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Conserved domains on  [gi|499238903|ref|WP_010936443|]
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bifunctional 5,10-methylenetetrahydrofolate dehydrogenase/5,10-methenyltetrahydrofolate cyclohydrolase [Dehalococcoides mccartyi]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
1-294 1.57e-177

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


:

Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 491.07  E-value: 1.57e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   1 MSAHIINGTEIAAAIREEIRSEVTALKAKhGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:COG0190    1 MMAQILDGKAVAAEIREELKERVAALKAK-GITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:COG0190   80 ALIDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTcig 240
Cdd:COG0190  160 HAVVVGRSNIVGKPLALLLLRR----NATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGIN--- 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499238903 241 YTPEGKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGL 294
Cdd:COG0190  233 RVEDGK--LVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQAGL 284
 
Name Accession Description Interval E-value
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
1-294 1.57e-177

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


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 491.07  E-value: 1.57e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   1 MSAHIINGTEIAAAIREEIRSEVTALKAKhGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:COG0190    1 MMAQILDGKAVAAEIREELKERVAALKAK-GITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:COG0190   80 ALIDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTcig 240
Cdd:COG0190  160 HAVVVGRSNIVGKPLALLLLRR----NATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGIN--- 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499238903 241 YTPEGKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGL 294
Cdd:COG0190  233 RVEDGK--LVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQAGL 284
PRK14190 PRK14190
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
1-294 3.22e-167

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


Pssm-ID: 184560 [Multi-domain]  Cd Length: 284  Bit Score: 464.87  E-value: 3.22e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   1 MSAHIINGTEIAAAIREEIRSEVTALKaKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:PRK14190   1 MMAVIIDGKEVAKEKREQLKEEVVKLK-EQGIVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PRK14190  80 ALIDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIG 240
Cdd:PRK14190 160 HVVVVGRSNIVGKPVGQLLLNE----NATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRLE 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499238903 241 YTPegkriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGL 294
Cdd:PRK14190 236 NGK-----LCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKRAGGR 284
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
116-289 5.51e-89

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: 262.49  E-value: 5.51e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 116 PDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHVVIVGRSNLVGKPLANILLQkapgANATVTICHS 195
Cdd:cd01080    1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLN----RNATVTVCHS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 196 GTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIGytPEGKRILSGDVDFEAVKEKAFAITPVPKGVGPM 275
Cdd:cd01080   77 KTKNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVP--DKSGGKLVGDVDFESAKEKASAITPVPGGVGPM 154
                        170
                 ....*....|....
gi 499238903 276 TIIMLMLNTLTAAK 289
Cdd:cd01080  155 TVAMLMKNTVEAAK 168
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
124-292 3.93e-88

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


Pssm-ID: 427036  Cd Length: 160  Bit Score: 259.71  E-value: 3.93e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  124 HPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHVVIVGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLI 203
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA----NATVTVCHSKTKDLAEI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  204 TSQADILVSAMGKPKFITADMVRQGAVVIDVGTtcigyTPEGKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLN 283
Cdd:pfam02882  77 TREADIVVVAVGKPELIKADWIKPGAVVIDVGI-----NRVGNGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQN 151

                  ....*....
gi 499238903  284 TLTAAKRAA 292
Cdd:pfam02882 152 TVEAAKRQL 160
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
187-234 4.67e-04

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


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 39.80  E-value: 4.67e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 499238903   187 NATVTICHSGTKNLPLITSQADILVSAM-----GKPKFITADMVRQ---GAVVIDV 234
Cdd:smart01002  64 GARFTTLYSQAELLEEAVKEADLVIGAVlipgaKAPKLVTREMVKSmkpGSVIVDV 119
 
Name Accession Description Interval E-value
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
1-294 1.57e-177

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


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 491.07  E-value: 1.57e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   1 MSAHIINGTEIAAAIREEIRSEVTALKAKhGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:COG0190    1 MMAQILDGKAVAAEIREELKERVAALKAK-GITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:COG0190   80 ALIDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTcig 240
Cdd:COG0190  160 HAVVVGRSNIVGKPLALLLLRR----NATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGIN--- 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499238903 241 YTPEGKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGL 294
Cdd:COG0190  233 RVEDGK--LVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQAGL 284
PRK14190 PRK14190
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
1-294 3.22e-167

