NCBI Conserved Domain Search

Conserved domains on [gi|489043168|ref|WP_002953468|]

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bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD [Campylobacter showae]

Protein Classification

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

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

CATH: 3.40.50.720|3.40.430.10

EC: 1.5.1.5|3.5.4.9

Gene Ontology: GO:0004488|GO:0003824|GO:0016787|GO:0009086|GO:0006164|GO:0006730

PubMed: 8485162

SCOP: 4000102

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

FolD

COG0190

5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...

1-283

0e+00

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

Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 503.01 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   1 MTILDGKNVSAQVKERVKNEALNLKNQGIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALI 80
Cdd:COG0190    3 AQILDGKAVAAEIREELKERVAALKAKGITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLALI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  81 DVLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAV 160
Cdd:COG0190   83 DELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHAV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 161 VIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDGKLKGD 240
Cdd:COG0190  163 VVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVEDGKLVGD 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 489043168 241 VKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKNRSKKA 283
Cdd:COG0190  243 VDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQAGLR 285

Name

Accession

Description

Interval

E-value

FolD

COG0190

5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...

1-283

0e+00

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

Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 503.01 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   1 MTILDGKNVSAQVKERVKNEALNLKNQGIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALI 80
Cdd:COG0190    3 AQILDGKAVAAEIREELKERVAALKAKGITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLALI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  81 DVLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAV 160
Cdd:COG0190   83 DELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHAV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 161 VIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDGKLKGD 240
Cdd:COG0190  163 VVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVEDGKLVGD 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 489043168 241 VKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKNRSKKA 283
Cdd:COG0190  243 VDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQAGLR 285

PRK14191

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

1-282

4.25e-167

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 464.24 E-value: 4.25e-167

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   1 MTILDGKNVSAQVKERVKNEALNLK-NQGIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIAL 79
Cdd:PRK14191   1 MVLLDGKALSYKIEKDLKNKIQILTaQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  80 IDVLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNA 159
Cdd:PRK14191  81 IKDLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 160 VVIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDGKLKG 239
Cdd:PRK14191 161 VIIGASNIVGKPLAMLMLNAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLNDGRLVG 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 489043168 240 DVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKNRSKK 282
Cdd:PRK14191 241 DVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEKRQRK 283

THF_DHG_CYH_C

pfam02882

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

123-279

4.12e-97

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

Pssm-ID: 427036 Cd Length: 160 Bit Score: 282.05 E-value: 4.12e-97

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  123 INVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAVVIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADI 202
Cdd:pfam02882   3 YNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITREADI 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489043168  203 LVAAIGRADFVTADMVKDGAVVIDVGINRMDDGKLKGDVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKNR 279
Cdd:pfam02882  83 VVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNTVEAAKRQ 159

NAD_bind_m-THF_DH_Cyclohyd

cd01080

NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...

113-277

7.38e-92

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: 269.04 E-value: 7.38e-92

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 113 PAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAVVIGRSNMVGKPMANLLLNANATVTVTHSKTRN 192
Cdd:cd01080    1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKTKN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 193 LKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDD---GKLKGDVKFDEVAPKCSFITPVPGGVGPMTIAMLL 269
Cdd:cd01080   81 LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDksgGKLVGDVDFESAKEKASAITPVPGGVGPMTVAMLM 160


                 ....*...
gi 489043168 270 SNTIKSAK 277
Cdd:cd01080  161 KNTVEAAK 168

AdoHcyase_NAD

smart00997

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

146-230

3.07e-04

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

Pssm-ID: 198065 [Multi-domain] Cd Length: 162 Bit Score: 40.51 E-value: 3.07e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   146 IFKAYDINLEGKNAVVIGRSnMVGKPMANLLLNANATVTVTHS-------------KTRNLKEICANADILVAAIGRADF 212
Cdd:smart00997  13 ILRATNVLLAGKNVVVAGYG-DVGKGVAARLRGLGARVIVTEIdpiraleaamdgfEVMKMEEAAKRADIFVTATGNKDV 91

                           90       100
                   ....*....|....*....|....*.
gi 489043168   213 VTADM---VKDGAVV-----IDVGIN 230
Cdd:smart00997  92 ITREHfraMKDGAILanaghFDVEID 117

Name

Accession

Description

Interval

E-value

FolD

COG0190

5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...

