL 313
Cdd:PLN02516 237 DVGTNAVSDPSKKSGyRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKRVF 297
PRK14167 PRK14167
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
20-309 8.43e-92

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


Pssm-ID: 184549 [Multi-domain]  Cd Length: 297  Bit Score: 275.50  E-value: 8.43e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  20 VISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 99
Cdd:PRK14167   4 IIDGNAVAAQIRDDLTDAIETLEDAG-VTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTID 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 100 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVV 179
Cdd:PRK14167  83 ELNADEDVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADVVV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 180 AGRSKNVGMPIAMLLhtdgAHERPGGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINR 259
Cdd:PRK14167 163 VGRSDIVGKPMANLL----IQKADGGNATVTVCHSRT--DDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINR 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 568940988 260 VQDPVTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAA 309
Cdd:PRK14167 237 VDADTEKGYELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAA 286
PRK14173 PRK14173
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
18-309 1.47e-90

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


Pssm-ID: 184551 [Multi-domain]  Cd Length: 287  Bit Score: 272.09  E-value: 1.47e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  18 AVVISGRKLAQQIKQEVQQEVEEWVAsgnkRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK14173   3 ARELSGPPAAEAVYAELRARLAKLPF----VPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14173  79 IARLNADPEVDGILVQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGKEV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLHtdgaherpGGDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14173 159 VVVGRSNIVGKPLAALLL--------REDATVTLAHSKTQ--DLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGI 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568940988 258 NRVQDPvTAKPKLVGDVDfEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAA 309
Cdd:PRK14173 229 NRVGGN-GGRDILTGDVH-PEVAEVAGALTPVPGGVGPMTVAMLMANTVIAA 278
PRK14166 PRK14166
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
20-314 8.69e-90

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


Pssm-ID: 172654 [Multi-domain]  Cd Length: 282  Bit Score: 269.97  E-value: 8.69e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  20 VISGRKLAQQIKQEVQQEVEEwVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 99
Cdd:PRK14166   3 LLDGKALSAKIKEELKEKNQF-LKSKGIESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALIN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 100 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLD-QYSMLPATPWGVWEIIKRTGIPTLGKNVV 178
Cdd:PRK14166  82 TLNHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGlESGFLPCTPLGVMKLLKAYEIDLEGKDAV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 179 VAGRSKNVGMPIAMLLHTDGaherpggdATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGIN 258
Cdd:PRK14166 162 IIGASNIVGRPMATMLLNAG--------ATVSVCHIKT--KDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGIN 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568940988 259 RVQdpvtaKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 314
Cdd:PRK14166 232 RLE-----SGKIVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAKNRLN 282
PLN02616 PLN02616
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
18-312 1.05e-89

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 215332 [Multi-domain]  Cd Length: 364  Bit Score: 272.65  E-value: 1.05e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  18 AVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PLN02616  73 AKVIDGKAVAKKIRDEITIEVSRMKESIGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKF 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSML--PATPWGVWEIIKRTGIPTLGK 175
Cdd:PLN02616 153 ISGFNNDPSVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMRGREPLfvPCTPKGCIELLHRYNVEIKGK 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 176 NVVVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTPK-EQLKKHtilADIVISAAGIPNLITADMIKEGAAVID 254
Cdd:PLN02616 233 RAVVIGRSNIVGMPAALLLQRE--------DATVSIVHSRTKNpEEITRE---ADIIISAVGQPNMVRGSWIKPGAVVID 301
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568940988 255 VGINRVQDPVTAKP-KLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKV 312
Cdd:PLN02616 302 VGINPVEDASSPRGyRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKRI 360
PRK14187 PRK14187
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
17-309 2.68e-88

