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Conserved domains on  [gi|1011990956|ref|WP_062793544|]
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MULTISPECIES: bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD [Shewanella]

Protein Classification

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase( domain architecture ID 11484949)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10792 PRK10792
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-284 0e+00

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


:

Pssm-ID: 236760 [Multi-domain]  Cd Length: 285  Bit Score: 606.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   1 MTAQLIDGKAIAQSIRQQLKQKVAARQAAGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELL 80
Cdd:PRK10792    1 MTAKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  81 ALIDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGL 160
Cdd:PRK10792   81 ALIDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 161 DAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSGRL 240
Cdd:PRK10792  161 NAVVVGASNIVGRPMSLELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLEDGKL 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1011990956 241 VGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQYHD 284
Cdd:PRK10792  241 VGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEEYHD 284
 
Name Accession Description Interval E-value
PRK10792 PRK10792
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-284 0e+00

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 236760 [Multi-domain]  Cd Length: 285  Bit Score: 606.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   1 MTAQLIDGKAIAQSIRQQLKQKVAARQAAGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELL 80
Cdd:PRK10792    1 MTAKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  81 ALIDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGL 160
Cdd:PRK10792   81 ALIDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 161 DAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSGRL 240
Cdd:PRK10792  161 NAVVVGASNIVGRPMSLELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLEDGKL 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1011990956 241 VGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQYHD 284
Cdd:PRK10792  241 VGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEEYHD 284
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
1-284 0e+00

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


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 523.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   1 MTAQLIDGKAIAQSIRQQLKQKVAARQAAGqRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELL 80
Cdd:COG0190     1 MMAQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  81 ALIDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGL 160
Cdd:COG0190    80 ALIDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 161 DAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSGRL 240
Cdd:COG0190   160 HAVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVEDGKL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1011990956 241 VGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQYHD 284
Cdd:COG0190   240 VGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQAG 283
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
124-283 4.48e-96

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


Pssm-ID: 427036  Cd Length: 160  Bit Score: 279.35  E-value: 4.48e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 124 HPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGLDAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRA 203
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITREA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 204 DLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSGRLVGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQYH 283
Cdd:pfam02882  81 DIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNTVEAAKRQL 160
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
116-280 1.10e-88

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: 260.95  E-value: 1.10e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 116 PDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGLDAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKD 195
Cdd:cd01080     1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKTKN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 196 LKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRL---DSGRLVGDVDFDVACERASHITPVPGGVGPMTIASLL 272
Cdd:cd01080    81 LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVpdkSGGKLVGDVDFESAKEKASAITPVPGGVGPMTVAMLM 160

                  ....*...
gi 1011990956 273 ENTLFAAE 280
Cdd:cd01080   161 KNTVEAAK 168
 
Name Accession Description Interval E-value
PRK10792 PRK10792
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-284 0e+00

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 236760 [Multi-domain]  Cd Length: 285  Bit Score: 606.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   1 MTAQLIDGKAIAQSIRQQLKQKVAARQAAGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELL 80
Cdd:PRK10792    1 MTAKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  81 ALIDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGL 160
Cdd:PRK10792   81 ALIDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 161 DAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSGRL 240
Cdd:PRK10792  161 NAVVVGASNIVGRPMSLELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLEDGKL 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1011990956 241 VGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQYHD 284
Cdd:PRK10792  241 VGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEEYHD 284
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
1-284 0e+00

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


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 523.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   1 MTAQLIDGKAIAQSIRQQLKQKVAARQAAGqRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELL 80
Cdd:COG0190     1 MMAQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  81 ALIDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGL 160
Cdd:COG0190    80 ALIDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 161 DAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSGRL 240
Cdd:COG0190   160 HAVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVEDGKL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1011990956 241 VGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQYHD 284
Cdd:COG0190   240 VGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQAG 283
PRK14189 PRK14189
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
1-281 3.37e-139

