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Conserved domains on  [gi|1189438236|ref|NP_001338240|]
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bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial isoform 3 [Homo sapiens]

Protein Classification

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

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

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 ...
 2-211 2.26e-89

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


:

Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 264.95  E-value: 2.26e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   2 AKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPR 81
Cdd:COG0190    12 AAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLALIDELNADPS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  82 VSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNV 161
Cdd:COG0190    91 VHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHAVVVGRSNIV 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1189438236 162 GMPIAMLLhtdgeHERpggDATVTIAHRYTPkeQLKIHTQLADIIIVAAG 211
Cdd:COG0190   171 GKPLALLL-----LRR---NATVTVCHSRTK--DLAEHTRQADILVAAVG 210
 
Name Accession Description Interval E-value
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
 2-211 2.26e-89

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


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 264.95  E-value: 2.26e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   2 AKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPR 81
Cdd:COG0190    12 AAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLALIDELNADPS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  82 VSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNV 161
Cdd:COG0190    91 VHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHAVVVGRSNIV 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1189438236 162 GMPIAMLLhtdgeHERpggDATVTIAHRYTPkeQLKIHTQLADIIIVAAG 211
Cdd:COG0190   171 GKPLALLL-----LRR---NATVTVCHSRTK--DLAEHTRQADILVAAVG 210
PRK14190 PRK14190
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 24-211 8.86e-76

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


Pssm-ID: 184560 [Multi-domain]  Cd Length: 284  Bit Score: 230.28  E-value: 8.86e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  24 PHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDERTICNG 103
Cdd:PRK14190   33 PGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLALIDRLNADPRINGILVQLPLPKHIDEKAVIER 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236 104 IAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTDgeherpggDAT 183
Cdd:PRK14190  113 ISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGKHVVVVGRSNIVGKPVGQLLLNE--------NAT 184

                         170       180
                  ....*....|....*....|....*...
gi 1189438236 184 VTIAHRYTPkeQLKIHTQLADIIIVAAG 211
Cdd:PRK14190  185 VTYCHSKTK--NLAELTKQADILIVAVG 210
THF_DHG_CYH pfam00763
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
1-111 2.10e-52

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;


Pssm-ID: 459930 [Multi-domain]  Cd Length: 115  Bit Score: 164.89  E-value: 2.10e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   1 MAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:pfam00763   6 IAKKIREELKEEVAALKAGG-RKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKLNADP 84

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1189438236  81 RVSGILVQLPLPDHVDERTICNGIAPEKDVD 111
Cdd:pfam00763  85 SVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
 106-211 2.46e-37

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: 128.06  E-value: 2.46e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236 106 PEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHtdgeherpGGDATVT 185
Cdd:cd01080     1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLL--------NRNATVT 72

                          90       100
                  ....*....|....*....|....*.
gi 1189438236 186 IAHRYTPKeqLKIHTQLADIIIVAAG 211
Cdd:cd01080    73 VCHSKTKN--LKEHTKQADIVIVAVG 96
 
Name Accession Description Interval E-value
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
 2-211 2.26e-89

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


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 264.95  E-value: 2.26e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   2 AKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPR 81
Cdd:COG0190    12 AAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLALIDELNADPS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  82 VSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNV 161
Cdd:COG0190    91 VHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHAVVVGRSNIV 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1189438236 162 GMPIAMLLhtdgeHERpggDATVTIAHRYTPkeQLKIHTQLADIIIVAAG 211
Cdd:COG0190   171 GKPLALLL-----LRR---NATVTVCHSRTK--DLAEHTRQADILVAAVG 210
PRK14190 PRK14190
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 24-211 8.86e-76

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


Pssm-ID: 184560 [Multi-domain]  Cd Length: 284  Bit Score: 230.28  E-value: 8.86e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  24 PHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDERTICNG 103
Cdd:PRK14190   33 PGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLALIDRLNADPRINGILVQLPLPKHIDEKAVIER 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236 104 IAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTDgeherpggDAT 183
Cdd:PRK14190  113 ISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGKHVVVVGRSNIVGKPVGQLLLNE--------NAT 184

                         170       180
                  ....*....|....*....|....*...
gi 1189438236 184 VTIAHRYTPkeQLKIHTQLADIIIVAAG 211
Cdd:PRK14190  185 VTYCHSKTK--NLAELTKQADILIVAVG 210
PRK10792 PRK10792
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 2-211 7.04e-66