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172675 [Multi-domain]  Cd Length: 294  Bit Score: 266.69  E-value: 2.68e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  17 EAVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLN 96
Cdd:PRK14187   1 ETNIIDGKKIANDITEILATCIDDLKRQHNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  97 SIRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYS--MLPATPWGVWEIIKRTGIPTLG 174
Cdd:PRK14187  81 KINELNNDDSVHGILVQLPVPNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQKKncLIPCTPKGCLYLIKTITRNLSG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 175 KNVVVAGRSKNVGMPIAMLLHtdgaherpGGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVID 254
Cdd:PRK14187 161 SDAVVIGRSNIVGKPMACLLL--------GENCTVTTVHSAT--RDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVID 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568940988 255 VGINRVQdpVTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAA 309
Cdd:PRK14187 231 VGINSIE--EGGVKKFVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAA 283
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
131-310 3.86e-87

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: 259.02  E-value: 3.86e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 131 PDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHtdgaherpGGDATVT 210
Cdd:cd01080    1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLL--------NRNATVT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 211 ISHRYTPKeqLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVQDPvtAKPKLVGDVDFEGVKKKAGYITPVP 290
Cdd:cd01080   73 VCHSKTKN--LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDK--SGGKLVGDVDFESAKEKASAITPVP 148
                        170       180
                 ....*....|....*....|
gi 568940988 291 GGVGPMTVAMLMKNTIIAAK 310
Cdd:cd01080  149 GGVGPMTVAMLMKNTVEAAK 168
PRK14175 PRK14175
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
18-310 5.72e-87

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184552 [Multi-domain]  Cd Length: 286  Bit Score: 262.93  E-value: 5.72e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  18 AVVISGRKLAQQIKQEVQQEVEEWVASGNKrPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK14175   3 AKILDGKQIAKDYRQGLQDQVEALKEKGFT-PKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLNE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14175  82 LNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGKNA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGi 257
Cdd:PRK14175 162 VVIGRSHIVGQPVSKLLLQ--------KNASVTILHSRS--KDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVG- 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568940988 258 nrvqDPVTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 310
Cdd:PRK14175 231 ----NTPDENGKLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEK 279
PRK14172 PRK14172
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
20-304 1.08e-86

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


Pssm-ID: 172660 [Multi-domain]  Cd Length: 278  Bit Score: 262.02  E-value: 1.08e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  20 VISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 99
Cdd:PRK14172   4 IINGKEVALKIKEEIKNFVEERKENGLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEIE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 100 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVV 179
Cdd:PRK14172  84 ELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVVV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 180 AGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINR 259
Cdd:PRK14172 164 IGRSNIVGKPVAQLLLNE--------NATVTICHSKT--KNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSS 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 568940988 260 VQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKN 304
Cdd:PRK14172 234 VNG------KITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKN 272
PRK14169 PRK14169
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
18-311 1.39e-83

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184550 [Multi-domain]  Cd Length: 282  Bit Score: 254.10  E-value: 1.39e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  18 AVVISGRKLAQQIKQEVQQEVEEwVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK14169   1 ATRLDGRAVSKKILADLKQTVAK-LAQQDVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14169  80 VAELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLhtdgaherPGGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14169 160 VIVGRSNIVGRPLAGLM--------VNHDATVTIAHSKT--RNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGI 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568940988 258 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 311
Cdd:PRK14169 230 SRGAD-----GKLLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKR 278
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
139-311 5.47e-83

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


Pssm-ID: 427036  Cd Length: 160  Bit Score: 248.15  E-value: 5.47e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  139 HVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTPk 218
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA--------NATVTVCHSKTK- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  219 eQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVQdpvtaKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTV 298
Cdd:pfam02882  72 -DLAEITREADIVVVAVGKPELIKADWIKPGAVVIDVGINRVG-----NGKLVGDVDFENVKEKASAITPVPGGVGPMTV 145
                         170
                  ....*....|...
gi 568940988  299 AMLMKNTIIAAKK 311
Cdd:pfam02882 146 AMLLQNTVEAAKR 158
PRK14171 PRK14171
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
20-310 2.13e-81