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 184559 [Multi-domain]  Cd Length: 285  Bit Score: 393.67  E-value: 3.37e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   1 MTAQLIDGKAIAQSIRQQLKQKVAARQAAGQRiPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELL 80
Cdd:PRK14189    1 MTAQLIDGNALSKQLRAEAAQRAAALTARGHQ-PGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  81 ALIDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGL 160
Cdd:PRK14189   80 ARIDELNRDPKIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 161 DAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSGRL 240
Cdd:PRK14189  160 HAVVIGRSNIVGKPMAMLLLQAGATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMNRDDAGKL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1011990956 241 VGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQ 281
Cdd:PRK14189  240 CGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAER 280
PRK14188 PRK14188
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
2-279 3.98e-138

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184558 [Multi-domain]  Cd Length: 296  Bit Score: 391.24  E-value: 3.98e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   2 TAQLIDGKAIAQSIRQQLKQKVAARQAAGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLA 81
Cdd:PRK14188    1 MATIIDGKAFAADVRATVAAEVARLKAAHGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  82 LIDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGLD 161
Cdd:PRK14188   81 LIARLNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 162 AVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDS---- 237
Cdd:PRK14188  161 AVVIGRSNLVGKPMAQLLLAANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIPApekg 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1011990956 238 ---GRLVGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAA 279
Cdd:PRK14188  241 egkTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAA 285
PRK14190 PRK14190
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
1-284 6.45e-138

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


Pssm-ID: 184560 [Multi-domain]  Cd Length: 284  Bit Score: 390.14  E-value: 6.45e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   1 MTAQLIDGKAIAQSIRQQLKQKVAARQAAGQrIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELL 80
Cdd:PRK14190    1 MMAVIIDGKEVAKEKREQLKEEVVKLKEQGI-VPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  81 ALIDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGL 160
Cdd:PRK14190   80 ALIDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 161 DAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSGRL 240
Cdd:PRK14190  160 HVVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRLENGKL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1011990956 241 VGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQYHD 284
Cdd:PRK14190  240 CGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKRAGG 283
PRK14191 PRK14191
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
4-280 1.66e-130

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172679 [Multi-domain]  Cd Length: 285  Bit Score: 371.79  E-value: 1.66e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   4 QLIDGKAIAQSIRQQLKQKVAARQAAGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLALI 83
Cdd:PRK14191    2 VLLDGKALSYKIEKDLKNKIQILTAQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  84 DSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGLDAV 163
Cdd:PRK14191   82 KDLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 164 VVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSGRLVGD 243
Cdd:PRK14191  162 IIGASNIVGKPLAMLMLNAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLNDGRLVGD 241
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1011990956 244 VDFDVACERASHITPVPGGVGPMTIASLLENTLFAAE 280
Cdd:PRK14191  242 VDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAE 278
PRK14184 PRK14184
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
4-276 4.45e-118

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


Pssm-ID: 237635 [Multi-domain]  Cd Length: 286  Bit Score: 340.21  E-value: 4.45e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   4 QLIDGKAIAQSIRQQLKQKVAARQAAGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLALI 83
Cdd:PRK14184    2 LLLDGKATAATIREELKTEVAALTARHGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  84 DSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGLDAV 163
Cdd:PRK14184   82 AELNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 164 VVGASNIVGRPMTLELLLAG----CTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSGr 239
Cdd:PRK14184  162 VVGRSNIVGKPLALMLGAPGkfanATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRTDDG- 240
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1011990956 240 LVGDVDFDVACERASHITPVPGGVGPMTIASLLENTL 276
Cdd:PRK14184  241 LVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTV 277
PRK14186 PRK14186
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
2-283 1.65e-117

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237636 [Multi-domain]  Cd Length: 297  Bit Score: 338.96  E-value: 1.65e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   2 TAQLIDGKAIAQSIRQQLKQKVAARQAAGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLA 81
Cdd:PRK14186    1 MALILDGKALAAEIEQRLQAQIESNLPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  82 LIDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGLD 161
Cdd:PRK14186   81 LIAQLNQDERVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 162 AVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDS---- 237
Cdd:PRK14186  161 AVVVGRSILVGKPLALMLLAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHRLPSsdgk 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1011990956 238 GRLVGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQYH 283
Cdd:PRK14186  241 TRLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSWQKRH 286
PRK14183 PRK14183
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
4-282 5.06e-116

