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Conserved domains on  [gi|446148872|ref|WP_000226727|]
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MULTISPECIES: bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD [Bacillus]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
 1-281 0e+00

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


:

Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 524.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   1 MVAVIIKGNEVAEKKRAQLTEEVVKLKEQGIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLA 80
Cdd:COG0190    1 MMAQILDGKAVAAEIREELKERVAALKAKGITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  81 EIDRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKH 160
Cdd:COG0190   81 LIDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 161 VVVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETGKLC 240
Cdd:COG0190  161 AVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVEDGKLV 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 446148872 241 GDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKRA 281
Cdd:COG0190  241 GDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQ 281
 
Name Accession Description Interval E-value
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
 1-281 0e+00

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


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 524.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   1 MVAVIIKGNEVAEKKRAQLTEEVVKLKEQGIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLA 80
Cdd:COG0190    1 MMAQILDGKAVAAEIREELKERVAALKAKGITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  81 EIDRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKH 160
Cdd:COG0190   81 LIDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 161 VVVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETGKLC 240
Cdd:COG0190  161 AVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVEDGKLV 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 446148872 241 GDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKRA 281
Cdd:COG0190  241 GDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQ 281
PRK14190 PRK14190
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 1-281 0e+00

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


Pssm-ID: 184560 [Multi-domain]  Cd Length: 284  Bit Score: 519.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   1 MVAVIIKGNEVAEKKRAQLTEEVVKLKEQGIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLA 80
Cdd:PRK14190   1 MMAVIIDGKEVAKEKREQLKEEVVKLKEQGIVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  81 EIDRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKH 160
Cdd:PRK14190  81 LIDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGKH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 161 VVVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETGKLC 240
Cdd:PRK14190 161 VVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRLENGKLC 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 446148872 241 GDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKRA 281
Cdd:PRK14190 241 GDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKRA 281
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
123-281 2.53e-98

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


Pssm-ID: 427036  Cd Length: 160  Bit Score: 285.13  E-value: 2.53e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  123 HPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKHVVVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLA 202
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITREA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446148872  203 DILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETGKLCGDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKRA 281
Cdd:pfam02882  81 DIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNTVEAAKRQ 159
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
 115-279 2.26e-93

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: 272.89  E-value: 2.26e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 115 PEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKHVVVIGRSNIVGKPVGQLFLNENATVTYCHSKTQN 194
Cdd:cd01080    1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKTKN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 195 MKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLE---TGKLCGDVDFDNVLDVAGYITPVPKGVGPMTITMLL 271
Cdd:cd01080   81 LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPdksGGKLVGDVDFESAKEKASAITPVPGGVGPMTVAMLM 160


                 ....*...
gi 446148872 272 HNTVESAK 279
Cdd:cd01080  161 KNTVEAAK 168
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
148-230 2.78e-03

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 37.43  E-value: 2.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   148 LVKETNLDISGKHVVVIGRSNiVGKPVGQLFLNENATVTYCHS-------------KTQNMKELTKLADILIVAVGRPKM 214
Cdd:smart00997  13 ILRATNVLLAGKNVVVAGYGD-VGKGVAARLRGLGARVIVTEIdpiraleaamdgfEVMKMEEAAKRADIFVTATGNKDV 91

                           90
                   ....*....|....*....
gi 446148872   215 VTADYL---KEGAVVIDVG 230
Cdd:smart00997  92 ITREHFramKDGAILANAG 110
 
Name Accession Description Interval E-value
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
 1-281 0e+00

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


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 524.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   1 MVAVIIKGNEVAEKKRAQLTEEVVKLKEQGIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLA 80
Cdd:COG0190    1 MMAQILDGKAVAAEIREELKERVAALKAKGITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  81 EIDRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKH 160
Cdd:COG0190   81 LIDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 161 VVVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETGKLC 240
Cdd:COG0190  161 AVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVEDGKLV 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 446148872 241 GDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKRA 281
Cdd:COG0190  241 GDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQ 281
PRK14190 PRK14190
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 1-281 0e+00

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


Pssm-ID: 184560 [Multi-domain]  Cd Length: 284  Bit Score: 519.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   1 MVAVIIKGNEVAEKKRAQLTEEVVKLKEQGIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLA 80
Cdd:PRK14190   1 MMAVIIDGKEVAKEKREQLKEEVVKLKEQGIVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  81 EIDRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKH 160
Cdd:PRK14190  81 LIDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGKH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 161 VVVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETGKLC 240
Cdd:PRK14190 161 VVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRLENGKLC 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 446148872 241 GDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKRA 281
Cdd:PRK14190 241 GDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKRA 281
PRK14189 PRK14189
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
1-281 2.98e-148

