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Conserved domains on  [gi|1333636823|ref|XP_023493743|]
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bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial isoform X4 [Equus caballus]

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

CATH:  3.40.50.720|3.40.430.10
EC:  1.5.1.5|3.5.4.9
Gene Ontology:  GO:0004488|GO:0003824|GO:0016787|GO:0009086|GO:0006164|GO:0006730
PubMed:  8485162
SCOP:  4000102

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 6.36e-140

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


:

Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 397.85  E-value: 6.36e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  51 AIIISGTEMAKQIQKEIQRGVESWISLGnRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDM 130
Cdd:COG0190     3 AQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 131 TDQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNV 210
Cdd:COG0190    82 IDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 211 VVAGRSKNVGMPIAMLLhtdgEHErpggDATVTIAHRYTPkeQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:COG0190   162 VVVGRSNIVGKPLALLL----LRR----NATVTVCHSRTK--DLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGI 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333636823 291 NYVHDpvtgkTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQ 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 6.36e-140

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


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 397.85  E-value: 6.36e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  51 AIIISGTEMAKQIQKEIQRGVESWISLGnRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDM 130
Cdd:COG0190     3 AQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 131 TDQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNV 210
Cdd:COG0190    82 IDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 211 VVAGRSKNVGMPIAMLLhtdgEHErpggDATVTIAHRYTPkeQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:COG0190   162 VVVGRSNIVGKPLALLL----LRR----NATVTVCHSRTK--DLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGI 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333636823 291 NYVHDpvtgkTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQ 344
Cdd:COG0190   232 NRVED-----GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280
PRK14190 PRK14190
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 51-346 1.25e-119

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


Pssm-ID: 184560 [Multi-domain]  Cd Length: 284  Bit Score: 346.61  E-value: 1.25e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  51 AIIISGTEMAKQIQKEIQRGVESwisLGNRR--PHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELL 128
Cdd:PRK14190    3 AVIIDGKEVAKEKREQLKEEVVK---LKEQGivPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 129 DMTDQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGK 208
Cdd:PRK14190   80 ALIDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 209 NVVVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTPkeQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDV 288
Cdd:PRK14190  160 HVVVVGRSNIVGKPVGQLLLNE--------NATVTYCHSKTK--NLAELTKQADILIVAVGKPKLITADMVKEGAVVIDV 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333636823 289 GINYVHDpvtgkTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQTL 346
Cdd:PRK14190  230 GVNRLEN-----GKLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKRAG 282
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
 164-343 3.67e-82

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: 247.08  E-value: 3.67e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 164 PEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNVVVAGRSKNVGMPIAMLLHtdgeherpGGDATVT 243
Cdd:cd01080     1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLL--------NRNATVT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 244 IAHRYTPKeqLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDPvtGKTKLVGDVDFEAVKRKAGFITPVP 323
Cdd:cd01080    73 VCHSKTKN--LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDK--SGGKLVGDVDFESAKEKASAITPVP 148

                         170       180
                  ....*....|....*....|
gi 1333636823 324 GGVGPVTVAMLLKNTLLAAK 343
Cdd:cd01080   149 GGVGPMTVAMLMKNTVEAAK 168
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
172-344 6.05e-77

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


Pssm-ID: 427036  Cd Length: 160  Bit Score: 233.13  E-value: 6.05e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 172 HIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNVVVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTPk 251
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA--------NATVTVCHSKTK- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 252 eQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGINYVhdpvtGKTKLVGDVDFEAVKRKAGFITPVPGGVGPVTV 331
Cdd:pfam02882  72 -DLAEITREADIVVVAVGKPELIKADWIKPGAVVIDVGINRV-----GNGKLVGDVDFENVKEKASAITPVPGGVGPMTV 145

                         170
                  ....*....|...
gi 1333636823 332 AMLLKNTLLAAKQ 344
Cdd:pfam02882 146 AMLLQNTVEAAKR 158
 
Name Accession Description Interval E-value
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
 51-344 6.36e-140

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


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 397.85  E-value: 6.36e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  51 AIIISGTEMAKQIQKEIQRGVESWISLGnRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDM 130
Cdd:COG0190     3 AQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 131 TDQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNV 210
Cdd:COG0190    82 IDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 211 VVAGRSKNVGMPIAMLLhtdgEHErpggDATVTIAHRYTPkeQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:COG0190   162 VVVGRSNIVGKPLALLL----LRR----NATVTVCHSRTK--DLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGI 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333636823 291 NYVHDpvtgkTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQ 344
Cdd:COG0190   232 NRVED-----GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280
PRK14190 PRK14190
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 51-346 1.25e-119