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 236760 [Multi-domain]  Cd Length: 285  Bit Score: 205.15  E-value: 7.04e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   2 AKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPR 81
Cdd:PRK10792   12 AQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELLALIDELNADPT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  82 VSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNV 161
Cdd:PRK10792   92 IDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGLNAVVVGASNIV 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1189438236 162 GMPIAMLLHTDGeherpggdATVTIAHRYTPkeQLKIHTQLADIIIVAAG 211
Cdd:PRK10792  172 GRPMSLELLLAG--------CTVTVCHRFTK--NLRHHVRNADLLVVAVG 211
PRK14186 PRK14186
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 1-211 1.66e-62

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237636 [Multi-domain]  Cd Length: 297  Bit Score: 196.82  E-value: 1.66e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   1 MAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14186   10 LAAEIEQRLQAQIESNLPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEALIAQLNQDE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14186   90 RVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKKAVVVGRSIL 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1189438236 161 VGMPIAMLLHTdgeherpgGDATVTIAHRYTPkeQLKIHTQLADIIIVAAG 211
Cdd:PRK14186  170 VGKPLALMLLA--------ANATVTIAHSRTQ--DLASITREADILVAAAG 210
PRK14189 PRK14189
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
1-211 1.36e-58

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 184559 [Multi-domain]  Cd Length: 285  Bit Score: 186.43  E-value: 1.36e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   1 MAKHIQKEIQRGVESWVSLGNRrPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14189   11 LSKQLRAEAAQRAAALTARGHQ-PGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLARIDELNRDP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14189   90 KIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGAHAVVIGRSNI 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1189438236 161 VGMPIAMLLHTDGeherpggdATVTIAHRYTPkeQLKIHTQLADIIIVAAG 211
Cdd:PRK14189  170 VGKPMAMLLLQAG--------ATVTICHSKTR--DLAAHTRQADIVVAAVG 210
PRK14191 PRK14191
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 5-211 1.65e-58

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172679 [Multi-domain]  Cd Length: 285  Bit Score: 186.13  E-value: 1.65e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   5 IQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSG 84
Cdd:PRK14191   13 IEKDLKNKIQILTAQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLIKDLNTDQNIDG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  85 ILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMP 164
Cdd:PRK14191   93 ILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVVIIGASNIVGKP 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1189438236 165 IAMLLHTDGeherpggdATVTIAHRYTpkEQLKIHTQLADIIIVAAG 211
Cdd:PRK14191  173 LAMLMLNAG--------ASVSVCHILT--KDLSFYTQNADIVCVGVG 209
PRK14179 PRK14179
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
1-211 1.98e-58

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 237634 [Multi-domain]  Cd Length: 284  Bit Score: 186.11  E-value: 1.98e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   1 MAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14179   10 LAQKMQAELAEKVAKLKEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDLIERYNQDP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14179   90 TWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHAVVIGRSNI 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1189438236 161 VGMPIAMLLHTDgeherpggDATVTIAHRYTPkeQLKIHTQLADIIIVAAG 211
Cdd:PRK14179  170 VGKPMAQLLLDK--------NATVTLTHSRTR--NLAEVARKADILVVAIG 210
PRK14185 PRK14185
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 1-211 4.09e-57

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184556 [Multi-domain]  Cd Length: 293  Bit Score: 183.11  E-value: 4.09e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   1 MAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14185    9 ISAQIKQEIAAEVAEIVAKGGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKVRELNQDD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14185   89 DVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCVVLGRSNI 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1189438236 161 VGMPIAMLLHTDGEherpGGDATVTIAHRYTPkeQLKIHTQLADIIIVAAG 211
Cdd:PRK14185  169 VGKPMAQLMMQKAY----PGDCTVTVCHSRSK--NLKKECLEADIIIAALG 213
PRK14188 PRK14188
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 2-211 1.20e-56