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 184559 [Multi-domain]  Cd Length: 285  Bit Score: 416.78  E-value: 2.98e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   1 MVAVIIKGNEVAEKKRAQLTEEVVKLKEQGIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLA 80
Cdd:PRK14189   1 MTAQLIDGNALSKQLRAEAAQRAAALTARGHQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  81 EIDRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKH 160
Cdd:PRK14189  81 RIDELNRDPKIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGAH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 161 VVVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETGKLC 240
Cdd:PRK14189 161 AVVIGRSNIVGKPMAMLLLQAGATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMNRDDAGKLC 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 446148872 241 GDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKRA 281
Cdd:PRK14189 241 GDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAERA 281
PRK10792 PRK10792
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 1-278 5.25e-135

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 236760 [Multi-domain]  Cd Length: 285  Bit Score: 383.11  E-value: 5.25e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   1 MVAVIIKGNEVAEKKRAQLTEEVVKLKEQGI-VPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLL 79
Cdd:PRK10792   1 MTAKIIDGKTIAQQVRSEVAQKVQARVAAGLrAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  80 AEIDRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGK 159
Cdd:PRK10792  81 ALIDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 160 HVVVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETGKL 239
Cdd:PRK10792 161 NAVVVGASNIVGRPMSLELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLEDGKL 240

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 446148872 240 CGDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESA 278
Cdd:PRK10792 241 VGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQAC 279
PRK14179 PRK14179
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
2-280 1.22e-134

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 237634 [Multi-domain]  Cd Length: 284  Bit Score: 382.18  E-value: 1.22e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   2 VAVIIKGNEVAEKKRAQLTEEVVKLKEQ-GIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLA 80
Cdd:PRK14179   1 MTEIIDGKALAQKMQAELAEKVAKLKEEkGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  81 EIDRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKH 160
Cdd:PRK14179  81 LIERYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 161 VVVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETGKLC 240
Cdd:PRK14179 161 AVVIGRSNIVGKPMAQLLLDKNATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMNRDENGKLI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 446148872 241 GDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKR 280
Cdd:PRK14179 241 GDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALR 280
PRK14188 PRK14188
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 3-281 3.24e-131

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184558 [Multi-domain]  Cd Length: 296  Bit Score: 373.91  E-value: 3.24e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   3 AVIIKGNEVAEKKRAQLTEEVVKLKEQ-GIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLAE 81
Cdd:PRK14188   2 ATIIDGKAFAADVRATVAAEVARLKAAhGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLAL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  82 IDRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKHV 161
Cdd:PRK14188  82 IARLNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLNA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 162 VVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLET----- 236
Cdd:PRK14188 162 VVIGRSNLVGKPMAQLLLAANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIPApekge 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 446148872 237 --GKLCGDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKRA 281
Cdd:PRK14188 242 gkTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACRA 288
PRK14191 PRK14191
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 4-279 1.25e-130

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172679 [Multi-domain]  Cd Length: 285  Bit Score: 372.18  E-value: 1.25e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   4 VIIKGNEVAEKKRAQLTEEVVKLK-EQGIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLAEI 82
Cdd:PRK14191   2 VLLDGKALSYKIEKDLKNKIQILTaQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  83 DRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKHVV 162
Cdd:PRK14191  82 KDLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 163 VIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETGKLCGD 242
Cdd:PRK14191 162 IIGASNIVGKPLAMLMLNAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLNDGRLVGD 241

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 446148872 243 VDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAK 279
Cdd:PRK14191 242 VDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAE 278
PRK14193 PRK14193
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 1-281 6.78e-122

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


Pssm-ID: 237637 [Multi-domain]  Cd Length: 284  Bit Score: 349.70  E-value: 6.78e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   1 MVAVIIKGNEVAEKKRAQLTEEVVKLKEQGIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLA 80
Cdd:PRK14193   1 MTAIILDGKATADEIKADLAERVAALKEKGITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELNA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  81 EIDRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKH 160
Cdd:PRK14193  81 VIDELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGAH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 161 VVVIGRSNIVGKPVGQLFL--NENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETGK 238
Cdd:PRK14193 161 VVVIGRGVTVGRPIGLLLTrrSENATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSRAGDGK 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 446148872 239 LCGDVDFDnVLDVAGYITPVPKGVGPMTITMLLHNTVESAKRA 281
Cdd:PRK14193 241 LVGDVHPD-VWEVAGAVSPNPGGVGPMTRAFLLTNVVERAERR 282
PRK14186 PRK14186
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 3-285 2.89e-121