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


Pssm-ID: 184560 [Multi-domain]  Cd Length: 284  Bit Score: 464.87  E-value: 3.22e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   1 MSAHIINGTEIAAAIREEIRSEVTALKaKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:PRK14190   1 MMAVIIDGKEVAKEKREQLKEEVVKLK-EQGIVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PRK14190  80 ALIDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIG 240
Cdd:PRK14190 160 HVVVVGRSNIVGKPVGQLLLNE----NATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRLE 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499238903 241 YTPegkriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGL 294
Cdd:PRK14190 236 NGK-----LCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKRAGGR 284
PRK14189 PRK14189
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
1-293 1.83e-131

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 184559 [Multi-domain]  Cd Length: 285  Bit Score: 374.41  E-value: 1.83e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   1 MSAHIINGTEIAAAIREEIRSEVTALKAKhGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:PRK14189   1 MTAQLIDGNALSKQLRAEAAQRAAALTAR-GHQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PRK14189  80 ARIDELNRDPKIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGttcIG 240
Cdd:PRK14189 160 HAVVIGRSNIVGKPMAMLLLQ----AGATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVG---MN 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499238903 241 YTPEGKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAG 293
Cdd:PRK14189 233 RDDAGK--LCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAERAAA 283
PRK14188 PRK14188
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
3-294 9.44e-129

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184558 [Multi-domain]  Cd Length: 296  Bit Score: 368.13  E-value: 9.44e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   3 AHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTL 82
Cdd:PRK14188   2 ATIIDGKAFAADVRATVAAEVARLKAAHGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  83 IARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHV 162
Cdd:PRK14188  82 IARLNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLNA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 163 VIVGRSNLVGKPLANILLqkapGANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIGY- 241
Cdd:PRK14188 162 VVIGRSNLVGKPMAQLLL----AANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIPAp 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499238903 242 -TPEGKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGL 294
Cdd:PRK14188 238 eKGEGKTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACRAAGL 291
PRK14184 PRK14184
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
4-294 9.89e-122

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


Pssm-ID: 237635 [Multi-domain]  Cd Length: 286  Bit Score: 349.84  E-value: 9.89e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   4 HIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLI 83
Cdd:PRK14184   2 LLLDGKATAATIREELKTEVAALTARHGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  84 ARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHVV 163
Cdd:PRK14184  82 AELNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 164 IVGRSNLVGKPLANILLQKAPGANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGttcIGYTP 243
Cdd:PRK14184 162 VVGRSNIVGKPLALMLGAPGKFANATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVG---INRTD 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499238903 244 EGkriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGL 294
Cdd:PRK14184 239 DG---LVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQSWKERVGL 286
PRK10792 PRK10792
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-288 8.19e-121

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 236760 [Multi-domain]  Cd Length: 285  Bit Score: 347.67  E-value: 8.19e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   1 MSAHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:PRK10792   1 MTAKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PRK10792  81 ALIDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGttcIG 240
Cdd:PRK10792 161 NAVVVGASNIVGRPMSLELLL----AGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVG---IN 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 499238903 241 YTPEGKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAA 288
Cdd:PRK10792 234 RLEDGK--LVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQAC 279
PRK14168 PRK14168
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-294 2.14e-117

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237633 [Multi-domain]  Cd Length: 297  Bit Score: 339.54  E-value: 2.14e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   1 MSAHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:PRK14168   1 MSAKIIKGTEIREEILEEIRGEVAELKEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLG--EPCFLPCTPHGVQELLIRSGIKIE 158
Cdd:PRK14168  81 ALIDKYNNDDSIHGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIGgdEVKFLPCTPAGIQEMLVRSGVETS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 159 GTHVVIVGRSNLVGKPLANILLQKAPGANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTC 238
Cdd:PRK14168 161 GAEVVVVGRSNIVGKPIANMMTQKGPGANATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVNR 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499238903 239 IGYTPE-GKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGL 294
Cdd:PRK14168 241 VGTNEStGKAILSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAKFHLSL 297
PRK14191 PRK14191
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
5-289 2.10e-116