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184558 [Multi-domain]  Cd Length: 296  Bit Score: 181.69  E-value: 1.20e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   2 AKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPR 81
Cdd:PRK14188   11 AADVRATVAAEVARLKAAHGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLALIARLNADPA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  82 VSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNV 161
Cdd:PRK14188   91 IHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLNAVVIGRSNLV 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1189438236 162 GMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAG 211
Cdd:PRK14188  171 GKPMAQLLLAA--------NATVTIAHSRT--RDLPAVCRRADILVAAVG 210
PRK14176 PRK14176
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 1-211 4.60e-55

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


Pssm-ID: 184553 [Multi-domain]  Cd Length: 287  Bit Score: 177.69  E-value: 4.60e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   1 MAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14176   16 LAKKIEAEVRSGVERLKSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELIDSLNKRK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14176   96 DVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGKNAVIVGHSNV 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1189438236 161 VGMPIA-MLLHTdgeherpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAG 211
Cdd:PRK14176  176 VGKPMAaMLLNR---------NATVSVCHVFT--DDLKKYTLDADILVVATG 216
PRK14184 PRK14184
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 2-211 9.63e-55

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


Pssm-ID: 237635 [Multi-domain]  Cd Length: 286  Bit Score: 176.51  E-value: 9.63e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   2 AKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPR 81
Cdd:PRK14184   10 AATIREELKTEVAALTARHGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLIAELNARPD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  82 VSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNV 161
Cdd:PRK14184   90 IDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAVVVGRSNIV 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1189438236 162 GMPIAMLLHTDGeherPGGDATVTIAHRYTPkeQLKIHTQLADIIIVAAG 211
Cdd:PRK14184  170 GKPLALMLGAPG----KFANATVTVCHSRTP--DLAEECREADFLFVAIG 213
PRK14168 PRK14168
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 3-211 8.93e-53

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237633 [Multi-domain]  Cd Length: 297  Bit Score: 171.98  E-value: 8.93e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   3 KHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRV 82
Cdd:PRK14168   13 EEILEEIRGEVAELKEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLALIDKYNNDDSI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  83 SGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCL--DQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14168   93 HGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIggDEVKFLPCTPAGIQEMLVRSGVETSGAEVVVVGRSNI 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1189438236 161 VGMPIAMLLHTDGeherPGGDATVTIAHryTPKEQLKIHTQLADIIIVAAG 211
Cdd:PRK14168  173 VGKPIANMMTQKG----PGANATVTIVH--TRSKNLARHCQRADILIVAAG 217
THF_DHG_CYH pfam00763
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
1-111 2.10e-52

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;


Pssm-ID: 459930 [Multi-domain]  Cd Length: 115  Bit Score: 164.89  E-value: 2.10e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   1 MAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:pfam00763   6 IAKKIREELKEEVAALKAGG-RKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKLNADP 84

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1189438236  81 RVSGILVQLPLPDHVDERTICNGIAPEKDVD 111
Cdd:pfam00763  85 SVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115
PRK14193 PRK14193
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 22-212 2.38e-52

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


Pssm-ID: 237637 [Multi-domain]  Cd Length: 284  Bit Score: 170.58  E-value: 2.38e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  22 RRPHLSIILVGDNPASHTYVRNKIRAASAVGICS---ELilkPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDER 98
Cdd:PRK14193   31 ITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSirrDL---PADATQEELNAVIDELNADPACTGYIVQLPLPKHLDEN 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  99 TICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLhtdgehERP 178
Cdd:PRK14193  108 AVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGAHVVVIGRGVTVGRPIGLLL------TRR 181

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1189438236 179 GGDATVTIAHryTPKEQLKIHTQLADIIIVAAGS 212
Cdd:PRK14193  182 SENATVTLCH--TGTRDLAAHTRRADIIVAAAGV 213
PRK14170 PRK14170
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 1-211 5.04e-52

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172658 [Multi-domain]  Cd Length: 284  Bit Score: 169.87  E-value: 5.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   1 MAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14170   10 LAKEIQEKVTREVAELVKEG-KKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSVVEELNEDK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14170   89 TIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRAVVIGRSNI 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1189438236 161 VGMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAG 211
Cdd:PRK14170  169 VGKPVAQLLLNE--------NATVTIAHSRT--KDLPQVAKEADILVVATG 209
PRK14175 PRK14175
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 3-211 1.02e-51