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237636 [Multi-domain]  Cd Length: 297  Bit Score: 348.59  E-value: 2.89e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   3 AVIIKGNEVAEKKRAQLTEEVVKLKEQ-GIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLAE 81
Cdd:PRK14186   2 ALILDGKALAAEIEQRLQAQIESNLPKaGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEAL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  82 IDRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKHV 161
Cdd:PRK14186  82 IAQLNQDERVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKKA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 162 VVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLET----G 237
Cdd:PRK14186 162 VVVGRSILVGKPLALMLLAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHRLPSsdgkT 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 446148872 238 KLCGDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKRAGVVC 285
Cdd:PRK14186 242 RLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSWQKRHGLS 289
PRK14184 PRK14184
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 5-279 1.33e-117

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


Pssm-ID: 237635 [Multi-domain]  Cd Length: 286  Bit Score: 339.06  E-value: 1.33e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   5 IIKGNEVAEKKRAQLTEEVVKLKEQ-GIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLAEID 83
Cdd:PRK14184   3 LLDGKATAATIREELKTEVAALTARhGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLIA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  84 RLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKHVVV 163
Cdd:PRK14184  83 ELNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAVV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 164 IGRSNIVGKPVGQLFLNE----NATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETGkL 239
Cdd:PRK14184 163 VGRSNIVGKPLALMLGAPgkfaNATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRTDDG-L 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 446148872 240 CGDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAK 279
Cdd:PRK14184 242 VGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQSWK 281
PRK14183 PRK14183
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 5-279 2.28e-115

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


Pssm-ID: 184555 [Multi-domain]  Cd Length: 281  Bit Score: 333.33  E-value: 2.28e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   5 IIKGNEVAEKKRAQLTEEVVKLK-EQGIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLAEID 83
Cdd:PRK14183   3 ILDGKALSDKIKENVKKEVDELKlVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETIA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  84 RLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKHVVV 163
Cdd:PRK14183  83 MMNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVCV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 164 IGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETGKLCGDV 243
Cdd:PRK14183 163 VGASNIVGKPMAALLLNANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINRTEDGRLVGDV 242

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 446148872 244 DFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAK 279
Cdd:PRK14183 243 DFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAK 278
PRK14175 PRK14175
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 1-281 1.11e-114

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184552 [Multi-domain]  Cd Length: 286  Bit Score: 331.50  E-value: 1.11e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   1 MVAVIIKGNEVAEKKRAQLTEEVVKLKEQGIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLA 80
Cdd:PRK14175   1 MVAKILDGKQIAKDYRQGLQDQVEALKEKGFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  81 EIDRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKH 160
Cdd:PRK14175  81 ELNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGKN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 161 VVVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETGKLC 240
Cdd:PRK14175 161 AVVIGRSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVGNTPDENGKLK 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 446148872 241 GDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKRA 281
Cdd:PRK14175 241 GDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEKMR 281
PRK14172 PRK14172
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 5-279 7.26e-114

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


Pssm-ID: 172660 [Multi-domain]  Cd Length: 278  Bit Score: 329.43  E-value: 7.26e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   5 IIKGNEVAEKKRAQLTEEVVKLKEQGI-VPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLAEID 83
Cdd:PRK14172   4 IINGKEVALKIKEEIKNFVEERKENGLsIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEIE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  84 RLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKHVVV 163
Cdd:PRK14172  84 ELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVVV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 164 IGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLEtGKLCGDV 243
Cdd:PRK14172 164 IGRSNIVGKPVAQLLLNENATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSVN-GKITGDV 242

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 446148872 244 DFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAK 279
Cdd:PRK14172 243 NFDKVIDKASYITPVPGGVGSLTTTLLIKNVCEALK 278
PRK14170 PRK14170
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 5-280 1.93e-112

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172658 [Multi-domain]  Cd Length: 284  Bit Score: 325.88  E-value: 1.93e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   5 IIKGNEVAEKKRAQLTEEVVKLKEQGIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLAEIDR 84
Cdd:PRK14170   4 IIDGKKLAKEIQEKVTREVAELVKEGKKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSVVEE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  85 LNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKHVVVI 164
Cdd:PRK14170  84 LNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRAVVI 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 165 GRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETGKLCGDVD 244
Cdd:PRK14170 164 GRSNIVGKPVAQLLLNENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDRDENNKLCGDVD 243

