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Conserved domains on  [gi|491602985|ref|WP_005460545|]
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MULTISPECIES: bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD [Vibrio]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10792 PRK10792
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-283 0e+00

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


:

Pssm-ID: 236760 [Multi-domain]  Cd Length: 285  Bit Score: 583.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   1 MTAQNIDGTLISQTVRSEVAARVKARVAAGLRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELL 80
Cdd:PRK10792   1 MTAKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  81 ALIDELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGK 160
Cdd:PRK10792  81 ALIDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSGKL 240
Cdd:PRK10792 161 NAVVVGASNIVGRPMSLELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLEDGKL 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 491602985 241 VGDVEYDKARESASFITPVPGGVGPMTVASLIENTMLACEQFH 283
Cdd:PRK10792 241 VGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEEYH 283
 
Name Accession Description Interval E-value
PRK10792 PRK10792
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-283 0e+00

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 236760 [Multi-domain]  Cd Length: 285  Bit Score: 583.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   1 MTAQNIDGTLISQTVRSEVAARVKARVAAGLRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELL 80
Cdd:PRK10792   1 MTAKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  81 ALIDELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGK 160
Cdd:PRK10792  81 ALIDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSGKL 240
Cdd:PRK10792 161 NAVVVGASNIVGRPMSLELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLEDGKL 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 491602985 241 VGDVEYDKARESASFITPVPGGVGPMTVASLIENTMLACEQFH 283
Cdd:PRK10792 241 VGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEEYH 283
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: 506.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   1 MTAQNIDGTLISQTVRSEVAARVKARVAAGlRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELL 80
Cdd:COG0190    1 MMAQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  81 ALIDELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGK 160
Cdd:COG0190   80 ALIDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSGKL 240
Cdd:COG0190  160 HAVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVEDGKL 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 491602985 241 VGDVEYDKARESASFITPVPGGVGPMTVASLIENTMLACEQFH 283
Cdd:COG0190  240 VGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQA 282
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
124-283 5.63e-98

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


Pssm-ID: 427036  Cd Length: 160  Bit Score: 284.36  E-value: 5.63e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  124 HPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGKHAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQA 203
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITREA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  204 DVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSGKLVGDVEYDKARESASFITPVPGGVGPMTVASLIENTMLACEQFH 283
Cdd:pfam02882  81 DIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNTVEAAKRQL 160
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
116-280 1.60e-94

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: 275.97  E-value: 1.60e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 116 PEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGKHAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKD 195
Cdd:cd01080    1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKTKN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 196 LESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRL---DSGKLVGDVEYDKARESASFITPVPGGVGPMTVASLI 272
Cdd:cd01080   81 LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVpdkSGGKLVGDVDFESAKEKASAITPVPGGVGPMTVAMLM 160

                 ....*...
gi 491602985 273 ENTMLACE 280
Cdd:cd01080  161 KNTVEAAK 168
 
Name Accession Description Interval E-value
PRK10792 PRK10792
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-283 0e+00

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 236760 [Multi-domain]  Cd Length: 285  Bit Score: 583.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   1 MTAQNIDGTLISQTVRSEVAARVKARVAAGLRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELL 80
Cdd:PRK10792   1 MTAKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  81 ALIDELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGK 160
Cdd:PRK10792  81 ALIDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSGKL 240
Cdd:PRK10792 161 NAVVVGASNIVGRPMSLELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLEDGKL 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 491602985 241 VGDVEYDKARESASFITPVPGGVGPMTVASLIENTMLACEQFH 283
Cdd:PRK10792 241 VGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEEYH 283
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: 506.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   1 MTAQNIDGTLISQTVRSEVAARVKARVAAGlRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELL 80
Cdd:COG0190    1 MMAQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  81 ALIDELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGK 160
Cdd:COG0190   80 ALIDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSGKL 240
Cdd:COG0190  160 HAVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVEDGKL 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 491602985 241 VGDVEYDKARESASFITPVPGGVGPMTVASLIENTMLACEQFH 283
Cdd:COG0190  240 VGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQA 282
PRK14189 PRK14189
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
1-281 4.57e-138

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 184559 [Multi-domain]  Cd Length: 285  Bit Score: 390.97  E-value: 4.57e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   1 MTAQNIDGTLISQTVRSEVAARVKARVAAGLRaPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELL 80
Cdd:PRK14189   1 MTAQLIDGNALSKQLRAEAAQRAAALTARGHQ-PGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  81 ALIDELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGK 160
Cdd:PRK14189  80 ARIDELNRDPKIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSGKL 240
Cdd:PRK14189 160 HAVVIGRSNIVGKPMAMLLLQAGATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMNRDDAGKL 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 491602985 241 VGDVEYDKARESASFITPVPGGVGPMTVASLIENTMLACEQ 281
Cdd:PRK14189 240 CGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAER 280
PRK14190 PRK14190
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
1-283 1.40e-132