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172679 [Multi-domain]  Cd Length: 285  Bit Score: 336.35  E-value: 2.10e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   5 IINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIA 84
Cdd:PRK14191   3 LLDGKALSYKIEKDLKNKIQILTAQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLIK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  85 RLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHVVI 164
Cdd:PRK14191  83 DLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVVI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 165 VGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGttcIGYTPE 244
Cdd:PRK14191 163 IGASNIVGKPLAMLMLN----AGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIG---INRLND 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 499238903 245 GKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAK 289
Cdd:PRK14191 236 GR--LVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAE 278
PRK14174 PRK14174
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
5-294 4.43e-115

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


Pssm-ID: 172662 [Multi-domain]  Cd Length: 295  Bit Score: 333.32  E-value: 4.43e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   5 IINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIA 84
Cdd:PRK14174   3 IIDGKKVSLDLKNELKTRVEAYRAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKIE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  85 RLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLG--EPCFLPCTPHGVQELLIRSGIKIEGTHV 162
Cdd:PRK14174  83 DLNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGhlDKCFVSCTPYGILELLGRYNIETKGKHC 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 163 VIVGRSNLVGKPLANILLQKAPGANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCI--G 240
Cdd:PRK14174 163 VVVGRSNIVGKPMANLMLQKLKESNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRIedP 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499238903 241 YTPEGKRiLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGL 294
Cdd:PRK14174 243 STKSGYR-LVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTLQSFERVNNL 295
PRK14193 PRK14193
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
1-293 1.64e-114

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


Pssm-ID: 237637 [Multi-domain]  Cd Length: 284  Bit Score: 331.59  E-value: 1.64e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   1 MSAHIINGTEIAAAIREEIRSEVTALKAKhGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:PRK14193   1 MTAIILDGKATADEIKADLAERVAALKEK-GITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PRK14193  80 AVIDELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQKAPgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIG 240
Cdd:PRK14193 160 HVVVIGRGVTVGRPIGLLLTRRSE--NATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSRAG 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499238903 241 ytpEGKriLSGDVDfEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAG 293
Cdd:PRK14193 238 ---DGK--LVGDVH-PDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAERRAG 284
PRK14167 PRK14167
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
3-294 4.49e-114

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


Pssm-ID: 184549 [Multi-domain]  Cd Length: 297  Bit Score: 330.97  E-value: 4.49e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   3 AHIINGTEIAAAIREEIRSEVTALkAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTL 82
Cdd:PRK14167   2 TEIIDGNAVAAQIRDDLTDAIETL-EDAGVTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  83 IARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHV 162
Cdd:PRK14167  81 IDELNADEDVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 163 VIVGRSNLVGKPLANILLQKAPGANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIGYT 242
Cdd:PRK14167 161 VVVGRSDIVGKPMANLLIQKADGGNATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINRVDAD 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499238903 243 PEGKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGL 294
Cdd:PRK14167 241 TEKGYELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAASLQEGV 292
PRK14186 PRK14186
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
3-294 3.44e-110

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237636 [Multi-domain]  Cd Length: 297  Bit Score: 320.86  E-value: 3.44e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   3 AHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTL 82
Cdd:PRK14186   2 ALILDGKALAAEIEQRLQAQIESNLPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  83 IARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHV 162
Cdd:PRK14186  82 IAQLNQDERVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKKA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 163 VIVGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIGyT 242
Cdd:PRK14186 162 VVVGRSILVGKPLALMLLA----ANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHRLP-S 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499238903 243 PEGKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGL 294
Cdd:PRK14186 237 SDGKTRLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSWQKRHGL 288
PRK14179 PRK14179
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
3-290 3.19e-109