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


Pssm-ID: 184555 [Multi-domain]  Cd Length: 281  Bit Score: 334.87  E-value: 5.06e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   4 QLIDGKAIAQSIRQQLKQKVAARQAAGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLALI 83
Cdd:PRK14183    2 QILDGKALSDKIKENVKKEVDELKLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  84 DSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGLDAV 163
Cdd:PRK14183   82 AMMNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVC 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 164 VVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSGRLVGD 243
Cdd:PRK14183  162 VVGASNIVGKPMAALLLNANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINRTEDGRLVGD 241
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1011990956 244 VDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQY 282
Cdd:PRK14183  242 VDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKNR 280
PRK14179 PRK14179
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
3-279 6.15e-114

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 237634 [Multi-domain]  Cd Length: 284  Bit Score: 329.41  E-value: 6.15e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   3 AQLIDGKAIAQSIRQQLKQKVAARQAAGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLAL 82
Cdd:PRK14179    2 TEIIDGKALAQKMQAELAEKVAKLKEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  83 IDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGLDA 162
Cdd:PRK14179   82 IERYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 163 VVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSGRLVG 242
Cdd:PRK14179  162 VVIGRSNIVGKPMAQLLLDKNATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMNRDENGKLIG 241
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1011990956 243 DVDFDVACERASHITPVPGGVGPMTIASLLENTLFAA 279
Cdd:PRK14179  242 DVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAA 278
PRK14166 PRK14166
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
5-280 1.48e-112

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


Pssm-ID: 172654 [Multi-domain]  Cd Length: 282  Bit Score: 326.21  E-value: 1.48e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   5 LIDGKAIAQSIRQQLKQKVAARQAAGQRiPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLALID 84
Cdd:PRK14166    3 LLDGKALSAKIKEELKEKNQFLKSKGIE-SCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  85 SLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPV-LRSCTPMGIMTLIKSTGIDTYGLDAV 163
Cdd:PRK14166   82 TLNHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGLESgFLPCTPLGVMKLLKAYEIDLEGKDAV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 164 VVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSGRLVGD 243
Cdd:PRK14166  162 IIGASNIVGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLESGKIVGD 241
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1011990956 244 VDFDVACERASHITPVPGGVGPMTIASLLENTLFAAE 280
Cdd:PRK14166  242 VDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAK 278
PRK14174 PRK14174
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
4-284 1.61e-107

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


Pssm-ID: 172662 [Multi-domain]  Cd Length: 295  Bit Score: 313.68  E-value: 1.61e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   4 QLIDGKAIAQSIRQQLKQKVAARQAAGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLALI 83
Cdd:PRK14174    2 LIIDGKKVSLDLKNELKTRVEAYRAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  84 DSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRL--AQRIPVLRSCTPMGIMTLIKSTGIDTYGLD 161
Cdd:PRK14174   82 EDLNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLvmGHLDKCFVSCTPYGILELLGRYNIETKGKH 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 162 AVVVGASNIVGRPMTlELLL-----AGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLD 236
Cdd:PRK14174  162 CVVVGRSNIVGKPMA-NLMLqklkeSNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRIE 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1011990956 237 -----SG-RLVGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQYHD 284
Cdd:PRK14174  241 dpstkSGyRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTLQSFERVNN 294
PRK14194 PRK14194
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-283 1.83e-106

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172682 [Multi-domain]  Cd Length: 301  Bit Score: 311.39  E-value: 1.83e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   1 MTAQLIDGKAIAQSIRQQLKQKVAARQAAGQRiPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELL 80
Cdd:PRK14194    2 MSAKLIDGKAAAARVLAQVREDVRTLKAAGIE-PALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  81 ALIDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGL 160
Cdd:PRK14194   81 ALIAELNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 161 DAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSG-- 238
Cdd:PRK14194  161 HAVVIGRSNIVGKPMAALLLQAHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINRIDDDgr 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1011990956 239 -RLVGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQYH 283
Cdd:PRK14194  241 sRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAARLQA 286
PRK14193 PRK14193
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
1-281 1.34e-104