1-283

0e+00

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

Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 503.01 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   1 MTILDGKNVSAQVKERVKNEALNLKNQGIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALI 80
Cdd:COG0190    3 AQILDGKAVAAEIREELKERVAALKAKGITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLALI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  81 DVLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAV 160
Cdd:COG0190   83 DELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHAV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 161 VIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDGKLKGD 240
Cdd:COG0190  163 VVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVEDGKLVGD 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 489043168 241 VKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKNRSKKA 283
Cdd:COG0190  243 VDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQAGLR 285

PRK14191

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

1-282

4.25e-167

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 464.24 E-value: 4.25e-167

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   1 MTILDGKNVSAQVKERVKNEALNLK-NQGIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIAL 79
Cdd:PRK14191   1 MVLLDGKALSYKIEKDLKNKIQILTaQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  80 IDVLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNA 159
Cdd:PRK14191  81 IKDLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 160 VVIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDGKLKG 239
Cdd:PRK14191 161 VIIGASNIVGKPLAMLMLNAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLNDGRLVG 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 489043168 240 DVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKNRSKK 282
Cdd:PRK14191 241 DVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEKRQRK 283

PRK14190

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

2-277

2.82e-144

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

Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 406.32 E-value: 2.82e-144

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   2 TILDGKNVSAQVKERVKNEALNLKNQGIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALID 81
Cdd:PRK14190   4 VIIDGKEVAKEKREQLKEEVVKLKEQGIVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLALID 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  82 VLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAVV 161
Cdd:PRK14190  84 RLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGKHVVV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 162 IGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDGKLKGDV 241
Cdd:PRK14190 164 VGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRLENGKLCGDV 243

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 489043168 242 KFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAK 277
Cdd:PRK14190 244 DFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAK 279

PRK14188

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

2-277

1.26e-141

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 400.10 E-value: 1.26e-141

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   2 TILDGKNVSAQVKERVKNEALNLKNQ-GIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALI 80
Cdd:PRK14188   3 TIIDGKAFAADVRATVAAEVARLKAAhGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLALI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  81 DVLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAV 160
Cdd:PRK14188  83 ARLNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLNAV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 161 VIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMD-----DG 235
Cdd:PRK14188 163 VIGRSNLVGKPMAQLLLAANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIPapekgEG 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 489043168 236 K--LKGDVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAK 277
Cdd:PRK14188 243 KtrLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAAC 286

PRK14189

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;

2-283

1.70e-134

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;

Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 381.73 E-value: 1.70e-134

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   2 TILDGKNVSAQVKERVKNEALNLKNQGIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALID 81
Cdd:PRK14189   4 QLIDGNALSKQLRAEAAQRAAALTARGHQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLARID 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  82 VLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAVV 161
Cdd:PRK14189  84 ELNRDPKIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGAHAVV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 162 IGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDGKLKGDV 241
Cdd:PRK14189 164 IGRSNIVGKPMAMLLLQAGATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMNRDDAGKLCGDV 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 489043168 242 KFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKNRSKKA 283
Cdd:PRK14189 244 DFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAERAAAAA 285

PRK14179

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;

1-282

4.49e-134

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;

Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 380.64 E-value: 4.49e-134

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   1 MTILDGKNVSAQVKERVKNEALNLK-NQGIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIAL 79
Cdd:PRK14179   2 TEIIDGKALAQKMQAELAEKVAKLKeEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  80 IDVLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNA 159
Cdd:PRK14179  82 IERYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 160 VVIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDGKLKG 239
Cdd:PRK14179 162 VVIGRSNIVGKPMAQLLLDKNATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMNRDENGKLIG 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 489043168 240 DVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKNRSKK 282
Cdd:PRK14179 242 DVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALRSLHK 284

PRK10792

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

1-279

1.91e-133

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 378.88 E-value: 1.91e-133

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   1 MT--ILDGKNVSAQVKERVKNEALNLKNQGIE-PALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELI 77
Cdd:PRK10792   1 MTakIIDGKTIAQQVRSEVAQKVQARVAAGLRaPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  78 ALIDVLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGK 157
Cdd:PRK10792  81 ALIDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 158 NAVVIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDGKL 237
Cdd:PRK10792 161 NAVVVGASNIVGRPMSLELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLEDGKL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 489043168 238 KGDVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKNR 279
Cdd:PRK10792 241 VGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEEY 282

PRK14166

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

1-281

9.61e-132

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

Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 374.75 E-value: 9.61e-132

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   1 MTILDGKNVSAQVKERVKNEALNLKNQGIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALI 80
Cdd:PRK14166   1 MTLLDGKALSAKIKEELKEKNQFLKSKGIESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  81 DVLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLD-GFVPCTPLGIMEIFKAYDINLEGKNA 159
Cdd:PRK14166  81 NTLNHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGLEsGFLPCTPLGVMKLLKAYEIDLEGKDA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 160 VVIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDGKLKG 239
Cdd:PRK14166 161 VIIGASNIVGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLESGKIVG 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 489043168 240 DVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKNRSK 281
Cdd:PRK14166 241 DVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAKNRLN 282