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184552 [Multi-domain]  Cd Length: 286  Bit Score: 168.94  E-value: 1.02e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   3 KHIQKEIQRGVESWVSLGNRR---PHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMD 79
Cdd:PRK14175    9 KQIAKDYRQGLQDQVEALKEKgftPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLNELNRLNND 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  80 PRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSK 159
Cdd:PRK14175   89 DSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGKNAVVIGRSH 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1189438236 160 NVGMPIAMLLHTdgeherpgGDATVTIAHRYTpkEQLKIHTQLADIIIVAAG 211
Cdd:PRK14175  169 IVGQPVSKLLLQ--------KNASVTILHSRS--KDMASYLKDADVIVSAVG 210
PRK14173 PRK14173
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 23-211 1.31e-51

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


Pssm-ID: 184551 [Multi-domain]  Cd Length: 287  Bit Score: 168.85  E-value: 1.31e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  23 RPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDERTICN 102
Cdd:PRK14173   29 VPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLELIARLNADPEVDGILVQLPLPPHIDFQRVLE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236 103 GIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHtdgeherpGGDA 182
Cdd:PRK14173  109 AIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGKEVVVVGRSNIVGKPLAALLL--------REDA 180

                         170       180
                  ....*....|....*....|....*....
gi 1189438236 183 TVTIAHRYTPkeQLKIHTQLADIIIVAAG 211
Cdd:PRK14173  181 TVTLAHSKTQ--DLPAVTRRADVLVVAVG 207
PRK14167 PRK14167
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 1-211 1.56e-51

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


Pssm-ID: 184549 [Multi-domain]  Cd Length: 297  Bit Score: 168.80  E-value: 1.56e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   1 MAKHIQKEIQRGVESWVSLGNRrPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14167   10 VAAQIRDDLTDAIETLEDAGVT-PGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTIDELNADE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14167   89 DVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADVVVVGRSDI 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1189438236 161 VGMPIAMLLHTDGeherPGGDATVTIAHRYTpkEQLKIHTQLADIIIVAAG 211
Cdd:PRK14167  169 VGKPMANLLIQKA----DGGNATVTVCHSRT--DDLAAKTRRADIVVAAAG 213
PLN02516 PLN02516
methylenetetrahydrofolate dehydrogenase (NADP+)
 1-211 2.58e-51

methylenetetrahydrofolate dehydrogenase (NADP+)


Pssm-ID: 178131 [Multi-domain]  Cd Length: 299  Bit Score: 168.15  E-value: 2.58e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   1 MAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PLN02516   17 IAKAIRSEIAEEVAQLSEKHGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISKVHELNANP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLD--QHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRS 158
Cdd:PLN02516   97 DVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMKgrEPLFLPCTPKGCLELLSRSGIPIKGKKAVVVGRS 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1189438236 159 KNVGMPIAMLLHTdgeherpgGDATVTIAHRYTPKEQLKIHTqlADIIIVAAG 211
Cdd:PLN02516  177 NIVGLPVSLLLLK--------ADATVTVVHSRTPDPESIVRE--ADIVIAAAG 219
PRK14177 PRK14177
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 1-228 3.35e-51

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172665 [Multi-domain]  Cd Length: 284  Bit Score: 167.46  E-value: 3.35e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   1 MAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14177   11 LSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLGVIDKLNLDP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14177   91 NVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGKNAVVVGRSPI 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438236 161 VGMPIAMLLHTdgeherpgGDATVTIAHRYTpkEQLKIHTQLADIIIVAAGSLSISHAgvQWRNHGSL 228
Cdd:PRK14177  171 LGKPMAMLLTE--------MNATVTLCHSKT--QNLPSIVRQADIIVGAVGKPEFIKA--DWISEGAV 226
PLN02616 PLN02616
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
 1-211 1.49e-50

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 215332 [Multi-domain]  Cd Length: 364  Bit Score: 168.26  E-value: 1.49e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   1 MAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PLN02616   81 VAKKIRDEITIEVSRMKESIGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKFISGFNNDP 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHS--LIPATASAVWEIIKRTGIQTFGKNVVVAGRS 158
Cdd:PLN02616  161 SVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMRGREplFVPCTPKGCIELLHRYNVEIKGKRAVVIGRS 240