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 237634 [Multi-domain]  Cd Length: 284  Bit Score: 318.23  E-value: 3.19e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   3 AHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTL 82
Cdd:PRK14179   2 TEIIDGKALAQKMQAELAEKVAKLKEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  83 IARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHV 162
Cdd:PRK14179  82 IERYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 163 VIVGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGttcIGYT 242
Cdd:PRK14179 162 VVIGRSNIVGKPMAQLLLDK----NATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVG---MNRD 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 499238903 243 PEGKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKR 290
Cdd:PRK14179 235 ENGK--LIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALR 280
PRK14173 PRK14173
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
1-293 1.29e-106

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


Pssm-ID: 184551 [Multi-domain]  Cd Length: 287  Bit Score: 311.76  E-value: 1.29e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   1 MSAHIINGTEIAAAIREEIRSEVTALKAkhgiVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:PRK14173   1 MAARELSGPPAAEAVYAELRARLAKLPF----VPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PRK14173  77 ELIARLNADPEVDGILVQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLqkapGANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIG 240
Cdd:PRK14173 157 EVVVVGRSNIVGKPLAALLL----REDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINRVG 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499238903 241 yTPEGKRILSGDVDFEaVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAG 293
Cdd:PRK14173 233 -GNGGRDILTGDVHPE-VAEVAGALTPVPGGVGPMTVAMLMANTVIAALRRRG 283
PRK14176 PRK14176
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
5-292 3.73e-106

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


Pssm-ID: 184553 [Multi-domain]  Cd Length: 287  Bit Score: 310.58  E-value: 3.73e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   5 IINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIA 84
Cdd:PRK14176  10 IIDGKALAKKIEAEVRSGVERLKSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELID 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  85 RLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHVVI 164
Cdd:PRK14176  90 SLNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGKNAVI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 165 VGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTcigyTPE 244
Cdd:PRK14176 170 VGHSNVVGKPMAAMLLNR----NATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGIT----KEE 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 499238903 245 GKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAA 292
Cdd:PRK14176 242 DK--VYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEKSL 287
PRK14175 PRK14175
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-296 4.95e-104

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184552 [Multi-domain]  Cd Length: 286  Bit Score: 304.92  E-value: 4.95e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   1 MSAHIINGTEIAAAIREEIRSEVTALKAKhGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:PRK14175   1 MVAKILDGKQIAKDYRQGLQDQVEALKEK-GFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PRK14175  80 NELNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTtcig 240
Cdd:PRK14175 160 NAVVIGRSHIVGQPVSKLLLQ----KNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVGN---- 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499238903 241 yTPEGKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGLVK 296
Cdd:PRK14175 232 -TPDENGKLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEKMRRGIDS 286
PRK14183 PRK14183
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
5-292 5.11e-100

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


Pssm-ID: 184555 [Multi-domain]  Cd Length: 281  Bit Score: 294.81  E-value: 5.11e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   5 IINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIA 84
Cdd:PRK14183   3 ILDGKALSDKIKENVKKEVDELKLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETIA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  85 RLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHVVI 164
Cdd:PRK14183  83 MMNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVCV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 165 VGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGttcIGYTPE 244
Cdd:PRK14183 163 VGASNIVGKPMAALLLN----ANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIG---INRTED 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 499238903 245 GKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAA 292
Cdd:PRK14183 236 GR--LVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKNRA 281
PRK14185 PRK14185
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
5-291 6.98e-100

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184556 [Multi-domain]  Cd Length: 293  Bit Score: 294.81  E-value: 6.98e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   5 IINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIA 84
Cdd:PRK14185   3 LIDGKAISAQIKQEIAAEVAEIVAKGGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKVR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  85 RLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHVVI 164
Cdd:PRK14185  83 ELNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCVV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 165 VGRSNLVGKPLANILLQKAPGANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCI--GYT 242
Cdd:PRK14185 163 LGRSNIVGKPMAQLMMQKAYPGDCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTRVpdATR 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 499238903 243 PEGKRiLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRA 291
Cdd:PRK14185 243 KSGFK-LTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKKA 290
PRK14172 PRK14172
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
5-289 1.62e-98