PRK14183

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

1-279

1.79e-128

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

Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 366.46 E-value: 1.79e-128

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   1 MTILDGKNVSAQVKERVKNEALNLKN-QGIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIAL 79
Cdd:PRK14183   1 MQILDGKALSDKIKENVKKEVDELKLvKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILET 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  80 IDVLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNA 159
Cdd:PRK14183  81 IAMMNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 160 VVIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDGKLKG 239
Cdd:PRK14183 161 CVVGASNIVGKPMAALLLNANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINRTEDGRLVG 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 489043168 240 DVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKNR 279
Cdd:PRK14183 241 DVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKNR 280

PRK14184

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

1-279

5.76e-125

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

Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 357.55 E-value: 5.76e-125

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   1 MTILDGKNVSAQVKERVKNEALNLKNQ-GIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIAL 79
Cdd:PRK14184   1 MLLLDGKATAATIREELKTEVAALTARhGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  80 IDVLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNA 159
Cdd:PRK14184  81 IAELNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 160 VVIGRSNMVGKPMANLLLN----ANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDG 235
Cdd:PRK14184 161 VVVGRSNIVGKPLALMLGApgkfANATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRTDDG 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 489043168 236 kLKGDVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKNR 279
Cdd:PRK14184 241 -LVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQSWKER 283

PRK14186

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

3-281

1.70e-122

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 351.67 E-value: 1.70e-122

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   3 ILDGKNVSAQVKERVKNE-ALNLKNQGIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALID 81
Cdd:PRK14186   4 ILDGKALAAEIEQRLQAQiESNLPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEALIA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  82 VLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAVV 161
Cdd:PRK14186  84 QLNQDERVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKKAVV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 162 IGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDD----GKL 237
Cdd:PRK14186 164 VGRSILVGKPLALMLLAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHRLPSsdgkTRL 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 489043168 238 KGDVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKNRSK 281
Cdd:PRK14186 244 CGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSWQKRHG 287

PRK14185

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

1-277

3.26e-113

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 327.94 E-value: 3.26e-113

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   1 MTILDGKNVSAQVKERVKNEALNLKNQG-IEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIAL 79
Cdd:PRK14185   1 MQLIDGKAISAQIKQEIAAEVAEIVAKGgKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  80 IDVLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNA 159
Cdd:PRK14185  81 VRELNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 160 VVIGRSNMVGKPMANLLLN----ANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDG 235
Cdd:PRK14185 161 VVLGRSNIVGKPMAQLMMQkaypGDCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTRVPDA 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 489043168 236 ------KLKGDVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAK 277
Cdd:PRK14185 241 trksgfKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGK 288

PRK14173

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

1-283

2.51e-110

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

Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 320.62 E-value: 2.51e-110

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   1 MTILDGKNVSAQVKERVKNEALNLKnqgIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALI 80
Cdd:PRK14173   3 ARELSGPPAAEAVYAELRARLAKLP---FVPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLELI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  81 DVLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAV 160
Cdd:PRK14173  80 ARLNADPEVDGILVQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGKEVV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 161 VIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRM--DDGK-- 236
Cdd:PRK14173 160 VVGRSNIVGKPLAALLLREDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINRVggNGGRdi 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 489043168 237 LKGDVKfDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKNRSKKA 283
Cdd:PRK14173 240 LTGDVH-PEVAEVAGALTPVPGGVGPMTVAMLMANTVIAALRRRGGR 285

PRK14176

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

3-278

1.51e-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: 1.51e-109

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   3 ILDGKNVSAQVKERVKNEALNLK-NQGIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALID 81
Cdd:PRK14176  10 IIDGKALAKKIEAEVRSGVERLKsNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELID 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  82 VLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAVV 161
Cdd:PRK14176  90 SLNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGKNAVI 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 162 IGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRmDDGKLKGDV 241
Cdd:PRK14176 170 VGHSNVVGKPMAAMLLNRNATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITK-EEDKVYGDV 248

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 489043168 242 KFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKN 278
Cdd:PRK14176 249 DFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEK 285

PRK14169

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

1-281

1.92e-109

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 318.04 E-value: 1.92e-109

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   1 MTILDGKNVSAQVKERVKNEALNLKNQGIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALI 80
Cdd:PRK14169   1 ATRLDGRAVSKKILADLKQTVAKLAQQDVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAKV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  81 DVLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAV 160
Cdd:PRK14169  81 AELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRVV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 161 VIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDGKLKGD 240
Cdd:PRK14169 161 IVGRSNIVGRPLAGLMVNHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRGADGKLLGD 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 489043168 241 VKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKNRSK 281
Cdd:PRK14169 241 VDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKRRAN 281