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172659 [Multi-domain]  Cd Length: 288  Bit Score: 248.72  E-value: 2.13e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  20 VISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 99
Cdd:PRK14171   4 IIDGKALANEILADLKLEIQELKSQTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKIN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 100 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRM--CLDQySMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14171  84 ELNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLhsGISQ-GFIPCTALGCLAVIKKYEPNLTGKNV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14171 163 VIIGRSNIVGKPLSALLLKE--------NCSVTICHSKT--HNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGI 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568940988 258 NRVqdpvtAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 310
Cdd:PRK14171 233 NRI-----SGNKIIGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKAFK 280
PRK14178 PRK14178
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
19-310 2.20e-81

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172666 [Multi-domain]  Cd Length: 279  Bit Score: 248.60  E-value: 2.20e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  19 VVISGRKLAQQIKQEVQQEVEEwvasGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSI 98
Cdd:PRK14178   1 MILDGKAVSEKRLELLKEEIIE----SGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  99 RKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVV 178
Cdd:PRK14178  77 RRLNEDPDINGILVQLPLPKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 179 VAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGIN 258
Cdd:PRK14178 157 VVGRSIDVGRPMAALLLN--------ADATVTICHSKT--ENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGIN 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568940988 259 RVQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 310
Cdd:PRK14178 227 QVNG------KLCGDVDFDAVKEIAGAITPVPGGVGPMTIATLMENTFDAAK 272
PLN02897 PLN02897
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
13-312 3.63e-81

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 178485 [Multi-domain]  Cd Length: 345  Bit Score: 250.26  E-value: 3.63e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  13 DTRNEAVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEE 92
Cdd:PLN02897  51 ETEQKTVVIDGNVIAEEIRTKIASEVRKMKKAVGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEG 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  93 ELLNSIRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSML--PATPWGVWEIIKRTGI 170
Cdd:PLN02897 131 QILSALRKFNEDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREPLfvSCTPKGCVELLIRSGV 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 171 PTLGKNVVVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYT--PKEQLKKhtilADIVISAAGIPNLITADMIKE 248
Cdd:PLN02897 211 EIAGKNAVVIGRSNIVGLPMSLLLQRH--------DATVSTVHAFTkdPEQITRK----ADIVIAAAGIPNLVRGSWLKP 278
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568940988 249 GAAVIDVGINRVQDPVTA-KPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKV 312
Cdd:PLN02897 279 GAVVIDVGTTPVEDSSCEfGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKRI 343
PRK14170 PRK14170
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
20-314 3.95e-81

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172658 [Multi-domain]  Cd Length: 284  Bit Score: 248.07  E-value: 3.95e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  20 VISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 99
Cdd:PRK14170   4 IIDGKKLAKEIQEKVTREVAELVKEG-KKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSVVE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 100 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVV 179
Cdd:PRK14170  83 ELNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRAVV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 180 AGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINR 259
Cdd:PRK14170 163 IGRSNIVGKPVAQLLLNE--------NATVTIAHSRT--KDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDR 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568940988 260 VQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 314
Cdd:PRK14170 233 DEN-----NKLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKRIWK 282
PRK14180 PRK14180
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
19-314 7.42e-81

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


Pssm-ID: 172668 [Multi-domain]  Cd Length: 282  Bit Score: 247.25  E-value: 7.42e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  19 VVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSI 98
Cdd:PRK14180   2 ILIDGKSLSKDLKERLATQVQEYKHHTAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  99 RKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCL-DQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14180  82 DQLNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLQLrDKKCLESCTPKGIMTMLREYGIKTEGAYA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14180 162 VVVGASNVVGKPVSQLLLN--------AKATVTTCHRFT--TDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGI 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568940988 258 NRVQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 314
Cdd:PRK14180 232 NHVDG------KIVGDVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQELNR 282
PRK14194 PRK14194
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
16-310 9.05e-79