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


Pssm-ID: 184560 [Multi-domain]  Cd Length: 284  Bit Score: 377.04  E-value: 1.40e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   1 MTAQNIDGTLISQTVRSEVAARVKARVAAGLrAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELL 80
Cdd:PRK14190   1 MMAVIIDGKEVAKEKREQLKEEVVKLKEQGI-VPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  81 ALIDELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGK 160
Cdd:PRK14190  80 ALIDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSGKL 240
Cdd:PRK14190 160 HVVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRLENGKL 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 491602985 241 VGDVEYDKARESASFITPVPGGVGPMTVASLIENTMLACEQFH 283
Cdd:PRK14190 240 CGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKRAG 282
PRK14184 PRK14184
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
6-278 1.38e-123

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


Pssm-ID: 237635 [Multi-domain]  Cd Length: 286  Bit Score: 354.08  E-value: 1.38e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   6 IDGTLISQTVRSEVAARVKARVAAGLRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLALIDE 85
Cdd:PRK14184   4 LDGKATAATIREELKTEVAALTARHGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLIAE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  86 LNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGKHAVVV 165
Cdd:PRK14184  84 LNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAVVV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 166 GASNIVGRPMTLELLLAG----CTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSGkLV 241
Cdd:PRK14184 164 GRSNIVGKPLALMLGAPGkfanATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRTDDG-LV 242
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 491602985 242 GDVEYDKARESASFITPVPGGVGPMTVASLIENTMLA 278
Cdd:PRK14184 243 GDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQS 279
PRK14188 PRK14188
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
2-279 2.45e-123

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184558 [Multi-domain]  Cd Length: 296  Bit Score: 353.88  E-value: 2.45e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   2 TAQNIDGTLISQTVRSEVAARVKARVAAGLRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLA 81
Cdd:PRK14188   1 MATIIDGKAFAADVRATVAAEVARLKAAHGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  82 LIDELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGKH 161
Cdd:PRK14188  81 LIARLNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 162 AVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDS---- 237
Cdd:PRK14188 161 AVVIGRSNLVGKPMAQLLLAANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIPApekg 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 491602985 238 ---GKLVGDVEYDKARESASFITPVPGGVGPMTVASLIENTMLAC 279
Cdd:PRK14188 241 egkTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAA 285
PRK14191 PRK14191
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
4-280 5.21e-123

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172679 [Multi-domain]  Cd Length: 285  Bit Score: 352.53  E-value: 5.21e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   4 QNIDGTLISQTVRSEVAARVKARVAAGLRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLALI 83
Cdd:PRK14191   2 VLLDGKALSYKIEKDLKNKIQILTAQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  84 DELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGKHAV 163
Cdd:PRK14191  82 KDLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 164 VVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSGKLVGD 243
Cdd:PRK14191 162 IIGASNIVGKPLAMLMLNAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLNDGRLVGD 241
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 491602985 244 VEYDKARESASFITPVPGGVGPMTVASLIENTMLACE 280
Cdd:PRK14191 242 VDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAE 278
PRK14186 PRK14186
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
2-283 6.76e-119

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237636 [Multi-domain]  Cd Length: 297  Bit Score: 342.81  E-value: 6.76e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   2 TAQNIDGTLISQTVRSEVAARVKARVAAGLRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLA 81
Cdd:PRK14186   1 MALILDGKALAAEIEQRLQAQIESNLPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  82 LIDELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGKH 161
Cdd:PRK14186  81 LIAQLNQDERVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 162 AVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDS---- 237
Cdd:PRK14186 161 AVVVGRSILVGKPLALMLLAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHRLPSsdgk 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 491602985 238 GKLVGDVEYDKARESASFITPVPGGVGPMTVASLIENTMLA-CEQFH 283
Cdd:PRK14186 241 TRLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSwQKRHG 287
PRK14183 PRK14183
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
4-282 1.08e-110

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


Pssm-ID: 184555 [Multi-domain]  Cd Length: 281  Bit Score: 321.39  E-value: 1.08e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   4 QNIDGTLISQTVRSEVAARVKARVAAGLRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLALI 83
Cdd:PRK14183   2 QILDGKALSDKIKENVKKEVDELKLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  84 DELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGKHAV 163
Cdd:PRK14183  82 AMMNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 164 VVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSGKLVGD 243
Cdd:PRK14183 162 VVGASNIVGKPMAALLLNANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINRTEDGRLVGD 241
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 491602985 244 VEYDKARESASFITPVPGGVGPMTVASLIENTMLACEQF 282
Cdd:PRK14183 242 VDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKNR 280
PRK14174 PRK14174
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
6-283 3.84e-108