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


Pssm-ID: 237637 [Multi-domain]  Cd Length: 284  Bit Score: 305.78  E-value: 1.34e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   1 MTAQLIDGKAIAQSIRQQLKQKVAARQAAGqRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELL 80
Cdd:PRK14193    1 MTAIILDGKATADEIKADLAERVAALKEKG-ITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  81 ALIDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGL 160
Cdd:PRK14193   80 AVIDELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 161 DAVVVGASNIVGRPMTLELLLAG--CTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSG 238
Cdd:PRK14193  160 HVVVIGRGVTVGRPIGLLLTRRSenATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSRAGDG 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011990956 239 RLVGDVDFDVAcERASHITPVPGGVGPMTIASLLENTLFAAEQ 281
Cdd:PRK14193  240 KLVGDVHPDVW-EVAGAVSPNPGGVGPMTRAFLLTNVVERAER 281
PRK14180 PRK14180
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
5-281 2.71e-103

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


Pssm-ID: 172668 [Multi-domain]  Cd Length: 282  Bit Score: 302.72  E-value: 2.71e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   5 LIDGKAIAQSIRQQLKQKVAARQAAGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLALID 84
Cdd:PRK14180    3 LIDGKSLSKDLKERLATQVQEYKHHTAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELID 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  85 SLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQR-IPVLRSCTPMGIMTLIKSTGIDTYGLDAV 163
Cdd:PRK14180   83 QLNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLQLRdKKCLESCTPKGIMTMLREYGIKTEGAYAV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 164 VVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDsGRLVGD 243
Cdd:PRK14180  163 VVGASNVVGKPVSQLLLNAKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHVD-GKIVGD 241
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1011990956 244 VDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQ 281
Cdd:PRK14180  242 VDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQE 279
PRK14167 PRK14167
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
3-284 6.15e-103

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


Pssm-ID: 184549 [Multi-domain]  Cd Length: 297  Bit Score: 302.08  E-value: 6.15e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   3 AQLIDGKAIAQSIRQQLKQKVAARQAAGQRiPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLAL 82
Cdd:PRK14167    2 TEIIDGNAVAAQIRDDLTDAIETLEDAGVT-PGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  83 IDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGLDA 162
Cdd:PRK14167   81 IDELNADEDVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 163 VVVGASNIVGRPMTLELLLAG----CTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSG 238
Cdd:PRK14167  161 VVVGRSDIVGKPMANLLIQKAdggnATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINRVDAD 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1011990956 239 -----RLVGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQYHD 284
Cdd:PRK14167  241 tekgyELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAASLQEG 291
PLN02516 PLN02516
methylenetetrahydrofolate dehydrogenase (NADP+)
2-281 6.62e-103

methylenetetrahydrofolate dehydrogenase (NADP+)


Pssm-ID: 178131 [Multi-domain]  Cd Length: 299  Bit Score: 302.20  E-value: 6.62e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   2 TAQLIDGKAIAQSIRQQLKQKVAARQAAGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLA 81
Cdd:PLN02516    8 VAQIIDGKAIAKAIRSEIAEEVAQLSEKHGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELIS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  82 LIDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQ--RIPVLRSCTPMGIMTLIKSTGIDTYG 159
Cdd:PLN02516   88 KVHELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMkgREPLFLPCTPKGCLELLSRSGIPIKG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 160 LDAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLD--- 236
Cdd:PLN02516  168 KKAVVVGRSNIVGLPVSLLLLKADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVSdps 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1011990956 237 --SG-RLVGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQ 281
Cdd:PLN02516  248 kkSGyRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKR 295
PRK14176 PRK14176
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
5-281 8.87e-102

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


Pssm-ID: 184553 [Multi-domain]  Cd Length: 287  Bit Score: 299.03  E-value: 8.87e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   5 LIDGKAIAQSIRQQLKQKVAARQAAGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLALID 84
Cdd:PRK14176   10 IIDGKALAKKIEAEVRSGVERLKSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELID 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  85 SLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGLDAVV 164
Cdd:PRK14176   90 SLNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGKNAVI 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 165 VGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDsGRLVGDV 244
Cdd:PRK14176  170 VGHSNVVGKPMAAMLLNRNATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITKEE-DKVYGDV 248
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1011990956 245 DFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQ 281
Cdd:PRK14176  249 DFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEK 285
PRK14185 PRK14185
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
4-281 9.34e-100