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


Pssm-ID: 172660 [Multi-domain]  Cd Length: 278  Bit Score: 290.53  E-value: 1.62e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   5 IINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIA 84
Cdd:PRK14172   4 IINGKEVALKIKEEIKNFVEERKENGLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEIE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  85 RLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHVVI 164
Cdd:PRK14172  84 ELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVVV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 165 VGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIgytpE 244
Cdd:PRK14172 164 IGRSNIVGKPVAQLLLNE----NATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSV----N 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 499238903 245 GKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAK 289
Cdd:PRK14172 236 GK--ITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKNVCEALK 278
PRK14194 PRK14194
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-292 1.78e-97

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172682 [Multi-domain]  Cd Length: 301  Bit Score: 289.05  E-value: 1.78e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   1 MSAHIINGTEIAAAIREEIRSEVTALKAKhGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:PRK14194   2 MSAKLIDGKAAAARVLAQVREDVRTLKAA-GIEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PRK14194  81 ALIAELNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIg 240
Cdd:PRK14194 161 HAVVIGRSNIVGKPMAALLLQ----AHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINRI- 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499238903 241 yTPEGKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAA 292
Cdd:PRK14194 236 -DDDGRSRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAARLQA 286
PLN02516 PLN02516
methylenetetrahydrofolate dehydrogenase (NADP+)
3-291 7.91e-97

methylenetetrahydrofolate dehydrogenase (NADP+)


Pssm-ID: 178131 [Multi-domain]  Cd Length: 299  Bit Score: 287.17  E-value: 7.91e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   3 AHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTL 82
Cdd:PLN02516   9 AQIIDGKAIAKAIRSEIAEEVAQLSEKHGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  83 IARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLG--EPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PLN02516  89 VHELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMKgrEPLFLPCTPKGCLELLSRSGIPIKGK 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIG 240
Cdd:PLN02516 169 KAVVVGRSNIVGLPVSLLLLK----ADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVS 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499238903 241 --YTPEGKRILsGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRA 291
Cdd:PLN02516 245 dpSKKSGYRLV-GDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKRV 296
PLN02616 PLN02616
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
2-290 2.72e-96

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 215332 [Multi-domain]  Cd Length: 364  Bit Score: 288.06  E-value: 2.72e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   2 SAHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLT 81
Cdd:PLN02616  72 GAKVIDGKAVAKKIRDEITIEVSRMKESIGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLK 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  82 LIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCL--GEPCFLPCTPHGVQELLIRSGIKIEG 159
Cdd:PLN02616 152 FISGFNNDPSVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMrgREPLFVPCTPKGCIELLHRYNVEIKG 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 160 THVVIVGRSNLVGKPLAnILLQKapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCI 239
Cdd:PLN02616 232 KRAVVIGRSNIVGMPAA-LLLQR---EDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPV 307
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499238903 240 --GYTPEGKRiLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKR 290
Cdd:PLN02616 308 edASSPRGYR-LVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKR 359
PRK14166 PRK14166
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
5-289 8.91e-96

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


Pssm-ID: 172654 [Multi-domain]  Cd Length: 282  Bit Score: 283.84  E-value: 8.91e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   5 IINGTEIAAAIREEIRSEVTALKAKhGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIA 84
Cdd:PRK14166   3 LLDGKALSAKIKEELKEKNQFLKSK-GIESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALIN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  85 RLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLG-EPCFLPCTPHGVQELLIRSGIKIEGTHVV 163
Cdd:PRK14166  82 TLNHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGlESGFLPCTPLGVMKLLKAYEIDLEGKDAV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 164 IVGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGttcIGYTP 243
Cdd:PRK14166 162 IIGASNIVGRPMATMLLN----AGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVG---INRLE 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 499238903 244 EGKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAK 289
Cdd:PRK14166 235 SGK--IVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAK 278
PRK14181 PRK14181
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
11-290 2.39e-95