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


Pssm-ID: 184560 [Multi-domain]  Cd Length: 284  Bit Score: 346.61  E-value: 1.25e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  51 AIIISGTEMAKQIQKEIQRGVESwisLGNRR--PHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELL 128
Cdd:PRK14190    3 AVIIDGKEVAKEKREQLKEEVVK---LKEQGivPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 129 DMTDQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGK 208
Cdd:PRK14190   80 ALIDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 209 NVVVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTPkeQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDV 288
Cdd:PRK14190  160 HVVVVGRSNIVGKPVGQLLLNE--------NATVTYCHSKTK--NLAELTKQADILIVAVGKPKLITADMVKEGAVVIDV 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333636823 289 GINYVHDpvtgkTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQTL 346
Cdd:PRK14190  230 GVNRLEN-----GKLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKRAG 282
PRK10792 PRK10792
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 51-344 1.47e-107

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 236760 [Multi-domain]  Cd Length: 285  Bit Score: 316.09  E-value: 1.47e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  51 AIIISGTEMAKQIQKEIQRGVESWISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDM 130
Cdd:PRK10792    3 AKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELLAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 131 TDQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNV 210
Cdd:PRK10792   83 IDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGLNA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 211 VVAGRSKNVGMPIAMLLHTDGeherpggdATVTIAHRYTPkeQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK10792  163 VVVGASNIVGRPMSLELLLAG--------CTVTVCHRFTK--NLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGI 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333636823 291 NYVHDpvtgkTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQ 344
Cdd:PRK10792  233 NRLED-----GKLVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEE 281
PRK14186 PRK14186
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 51-344 3.16e-101

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237636 [Multi-domain]  Cd Length: 297  Bit Score: 300.44  E-value: 3.16e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  51 AIIISGTEMAKQIQKEIQRGVESWISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDM 130
Cdd:PRK14186    2 ALILDGKALAAEIEQRLQAQIESNLPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 131 TDQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNV 210
Cdd:PRK14186   82 IAQLNQDERVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKKA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 211 VVAGRSKNVGMPIAMLLHTdgeherpgGDATVTIAHRYTPkeQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14186  162 VVVGRSILVGKPLALMLLA--------ANATVTIAHSRTQ--DLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGI 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333636823 291 NYVHDPvTGKTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQ 344
Cdd:PRK14186  232 HRLPSS-DGKTRLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSWQK 284
PRK14191 PRK14191
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 53-343 4.03e-96

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172679 [Multi-domain]  Cd Length: 285  Bit Score: 287.05  E-value: 4.03e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  53 IISGTEMAKQIQKEIQRGVESWISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDMTD 132
Cdd:PRK14191    3 LLDGKALSYKIEKDLKNKIQILTAQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLIK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 133 QLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNVVV 212
Cdd:PRK14191   83 DLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVVI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 213 AGRSKNVGMPIAMLLHTDGeherpggdATVTIAHRYTpkEQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGINY 292
Cdd:PRK14191  163 IGASNIVGKPLAMLMLNAG--------ASVSVCHILT--KDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINR 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1333636823 293 VHDpvtgkTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAK 343
Cdd:PRK14191  233 LND-----GRLVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAE 278
PRK14189 PRK14189
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
51-345 4.97e-95

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 184559 [Multi-domain]  Cd Length: 285  Bit Score: 283.89  E-value: 4.97e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  51 AIIISGTEMAKQIQKEIQRGVESWISLGNRrPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDM 130
Cdd:PRK14189    3 AQLIDGNALSKQLRAEAAQRAAALTARGHQ-PGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 131 TDQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNV 210
Cdd:PRK14189   82 IDELNRDPKIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGAHA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 211 VVAGRSKNVGMPIAMLLHTDGeherpggdATVTIAHRYTPkeQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14189  162 VVIGRSNIVGKPMAMLLLQAG--------ATVTICHSKTR--DLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGM 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1333636823 291 NYVHDpvtgkTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQT 345
Cdd:PRK14189  232 NRDDA-----GKLCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAERA 281
PRK14176 PRK14176
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 49-346 1.46e-92

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


Pssm-ID: 184553 [Multi-domain]  Cd Length: 287  Bit Score: 277.84  E-value: 1.46e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  49 HDAIIISGTEMAKQIQKEIQRGVESWISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELL 128
Cdd:PRK14176    6 YESRIIDGKALAKKIEAEVRSGVERLKSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 129 DMTDQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGK 208
Cdd:PRK14176   86 ELIDSLNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGK 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 209 NVVVAGRSKNVGMPIA-MLLHTdgeherpggDATVTIAHRYTpkEQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVID 287
Cdd:PRK14176  166 NAVIVGHSNVVGKPMAaMLLNR---------NATVSVCHVFT--DDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFD 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333636823 288 VGINYVHDpvtgktKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQTL 346
Cdd:PRK14176  235 VGITKEED------KVYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEKSL 287
PRK14188 PRK14188
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 51-345 1.84e-91