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184556 [Multi-domain]  Cd Length: 293  Bit Score: 294.04  E-value: 9.34e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   4 QLIDGKAIAQSIRQQLKQKVAARQAAGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLALI 83
Cdd:PRK14185    2 QLIDGKAISAQIKQEIAAEVAEIVAKGGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  84 DSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGLDAV 163
Cdd:PRK14185   82 RELNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 164 VVGASNIVGRPMTLELLLAG----CTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRL---- 235
Cdd:PRK14185  162 VLGRSNIVGKPMAQLMMQKAypgdCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTRVpdat 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1011990956 236 -DSG-RLVGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQ 281
Cdd:PRK14185  242 rKSGfKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKK 289
PRK14187 PRK14187
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
5-279 1.60e-99

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172675 [Multi-domain]  Cd Length: 294  Bit Score: 293.27  E-value: 1.60e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   5 LIDGKAIAQSIRQQLKQKVAARQAAGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLALID 84
Cdd:PRK14187    4 IIDGKKIANDITEILATCIDDLKRQHNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKIN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  85 SLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRL--AQRIPVLRSCTPMGIMTLIKSTGIDTYGLDA 162
Cdd:PRK14187   84 ELNNDDSVHGILVQLPVPNHIDKNLIINTIDPEKDVDGFHNENVGRLftGQKKNCLIPCTPKGCLYLIKTITRNLSGSDA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 163 VVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSG---R 239
Cdd:PRK14187  164 VVIGRSNIVGKPMACLLLGENCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSIEEGgvkK 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1011990956 240 LVGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAA 279
Cdd:PRK14187  244 FVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAA 283
PRK14173 PRK14173
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
1-280 3.16e-98

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


Pssm-ID: 184551 [Multi-domain]  Cd Length: 287  Bit Score: 289.81  E-value: 3.16e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   1 MTAQLIDGKAIAQSIRQQLKQKVAARQAagqrIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELL 80
Cdd:PRK14173    1 MAARELSGPPAAEAVYAELRARLAKLPF----VPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  81 ALIDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGL 160
Cdd:PRK14173   77 ELIARLNADPEVDGILVQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 161 DAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRL--DSG 238
Cdd:PRK14173  157 EVVVVGRSNIVGKPLAALLLREDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINRVggNGG 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1011990956 239 R--LVGDVDFDVAcERASHITPVPGGVGPMTIASLLENTLFAAE 280
Cdd:PRK14173  237 RdiLTGDVHPEVA-EVAGALTPVPGGVGPMTVAMLMANTVIAAL 279
PRK14182 PRK14182
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
5-276 7.69e-98

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


Pssm-ID: 172670 [Multi-domain]  Cd Length: 282  Bit Score: 288.84  E-value: 7.69e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   5 LIDGKAIAQSIRQQLKQKVAARQAAGQRiPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLALID 84
Cdd:PRK14182    3 LIDGKQIAAKVKGEVATEVRALAARGVQ-TGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  85 SLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIP-VLRSCTPMGIMTLIKSTGIDTYGLDAV 163
Cdd:PRK14182   82 RLNADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAgVPRPCTPAGVMRMLDEARVDPKGKRAL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 164 VVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSGRLVGD 243
Cdd:PRK14182  162 VVGRSNIVGKPMAMMLLERHATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLADGKLVGD 241
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1011990956 244 VDFDVACERASHITPVPGGVGPMTIASLLENTL 276
Cdd:PRK14182  242 VEFAAAAARASAITPVPGGVGPMTRAMLLVNTV 274
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
124-283 4.48e-96

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


Pssm-ID: 427036  Cd Length: 160  Bit Score: 279.35  E-value: 4.48e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 124 HPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGLDAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRA 203
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITREA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 204 DLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSGRLVGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQYH 283
Cdd:pfam02882  81 DIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNTVEAAKRQL 160
PRK14169 PRK14169
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
3-281 6.16e-96

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184550 [Multi-domain]  Cd Length: 282  Bit Score: 283.76  E-value: 6.16e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   3 AQLIDGKAIAQSIRQQLKQKVAARQAAGQrIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLAL 82
Cdd:PRK14169    1 ATRLDGRAVSKKILADLKQTVAKLAQQDV-TPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  83 IDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGLDA 162
Cdd:PRK14169   80 VAELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 163 VVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSGRLVG 242
Cdd:PRK14169  160 VIVGRSNIVGRPLAGLMVNHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRGADGKLLG 239
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1011990956 243 DVDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQ 281
Cdd:PRK14169  240 DVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKR 278
PRK14175 PRK14175
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-280 1.02e-95