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 446148872 245 FDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKR 280
Cdd:PRK14170 244 FDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKR 279
PRK14169 PRK14169
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 3-280 5.52e-111

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184550 [Multi-domain]  Cd Length: 282  Bit Score: 322.28  E-value: 5.52e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   3 AVIIKGNEVAEKKRAQLTEEVVKLKEQGIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLAEI 82
Cdd:PRK14169   1 ATRLDGRAVSKKILADLKQTVAKLAQQDVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAKV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  83 DRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKHVV 162
Cdd:PRK14169  81 AELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRVV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 163 VIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETGKLCGD 242
Cdd:PRK14169 161 IVGRSNIVGRPLAGLMVNHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRGADGKLLGD 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 446148872 243 VDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKR 280
Cdd:PRK14169 241 VDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKR 278
PRK14174 PRK14174
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 4-281 1.50e-110

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


Pssm-ID: 172662 [Multi-domain]  Cd Length: 295  Bit Score: 321.38  E-value: 1.50e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   4 VIIKGNEVAEKKRAQLTEEVVKLKEQ-GIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLAEI 82
Cdd:PRK14174   2 LIIDGKKVSLDLKNELKTRVEAYRAKtGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  83 DRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQ--DTFLPCTPHGIVELVKETNLDISGKH 160
Cdd:PRK14174  82 EDLNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGHldKCFVSCTPYGILELLGRYNIETKGKH 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 161 VVVIGRSNIVGKPVGQLFLNE----NATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLET 236
Cdd:PRK14174 162 CVVVGRSNIVGKPMANLMLQKlkesNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRIED 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446148872 237 G------KLCGDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKRA 281
Cdd:PRK14174 242 PstksgyRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTLQSFERV 292
PRK14176 PRK14176
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 5-280 1.52e-109

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


Pssm-ID: 184553 [Multi-domain]  Cd Length: 287  Bit Score: 318.67  E-value: 1.52e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   5 IIKGNEVAEKKRAQLTEEVVKLK-EQGIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLAEID 83
Cdd:PRK14176  10 IIDGKALAKKIEAEVRSGVERLKsNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELID 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  84 RLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKHVVV 163
Cdd:PRK14176  90 SLNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGKNAVI 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 164 IGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRlETGKLCGDV 243
Cdd:PRK14176 170 VGHSNVVGKPMAAMLLNRNATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITK-EEDKVYGDV 248

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 446148872 244 DFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKR 280
Cdd:PRK14176 249 DFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEK 285
PRK14166 PRK14166
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 5-279 2.05e-109

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


Pssm-ID: 172654 [Multi-domain]  Cd Length: 282  Bit Score: 318.12  E-value: 2.05e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   5 IIKGNEVAEKKRAQLTEEVVKLKEQGIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLAEIDR 84
Cdd:PRK14166   3 LLDGKALSAKIKEELKEKNQFLKSKGIESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALINT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  85 LNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTG-QDTFLPCTPHGIVELVKETNLDISGKHVVV 163
Cdd:PRK14166  83 LNHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGlESGFLPCTPLGVMKLLKAYEIDLEGKDAVI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 164 IGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETGKLCGDV 243
Cdd:PRK14166 163 IGASNIVGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLESGKIVGDV 242

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 446148872 244 DFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAK 279
Cdd:PRK14166 243 DFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAK 278
PRK14173 PRK14173
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 1-280 7.53e-108

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


Pssm-ID: 184551 [Multi-domain]  Cd Length: 287  Bit Score: 314.46  E-value: 7.53e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   1 MVAVIIKGNEVAEKKRAQLTEEVVKLKeqgIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLA 80
Cdd:PRK14173   1 MAARELSGPPAAEAVYAELRARLAKLP---FVPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  81 EIDRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKH 160
Cdd:PRK14173  78 LIARLNADPEVDGILVQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGKE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 161 VVVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRL--ETGK 238
Cdd:PRK14173 158 VVVVGRSNIVGKPLAALLLREDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINRVggNGGR 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 446148872 239 --LCGDVDfDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKR 280
Cdd:PRK14173 238 diLTGDVH-PEVAEVAGALTPVPGGVGPMTVAMLMANTVIAALR 280
PRK14194 PRK14194
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 1-279 9.07e-108