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172682 [Multi-domain]  Cd Length: 301  Bit Score: 242.44  E-value: 9.05e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  16 NEAVVISGRKLAQQIKQEVQQEVEEWVASGNKrPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELL 95
Cdd:PRK14194   2 MSAKLIDGKAAAARVLAQVREDVRTLKAAGIE-PALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  96 NSIRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGK 175
Cdd:PRK14194  81 ALIAELNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 176 NVVVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHryTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDV 255
Cdd:PRK14194 161 HAVVIGRSNIVGKPMAALLLQ--------AHCSVTVVH--SRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDV 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568940988 256 GINRVQDpvTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 310
Cdd:PRK14194 231 GINRIDD--DGRSRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAAR 283
PRK14177 PRK14177
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
17-315 2.08e-78

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172665 [Multi-domain]  Cd Length: 284  Bit Score: 241.03  E-value: 2.08e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  17 EAVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLN 96
Cdd:PRK14177   2 SPILLDGKKLSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  97 SIRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKN 176
Cdd:PRK14177  82 VIDKLNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGKN 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 177 VVVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVG 256
Cdd:PRK14177 162 AVVVGRSPILGKPMAMLLTE--------MNATVTLCHSKT--QNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAG 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568940988 257 INrvqdpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRP 315
Cdd:PRK14177 232 YN---------PGNVGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFKEHFTP 281
PRK14181 PRK14181
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
19-305 6.38e-77

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172669 [Multi-domain]  Cd Length: 287  Bit Score: 237.45  E-value: 6.38e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  19 VVISGRKLAQQIKQEVQQEVeewvASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSI 98
Cdd:PRK14181   1 MLLKGAPAAEHILATIKENI----SASSTAPGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  99 RKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQY-SMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14181  77 HRLNNDPNIHGILVQLPLPKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGETdGFIPCTPAGIIELLKYYEIPLHGRHV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLhtdgAHERPGGDATVTISHryTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14181 157 AIVGRSNIVGKPLAALL----MQKHPDTNATVTLLH--SQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGT 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568940988 258 NRVQdpvTAKPK---LVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNT 305
Cdd:PRK14181 231 SRVP---AANPKgyiLVGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNT 278
PRK14192 PRK14192
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
18-314 4.09e-76

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184561 [Multi-domain]  Cd Length: 283  Bit Score: 235.13  E-value: 4.09e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  18 AVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK14192   3 ALVLDGKALAKQIEEELSVRVEALKAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLAK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14192  83 IEELNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGKHA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14192 163 VVVGRSAILGKPMAMMLLN--------ANATVTICHSRT--QNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGF 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568940988 258 NRVQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 314
Cdd:PRK14192 233 HPRDG------GGVGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKALG 283
PRK14182 PRK14182
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
20-314 5.11e-72

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


Pssm-ID: 172670 [Multi-domain]  Cd Length: 282  Bit Score: 224.52  E-value: 5.11e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988  20 VISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 99
Cdd:PRK14182   3 LIDGKQIAAKVKGEVATEVRALAARG-VQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 100 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSM-LPATPWGVWEIIKRTGIPTLGKNVV 178
Cdd:PRK14182  82 RLNADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGVpRPCTPAGVMRMLDEARVDPKGKRAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 179 VAGRSKNVGMPIAMLLhtdgaHERpggDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGIN 258
Cdd:PRK14182 162 VVGRSNIVGKPMAMML-----LER---HATVTIAHSRT--ADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMN 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568940988 259 RVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 314
Cdd:PRK14182 232 RLAD-----GKLVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKRTAR 282
THF_DHG_CYH pfam00763
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
21-136 2.60e-60

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;


Pssm-ID: 459930 [Multi-domain]  Cd Length: 115  Bit Score: 188.77  E-value: 2.60e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988   21 ISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIRK 100
Cdd:pfam00763   1 IDGKAIAKKIREELKEEVAALKAGG-RKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDK 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568940988  101 LNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVD 136
Cdd:pfam00763  80 LNADPSVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115
NAD_bind_m-THF_DH_Cyclohyd_like cd05212
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ...
154-310 1.14e-20