PRK14194

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

3-277

8.85e-108

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 314.48 E-value: 8.85e-108

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   3 ILDGKNVSAQVKERVKNEALNLKNQGIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALIDV 82
Cdd:PRK14194   6 LIDGKAAAARVLAQVREDVRTLKAAGIEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLLALIAE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  83 LNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAVVI 162
Cdd:PRK14194  86 LNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGKHAVVI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 163 GRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDG---KLKG 239
Cdd:PRK14194 166 GRSNIVGKPMAALLLQAHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINRIDDDgrsRLVG 245

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 489043168 240 DVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAK 277
Cdd:PRK14194 246 DVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAAR 283

PRK14174

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

1-275

2.29e-107

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

Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 313.29 E-value: 2.29e-107

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   1 MTILDGKNVSAQVKERVKNEALNLKNQ-GIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIAL 79
Cdd:PRK14174   1 MLIIDGKKVSLDLKNELKTRVEAYRAKtGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  80 IDVLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASG-LDG-FVPCTPLGIMEIFKAYDINLEGK 157
Cdd:PRK14174  81 IEDLNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGhLDKcFVSCTPYGILELLGRYNIETKGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 158 NAVVIGRSNMVGKPMANLLLN----ANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMD 233
Cdd:PRK14174 161 HCVVVGRSNIVGKPMANLMLQklkeSNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRIE 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 489043168 234 DG------KLKGDVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKS 275
Cdd:PRK14174 241 DPstksgyRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTLQS 288

PRK14175

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

3-279

1.26e-105

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 308.38 E-value: 1.26e-105

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   3 ILDGKNVSAQVKERVKNEALNLKNQGIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALIDV 82
Cdd:PRK14175   5 ILDGKQIAKDYRQGLQDQVEALKEKGFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLNELNR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  83 LNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAVVI 162
Cdd:PRK14175  85 LNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGKNAVVI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 163 GRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDGKLKGDVK 242
Cdd:PRK14175 165 GRSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVGNTPDENGKLKGDVD 244

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 489043168 243 FDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKNR 279
Cdd:PRK14175 245 YDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEKMR 281

PRK14172

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

3-277

2.57e-105

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

Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 307.48 E-value: 2.57e-105

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   3 ILDGKNVSAQVKERVKNEALNLKNQGIE-PALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALID 81
Cdd:PRK14172   4 IINGKEVALKIKEEIKNFVEERKENGLSiPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEIE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  82 VLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAVV 161
Cdd:PRK14172  84 ELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVVV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 162 IGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMdDGKLKGDV 241
Cdd:PRK14172 164 IGRSNIVGKPVAQLLLNENATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSV-NGKITGDV 242

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 489043168 242 KFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAK 277
Cdd:PRK14172 243 NFDKVIDKASYITPVPGGVGSLTTTLLIKNVCEALK 278

PRK14178

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

2-280

3.20e-104

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 304.84 E-value: 3.20e-104

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   2 TILDGKNVSAQVKERVKNEalnLKNQGIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALID 81
Cdd:PRK14178   1 MILDGKAVSEKRLELLKEE---IIESGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  82 VLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAVV 161
Cdd:PRK14178  78 RLNEDPDINGILVQLPLPKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAVV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 162 IGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMdDGKLKGDV 241
Cdd:PRK14178 158 VGRSIDVGRPMAALLLNADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQV-NGKLCGDV 236

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 489043168 242 KFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKNRS 280
Cdd:PRK14178 237 DFDAVKEIAGAITPVPGGVGPMTIATLMENTFDAAKMRC 275

PRK14193

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

2-276

7.42e-104

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

Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 303.86 E-value: 7.42e-104

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   2 TILDGKNVSAQVKERVKNEALNLKNQGIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALID 81
Cdd:PRK14193   4 IILDGKATADEIKADLAERVAALKEKGITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELNAVID 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  82 VLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAVV 161
Cdd:PRK14193  84 ELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGAHVVV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 162 IGRSNMVGKPMANLLL--NANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDGKLKG 239
Cdd:PRK14193 164 IGRGVTVGRPIGLLLTrrSENATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSRAGDGKLVG 243

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 489043168 240 DVKFDeVAPKCSFITPVPGGVGPMTIAMLLSNTIKSA 276
Cdd:PRK14193 244 DVHPD-VWEVAGAVSPNPGGVGPMTRAFLLTNVVERA 279

PRK14170

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

3-277

9.50e-100

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 293.52 E-value: 9.50e-100

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   3 ILDGKNVSAQVKERVKNEALNLKNQGIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALIDV 82
Cdd:PRK14170   4 IIDGKKLAKEIQEKVTREVAELVKEGKKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSVVEE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  83 LNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAVVI 162
Cdd:PRK14170  84 LNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRAVVI 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 163 GRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDGKLKGDVK 242
Cdd:PRK14170 164 GRSNIVGKPVAQLLLNENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDRDENNKLCGDVD 243