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172682 [Multi-domain]  Cd Length: 301  Bit Score: 314.48  E-value: 9.07e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   1 MVAVIIKGNEVAEKKRAQLTEEVVKLKEQGIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLA 80
Cdd:PRK14194   2 MSAKLIDGKAAAARVLAQVREDVRTLKAAGIEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  81 EIDRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKH 160
Cdd:PRK14194  82 LIAELNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGKH 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 161 VVVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETG--- 237
Cdd:PRK14194 162 AVVIGRSNIVGKPMAALLLQAHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINRIDDDgrs 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 446148872 238 KLCGDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAK 279
Cdd:PRK14194 242 RLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAAR 283
PRK14167 PRK14167
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 5-278 4.37e-107

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


Pssm-ID: 184549 [Multi-domain]  Cd Length: 297  Bit Score: 312.87  E-value: 4.37e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   5 IIKGNEVAEKKRAQLTEEVVKLKEQGIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLAEIDR 84
Cdd:PRK14167   4 IIDGNAVAAQIRDDLTDAIETLEDAGVTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTIDE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  85 LNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKHVVVI 164
Cdd:PRK14167  84 LNADEDVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADVVVV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 165 GRSNIVGKPVGQLFLNE----NATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETG--- 237
Cdd:PRK14167 164 GRSDIVGKPMANLLIQKadggNATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINRVDADtek 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 446148872 238 --KLCGDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESA 278
Cdd:PRK14167 244 gyELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAA 286
PLN02616 PLN02616
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
 3-280 5.93e-105

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 215332 [Multi-domain]  Cd Length: 364  Bit Score: 310.01  E-value: 5.93e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   3 AVIIKGNEVAEKKRAQLTEEVVKLKEQ-GIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLAE 81
Cdd:PLN02616  73 AKVIDGKAVAKKIRDEITIEVSRMKESiGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKF 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  82 IDRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRM-MTGQDT-FLPCTPHGIVELVKETNLDISGK 159
Cdd:PLN02616 153 ISGFNNDPSVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLaMRGREPlFVPCTPKGCIELLHRYNVEIKGK 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 160 HVVVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETG-- 237
Cdd:PLN02616 233 RAVVIGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPVEDAss 312

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 446148872 238 ----KLCGDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKR 280
Cdd:PLN02616 313 prgyRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKR 359
PRK14178 PRK14178
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 4-279 7.67e-105

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172666 [Multi-domain]  Cd Length: 279  Bit Score: 306.38  E-value: 7.67e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   4 VIIKGNEVAEKKRAQLTEEVVklkEQGIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLAEID 83
Cdd:PRK14178   1 MILDGKAVSEKRLELLKEEII---ESGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  84 RLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKHVVV 163
Cdd:PRK14178  78 RLNEDPDINGILVQLPLPKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAVV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 164 IGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLEtGKLCGDV 243
Cdd:PRK14178 158 VGRSIDVGRPMAALLLNADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQVN-GKLCGDV 236

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 446148872 244 DFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAK 279
Cdd:PRK14178 237 DFDAVKEIAGAITPVPGGVGPMTIATLMENTFDAAK 272
PRK14168 PRK14168
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 1-279 4.50e-101

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237633 [Multi-domain]  Cd Length: 297  Bit Score: 297.56  E-value: 4.50e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   1 MVAVIIKGNEVAEKKRAQLTEEVVKLKEQ-GIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLL 79
Cdd:PRK14168   1 MSAKIIKGTEIREEILEEIRGEVAELKEKyGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  80 AEIDRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQD--TFLPCTPHGIVELVKETNLDIS 157
Cdd:PRK14168  81 ALIDKYNNDDSIHGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIGGDevKFLPCTPAGIQEMLVRSGVETS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 158 GKHVVVIGRSNIVGKPVGQLFLNE----NATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNR 233
Cdd:PRK14168 161 GAEVVVVGRSNIVGKPIANMMTQKgpgaNATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVNR 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446148872 234 L----ETGK--LCGDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAK 279
Cdd:PRK14168 241 VgtneSTGKaiLSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAK 292
PLN02516 PLN02516
methylenetetrahydrofolate dehydrogenase (NADP+)
 2-281 1.09e-100

methylenetetrahydrofolate dehydrogenase (NADP+)