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184558 [Multi-domain]  Cd Length: 296  Bit Score: 275.30  E-value: 1.84e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  51 AIIISGTEMAKQIQKEIQRGVESWISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDM 130
Cdd:PRK14188    2 ATIIDGKAFAADVRATVAAEVARLKAAHGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 131 TDQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNV 210
Cdd:PRK14188   82 IARLNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLNA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 211 VVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14188  162 VVIGRSNLVGKPMAQLLLAA--------NATVTIAHSRT--RDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGI 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333636823 291 NYVHDP--VTGKTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQT 345
Cdd:PRK14188  232 NRIPAPekGEGKTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACRA 288
PRK14179 PRK14179
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
51-346 3.52e-89

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 237634 [Multi-domain]  Cd Length: 284  Bit Score: 269.31  E-value: 3.52e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  51 AIIISGTEMAKQIQKEIQRGVESWISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDM 130
Cdd:PRK14179    2 TEIIDGKALAQKMQAELAEKVAKLKEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 131 TDQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNV 210
Cdd:PRK14179   82 IERYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 211 VVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14179  162 VVIGRSNIVGKPMAQLLLDK--------NATVTLTHSRT--RNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGM 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333636823 291 NYVHDpvtgkTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQTL 346
Cdd:PRK14179  232 NRDEN-----GKLIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALRSL 282
PRK14167 PRK14167
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 53-342 3.65e-88

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


Pssm-ID: 184549 [Multi-domain]  Cd Length: 297  Bit Score: 267.03  E-value: 3.65e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  53 IISGTEMAKQIQKEIQRGVESWISLGNRrPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDMTD 132
Cdd:PRK14167    4 IIDGNAVAAQIRDDLTDAIETLEDAGVT-PGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTID 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 133 QLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNVVV 212
Cdd:PRK14167   83 ELNADEDVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADVVV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 213 AGRSKNVGMPIAMLLHTDGeherPGGDATVTIAHRYTpkEQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGINY 292
Cdd:PRK14167  163 VGRSDIVGKPMANLLIQKA----DGGNATVTVCHSRT--DDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINR 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1333636823 293 VHDPVTGKTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAA 342
Cdd:PRK14167  237 VDADTEKGYELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAA 286
PRK14184 PRK14184
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 52-344 3.66e-87

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


Pssm-ID: 237635 [Multi-domain]  Cd Length: 286  Bit Score: 263.95  E-value: 3.66e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  52 IIISGTEMAKQIQKEIQRGVESWISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDMT 131
Cdd:PRK14184    2 LLLDGKATAATIREELKTEVAALTARHGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 132 DQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNVV 211
Cdd:PRK14184   82 AELNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 212 VAGRSKNVGMPIAMLLHTDGeherPGGDATVTIAHRYTPkeQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGIN 291
Cdd:PRK14184  162 VVGRSNIVGKPLALMLGAPG----KFANATVTVCHSRTP--DLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGIN 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333636823 292 YVHDpvtgktKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQ 344
Cdd:PRK14184  236 RTDD------GLVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQSWKE 282
PRK14168 PRK14168
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 51-343 6.82e-87

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237633 [Multi-domain]  Cd Length: 297  Bit Score: 263.66  E-value: 6.82e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  51 AIIISGTEMAKQIQKEIQRGVESWISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDM 130
Cdd:PRK14168    3 AKIIKGTEIREEILEEIRGEVAELKEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 131 TDQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCL--DQHSLMPATASAVWEIIKRAGIETFGK 208
Cdd:PRK14168   83 IDKYNNDDSIHGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIggDEVKFLPCTPAGIQEMLVRSGVETSGA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 209 NVVVAGRSKNVGMPIAMLLHTDGeherPGGDATVTIAHryTPKEQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDV 288
Cdd:PRK14168  163 EVVVVGRSNIVGKPIANMMTQKG----PGANATVTIVH--TRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDV 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333636823 289 GINYV-HDPVTGKTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAK 343
Cdd:PRK14168  237 GVNRVgTNESTGKAILSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAK 292
PRK14174 PRK14174
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 52-339 8.72e-87

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


Pssm-ID: 172662 [Multi-domain]  Cd Length: 295  Bit Score: 263.60  E-value: 8.72e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  52 IIISGTEMAKQIQKEIQRGVESWISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDMT 131
Cdd:PRK14174    2 LIIDGKKVSLDLKNELKTRVEAYRAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 132 DQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQ--HSLMPATASAVWEIIKRAGIETFGKN 209
Cdd:PRK14174   82 EDLNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGHldKCFVSCTPYGILELLGRYNIETKGKH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 210 VVVAGRSKNVGMPIAMLLHtdgeHERPGGDATVTIAHRYTPkeQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVG 289
Cdd:PRK14174  162 CVVVGRSNIVGKPMANLML----QKLKESNCTVTICHSATK--DIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVG 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1333636823 290 INYVHDPVTGK-TKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTL 339
Cdd:PRK14174  236 INRIEDPSTKSgYRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTL 286
PRK14183 PRK14183
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 53-344 1.92e-86