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172669 [Multi-domain]  Cd Length: 287  Bit Score: 282.91  E-value: 2.39e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  11 IAAAIREEIRSEVTAlkakhgivPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIARLNADP 90
Cdd:PRK14181  12 ILATIKENISASSTA--------PGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLIHRLNNDP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  91 KISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGE-PCFLPCTPHGVQELLIRSGIKIEGTHVVIVGRSN 169
Cdd:PRK14181  84 NIHGILVQLPLPKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGEtDGFIPCTPAGIIELLKYYEIPLHGRHVAIVGRSN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 170 LVGKPLANILLQKAPGANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIGYTPEGKRIL 249
Cdd:PRK14181 164 IVGKPLAALLMQKHPDTNATVTLLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRVPAANPKGYIL 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 499238903 250 SGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKR 290
Cdd:PRK14181 244 VGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNTWESYLR 284
PRK14169 PRK14169
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
3-292 3.48e-95

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184550 [Multi-domain]  Cd Length: 282  Bit Score: 282.60  E-value: 3.48e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   3 AHIINGTEIAAAIREEIRSEVTALkAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTL 82
Cdd:PRK14169   1 ATRLDGRAVSKKILADLKQTVAKL-AQQDVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  83 IARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHV 162
Cdd:PRK14169  80 VAELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 163 VIVGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGttcIGYT 242
Cdd:PRK14169 160 VIVGRSNIVGRPLAGLMVN----HDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVG---ISRG 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 499238903 243 PEGKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAA 292
Cdd:PRK14169 233 ADGK--LLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKRRA 280
PRK14178 PRK14178
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
5-289 2.81e-94

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172666 [Multi-domain]  Cd Length: 279  Bit Score: 279.81  E-value: 2.81e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   5 IINGTEIAAAIREEIRSEVTalkaKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIA 84
Cdd:PRK14178   2 ILDGKAVSEKRLELLKEEII----ESGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  85 RLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHVVI 164
Cdd:PRK14178  78 RLNEDPDINGILVQLPLPKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAVV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 165 VGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIgytpE 244
Cdd:PRK14178 158 VGRSIDVGRPMAALLLN----ADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQV----N 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 499238903 245 GKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAK 289
Cdd:PRK14178 230 GK--LCGDVDFDAVKEIAGAITPVPGGVGPMTIATLMENTFDAAK 272
PRK14192 PRK14192
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-293 9.09e-94

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184561 [Multi-domain]  Cd Length: 283  Bit Score: 278.65  E-value: 9.09e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   1 MSAHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:PRK14192   1 MMALVLDGKALAKQIEEELSVRVEALKAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PRK14192  81 AKIEELNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVgttciG 240
Cdd:PRK14192 161 HAVVVGRSAILGKPMAMMLLN----ANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDA-----G 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499238903 241 YTPEGKRILsGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAG 293
Cdd:PRK14192 232 FHPRDGGGV-GDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKALG 283
PRK14187 PRK14187
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
3-294 5.85e-90

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172675 [Multi-domain]  Cd Length: 294  Bit Score: 269.39  E-value: 5.85e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   3 AHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTL 82
Cdd:PRK14187   2 TNIIDGKKIANDITEILATCIDDLKRQHNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  83 IARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEP--CFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PRK14187  82 INELNNDDSVHGILVQLPVPNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQKknCLIPCTPKGCLYLIKTITRNLSGS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIg 240
Cdd:PRK14187 162 DAVVIGRSNIVGKPMACLLLGE----NCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSI- 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499238903 241 yTPEGKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGL 294
Cdd:PRK14187 237 -EEGGVKKFVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAACNQKGI 289
PRK14177 PRK14177
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-289 1.85e-89

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172665 [Multi-domain]  Cd Length: 284  Bit Score: 268.00  E-value: 1.85e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   1 MSAHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:PRK14177   1 MSPILLDGKKLSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PRK14177  81 GVIDKLNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVgttciG 240
Cdd:PRK14177 161 NAVVVGRSPILGKPMAMLLTE----MNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDA-----G 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 499238903 241 YTPEGkrilSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAK 289
Cdd:PRK14177 232 YNPGN----VGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFK 276
PLN02897 PLN02897
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
2-291 3.28e-89