Pssm-ID: 178131 [Multi-domain]  Cd Length: 299  Bit Score: 296.80  E-value: 1.09e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   2 VAVIIKGNEVAEKKRAQLTEEVVKLKEQ-GIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLA 80
Cdd:PLN02516   8 VAQIIDGKAIAKAIRSEIAEEVAQLSEKhGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELIS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  81 EIDRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRM-MTGQD-TFLPCTPHGIVELVKETNLDISG 158
Cdd:PLN02516  88 KVHELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLaMKGREpLFLPCTPKGCLELLSRSGIPIKG 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 159 KHVVVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETG- 237
Cdd:PLN02516 168 KKAVVVGRSNIVGLPVSLLLLKADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVSDPs 247

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 446148872 238 -----KLCGDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKRA 281
Cdd:PLN02516 248 kksgyRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKRV 296
PRK14185 PRK14185
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 5-281 4.58e-100

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184556 [Multi-domain]  Cd Length: 293  Bit Score: 294.81  E-value: 4.58e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   5 IIKGNEVAEKKRAQLTEEVVKLKEQG-IVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLAEID 83
Cdd:PRK14185   3 LIDGKAISAQIKQEIAAEVAEIVAKGgKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKVR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  84 RLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKHVVV 163
Cdd:PRK14185  83 ELNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCVV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 164 IGRSNIVGKPVGQLFLNE----NATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETG-- 237
Cdd:PRK14185 163 LGRSNIVGKPMAQLMMQKaypgDCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTRVPDAtr 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 446148872 238 ----KLCGDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKRA 281
Cdd:PRK14185 243 ksgfKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKKA 290
PRK14171 PRK14171
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 5-281 6.13e-100

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172659 [Multi-domain]  Cd Length: 288  Bit Score: 294.17  E-value: 6.13e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   5 IIKGNEVAEKKRAQLTEEVVKLKEQ-GIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLAEID 83
Cdd:PRK14171   4 IIDGKALANEILADLKLEIQELKSQtNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKIN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  84 RLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDT-FLPCTPHGIVELVKETNLDISGKHVV 162
Cdd:PRK14171  84 ELNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSGISQgFIPCTALGCLAVIKKYEPNLTGKNVV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 163 VIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETGKLCGD 242
Cdd:PRK14171 164 IIGRSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRISGNKIIGD 243

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 446148872 243 VDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKRA 281
Cdd:PRK14171 244 VDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKAFKDS 282
PRK14177 PRK14177
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 1-279 1.19e-98

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172665 [Multi-domain]  Cd Length: 284  Bit Score: 290.72  E-value: 1.19e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   1 MVAVIIKGNEVAEKKRAQLTEEVVKLKEQGI-VPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLL 79
Cdd:PRK14177   1 MSPILLDGKKLSEKIRNEIRETIEERKTKNKrIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  80 AEIDRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGK 159
Cdd:PRK14177  81 GVIDKLNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 160 HVVVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNrleTGKL 239
Cdd:PRK14177 161 NAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYN---PGNV 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 446148872 240 cGDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAK 279
Cdd:PRK14177 238 -GDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFK 276
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
123-281 2.53e-98

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


Pssm-ID: 427036  Cd Length: 160  Bit Score: 285.13  E-value: 2.53e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  123 HPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKHVVVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLA 202
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITREA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446148872  203 DILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETGKLCGDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKRA 281
Cdd:pfam02882  81 DIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNTVEAAKRQ 159
PRK14182 PRK14182
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 5-282 9.96e-98

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


Pssm-ID: 172670 [Multi-domain]  Cd Length: 282  Bit Score: 288.46  E-value: 9.96e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   5 IIKGNEVAEKKRAQLTEEVVKLKEQGIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLAEIDR 84
Cdd:PRK14182   3 LIDGKQIAAKVKGEVATEVRALAARGVQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIAR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  85 LNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTG-QDTFLPCTPHGIVELVKETNLDISGKHVVV 163
Cdd:PRK14182  83 LNADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGiAGVPRPCTPAGVMRMLDEARVDPKGKRALV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 164 IGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETGKLCGDV 243
Cdd:PRK14182 163 VGRSNIVGKPMAMMLLERHATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLADGKLVGDV 242

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 446148872 244 DFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKRAG 282
Cdd:PRK14182 243 EFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKRTA 281
PRK14192 PRK14192
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 1-281 2.26e-97