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


Pssm-ID: 184555 [Multi-domain]  Cd Length: 281  Bit Score: 262.07  E-value: 1.92e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  53 IISGTEMAKQIQKEIQRGVESWISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDMTD 132
Cdd:PRK14183    3 ILDGKALSDKIKENVKKEVDELKLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETIA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 133 QLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNVVV 212
Cdd:PRK14183   83 MMNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVCV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 213 AGRSKNVGMPIAMLLHTDGeherpggdATVTIAHRYTpkEQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGINY 292
Cdd:PRK14183  163 VGASNIVGKPMAALLLNAN--------ATVDICHIFT--KDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINR 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333636823 293 VHDpvtgkTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQ 344
Cdd:PRK14183  233 TED-----GRLVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKN 279
PRK14185 PRK14185
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 53-347 3.92e-86

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184556 [Multi-domain]  Cd Length: 293  Bit Score: 261.69  E-value: 3.92e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  53 IISGTEMAKQIQKEIQRGVESWISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDMTD 132
Cdd:PRK14185    3 LIDGKAISAQIKQEIAAEVAEIVAKGGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKVR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 133 QLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNVVV 212
Cdd:PRK14185   83 ELNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCVV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 213 AGRSKNVGMPIAMLLHTDGEherpGGDATVTIAHRYTPkeQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGINY 292
Cdd:PRK14185  163 LGRSNIVGKPMAQLMMQKAY----PGDCTVTVCHSRSK--NLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTR 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333636823 293 VHDPVTGKT-KLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQTLY 347
Cdd:PRK14185  237 VPDATRKSGfKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKKAIY 292
PLN02516 PLN02516
methylenetetrahydrofolate dehydrogenase (NADP+)
 49-344 1.73e-85

methylenetetrahydrofolate dehydrogenase (NADP+)


Pssm-ID: 178131 [Multi-domain]  Cd Length: 299  Bit Score: 260.21  E-value: 1.73e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  49 HDAIIISGTEMAKQIQKEIQRGVESWISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELL 128
Cdd:PLN02516    7 HVAQIIDGKAIAKAIRSEIAEEVAQLSEKHGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 129 DMTDQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLD--QHSLMPATASAVWEIIKRAGIETF 206
Cdd:PLN02516   87 SKVHELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMKgrEPLFLPCTPKGCLELLSRSGIPIK 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 207 GKNVVVAGRSKNVGMPIAMLLHTdgeherpgGDATVTIAHRYTPKEQLKIHTqlADVIIVAAGIPKLITSDMVKEGAAVI 286
Cdd:PLN02516  167 GKKAVVVGRSNIVGLPVSLLLLK--------ADATVTVVHSRTPDPESIVRE--ADIVIAAAGQAMMIKGDWIKPGAAVI 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 287 DVGINYVHDPvTGKT--KLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQ 344
Cdd:PLN02516  237 DVGTNAVSDP-SKKSgyRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKR 295
PRK14175 PRK14175
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 51-343 8.25e-84

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184552 [Multi-domain]  Cd Length: 286  Bit Score: 255.61  E-value: 8.25e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  51 AIIISGTEMAKQIQKEIQRGVESWISLGnRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDM 130
Cdd:PRK14175    3 AKILDGKQIAKDYRQGLQDQVEALKEKG-FTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLNE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 131 TDQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNV 210
Cdd:PRK14175   82 LNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGKNA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 211 VVAGRSKNVGMPIAMLLHTdgeherpgGDATVTIAHRYTpkEQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGi 290
Cdd:PRK14175  162 VVIGRSHIVGQPVSKLLLQ--------KNASVTILHSRS--KDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVG- 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333636823 291 nyvhDPVTGKTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAK 343
Cdd:PRK14175  231 ----NTPDENGKLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEK 279
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
 164-343 3.67e-82

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: 247.08  E-value: 3.67e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 164 PEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNVVVAGRSKNVGMPIAMLLHtdgeherpGGDATVT 243
Cdd:cd01080     1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLL--------NRNATVT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 244 IAHRYTPKeqLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDPvtGKTKLVGDVDFEAVKRKAGFITPVP 323
Cdd:cd01080    73 VCHSKTKN--LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDK--SGGKLVGDVDFESAKEKASAITPVP 148

                         170       180
                  ....*....|....*....|
gi 1333636823 324 GGVGPVTVAMLLKNTLLAAK 343
Cdd:cd01080   149 GGVGPMTVAMLMKNTVEAAK 168
PRK14166 PRK14166
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 53-346 4.07e-82