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 489043168 243 FDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAK 277
Cdd:PRK14170 244 FDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAK 278

PRK14182

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

1-281

7.34e-99

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

Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 291.16 E-value: 7.34e-99

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   1 MTILDGKNVSAQVKERVKNEALNLKNQGIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALI 80
Cdd:PRK14182   1 MNLIDGKQIAAKVKGEVATEVRALAARGVQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  81 DVLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFV-PCTPLGIMEIFKAYDINLEGKNA 159
Cdd:PRK14182  81 ARLNADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGVPrPCTPAGVMRMLDEARVDPKGKRA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 160 VVIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDGKLKG 239
Cdd:PRK14182 161 LVVGRSNIVGKPMAMMLLERHATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLADGKLVG 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 489043168 240 DVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKNRSK 281
Cdd:PRK14182 241 DVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKRTAR 282

THF_DHG_CYH_C

pfam02882

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

123-279

4.12e-97

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

Pssm-ID: 427036 Cd Length: 160 Bit Score: 282.05 E-value: 4.12e-97

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  123 INVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAVVIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADI 202
Cdd:pfam02882   3 YNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITREADI 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489043168  203 LVAAIGRADFVTADMVKDGAVVIDVGINRMDDGKLKGDVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKNR 279
Cdd:pfam02882  83 VVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNTVEAAKRQ 159

PRK14167

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

2-276

4.20e-97

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

Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 287.44 E-value: 4.20e-97

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   2 TILDGKNVSAQVKERVKNEALNLKNQGIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALID 81
Cdd:PRK14167   3 EIIDGNAVAAQIRDDLTDAIETLEDAGVTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  82 VLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAVV 161
Cdd:PRK14167  83 ELNADEDVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADVVV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 162 IGRSNMVGKPMANLLLN----ANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDG-- 235
Cdd:PRK14167 163 VGRSDIVGKPMANLLIQkadgGNATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINRVDADte 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 489043168 236 ---KLKGDVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSA 276
Cdd:PRK14167 243 kgyELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAA 286

PLN02616

tetrahydrofolate dehydrogenase/cyclohydrolase, putative

3-277

2.73e-96

tetrahydrofolate dehydrogenase/cyclohydrolase, putative

Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 287.67 E-value: 2.73e-96

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   3 ILDGKNVSAQVKERVKNEALNLKNQ-GIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALID 81
Cdd:PLN02616  75 VIDGKAVAKKIRDEITIEVSRMKESiGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKFIS 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  82 VLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLA-SGLDG-FVPCTPLGIMEIFKAYDINLEGKNA 159
Cdd:PLN02616 155 GFNNDPSVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAmRGREPlFVPCTPKGCIELLHRYNVEIKGKRA 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 160 VVIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDG---- 235
Cdd:PLN02616 235 VVIGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPVEDAsspr 314

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 489043168 236 --KLKGDVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAK 277
Cdd:PLN02616 315 gyRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAK 358

PRK14171

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

3-278

3.49e-95

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 282.23 E-value: 3.49e-95

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   3 ILDGKNVSAQVKERVKNEALNLKNQ-GIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALID 81
Cdd:PRK14171   4 IIDGKALANEILADLKLEIQELKSQtNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKIN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  82 VLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLD-GFVPCTPLGIMEIFKAYDINLEGKNAV 160
Cdd:PRK14171  84 ELNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSGISqGFIPCTALGCLAVIKKYEPNLTGKNVV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 161 VIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDGKLKGD 240
Cdd:PRK14171 164 IIGRSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRISGNKIIGD 243

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 489043168 241 VKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKN 278
Cdd:PRK14171 244 VDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKAFKD 281

PRK14181

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

3-280

6.27e-94

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 279.05 E-value: 6.27e-94

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   3 ILDGKNVSAQVKERVKNEalnLKNQGIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALIDV 82
Cdd:PRK14181   2 LLKGAPAAEHILATIKEN---ISASSTAPGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLIHR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  83 LNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASG-LDGFVPCTPLGIMEIFKAYDINLEGKNAVV 161
Cdd:PRK14181  79 LNNDPNIHGILVQLPLPKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGeTDGFIPCTPAGIIELLKYYEIPLHGRHVAI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 162 IGRSNMVGKPMANLLL----NANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRM--DDG 235
Cdd:PRK14181 159 VGRSNIVGKPLAALLMqkhpDTNATVTLLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRVpaANP 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 489043168 236 K---LKGDVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKNRS 280
Cdd:PRK14181 239 KgyiLVGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNTWESYLRHS 286

PRK14177

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

3-277

1.40e-93

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 278.01 E-value: 1.40e-93

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   3 ILDGKNVSAQVKERVKNEALNLKNQGIE-PALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALID 81
Cdd:PRK14177   5 LLDGKKLSEKIRNEIRETIEERKTKNKRiPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLGVID 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  82 VLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAVV 161
Cdd:PRK14177  85 KLNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGKNAVV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 162 IGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINrmdDGKLkGDV 241
Cdd:PRK14177 165 VGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYN---PGNV-GDI 240

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 489043168 242 KFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAK 277
Cdd:PRK14177 241 EISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFK 276

NAD_bind_m-THF_DH_Cyclohyd

cd01080

NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...