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184552 [Multi-domain]  Cd Length: 286  Bit Score: 283.35  E-value: 1.02e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   1 MTAQLIDGKAIAQSIRQQLKQKVAARQAAGQrIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELL 80
Cdd:PRK14175    1 MVAKILDGKQIAKDYRQGLQDQVEALKEKGF-TPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  81 ALIDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGL 160
Cdd:PRK14175   80 NELNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 161 DAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSGRL 240
Cdd:PRK14175  160 NAVVIGRSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVGNTPDENGKL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1011990956 241 VGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAAE 280
Cdd:PRK14175  240 KGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEK 279
PRK14192 PRK14192
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-281 1.08e-95

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184561 [Multi-domain]  Cd Length: 283  Bit Score: 283.28  E-value: 1.08e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   1 MTAQLIDGKAIAQSIRQQLKQKVAARQAAGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELL 80
Cdd:PRK14192    1 MMALVLDGKALAKQIEEELSVRVEALKAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  81 ALIDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGL 160
Cdd:PRK14192   81 AKIEELNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 161 DAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSGRl 240
Cdd:PRK14192  161 HAVVVGRSAILGKPMAMMLLNANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFHPRDGGG- 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1011990956 241 VGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQ 281
Cdd:PRK14192  240 VGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEK 280
PLN02616 PLN02616
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
3-284 1.82e-95

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 215332 [Multi-domain]  Cd Length: 364  Bit Score: 285.74  E-value: 1.82e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   3 AQLIDGKAIAQSIRQQLKQKVAARQAAGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLAL 82
Cdd:PLN02616   73 AKVIDGKAVAKKIRDEITIEVSRMKESIGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKF 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  83 IDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQ--RIPVLRSCTPMGIMTLIKSTGIDTYGL 160
Cdd:PLN02616  153 ISGFNNDPSVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMrgREPLFVPCTPKGCIELLHRYNVEIKGK 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 161 DAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSG-- 238
Cdd:PLN02616  233 RAVVIGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPVEDAss 312
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1011990956 239 ----RLVGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQYHD 284
Cdd:PLN02616  313 prgyRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKRIHN 362
PRK14172 PRK14172
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
4-274 1.05e-94

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


Pssm-ID: 172660 [Multi-domain]  Cd Length: 278  Bit Score: 280.51  E-value: 1.05e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   4 QLIDGKAIAQSIRQQLKQKVAARQAAGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLALI 83
Cdd:PRK14172    3 QIINGKEVALKIKEEIKNFVEERKENGLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  84 DSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGLDAV 163
Cdd:PRK14172   83 EELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 164 VVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDsGRLVGD 243
Cdd:PRK14172  163 VIGRSNIVGKPVAQLLLNENATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSVN-GKITGD 241
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1011990956 244 VDFDVACERASHITPVPGGVGPMTIASLLEN 274
Cdd:PRK14172  242 VNFDKVIDKASYITPVPGGVGSLTTTLLIKN 272
PRK14178 PRK14178
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
5-279 1.58e-94

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172666 [Multi-domain]  Cd Length: 279  Bit Score: 280.19  E-value: 1.58e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   5 LIDGKAIAQSIRQQLKQKVAArqaaGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLALID 84
Cdd:PRK14178    2 ILDGKAVSEKRLELLKEEIIE----SGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  85 SLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGLDAVV 164
Cdd:PRK14178   78 RLNEDPDINGILVQLPLPKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAVV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 165 VGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDsGRLVGDV 244
Cdd:PRK14178  158 VGRSIDVGRPMAALLLNADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQVN-GKLCGDV 236
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1011990956 245 DFDVACERASHITPVPGGVGPMTIASLLENTLFAA 279
Cdd:PRK14178  237 DFDAVKEIAGAITPVPGGVGPMTIATLMENTFDAA 271
PLN02897 PLN02897
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
2-284 4.45e-94