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


Pssm-ID: 172654 [Multi-domain]  Cd Length: 282  Bit Score: 251.10  E-value: 4.07e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  53 IISGTEMAKQIQKEIQRGVESWISLGnRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDMTD 132
Cdd:PRK14166    3 LLDGKALSAKIKEELKEKNQFLKSKG-IESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 133 QLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHS-LMPATASAVWEIIKRAGIETFGKNVV 211
Cdd:PRK14166   82 TLNHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGLESgFLPCTPLGVMKLLKAYEIDLEGKDAV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 212 VAGRSKNVGMPIAMLLHTDGeherpggdATVTIAHRYTpkEQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGIN 291
Cdd:PRK14166  162 IIGASNIVGRPMATMLLNAG--------ATVSVCHIKT--KDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGIN 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1333636823 292 YVHdpvtgKTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQTL 346
Cdd:PRK14166  232 RLE-----SGKIVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAKNRL 281
PRK14193 PRK14193
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 51-346 2.01e-81

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


Pssm-ID: 237637 [Multi-domain]  Cd Length: 284  Bit Score: 249.16  E-value: 2.01e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  51 AIIISGTEMAKQIQKEIQRGVESWISLGnRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDM 130
Cdd:PRK14193    3 AIILDGKATADEIKADLAERVAALKEKG-ITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELNAV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 131 TDQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNV 210
Cdd:PRK14193   82 IDELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGAHV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 211 VVAGRSKNVGMPIAMLLhtdgehERPGGDATVTIAHryTPKEQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14193  162 VVIGRGVTVGRPIGLLL------TRRSENATVTLCH--TGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGV 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333636823 291 NYVhdpvtGKTKLVGDVDfEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQTL 346
Cdd:PRK14193  234 SRA-----GDGKLVGDVH-PDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAERRA 283
PLN02616 PLN02616
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
 44-345 4.01e-81

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 215332 [Multi-domain]  Cd Length: 364  Bit Score: 251.46  E-value: 4.01e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  44 SSGVRHDAIIISGTEMAKQIQKEIQRGVESWISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVS 123
Cdd:PLN02616   66 DTGSEGGAKVIDGKAVAKKIRDEITIEVSRMKESIGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDST 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 124 QEELLDMTDQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHS--LMPATASAVWEIIKRA 201
Cdd:PLN02616  146 EQEVLKFISGFNNDPSVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMRGREplFVPCTPKGCIELLHRY 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 202 GIETFGKNVVVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYT--PKEQlkihTQLADVIIVAAGIPKLITSDMV 279
Cdd:PLN02616  226 NVEIKGKRAVVIGRSNIVGMPAALLLQRE--------DATVSIVHSRTknPEEI----TREADIIISAVGQPNMVRGSWI 293

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333636823 280 KEGAAVIDVGINYVHDPVTGKT-KLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQT 345
Cdd:PLN02616  294 KPGAVVIDVGINPVEDASSPRGyRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKRI 360
PRK14173 PRK14173
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 51-342 2.77e-80

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


Pssm-ID: 184551 [Multi-domain]  Cd Length: 287  Bit Score: 246.66  E-value: 2.77e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  51 AIIISGTEMAKQIQKEIQRGVESWislgNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDM 130
Cdd:PRK14173    3 ARELSGPPAAEAVYAELRARLAKL----PFVPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLEL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 131 TDQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNV 210
Cdd:PRK14173   79 IARLNADPEVDGILVQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGKEV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 211 VVAGRSKNVGMPIAMLLHtdgeherpGGDATVTIAHRYTPkeQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14173  159 VVVGRSNIVGKPLAALLL--------REDATVTLAHSKTQ--DLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGI 228

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333636823 291 NYVHDPvTGKTKLVGDVDFEaVKRKAGFITPVPGGVGPVTVAMLLKNTLLAA 342
Cdd:PRK14173  229 NRVGGN-GGRDILTGDVHPE-VAEVAGALTPVPGGVGPMTVAMLMANTVIAA 278
PRK14187 PRK14187
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 51-342 3.18e-77

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172675 [Multi-domain]  Cd Length: 294  Bit Score: 238.96  E-value: 3.18e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  51 AIIISGTEMAKQIQKEIQRGVESWISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDM 130
Cdd:PRK14187    2 TNIIDGKKIANDITEILATCIDDLKRQHNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 131 TDQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQ--HSLMPATASAVWEIIKRAGIETFGK 208
Cdd:PRK14187   82 INELNNDDSVHGILVQLPVPNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQkkNCLIPCTPKGCLYLIKTITRNLSGS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 209 NVVVAGRSKNVGMPIAMLLHtdgeherpGGDATVTIAHRYTpkEQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDV 288
Cdd:PRK14187  162 DAVVIGRSNIVGKPMACLLL--------GENCTVTTVHSAT--RDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDV 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333636823 289 GINYVHdpVTGKTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAA 342
Cdd:PRK14187  232 GINSIE--EGGVKKFVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAA 283
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
172-344 6.05e-77