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 178485 [Multi-domain]  Cd Length: 345  Bit Score: 269.52  E-value: 3.28e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   2 SAHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLT 81
Cdd:PLN02897  55 KTVVIDGNVIAEEIRTKIASEVRKMKKAVGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILS 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  82 LIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCL--GEPCFLPCTPHGVQELLIRSGIKIEG 159
Cdd:PLN02897 135 ALRKFNEDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMrgREPLFVSCTPKGCVELLIRSGVEIAG 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 160 THVVIVGRSNLVGKPLAnILLQKapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCI 239
Cdd:PLN02897 215 KNAVVIGRSNIVGLPMS-LLLQR---HDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPV 290
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499238903 240 -GYTPEGKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRA 291
Cdd:PLN02897 291 eDSSCEFGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKRI 343
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
116-289 5.51e-89

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: 262.49  E-value: 5.51e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 116 PDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHVVIVGRSNLVGKPLANILLQkapgANATVTICHS 195
Cdd:cd01080    1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLN----RNATVTVCHS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 196 GTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIGytPEGKRILSGDVDFEAVKEKAFAITPVPKGVGPM 275
Cdd:cd01080   77 KTKNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVP--DKSGGKLVGDVDFESAKEKASAITPVPGGVGPM 154
                        170
                 ....*....|....
gi 499238903 276 TIIMLMLNTLTAAK 289
Cdd:cd01080  155 TVAMLMKNTVEAAK 168
PRK14180 PRK14180
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
5-289 7.34e-89

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


Pssm-ID: 172668 [Multi-domain]  Cd Length: 282  Bit Score: 266.51  E-value: 7.34e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   5 IINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIA 84
Cdd:PRK14180   3 LIDGKSLSKDLKERLATQVQEYKHHTAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELID 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  85 RLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCL-GEPCFLPCTPHGVQELLIRSGIKIEGTHVV 163
Cdd:PRK14180  83 QLNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLQLrDKKCLESCTPKGIMTMLREYGIKTEGAYAV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 164 IVGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIgytp 243
Cdd:PRK14180 163 VVGASNVVGKPVSQLLLN----AKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHV---- 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 499238903 244 EGKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAK 289
Cdd:PRK14180 235 DGK--IVGDVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQ 278
PRK14182 PRK14182
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
5-292 7.55e-89

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


Pssm-ID: 172670 [Multi-domain]  Cd Length: 282  Bit Score: 266.50  E-value: 7.55e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   5 IINGTEIAAAIREEIRSEVTALKAKhGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIA 84
Cdd:PRK14182   3 LIDGKQIAAKVKGEVATEVRALAAR-GVQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  85 RLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCF-LPCTPHGVQELLIRSGIKIEGTHVV 163
Cdd:PRK14182  82 RLNADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGVpRPCTPAGVMRMLDEARVDPKGKRAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 164 IVGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIGytp 243
Cdd:PRK14182 162 VVGRSNIVGKPMAMMLLER----HATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLA--- 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 499238903 244 EGKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAA 292
Cdd:PRK14182 235 DGK--LVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKRTA 281
PRK14170 PRK14170
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
3-290 1.59e-88

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172658 [Multi-domain]  Cd Length: 284  Bit Score: 265.40  E-value: 1.59e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   3 AHIINGTEIAAAIREEIRSEVTALkAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTL 82
Cdd:PRK14170   2 GEIIDGKKLAKEIQEKVTREVAEL-VKEGKKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  83 IARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHV 162
Cdd:PRK14170  81 VEELNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 163 VIVGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTtcigyT 242
Cdd:PRK14170 161 VVIGRSNIVGKPVAQLLLNE----NATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGM-----D 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 499238903 243 PEGKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKR 290
Cdd:PRK14170 232 RDENNKLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKR 279
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
124-292 3.93e-88

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


Pssm-ID: 427036  Cd Length: 160  Bit Score: 259.71  E-value: 3.93e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  124 HPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHVVIVGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLI 203
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA----NATVTVCHSKTKDLAEI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  204 TSQADILVSAMGKPKFITADMVRQGAVVIDVGTtcigyTPEGKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLN 283
Cdd:pfam02882  77 TREADIVVVAVGKPELIKADWIKPGAVVIDVGI-----NRVGNGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQN 151