113-277

7.38e-92

Pssm-ID: 133448 Cd Length: 168 Bit Score: 269.04 E-value: 7.38e-92

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 113 PAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAVVIGRSNMVGKPMANLLLNANATVTVTHSKTRN 192
Cdd:cd01080    1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKTKN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 193 LKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDD---GKLKGDVKFDEVAPKCSFITPVPGGVGPMTIAMLL 269
Cdd:cd01080   81 LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDksgGKLVGDVDFESAKEKASAITPVPGGVGPMTVAMLM 160


                 ....*...
gi 489043168 270 SNTIKSAK 277
Cdd:cd01080  161 KNTVEAAK 168

PRK14187

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

3-281

1.76e-91

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 272.86 E-value: 1.76e-91

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   3 ILDGKNVSAQVKERVKNEALNLKNQ-GIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALID 81
Cdd:PRK14187   4 IIDGKKIANDITEILATCIDDLKRQhNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKIN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  82 VLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASG--LDGFVPCTPLGIMEIFKAYDINLEGKNA 159
Cdd:PRK14187  84 ELNNDDSVHGILVQLPVPNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGqkKNCLIPCTPKGCLYLIKTITRNLSGSDA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 160 VVIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDG---K 236
Cdd:PRK14187 164 VVIGRSNIVGKPMACLLLGENCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSIEEGgvkK 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 489043168 237 LKGDVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAKNRSK 281
Cdd:PRK14187 244 FVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAACNQKG 288

PRK14180

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

1-277

8.37e-91

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

Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 270.75 E-value: 8.37e-91

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   1 MTILDGKNVSAQVKERVKNEALNLKNQ-GIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIAL 79
Cdd:PRK14180   1 MILIDGKSLSKDLKERLATQVQEYKHHtAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  80 IDVLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLA-SGLDGFVPCTPLGIMEIFKAYDINLEGKN 158
Cdd:PRK14180  81 IDQLNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLQlRDKKCLESCTPKGIMTMLREYGIKTEGAY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 159 AVVIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMdDGKLK 238
Cdd:PRK14180 161 AVVVGASNVVGKPVSQLLLNAKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHV-DGKIV 239

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 489043168 239 GDVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAK 277
Cdd:PRK14180 240 GDVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQ 278

PLN02516

methylenetetrahydrofolate dehydrogenase (NADP+)

2-277

5.50e-89

methylenetetrahydrofolate dehydrogenase (NADP+)

Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 266.76 E-value: 5.50e-89

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   2 TILDGKNVSAQVKERVKNEALNLKNQ-GIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALI 80
Cdd:PLN02516  10 QIIDGKAIAKAIRSEIAEEVAQLSEKhGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISKV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  81 DVLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLA-SGLDG-FVPCTPLGIMEIFKAYDINLEGKN 158
Cdd:PLN02516  90 HELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAmKGREPlFLPCTPKGCLELLSRSGIPIKGKK 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 159 AVVIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDG--- 235
Cdd:PLN02516 170 AVVVGRSNIVGLPVSLLLLKADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVSDPskk 249

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 489043168 236 ---KLKGDVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAK 277
Cdd:PLN02516 250 sgyRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAK 294

PLN02897

tetrahydrofolate dehydrogenase/cyclohydrolase, putative

3-277

1.60e-88

tetrahydrofolate dehydrogenase/cyclohydrolase, putative

Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 267.21 E-value: 1.60e-88

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   3 ILDGKNVSAQVKERVKNEALNLKNQ-GIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALID 81
Cdd:PLN02897  58 VIDGNVIAEEIRTKIASEVRKMKKAvGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILSALR 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  82 VLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLAsgLDG----FVPCTPLGIMEIFKAYDINLEGK 157
Cdd:PLN02897 138 KFNEDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLA--MRGreplFVSCTPKGCVELLIRSGVEIAGK 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 158 NAVVIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDG-- 235
Cdd:PLN02897 216 NAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPVEDSsc 295

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 489043168 236 ----KLKGDVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAK 277
Cdd:PLN02897 296 efgyRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAK 341