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 178485 [Multi-domain]  Cd Length: 345  Bit Score: 281.46  E-value: 4.45e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   2 TAQLIDGKAIAQSIRQQLKQKVAARQAAGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLA 81
Cdd:PLN02897   55 KTVVIDGNVIAEEIRTKIASEVRKMKKAVGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILS 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  82 LIDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQ--RIPVLRSCTPMGIMTLIKSTGIDTYG 159
Cdd:PLN02897  135 ALRKFNEDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMrgREPLFVSCTPKGCVELLIRSGVEIAG 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 160 LDAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSG- 238
Cdd:PLN02897  215 KNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPVEDSs 294
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1011990956 239 -----RLVGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQYHD 284
Cdd:PLN02897  295 cefgyRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKRIFL 345
PRK14177 PRK14177
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-282 1.90e-92

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172665 [Multi-domain]  Cd Length: 284  Bit Score: 274.93  E-value: 1.90e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   1 MTAQLIDGKAIAQSIRQQLKQKVAARQAAGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELL 80
Cdd:PRK14177    1 MSPILLDGKKLSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  81 ALIDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGL 160
Cdd:PRK14177   81 GVIDKLNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 161 DAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDsgrl 240
Cdd:PRK14177  161 NAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYNPGN---- 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1011990956 241 VGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQY 282
Cdd:PRK14177  237 VGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFKEH 278
PRK14170 PRK14170
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
3-281 3.48e-91

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172658 [Multi-domain]  Cd Length: 284  Bit Score: 271.95  E-value: 3.48e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   3 AQLIDGKAIAQSIRQQLKQKVAARQAAGQRiPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLAL 82
Cdd:PRK14170    2 GEIIDGKKLAKEIQEKVTREVAELVKEGKK-PGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  83 IDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGLDA 162
Cdd:PRK14170   81 VEELNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 163 VVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSGRLVG 242
Cdd:PRK14170  161 VVIGRSNIVGKPVAQLLLNENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDRDENNKLCG 240
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1011990956 243 DVDFDVACERASHITPVPGGVGPMTIASLLENTLFAAEQ 281
Cdd:PRK14170  241 DVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKR 279
PRK14168 PRK14168
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-279 7.62e-90

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237633 [Multi-domain]  Cd Length: 297  Bit Score: 269.05  E-value: 7.62e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   1 MTAQLIDGKAIAQSIRQQLKQKVAARQAAGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELL 80
Cdd:PRK14168    1 MSAKIIKGTEIREEILEEIRGEVAELKEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  81 ALIDSLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRL---AQRIPVLrSCTPMGIMTLIKSTGIDT 157
Cdd:PRK14168   81 ALIDKYNNDDSIHGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLmigGDEVKFL-PCTPAGIQEMLVRSGVET 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 158 YGLDAVVVGASNIVGRPMTLELLLAG----CTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGIN 233
Cdd:PRK14168  160 SGAEVVVVGRSNIVGKPIANMMTQKGpganATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVN 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1011990956 234 RL----DSGR--LVGDVDFDVACERASHITPVPGGVGPMTIASLLENTLFAA 279
Cdd:PRK14168  240 RVgtneSTGKaiLSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSA 291
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
116-280 1.10e-88

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: 260.95  E-value: 1.10e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 116 PDKDVDGFHPYNVGRLAQRIPVLRSCTPMGIMTLIKSTGIDTYGLDAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKD 195
Cdd:cd01080     1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKTKN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 196 LKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRL---DSGRLVGDVDFDVACERASHITPVPGGVGPMTIASLL 272
Cdd:cd01080    81 LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVpdkSGGKLVGDVDFESAKEKASAITPVPGGVGPMTVAMLM 160

                  ....*...
gi 1011990956 273 ENTLFAAE 280
Cdd:cd01080   161 KNTVEAAK 168
PRK14171 PRK14171
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
5-278 3.04e-83