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


Pssm-ID: 172662 [Multi-domain]  Cd Length: 295  Bit Score: 315.22  E-value: 3.84e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   6 IDGTLISQTVRSEVAARVKARVAAGLRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLALIDE 85
Cdd:PRK14174   4 IDGKKVSLDLKNELKTRVEAYRAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKIED 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  86 LNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQ-RIPK-LRSCTPKGIITLLDRYNIELRGKHAV 163
Cdd:PRK14174  84 LNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMgHLDKcFVSCTPYGILELLGRYNIETKGKHCV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 164 VVGASNIVGRPMTlELLL-----AGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLD-- 236
Cdd:PRK14174 164 VVGRSNIVGKPMA-NLMLqklkeSNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRIEdp 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491602985 237 ---SG-KLVGDVEYDKARESASFITPVPGGVGPMTVASLIENTMLACEQFH 283
Cdd:PRK14174 243 stkSGyRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTLQSFERVN 293
PRK14193 PRK14193
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
1-281 3.61e-107

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


Pssm-ID: 237637 [Multi-domain]  Cd Length: 284  Bit Score: 312.33  E-value: 3.61e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   1 MTAQNIDGTLISQTVRSEVAARVKARVAAGlRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELL 80
Cdd:PRK14193   1 MTAIILDGKATADEIKADLAERVAALKEKG-ITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  81 ALIDELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGK 160
Cdd:PRK14193  80 AVIDELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 161 HAVVVGASNIVGRPMTLELLLAG--CTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSG 238
Cdd:PRK14193 160 HVVVIGRGVTVGRPIGLLLTRRSenATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSRAGDG 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 491602985 239 KLVGDVEYDkARESASFITPVPGGVGPMTVASLIENTMLACEQ 281
Cdd:PRK14193 240 KLVGDVHPD-VWEVAGAVSPNPGGVGPMTRAFLLTNVVERAER 281
PRK14179 PRK14179
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
3-279 1.25e-106

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 237634 [Multi-domain]  Cd Length: 284  Bit Score: 311.30  E-value: 1.25e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   3 AQNIDGTLISQTVRSEVAARVKARVAAGLRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLAL 82
Cdd:PRK14179   2 TEIIDGKALAQKMQAELAEKVAKLKEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  83 IDELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGKHA 162
Cdd:PRK14179  82 IERYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 163 VVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSGKLVG 242
Cdd:PRK14179 162 VVIGRSNIVGKPMAQLLLDKNATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMNRDENGKLIG 241
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 491602985 243 DVEYDKARESASFITPVPGGVGPMTVASLIENTMLAC 279
Cdd:PRK14179 242 DVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAA 278
PRK14166 PRK14166
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
6-276 4.57e-106

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


Pssm-ID: 172654 [Multi-domain]  Cd Length: 282  Bit Score: 309.65  E-value: 4.57e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   6 IDGTLISQTVRSEVAARVKARVAAGLRaPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLALIDE 85
Cdd:PRK14166   4 LDGKALSAKIKEELKEKNQFLKSKGIE-SCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALINT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  86 LNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPK-LRSCTPKGIITLLDRYNIELRGKHAVV 164
Cdd:PRK14166  83 LNHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGLESgFLPCTPLGVMKLLKAYEIDLEGKDAVI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 165 VGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSGKLVGDV 244
Cdd:PRK14166 163 IGASNIVGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLESGKIVGDV 242
                        250       260       270
                 ....*....|....*....|....*....|..
gi 491602985 245 EYDKARESASFITPVPGGVGPMTVASLIENTM 276
Cdd:PRK14166 243 DFEEVSKKSSYITPVPGGVGPMTIAMLLENTV 274
PRK14194 PRK14194
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-286 1.20e-101

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172682 [Multi-domain]  Cd Length: 301  Bit Score: 299.07  E-value: 1.20e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   1 MTAQNIDGTLISQTVRSEVAARVKARVAAGLRaPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELL 80
Cdd:PRK14194   2 MSAKLIDGKAAAARVLAQVREDVRTLKAAGIE-PALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  81 ALIDELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGK 160
Cdd:PRK14194  81 ALIAELNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSG-- 238
Cdd:PRK14194 161 HAVVIGRSNIVGKPMAALLLQAHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINRIDDDgr 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 491602985 239 -KLVGDVEYDKARESASFITPVPGGVGPMTVASLIENTMLACEQFHTEQ 286
Cdd:PRK14194 241 sRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAARLQAHAQ 289
PRK14178 PRK14178
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
34-278 1.48e-101