PRK14192

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

2-277

3.89e-88

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 264.02 E-value: 3.89e-88

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   2 TILDGKNVSAQVKERVKNEALNLKNQ-GIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALI 80
Cdd:PRK14192   4 LVLDGKALAKQIEEELSVRVEALKAKtGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLAKI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  81 DVLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDGFVPCTPLGIMEIFKAYDINLEGKNAV 160
Cdd:PRK14192  84 EELNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGKHAV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 161 VIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRMDDGKLkGD 240
Cdd:PRK14192 164 VVGRSAILGKPMAMMLLNANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFHPRDGGGV-GD 242

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 489043168 241 VKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAK 277
Cdd:PRK14192 243 IELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAE 279

PRK14168

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

3-277

5.76e-84

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 254.03 E-value: 5.76e-84

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   3 ILDGKNVSAQVKERVKNEALNLKNQ-GIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALID 81
Cdd:PRK14168   5 IIKGTEIREEILEEIRGEVAELKEKyGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLALID 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  82 VLNLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVDGFAAINVGKLASGLDG--FVPCTPLGIMEIFKAYDINLEGKNA 159
Cdd:PRK14168  85 KYNNDDSIHGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIGGDEvkFLPCTPAGIQEMLVRSGVETSGAEV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 160 VVIGRSNMVGKPMANLLLN----ANATVTVTHSKTRNLKEICANADILVAAIGRADFVTADMVKDGAVVIDVGINRM--- 232
Cdd:PRK14168 165 VVVGRSNIVGKPIANMMTQkgpgANATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVNRVgtn 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 489043168 233 -DDGK--LKGDVKFDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAK 277
Cdd:PRK14168 245 eSTGKaiLSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAK 292

THF_DHG_CYH

pfam00763

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;

4-118

1.62e-55

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;

Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 174.90 E-value: 1.62e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168    4 LDGKNVSAQVKERVKNEALNLKNQGIEPALAVILVGEDKASQTYVAAKEKACIACEIKSVMHRLPESTTQSELIALIDVL 83
Cdd:pfam00763   1 IDGKAIAKKIREELKEEVAALKAGGRKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKL 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 489043168   84 NLDDGIDGILVQLPLPKHIDTNKILETIRPAKDVD 118
Cdd:pfam00763  81 NADPSVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115

NAD_bind_m-THF_DH_Cyclohyd_like

cd05212

NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ...

137-277

1.00e-31

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: 114.53 E-value: 1.00e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 137 PCTPLGIMEIFKA-------YDINLEGKNAVVIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADILVAAIGR 209
Cdd:cd05212    2 PCTPLFVSPVAKAvkellnkEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSPK 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489043168 210 ADFVTADMVKDGAVVIDVGINRMDDgklkgdvkfDEVAPKCSFITPVPGGVGPMTIAMLLSNTIKSAK 277
Cdd:cd05212   82 PEKVPTEWIKPGATVINCSPTKLSG---------DDVKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140

NAD_bind_m-THF_DH

cd01079

NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ...

113-279

2.10e-15

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: 72.84 E-value: 2.10e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 113 PAKDVDGFAAINVGKLASG---LDG------FVPCTPLGIMEIFK---------AYDINLEGKNAVVIGRSNMVGKPMAN 174
Cdd:cd01079    1 PHKDVEGLSHKYIFNLYHNirfLDPenrkksILPCTPLAIVKILEflgiynkilPYGNRLYGKTITIINRSEVVGRPLAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 175 LLLNANATV---------------------TVTHSKTRNLKEICANADILVAAIGRADF-VTADMVKDGAVVIDVGINRM 232
Cdd:cd01079   81 LLANDGARVysvdingiqvftrgesirhekHHVTDEEAMTLDCLSQSDVVITGVPSPNYkVPTELLKDGAICINFASIKN 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 489043168 233 DDgklkgdvkfDEVAPKCSFITPVpggVGPMTIAMLLSNTIKSAKNR 279
Cdd:cd01079  161 FE---------PSVKEKASIYVPS---IGKVTIAMLLRNLLRLYHNQ 195

AdoHcyase_NAD

smart00997

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

146-230

3.07e-04

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

Pssm-ID: 198065 [Multi-domain] Cd Length: 162 Bit Score: 40.51 E-value: 3.07e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168   146 IFKAYDINLEGKNAVVIGRSnMVGKPMANLLLNANATVTVTHS-------------KTRNLKEICANADILVAAIGRADF 212
Cdd:smart00997  13 ILRATNVLLAGKNVVVAGYG-DVGKGVAARLRGLGARVIVTEIdpiraleaamdgfEVMKMEEAAKRADIFVTATGNKDV 91

                           90       100
                   ....*....|....*....|....*.
gi 489043168   213 VTADM---VKDGAVV-----IDVGIN 230
Cdd:smart00997  92 ITREHfraMKDGAILanaghFDVEID 117

AlaDh_PNT_C

smart01002

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...