                  ....*....
gi 499238903  284 TLTAAKRAA 292
Cdd:pfam02882 152 TVEAAKRQL 160
PRK14171 PRK14171
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
4-295 9.62e-86

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172659 [Multi-domain]  Cd Length: 288  Bit Score: 258.73  E-value: 9.62e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903   4 HIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLI 83
Cdd:PRK14171   3 NIIDGKALANEILADLKLEIQELKSQTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903  84 ARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLG-EPCFLPCTPHGVQELLIRSGIKIEGTHV 162
Cdd:PRK14171  83 NELNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSGiSQGFIPCTALGCLAVIKKYEPNLTGKNV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 163 VIVGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIGyt 242
Cdd:PRK14171 163 VIIGRSNIVGKPLSALLLKE----NCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRIS-- 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499238903 243 peGKRILsGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGLV 295
Cdd:PRK14171 237 --GNKII-GDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKAFKDSLYTL 286
THF_DHG_CYH pfam00763
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
6-121 3.83e-58

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;


Pssm-ID: 459930 [Multi-domain]  Cd Length: 115  Bit Score: 181.83  E-value: 3.83e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903    6 INGTEIAAAIREEIRSEVTALKAkHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIAR 85
Cdd:pfam00763   1 IDGKAIAKKIREELKEEVAALKA-GGRKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDK 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 499238903   86 LNADPKISGILVQVPLPVQISENLVLNAINPDKDVD 121
Cdd:pfam00763  80 LNADPSVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115
NAD_bind_m-THF_DH_Cyclohyd_like cd05212
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ...
136-289 6.97e-24

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: 94.50  E-value: 6.97e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 136 PCFLPCTPHGVQELLIRSGIKIEGTHVVIVGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMG 215
Cdd:cd05212    5 PLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRD----GATVYSCDWKTIQLQSKVHDADVVVVGSP 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499238903 216 KPKFITADMVRQGAVVIDVGTTcigytpegkrILSGDVdfeaVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAK 289
Cdd:cd05212   81 KPEKVPTEWIKPGATVINCSPT----------KLSGDD----VKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140
NAD_bind_m-THF_DH cd01079
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ...
116-285 5.33e-13

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: 66.30  E-value: 5.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 116 PDKDVDGFHPVNVGRMCLGE---------PCFLPCTP---------HGVQELLIRSGIKIEGTHVVIVGRSNLVGKPLAN 177
Cdd:cd01079    1 PHKDVEGLSHKYIFNLYHNIrfldpenrkKSILPCTPlaivkilefLGIYNKILPYGNRLYGKTITIINRSEVVGRPLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 178 IL-----------------LQKAPGANATVTICHSGTKNLPLITSQADILVSAMGKPKF-ITADMVRQGAVVIDVgttci 239
Cdd:cd01079   81 LLandgarvysvdingiqvFTRGESIRHEKHHVTDEEAMTLDCLSQSDVVITGVPSPNYkVPTELLKDGAICINF----- 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 499238903 240 gytpegkrilSGDVDFEA-VKEKAFAITPVpkgVGPMTIIMLMLNTL 285
Cdd:cd01079  156 ----------ASIKNFEPsVKEKASIYVPS---IGKVTIAMLLRNLL 189
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
187-234 4.67e-04

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


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 39.80  E-value: 4.67e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 499238903   187 NATVTICHSGTKNLPLITSQADILVSAM-----GKPKFITADMVRQ---GAVVIDV 234
Cdd:smart01002  64 GARFTTLYSQAELLEEAVKEADLVIGAVlipgaKAPKLVTREMVKSmkpGSVIVDV 119
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
190-234 7.65e-03

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


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 37.38  E-value: 7.65e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499238903 190 VTICHSGTKNLPLITSQADILVSAM----GK-PKFITADMVRQ---GAVVIDV 234
Cdd:cd05305  215 VTTLYSNPANLEEALKEADLVIGAVlipgAKaPKLVTEEMVKTmkpGSVIVDV 267
 
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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