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


Pssm-ID: 427036  Cd Length: 160  Bit Score: 233.13  E-value: 6.05e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 172 HIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNVVVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTPk 251
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA--------NATVTVCHSKTK- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 252 eQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGINYVhdpvtGKTKLVGDVDFEAVKRKAGFITPVPGGVGPVTV 331
Cdd:pfam02882  72 -DLAEITREADIVVVAVGKPELIKADWIKPGAVVIDVGINRV-----GNGKLVGDVDFENVKEKASAITPVPGGVGPMTV 145

                         170
                  ....*....|...
gi 1333636823 332 AMLLKNTLLAAKQ 344
Cdd:pfam02882 146 AMLLQNTVEAAKR 158
PRK14172 PRK14172
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 52-337 7.96e-77

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


Pssm-ID: 172660 [Multi-domain]  Cd Length: 278  Bit Score: 237.37  E-value: 7.96e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  52 IIISGTEMAKQIQKEIQRGVESWISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDMT 131
Cdd:PRK14172    3 QIINGKEVALKIKEEIKNFVEERKENGLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 132 DQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNVV 211
Cdd:PRK14172   83 EELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 212 VAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGIN 291
Cdd:PRK14172  163 VIGRSNIVGKPVAQLLLNE--------NATVTICHSKT--KNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTS 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1333636823 292 YVHDpvtgktKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKN 337
Cdd:PRK14172  233 SVNG------KITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKN 272
PRK14170 PRK14170
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 53-344 4.73e-76

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172658 [Multi-domain]  Cd Length: 284  Bit Score: 235.74  E-value: 4.73e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  53 IISGTEMAKQIQKEIQRGVESWISLGnRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDMTD 132
Cdd:PRK14170    4 IIDGKKLAKEIQEKVTREVAELVKEG-KKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSVVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 133 QLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNVVV 212
Cdd:PRK14170   83 ELNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRAVV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 213 AGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGINY 292
Cdd:PRK14170  163 IGRSNIVGKPVAQLLLNE--------NATVTIAHSRT--KDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDR 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333636823 293 VHDpvtgkTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQ 344
Cdd:PRK14170  233 DEN-----NKLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKR 279
PRK14180 PRK14180
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 52-344 2.83e-75

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


Pssm-ID: 172668 [Multi-domain]  Cd Length: 282  Bit Score: 233.77  E-value: 2.83e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  52 IIISGTEMAKQIQKEIQRGVESWISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDMT 131
Cdd:PRK14180    2 ILIDGKSLSKDLKERLATQVQEYKHHTAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 132 DQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCL-DQHSLMPATASAVWEIIKRAGIETFGKNV 210
Cdd:PRK14180   82 DQLNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLQLrDKKCLESCTPKGIMTMLREYGIKTEGAYA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 211 VVAGRSKNVGMPIAMLLHTdgeherpgGDATVTIAHRYTpkEQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14180  162 VVVGASNVVGKPVSQLLLN--------AKATVTTCHRFT--TDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGI 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333636823 291 NYVhdpvtgKTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQ 344
Cdd:PRK14180  232 NHV------DGKIVGDVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQE 279
PRK14171 PRK14171
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 53-347 6.58e-75

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172659 [Multi-domain]  Cd Length: 288  Bit Score: 232.93  E-value: 6.58e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  53 IISGTEMAKQIQKEIQRGVESWISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDMTD 132
Cdd:PRK14171    4 IIDGKALANEILADLKLEIQELKSQTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKIN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 133 QLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRL--CLDQhSLMPATASAVWEIIKRAGIETFGKNV 210
Cdd:PRK14171   84 ELNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLhsGISQ-GFIPCTALGCLAVIKKYEPNLTGKNV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 211 VVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14171  163 VIIGRSNIVGKPLSALLLKE--------NCSVTICHSKT--HNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGI 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333636823 291 NYVhdpvtGKTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQTLY 347
Cdd:PRK14171  233 NRI-----SGNKIIGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKAFKDSLY 284
PRK14178 PRK14178
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 75-343 2.06e-74

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172666 [Multi-domain]  Cd Length: 279  Bit Score: 231.27  E-value: 2.06e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  75 ISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDMTDQLNMDPRVSGILVQLPLPDHVD 154
Cdd:PRK14178   20 IIESGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIRRLNEDPDINGILVQLPLPKGVD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 155 ERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNVVVAGRSKNVGMPIAMLLHTdgehe 234
Cdd:PRK14178  100 TERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAVVVGRSIDVGRPMAALLLN----- 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 235 rpgGDATVTIAHRYTpkEQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDpvtgktKLVGDVDFEAVKR 314
Cdd:PRK14178  175 ---ADATVTICHSKT--ENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQVNG------KLCGDVDFDAVKE 243