180-229

1.14e-03

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: 38.64 E-value: 1.14e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 489043168   180 NATVTVTHSKTRNLKEICANADILVAAI----GRAD-FVTADMV---KDGAVVIDVGI 229
Cdd:smart01002  64 GARFTTLYSQAELLEEAVKEADLVIGAVlipgAKAPkLVTREMVksmKPGSVIVDVAA 121

AdoHcyase_NAD

pfam00670

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

146-228

1.74e-03

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

Pssm-ID: 395543 [Multi-domain] Cd Length: 162 Bit Score: 38.10 E-value: 1.74e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168  146 IFKAYDINLEGKNAVVIGRSNmVGKPMANLLLNANATVTVTHS-------------KTRNLKEICANADILVAAIGRADF 212
Cdd:pfam00670  13 IKRATDVMIAGKVAVVCGYGD-VGKGCAASLKGQGARVIVTEIdpicalqaamegfQVVTLEEVVDKADIFVTTTGNKDI 91

                          90
                  ....*....|....*....
gi 489043168  213 VTADM---VKDGAVVIDVG 228
Cdd:pfam00670  92 ITGEHmakMKNDAIVCNIG 110

PRK06949

SDR family oxidoreductase;

149-216

1.94e-03

SDR family oxidoreductase;

Pssm-ID: 180773 [Multi-domain] Cd Length: 258 Bit Score: 38.97 E-value: 1.94e-03

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489043168 149 AYDINLEGKNAVVIGRSNMVGKPMANLLLNANATVTVTHSKTRNLKEICANADilvAAIGRADFVTAD 216
Cdd:PRK06949   2 GRSINLEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIE---AEGGAAHVVSLD 66

PRK05476

S-adenosyl-L-homocysteine hydrolase; Provisional

142-230

4.54e-03

S-adenosyl-L-homocysteine hydrolase; Provisional

Pssm-ID: 235488 [Multi-domain] Cd Length: 425 Bit Score: 38.18 E-value: 4.54e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 142 GIMeifKAYDINLEGKNAVVIGRSNmVGKPMANLLLNANATVTVThsktrNLKEICA------------------NADIL 203
Cdd:PRK05476 201 GIK---RATNVLIAGKVVVVAGYGD-VGKGCAQRLRGLGARVIVT-----EVDPICAlqaamdgfrvmtmeeaaeLGDIF 271

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489043168 204 VAAIGRADFVTADM---VKDGAVV-----IDVGIN 230
Cdd:PRK05476 272 VTATGNKDVITAEHmeaMKDGAILanighFDNEID 306

SAHH

cd00401

S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...

146-228

4.64e-03

S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine hydrolase (SAHH, AdoHycase) catalyzes the hydrolysis of S-adenosyl-L-homocysteine (AdoHyc) to form adenosine (Ado) and homocysteine (Hcy). The equilibrium lies far on the side of AdoHyc synthesis, but in nature the removal of Ado and Hyc is sufficiently fast, so that the net reaction is in the direction of hydrolysis. Since AdoHyc is a potent inhibitor of S-adenosyl-L-methionine dependent methyltransferases, AdoHycase plays a critical role in the modulation of the activity of various methyltransferases. The enzyme forms homotetramers, with each monomer binding one molecule of NAD+.

Pssm-ID: 240619 [Multi-domain] Cd Length: 402 Bit Score: 38.21 E-value: 4.64e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 146 IFKAYDINLEGKNAVVIGRSNmVGKPMANLLLNANATVTVTHS-------------KTRNLKEICANADILVAAIGRADF 212
Cdd:cd00401  185 IKRATNVLIAGKVVVVAGYGW-VGKGCAMRARGLGARVIVTEVdpicalqaamdgfEVMPMEEAAKIGDIFVTATGNKDV 263

                         90
                 ....*....|....*....
gi 489043168 213 VTADMV---KDGAVVIDVG 228
Cdd:cd00401  264 IRGEHFekmKDGAILCNAG 282

PRK13394

3-hydroxybutyrate dehydrogenase; Provisional

153-231

7.22e-03

3-hydroxybutyrate dehydrogenase; Provisional

Pssm-ID: 184025 [Multi-domain] Cd Length: 262 Bit Score: 37.18 E-value: 7.22e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489043168 153 NLEGKNAVVIGRSNMVGKPMANLLLNANATVTVThsktrNLKEICANA--DILVAAIGRADFVTADMVKDGAVviDVGIN 230
Cdd:PRK13394   4 NLNGKTAVVTGAASGIGKEIALELARAGAAVAIA-----DLNQDGANAvaDEINKAGGKAIGVAMDVTNEDAV--NAGID 76


                 .
gi 489043168 231 R 231
Cdd:PRK13394  77 K 77

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