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1189438236 159 KNVGMPIAMLLHTDgeherpggDATVTIAHRYT--PKEQlkihTQLADIIIVAAG 211
Cdd:PLN02616  241 NIVGMPAALLLQRE--------DATVSIVHSRTknPEEI----TREADIIISAVG 283
PRK14183 PRK14183
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 1-211 3.88e-49

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


Pssm-ID: 184555 [Multi-domain]  Cd Length: 281  Bit Score: 162.31  E-value: 3.88e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   1 MAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14183    9 LSDKIKENVKKEVDELKLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETIAMMNNNP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14183   89 NIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVCVVGASNI 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1189438236 161 VGMPIAMLLHTDGeherpggdATVTIAHRYTpkEQLKIHTQLADIIIVAAG 211
Cdd:PRK14183  169 VGKPMAALLLNAN--------ATVDICHIFT--KDLKAHTKKADIVIVGVG 209
PRK14174 PRK14174
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 5-211 5.42e-49

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


Pssm-ID: 172662 [Multi-domain]  Cd Length: 295  Bit Score: 162.30  E-value: 5.42e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   5 IQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSG 84
Cdd:PRK14174   13 LKNELKTRVEAYRAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKIEDLNNDPDVHG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  85 ILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQ--HSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVG 162
Cdd:PRK14174   93 ILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGHldKCFVSCTPYGILELLGRYNIETKGKHCVVVGRSNIVG 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1189438236 163 MPIAMLLHtdgeHERPGGDATVTIAHRYTPkeQLKIHTQLADIIIVAAG 211
Cdd:PRK14174  173 KPMANLML----QKLKESNCTVTICHSATK--DIPSYTRQADILIAAIG 215
PRK14169 PRK14169
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 1-211 1.89e-48

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184550 [Multi-domain]  Cd Length: 282  Bit Score: 160.50  E-value: 1.89e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   1 MAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14169    9 VSKKILADLKQTVAKLAQQD-VTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAKVAELNHDP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14169   88 DVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRVVIVGRSNI 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1189438236 161 VGMPIAMLLhtdgeherPGGDATVTIAHRYTpkEQLKIHTQLADIIIVAAG 211
Cdd:PRK14169  168 VGRPLAGLM--------VNHDATVTIAHSKT--RNLKQLTKEADILVVAVG 208
PLN02897 PLN02897
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
 3-211 3.77e-48

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 178485 [Multi-domain]  Cd Length: 345  Bit Score: 161.28  E-value: 3.77e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   3 KHIQKEIQRGVESWV-----SLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLN 77
Cdd:PLN02897   62 NVIAEEIRTKIASEVrkmkkAVG-KVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILSALRKFN 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  78 MDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHS--LIPATASAVWEIIKRTGIQTFGKNVVVA 155
Cdd:PLN02897  141 EDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREplFVSCTPKGCVELLIRSGVEIAGKNAVVI 220

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438236 156 GRSKNVGMPIAMLLHtdgEHerpggDATVTIAHRYTPK-EQLkihTQLADIIIVAAG 211
Cdd:PLN02897  221 GRSNIVGLPMSLLLQ---RH-----DATVSTVHAFTKDpEQI---TRKADIVIAAAG 266
PRK14171 PRK14171
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 1-212 1.71e-46

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172659 [Multi-domain]  Cd Length: 288  Bit Score: 155.50  E-value: 1.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   1 MAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14171   10 LANEILADLKLEIQELKSQTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKINELNLDN 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRL--CLDQhSLIPATASAVWEIIKRTGIQTFGKNVVVAGRS 158
Cdd:PRK14171   90 EISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLhsGISQ-GFIPCTALGCLAVIKKYEPNLTGKNVVIIGRS 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1189438236 159 KNVGMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAGS 212
Cdd:PRK14171  169 NIVGKPLSALLLKE--------NCSVTICHSKT--HNLSSITSKADIVVAAIGS 212
PRK14172 PRK14172
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 1-211 3.96e-46

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


Pssm-ID: 172660 [Multi-domain]  Cd Length: 278  Bit Score: 154.17  E-value: 3.96e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   1 MAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14172   10 VALKIKEEIKNFVEERKENGLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEIEELNKDN 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14172   90 NVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVVVIGRSNI 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1189438236 161 VGMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAG 211
Cdd:PRK14172  170 VGKPVAQLLLNE--------NATVTICHSKT--KNLKEVCKKADILVVAIG 210
PRK14166 PRK14166
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 24-215 5.36e-46