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184561 [Multi-domain]  Cd Length: 283  Bit Score: 287.51  E-value: 2.26e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   1 MVAVIIKGNEVAEKKRAQLTEEVVKLKEQ-GIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLL 79
Cdd:PRK14192   1 MMALVLDGKALAKQIEEELSVRVEALKAKtGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  80 AEIDRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGK 159
Cdd:PRK14192  81 AKIEELNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 160 HVVVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETGKl 239
Cdd:PRK14192 161 HAVVVGRSAILGKPMAMMLLNANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFHPRDGGG- 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 446148872 240 CGDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKRA 281
Cdd:PRK14192 240 VGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKA 281
PLN02897 PLN02897
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
 3-281 4.99e-97

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 178485 [Multi-domain]  Cd Length: 345  Bit Score: 288.78  E-value: 4.99e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   3 AVIIKGNEVAEKKRAQLTEEVVKLKEQ-GIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLAE 81
Cdd:PLN02897  56 TVVIDGNVIAEEIRTKIASEVRKMKKAvGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILSA 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  82 IDRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRM-MTGQDT-FLPCTPHGIVELVKETNLDISGK 159
Cdd:PLN02897 136 LRKFNEDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLaMRGREPlFVSCTPKGCVELLIRSGVEIAGK 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 160 HVVVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETG-- 237
Cdd:PLN02897 216 NAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPVEDSsc 295

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 446148872 238 ----KLCGDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKRA 281
Cdd:PLN02897 296 efgyRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKRI 343
PRK14180 PRK14180
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 4-279 1.56e-94

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


Pssm-ID: 172668 [Multi-domain]  Cd Length: 282  Bit Score: 280.38  E-value: 1.56e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   4 VIIKGNEVAEKKRAQLTEEVVKLKEQ-GIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLAEI 82
Cdd:PRK14180   2 ILIDGKSLSKDLKERLATQVQEYKHHtAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  83 DRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRM-MTGQDTFLPCTPHGIVELVKETNLDISGKHV 161
Cdd:PRK14180  82 DQLNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLqLRDKKCLESCTPKGIMTMLREYGIKTEGAYA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 162 VVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLEtGKLCG 241
Cdd:PRK14180 162 VVVGASNVVGKPVSQLLLNAKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHVD-GKIVG 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 446148872 242 DVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAK 279
Cdd:PRK14180 241 DVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQ 278
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
 115-279 2.26e-93

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: 272.89  E-value: 2.26e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 115 PEKDVDGFHPISVGRMMTGQDTFLPCTPHGIVELVKETNLDISGKHVVVIGRSNIVGKPVGQLFLNENATVTYCHSKTQN 194
Cdd:cd01080    1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKTKN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 195 MKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLE---TGKLCGDVDFDNVLDVAGYITPVPKGVGPMTITMLL 271
Cdd:cd01080   81 LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPdksGGKLVGDVDFESAKEKASAITPVPGGVGPMTVAMLM 160


                 ....*...
gi 446148872 272 HNTVESAK 279
Cdd:cd01080  161 KNTVEAAK 168
PRK14187 PRK14187
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 3-278 3.96e-93

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172675 [Multi-domain]  Cd Length: 294  Bit Score: 277.09  E-value: 3.96e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   3 AVIIKGNEVAEKKRAQLTEEVVKLKEQ-GIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLAE 81
Cdd:PRK14187   2 TNIIDGKKIANDITEILATCIDDLKRQhNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  82 IDRLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQ--DTFLPCTPHGIVELVKETNLDISGK 159
Cdd:PRK14187  82 INELNNDDSVHGILVQLPVPNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQkkNCLIPCTPKGCLYLIKTITRNLSGS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 160 HVVVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETG-- 237
Cdd:PRK14187 162 DAVVIGRSNIVGKPMACLLLGENCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSIEEGgv 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 446148872 238 -KLCGDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESA 278
Cdd:PRK14187 242 kKFVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAA 283
PRK14181 PRK14181
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 4-280 5.90e-92

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172669 [Multi-domain]  Cd Length: 287  Bit Score: 274.05  E-value: 5.90e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   4 VIIKGNEVAEKKRAQLTEEVvklKEQGIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLAEID 83
Cdd:PRK14181   1 MLLKGAPAAEHILATIKENI---SASSTAPGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLIH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872  84 RLNGDDRINGILVQLPLPKHIEEKAIIERISPEKDVDGFHPISVGRMMTGQ-DTFLPCTPHGIVELVKETNLDISGKHVV 162
Cdd:PRK14181  78 RLNNDPNIHGILVQLPLPKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGEtDGFIPCTPAGIIELLKYYEIPLHGRHVA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 163 VIGRSNIVGKPVGQLFLNE----NATVTYCHSKTQNMKELTKLADILIVAVGRPKMVTADYLKEGAVVIDVGVNRLETGK 238
Cdd:PRK14181 158 IVGRSNIVGKPLAALLMQKhpdtNATVTLLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRVPAAN 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 446148872 239 -----LCGDVDFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAKR 280
Cdd:PRK14181 238 pkgyiLVGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNTWESYLR 284
THF_DHG_CYH pfam00763
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
6-120 2.80e-63