                         250       260
                  ....*....|....*....|....*....
gi 1333636823 315 KAGFITPVPGGVGPVTVAMLLKNTLLAAK 343
Cdd:PRK14178  244 IAGAITPVPGGVGPMTIATLMENTFDAAK 272
PRK14177 PRK14177
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 50-344 8.87e-74

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172665 [Multi-domain]  Cd Length: 284  Bit Score: 229.86  E-value: 8.87e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  50 DAIIISGTEMAKQIQKEIQRGVESWISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLD 129
Cdd:PRK14177    2 SPILLDGKKLSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 130 MTDQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKN 209
Cdd:PRK14177   82 VIDKLNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGKN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 210 VVVAGRSKNVGMPIAMLLHTdgeherpgGDATVTIAHRYTpkEQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVG 289
Cdd:PRK14177  162 AVVVGRSPILGKPMAMLLTE--------MNATVTLCHSKT--QNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAG 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1333636823 290 INyvhdpvTGKtklVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQ 344
Cdd:PRK14177  232 YN------PGN---VGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFKE 277
PLN02897 PLN02897
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
 49-345 1.25e-73

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 178485 [Multi-domain]  Cd Length: 345  Bit Score: 231.39  E-value: 1.25e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  49 HDAIIISGTEMAKQIQKEIQRGVESWISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELL 128
Cdd:PLN02897   54 QKTVVIDGNVIAEEIRTKIASEVRKMKKAVGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQIL 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 129 DMTDQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHS--LMPATASAVWEIIKRAGIETF 206
Cdd:PLN02897  134 SALRKFNEDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREplFVSCTPKGCVELLIRSGVEIA 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 207 GKNVVVAGRSKNVGMPIAMLLHtdgEHerpggDATVTIAHRYTPK-EQLkihTQLADVIIVAAGIPKLITSDMVKEGAAV 285
Cdd:PLN02897  214 GKNAVVIGRSNIVGLPMSLLLQ---RH-----DATVSTVHAFTKDpEQI---TRKADIVIAAAGIPNLVRGSWLKPGAVV 282

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333636823 286 IDVGINYVHDPVTG-KTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQT 345
Cdd:PLN02897  283 IDVGTTPVEDSSCEfGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKRI 343
PRK14169 PRK14169
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 51-346 4.04e-73

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184550 [Multi-domain]  Cd Length: 282  Bit Score: 227.91  E-value: 4.04e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  51 AIIISGTEMAKQIQKEIQRGVESwISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDM 130
Cdd:PRK14169    1 ATRLDGRAVSKKILADLKQTVAK-LAQQDVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 131 TDQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNV 210
Cdd:PRK14169   80 VAELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 211 VVAGRSKNVGMPIAMLLhtdgeherPGGDATVTIAHRYTpkEQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14169  160 VIVGRSNIVGRPLAGLM--------VNHDATVTIAHSKT--RNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGI 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333636823 291 NYVHDpvtgkTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQTL 346
Cdd:PRK14169  230 SRGAD-----GKLLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKRRA 280
PRK14194 PRK14194
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 53-344 1.11e-70

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172682 [Multi-domain]  Cd Length: 301  Bit Score: 222.41  E-value: 1.11e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  53 IISGTEMAKQIQKEIQRGVESwISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDMTD 132
Cdd:PRK14194    6 LIDGKAAAARVLAQVREDVRT-LKAAGIEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLLALIA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 133 QLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNVVV 212
Cdd:PRK14194   85 ELNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGKHAVV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 213 AGRSKNVGMPIAMLLHTdgeherpgGDATVTIAHryTPKEQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGINY 292
Cdd:PRK14194  165 IGRSNIVGKPMAALLLQ--------AHCSVTVVH--SRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINR 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333636823 293 VHDpvTGKTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQ 344
Cdd:PRK14194  235 IDD--DGRSRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAARL 284
PRK14181 PRK14181
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 52-338 6.39e-69

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172669 [Multi-domain]  Cd Length: 287  Bit Score: 217.42  E-value: 6.39e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  52 IIISGTEMAKQIQKEIQRGveswISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDMT 131
Cdd:PRK14181    1 MLLKGAPAAEHILATIKEN----ISASSTAPGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 132 DQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQ-HSLMPATASAVWEIIKRAGIETFGKNV 210
Cdd:PRK14181   77 HRLNNDPNIHGILVQLPLPKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGEtDGFIPCTPAGIIELLKYYEIPLHGRHV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 211 VVAGRSKNVGMPIAMLLHtdgeHERPGGDATVTIAHryTPKEQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14181  157 AIVGRSNIVGKPLAALLM----QKHPDTNATVTLLH--SQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGT 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1333636823 291 NYVHDPVTGKTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNT 338
Cdd:PRK14181  231 SRVPAANPKGYILVGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNT 278
PRK14192 PRK14192
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 51-346 8.70e-66