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


Pssm-ID: 172654 [Multi-domain]  Cd Length: 282  Bit Score: 154.03  E-value: 5.36e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  24 PHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDERTICNG 103
Cdd:PRK14166   31 SCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALINTLNHDDSVHGILVQLPLPDHICKDLILES 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236 104 IAPEKDVDGFHIINIGRLCLDQHS-LIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTDGeherpggdA 182
Cdd:PRK14166  111 IISSKDVDGFHPINVGYLNLGLESgFLPCTPLGVMKLLKAYEIDLEGKDAVIIGASNIVGRPMATMLLNAG--------A 182

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1189438236 183 TVTIAHRYTpkEQLKIHTQLADIIIVAAGSLSI 215
Cdd:PRK14166  183 TVSVCHIKT--KDLSLYTRQADLIIVAAGCVNL 213
PRK14178 PRK14178
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 24-211 4.77e-45

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172666 [Multi-domain]  Cd Length: 279  Bit Score: 151.53  E-value: 4.77e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  24 PHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDERTICNG 103
Cdd:PRK14178   27 PRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIRRLNEDPDINGILVQLPLPKGVDTERVIAA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236 104 IAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTdgeherpgGDAT 183
Cdd:PRK14178  107 ILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAVVVGRSIDVGRPMAALLLN--------ADAT 178

                         170       180
                  ....*....|....*....|....*...
gi 1189438236 184 VTIAHRYTpkEQLKIHTQLADIIIVAAG 211
Cdd:PRK14178  179 VTICHSKT--ENLKAELRQADILVSAAG 204
PRK14187 PRK14187
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 24-228 6.30e-45

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172675 [Multi-domain]  Cd Length: 294  Bit Score: 151.52  E-value: 6.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  24 PHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDERTICNG 103
Cdd:PRK14187   33 PCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKINELNNDDSVHGILVQLPVPNHIDKNLIINT 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236 104 IAPEKDVDGFHIINIGRLCLDQ--HSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHtdgeherpGGD 181
Cdd:PRK14187  113 IDPEKDVDGFHNENVGRLFTGQkkNCLIPCTPKGCLYLIKTITRNLSGSDAVVIGRSNIVGKPMACLLL--------GEN 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1189438236 182 ATVTIAHRYTpkEQLKIHTQLADIIIVAAGSLSISHAGvqWRNHGSL 228
Cdd:PRK14187  185 CTVTTVHSAT--RDLADYCSKADILVAAVGIPNFVKYS--WIKKGAI 227
PRK14181 PRK14181
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 17-211 7.83e-45

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172669 [Multi-domain]  Cd Length: 287  Bit Score: 151.17  E-value: 7.83e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  17 VSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVD 96
Cdd:PRK14181   20 ISASSTAPGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLIHRLNNDPNIHGILVQLPLPKHLD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  97 ERTICNGIAPEKDVDGFHIINIGRLCLDQ-HSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHtdgeH 175
Cdd:PRK14181  100 AQAILQAISPDKDVDGLHPVNMGKLLLGEtDGFIPCTPAGIIELLKYYEIPLHGRHVAIVGRSNIVGKPLAALLM----Q 175

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1189438236 176 ERPGGDATVTIAHryTPKEQLKIHTQLADIIIVAAG 211
Cdd:PRK14181  176 KHPDTNATVTLLH--SQSENLTEILKTADIIIAAIG 209
PRK14192 PRK14192
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 1-211 8.03e-45

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184561 [Multi-domain]  Cd Length: 283  Bit Score: 151.15  E-value: 8.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   1 MAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14192   11 LAKQIEEELSVRVEALKAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLAKIEELNANP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKN 160
Cdd:PRK14192   91 DVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGKHAVVVGRSAI 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1189438236 161 VGMPIAMLLHTdgeherpgGDATVTIAHRYTpkEQLKIHTQLADIIIVAAG 211
Cdd:PRK14192  171 LGKPMAMMLLN--------ANATVTICHSRT--QNLPELVKQADIIVGAVG 211
PRK14180 PRK14180
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 24-211 8.36e-45