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;


Pssm-ID: 459930 [Multi-domain]  Cd Length: 115  Bit Score: 194.55  E-value: 2.80e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872    6 IKGNEVAEKKRAQLTEEVVKLKEQGIVPGLAVILVGEDPASRSYVKGKEKGCEQVGIYSELIEFPETITEERLLAEIDRL 85
Cdd:pfam00763   1 IDGKAIAKKIREELKEEVAALKAGGRKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKL 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 446148872   86 NGDDRINGILVQLPLPKHIEEKAIIERISPEKDVD 120
Cdd:pfam00763  81 NADPSVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115
NAD_bind_m-THF_DH_Cyclohyd_like cd05212
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ...
 138-279 2.90e-32

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: 116.07  E-value: 2.90e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 138 LPCTPHGIVELVKET-------NLDISGKHVVVIGRSNIVGKPVGQLFLNENATVTYCHSKTQNMKELTKLADILIVAVG 210
Cdd:cd05212    1 GPCTPLFVSPVAKAVkellnkeGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446148872 211 RPKMVTADYLKEGAVVIDVGVNRLEtgklcgdvdFDNVLDVAGYITPVPKGVGPMTITMLLHNTVESAK 279
Cdd:cd05212   81 KPEKVPTEWIKPGATVINCSPTKLS---------GDDVKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140
NAD_bind_m-THF_DH cd01079
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ...
 115-275 5.30e-14

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: 68.99  E-value: 5.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 115 PEKDVDGFHPISVG------RMMTGQDTF---LPCTPHGIVELVKETN---------LDISGKHVVVIGRSNIVGKPVGQ 176
Cdd:cd01079    1 PHKDVEGLSHKYIFnlyhniRFLDPENRKksiLPCTPLAIVKILEFLGiynkilpygNRLYGKTITIINRSEVVGRPLAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 177 LFLNENATV---------------------TYCHSKTQNMKELTKLADILIVAVGRPKM-VTADYLKEGAVVIDVGvnrl 234
Cdd:cd01079   81 LLANDGARVysvdingiqvftrgesirhekHHVTDEEAMTLDCLSQSDVVITGVPSPNYkVPTELLKDGAICINFA---- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446148872 235 etgklCGDVDFDNVLDVAGYITPVpkgVGPMTITMLLHNTV 275
Cdd:cd01079  157 -----SIKNFEPSVKEKASIYVPS---IGKVTIAMLLRNLL 189
NAD_bind_amino_acid_DH cd05191
NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH) ...
 140-230 8.78e-05

NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and are found in glutamate, leucine, and phenylalanine DHs (DHs), methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate 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: 133449 [Multi-domain]  Cd Length: 86  Bit Score: 40.44  E-value: 8.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872 140 CTPHGIVELVKE----TNLDISGKHVVVIGRSNiVGKPVGQLFLNE-NATVTYCHSktqnmkeltklaDILIVAVGRPKM 214
Cdd:cd05191    1 ATAAGAVALLKAagkvTNKSLKGKTVVVLGAGE-VGKGIAKLLADEgGKKVVLCDR------------DILVTATPAGVP 67

                         90
                 ....*....|....*....
gi 446148872 215 VTAD---YLKEGAVVIDVG 230
Cdd:cd05191   68 VLEEataKINEGAVVIDLA 86
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
148-230 2.78e-03

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 37.43  E-value: 2.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446148872   148 LVKETNLDISGKHVVVIGRSNiVGKPVGQLFLNENATVTYCHS-------------KTQNMKELTKLADILIVAVGRPKM 214
Cdd:smart00997  13 ILRATNVLLAGKNVVVAGYGD-VGKGVAARLRGLGARVIVTEIdpiraleaamdgfEVMKMEEAAKRADIFVTATGNKDV 91

                           90
                   ....*....|....*....
gi 446148872   215 VTADYL---KEGAVVIDVG 230
Cdd:smart00997  92 ITREHFramKDGAILANAG 110
 
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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