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184561 [Multi-domain]  Cd Length: 283  Bit Score: 209.32  E-value: 8.70e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  51 AIIISGTEMAKQIQKEIQRGVESWISLGNRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDM 130
Cdd:PRK14192    3 ALVLDGKALAKQIEEELSVRVEALKAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLAK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 131 TDQLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSLMPATASAVWEIIKRAGIETFGKNV 210
Cdd:PRK14192   83 IEELNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGKHA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 211 VVAGRSKNVGMPIAMLLHTdgeherpgGDATVTIAHRYTpkEQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14192  163 VVVGRSAILGKPMAMMLLN--------ANATVTICHSRT--QNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGF 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333636823 291 nyvHDPVTGKtklVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQTL 346
Cdd:PRK14192  233 ---HPRDGGG---VGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKAL 282
PRK14182 PRK14182
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 53-345 1.69e-63

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


Pssm-ID: 172670 [Multi-domain]  Cd Length: 282  Bit Score: 203.33  E-value: 1.69e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  53 IISGTEMAKQIQKEIQRGVESWISLGnRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDMTD 132
Cdd:PRK14182    3 LIDGKQIAAKVKGEVATEVRALAARG-VQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 133 QLNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVDGFHIINIGRLCLDQHSL-MPATASAVWEIIKRAGIETFGKNVV 211
Cdd:PRK14182   82 RLNADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGVpRPCTPAGVMRMLDEARVDPKGKRAL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 212 VAGRSKNVGMPIAMLLhtdgeHERpggDATVTIAHRYTpkEQLKIHTQLADVIIVAAGIPKLITSDMVKEGAAVIDVGIN 291
Cdd:PRK14182  162 VVGRSNIVGKPMAMML-----LER---HATVTIAHSRT--ADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMN 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333636823 292 YVHDpvtgkTKLVGDVDFEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAKQT 345
Cdd:PRK14182  232 RLAD-----GKLVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKRT 280
THF_DHG_CYH pfam00763
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
54-169 3.60e-52

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;


Pssm-ID: 459930 [Multi-domain]  Cd Length: 115  Bit Score: 168.35  E-value: 3.60e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823  54 ISGTEMAKQIQKEIQRGVESWISLGnRRPHLSIILVGDNPASHTYVRRKIRAASAVGICSEIILKPKDVSQEELLDMTDQ 133
Cdd:pfam00763   1 IDGKAIAKKIREELKEEVAALKAGG-RKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDK 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1333636823 134 LNMDPRVSGILVQLPLPDHVDERTVCNGIAPEKDVD 169
Cdd:pfam00763  80 LNADPSVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115
NAD_bind_m-THF_DH_Cyclohyd_like cd05212
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ...
 188-343 1.81e-21

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: 88.72  E-value: 1.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 188 PATASAVWEIIKRAGIETFGKNVVVAGRSKNVGMPIAMLLHTDGeherpggdATVTIAHRYTPKEQLKIHTqlADVIIVA 267
Cdd:cd05212     9 SPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDG--------ATVYSCDWKTIQLQSKVHD--ADVVVVG 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333636823 268 AGIPKLITSDMVKEGAAVIDVGINYVHDpvtgktklvgdvdfEAVKRKAGFITPVPGGVGPVTVAMLLKNTLLAAK 343
Cdd:cd05212    79 SPKPEKVPTEWIKPGATVINCSPTKLSG--------------DDVKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140
NAD_bind_m-THF_DH cd01079
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ...
 164-339 1.14e-09

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: 57.44  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 164 PEKDVDGFHIINIGRLC-----LD----QHSLMPATASAVWEIIKRAGI---------ETFGKNVVVAGRSKNVGMPIAM 225
Cdd:cd01079     1 PHKDVEGLSHKYIFNLYhnirfLDpenrKKSILPCTPLAIVKILEFLGIynkilpygnRLYGKTITIINRSEVVGRPLAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333636823 226 LLHTDGE-------------HERPGGDATVTIAHRYTPKEQLKIhtQLADVIIVAAGIPKL-ITSDMVKEGAAVIDVGin 291
Cdd:cd01079    81 LLANDGArvysvdingiqvfTRGESIRHEKHHVTDEEAMTLDCL--SQSDVVITGVPSPNYkVPTELLKDGAICINFA-- 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1333636823 292 yvhdpvtgktklvGDVDFEA-VKRKAGFITPVpggVGPVTVAMLLKNTL 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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