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172659 [Multi-domain]  Cd Length: 288  Bit Score: 251.80  E-value: 3.04e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   5 LIDGKAIAQSIRQQLKQKVAARQAAGQRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLALID 84
Cdd:PRK14171    4 IIDGKALANEILADLKLEIQELKSQTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKIN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  85 SLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGRLAQRIPV-LRSCTPMGIMTLIKSTGIDTYGLDAV 163
Cdd:PRK14171   84 ELNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSGISQgFIPCTALGCLAVIKKYEPNLTGKNVV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 164 VVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSGRLVGD 243
Cdd:PRK14171  164 IIGRSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRISGNKIIGD 243
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1011990956 244 VDFDVACERASHITPVPGGVGPMTIASLLENTLFA 278
Cdd:PRK14171  244 VDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKA 278
PRK14181 PRK14181
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
5-275 1.34e-76

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172669 [Multi-domain]  Cd Length: 287  Bit Score: 234.76  E-value: 1.34e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   5 LIDGKAIAQSIRQQLKQKVAARQAAgqriPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLALID 84
Cdd:PRK14181    2 LLKGAPAAEHILATIKENISASSTA----PGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLIH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956  85 SLNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVDGFHPYNVGR-LAQRIPVLRSCTPMGIMTLIKSTGIDTYGLDAV 163
Cdd:PRK14181   78 RLNNDPNIHGILVQLPLPKHLDAQAILQAISPDKDVDGLHPVNMGKlLLGETDGFIPCTPAGIIELLKYYEIPLHGRHVA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 164 VVGASNIVGRPMTLELLL----AGCTTTTCHRFTKDLKDKVSRADLLVVAVGKPDFIPGSWIKPGAIVIDVGINRLDSGR 239
Cdd:PRK14181  158 IVGRSNIVGKPLAALLMQkhpdTNATVTLLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRVPAAN 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1011990956 240 -----LVGDVDFDVACERASHITPVPGGVGPMTIASLLENT 275
Cdd:PRK14181  238 pkgyiLVGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNT 278
THF_DHG_CYH pfam00763
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
6-121 1.16e-65

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;


Pssm-ID: 459930 [Multi-domain]  Cd Length: 115  Bit Score: 200.71  E-value: 1.16e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956   6 IDGKAIAQSIRQQLKQKVAARQAAGqRIPGLAVILVGADPASQVYVGSKRKACEEVGFISRSYDLPDSTSEEELLALIDS 85
Cdd:pfam00763   1 IDGKAIAKKIREELKEEVAALKAGG-RKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDK 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1011990956  86 LNEDAAIDGILVQLPLPEHIKESKVIERIRPDKDVD 121
Cdd:pfam00763  80 LNADPSVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115
NAD_bind_m-THF_DH_Cyclohyd_like cd05212
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ...
141-276 1.38e-34

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: 122.23  E-value: 1.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 141 CTPMGIMTLIKSTGI-------DTYGLDAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLKDKVSRADLLVVAVGKP 213
Cdd:cd05212     3 CTPLFVSPVAKAVKEllnkegvRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSPKP 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1011990956 214 DFIPGSWIKPGAIVIDVGINRLDSgrlvgdvdfDVACERASHITPVPGGVGPMTIASLLENTL 276
Cdd:cd05212    83 EKVPTEWIKPGATVINCSPTKLSG---------DDVKESASLYVPMTGGVGKLTVAMRMQNMV 136
NAD_bind_m-THF_DH cd01079
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ...
116-276 2.76e-11

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: 61.29  E-value: 2.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 116 PDKDVDGFHPYNVGRLAQRIPVLRS---------CTPMGIMTLIKSTGI---------DTYGLDAVVVGASNIVGRPMTL 177
Cdd:cd01079     1 PHKDVEGLSHKYIFNLYHNIRFLDPenrkksilpCTPLAIVKILEFLGIynkilpygnRLYGKTITIINRSEVVGRPLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011990956 178 ELLLAGCTT---------------------TTCHRFTKDLKDKVSRADLLVVAVGKPDF-IPGSWIKPGAIVIDVGinrl 235
Cdd:cd01079    81 LLANDGARVysvdingiqvftrgesirhekHHVTDEEAMTLDCLSQSDVVITGVPSPNYkVPTELLKDGAICINFA---- 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1011990956 236 dsgrlvGDVDFDVACERASHITpVPGgVGPMTIASLLENTL 276
Cdd:cd01079   157 ------SIKNFEPSVKEKASIY-VPS-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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