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: 86.41  E-value: 1.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 154 LPATPWGVWEIIKRTGI-------PTLGKNVVVAGRSKNVGMPIAMLLHTDGAherpggdaTVTISHRYTPKEQLKKHTi 226
Cdd:cd05212    1 GPCTPLFVSPVAKAVKEllnkegvRLDGKKVLVVGRSGIVGAPLQCLLQRDGA--------TVYSCDWKTIQLQSKVHD- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 227 lADIVISAAGIPNLITADMIKEGAAVIDVGINrvqdpvtakpKLVGDVdfegVKKKAGYITPVPGGVGPMTVAMLMKNTI 306
Cdd:cd05212   72 -ADVVVVGSPKPEKVPTEWIKPGATVINCSPT----------KLSGDD----VKESASLYVPMTGGVGKLTVAMRMQNMV 136

                 ....
gi 568940988 307 IAAK 310
Cdd:cd05212  137 RSVR 140
NAD_bind_m-THF_DH cd01079
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ...
131-306 3.62e-12

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: 64.37  E-value: 3.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 131 PDKDVDGFHVINVGRMC-----LD----QYSMLPATPWGVWEIIKRTGI---------PTLGKNVVVAGRSKNVGMPIAM 192
Cdd:cd01079    1 PHKDVEGLSHKYIFNLYhnirfLDpenrKKSILPCTPLAIVKILEFLGIynkilpygnRLYGKTITIINRSEVVGRPLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 193 LLHTDGAH----ERPGGDA-TVTISHRYTPK------EQLKKHTILADIVISAAGIPNL-ITADMIKEGAAVIDVGinrv 260
Cdd:cd01079   81 LLANDGARvysvDINGIQVfTRGESIRHEKHhvtdeeAMTLDCLSQSDVVITGVPSPNYkVPTELLKDGAICINFA---- 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568940988 261 qdpvtakpklvGDVDFE-GVKKKAGYITPVpggVGPMTVAMLMKNTI 306
Cdd:cd01079  157 -----------SIKNFEpSVKEKASIYVPS---IGKVTIAMLLRNLL 189
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
219-257 2.84e-03

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 37.49  E-value: 2.84e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 568940988   219 EQLKKHTILADIVISAAGIPN-----LITADMI---KEGAAVIDVGI 257
Cdd:smart01002  75 ELLEEAVKEADLVIGAVLIPGakapkLVTREMVksmKPGSVIVDVAA 121
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
204-257 3.13e-03

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 38.93  E-value: 3.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568940988 204 GGDATVTISHRYTPKEQLKKhtilADIVISAAGIPN-----LITADMI---KEGAAVIDVGI 257
Cdd:cd05305  212 GGRVTTLYSNPANLEEALKE----ADLVIGAVLIPGakapkLVTEEMVktmKPGSVIVDVAI 269
Ald COG0686
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ...
200-257 4.59e-03

Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and metabolism]; Alanine dehydrogenase (includes sporulation protein SpoVN) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440450 [Multi-domain]  Cd Length: 372  Bit Score: 38.45  E-value: 4.59e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568940988 200 HERPGGDATVTISHRYTPKEQLKKhtilADIVISAAGIPN-----LITADMI---KEGAAVIDVGI 257
Cdd:COG0686  208 DDIFGGRVTTLYSNPANIEEALKE----ADLVIGAVLIPGarapkLVTREMVkrmKPGSVIVDVAI 269
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
214-257 5.04e-03

Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 426165 [Multi-domain]  Cd Length: 213  Bit Score: 37.86  E-value: 5.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568940988  214 RYTPKEQLKKHTILADIVISAAGI-----PNLITADMI---KEGAAVIDVGI 257
Cdd:pfam01262  79 LYSQAELIAEAVKEADLVIGTALIpgakaPKLVTREMVksmKPGSVIVDVAI 130
 
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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