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


Pssm-ID: 172668 [Multi-domain]  Cd Length: 282  Bit Score: 150.95  E-value: 8.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  24 PHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDERTICNG 103
Cdd:PRK14180   32 PKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELIDQLNNDSSVHAILVQLPLPAHINKNNVIYS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236 104 IAPEKDVDGFHIINIGRLCL-DQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTdgeherpgGDA 182
Cdd:PRK14180  112 IKPEKDVDGFHPTNVGRLQLrDKKCLESCTPKGIMTMLREYGIKTEGAYAVVVGASNVVGKPVSQLLLN--------AKA 183

                         170       180
                  ....*....|....*....|....*....
gi 1189438236 183 TVTIAHRYTpkEQLKIHTQLADIIIVAAG 211
Cdd:PRK14180  184 TVTTCHRFT--TDLKSHTTKADILIVAVG 210
PRK14194 PRK14194
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 23-211 1.81e-41

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172682 [Multi-domain]  Cd Length: 301  Bit Score: 143.06  E-value: 1.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  23 RPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDERTICN 102
Cdd:PRK14194   33 EPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLLALIAELNADPSVNGILLQLPLPAHIDEARVLQ 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236 103 GIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTdgeherpgGDA 182
Cdd:PRK14194  113 AINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGKHAVVIGRSNIVGKPMAALLLQ--------AHC 184

                         170       180
                  ....*....|....*....|....*....
gi 1189438236 183 TVTIAHryTPKEQLKIHTQLADIIIVAAG 211
Cdd:PRK14194  185 SVTVVH--SRSTDAKALCRQADIVVAAVG 211
PRK14182 PRK14182
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 1-211 7.02e-39

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


Pssm-ID: 172670 [Multi-domain]  Cd Length: 282  Bit Score: 135.53  E-value: 7.02e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236   1 MAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDP 80
Cdd:PRK14182    9 IAAKVKGEVATEVRALAARG-VQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIARLNADP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236  81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLI-PATASAVWEIIKRTGIQTFGKNVVVAGRSK 159
Cdd:PRK14182   88 AVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGVPrPCTPAGVMRMLDEARVDPKGKRALVVGRSN 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1189438236 160 NVGMPIAMLLhtdgeHERpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAG 211
Cdd:PRK14182  168 IVGKPMAMML-----LER---HATVTIAHSRT--ADLAGEVGRADILVAAIG 209
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
 106-211 2.46e-37

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: 128.06  E-value: 2.46e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236 106 PEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHtdgeherpGGDATVT 185
Cdd:cd01080     1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLL--------NRNATVT 72

                          90       100
                  ....*....|....*....|....*.
gi 1189438236 186 IAHRYTPKeqLKIHTQLADIIIVAAG 211
Cdd:cd01080    73 VCHSKTKN--LKEHTKQADIVIVAVG 96
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
114-211 8.24e-33

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


Pssm-ID: 427036  Cd Length: 160  Bit Score: 116.41  E-value: 8.24e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236 114 HIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTPk 193
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA--------NATVTVCHSKTK- 71

                          90
                  ....*....|....*...
gi 1189438236 194 eQLKIHTQLADIIIVAAG 211
Cdd:pfam02882  72 -DLAEITREADIVVVAVG 88
NAD_bind_m-THF_DH_Cyclohyd_like cd05212
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ...
 129-212 1.09e-06

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: 46.73  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236 129 IPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTDGeherpggdATVTIAHRYTPKEQLKIHTqlADIIIV 208
Cdd:cd05212     8 VSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDG--------ATVYSCDWKTIQLQSKVHD--ADVVVV 77


                  ....
gi 1189438236 209 AAGS 212
Cdd:cd05212    78 GSPK 81
NAD_bind_m-THF_DH cd01079
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ...
 106-173 2.02e-04

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: 40.87  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438236 106 PEKDVDGFHIINIGRLC-----LD----QHSLIPATASAVWEIIKRTGI---------QTFGKNVVVAGRSKNVGMPIAM 167
Cdd:cd01079     1 PHKDVEGLSHKYIFNLYhnirfLDpenrKKSILPCTPLAIVKILEFLGIynkilpygnRLYGKTITIINRSEVVGRPLAA 80


                  ....*.
gi 1189438236 168 LLHTDG 173
Cdd:cd01079    81 LLANDG 86
 
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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