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172666 [Multi-domain]  Cd Length: 279  Bit Score: 297.91  E-value: 1.48e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  34 PGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLALIDELNNDNEIDGILVQLPLPAGIDTTHVLER 113
Cdd:PRK14178  27 PRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIRRLNEDPDINGILVQLPLPKGVDTERVIAA 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 114 IHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGKHAVVVGASNIVGRPMTLELLLAGCTTTTCHRFT 193
Cdd:PRK14178 107 ILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAVVVGRSIDVGRPMAALLLNADATVTICHSKT 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 194 KDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDsGKLVGDVEYDKARESASFITPVPGGVGPMTVASLIE 273
Cdd:PRK14178 187 ENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQVN-GKLCGDVDFDAVKEIAGAITPVPGGVGPMTIATLME 265

                 ....*
gi 491602985 274 NTMLA 278
Cdd:PRK14178 266 NTFDA 270
PRK14176 PRK14176
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
6-281 5.35e-100

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


Pssm-ID: 184553 [Multi-domain]  Cd Length: 287  Bit Score: 294.41  E-value: 5.35e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   6 IDGTLISQTVRSEVAARVKARVAAGLRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLALIDE 85
Cdd:PRK14176  11 IDGKALAKKIEAEVRSGVERLKSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELIDS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  86 LNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGKHAVVV 165
Cdd:PRK14176  91 LNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGKNAVIV 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 166 GASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDsGKLVGDVE 245
Cdd:PRK14176 171 GHSNVVGKPMAAMLLNRNATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITKEE-DKVYGDVD 249
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 491602985 246 YDKARESASFITPVPGGVGPMTVASLIENTMLACEQ 281
Cdd:PRK14176 250 FENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEK 285
PRK14180 PRK14180
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
6-283 1.66e-99

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


Pssm-ID: 172668 [Multi-domain]  Cd Length: 282  Bit Score: 293.09  E-value: 1.66e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   6 IDGTLISQTVRSEVAARVKARVAAGLRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLALIDE 85
Cdd:PRK14180   4 IDGKSLSKDLKERLATQVQEYKHHTAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELIDQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  86 LNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPK-LRSCTPKGIITLLDRYNIELRGKHAVV 164
Cdd:PRK14180  84 LNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLQLRDKKcLESCTPKGIMTMLREYGIKTEGAYAVV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 165 VGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDsGKLVGDV 244
Cdd:PRK14180 164 VGASNVVGKPVSQLLLNAKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHVD-GKIVGDV 242
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 491602985 245 EYDKARESASFITPVPGGVGPMTVASLIENTMLACEQFH 283
Cdd:PRK14180 243 DFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQELN 281
PRK14167 PRK14167
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
3-278 1.53e-98

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


Pssm-ID: 184549 [Multi-domain]  Cd Length: 297  Bit Score: 290.91  E-value: 1.53e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   3 AQNIDGTLISQTVRSEVAARVKARVAAGLRaPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLAL 82
Cdd:PRK14167   2 TEIIDGNAVAAQIRDDLTDAIETLEDAGVT-PGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  83 IDELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGKHA 162
Cdd:PRK14167  81 IDELNADEDVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 163 VVVGASNIVGRPMTLELLLAG----CTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSG 238
Cdd:PRK14167 161 VVVGRSDIVGKPMANLLIQKAdggnATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINRVDAD 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 491602985 239 -----KLVGDVEYDKARESASFITPVPGGVGPMTVASLIENTMLA 278
Cdd:PRK14167 241 tekgyELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKA 285
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
124-283 5.63e-98

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


Pssm-ID: 427036  Cd Length: 160  Bit Score: 284.36  E-value: 5.63e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  124 HPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGKHAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQA 203
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITREA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  204 DVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSGKLVGDVEYDKARESASFITPVPGGVGPMTVASLIENTMLACEQFH 283
Cdd:pfam02882  81 DIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNTVEAAKRQL 160
PRK14173 PRK14173
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
1-280 9.77e-97

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


Pssm-ID: 184551 [Multi-domain]  Cd Length: 287  Bit Score: 285.96  E-value: 9.77e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   1 MTAQNIDGTLISQTVRSEVAARVKARVAAglraPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELL 80
Cdd:PRK14173   1 MAARELSGPPAAEAVYAELRARLAKLPFV----PHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  81 ALIDELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGK 160
Cdd:PRK14173  77 ELIARLNADPEVDGILVQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRL--DSG 238
Cdd:PRK14173 157 EVVVVGRSNIVGKPLAALLLREDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINRVggNGG 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 491602985 239 K--LVGDVEYDKArESASFITPVPGGVGPMTVASLIENTMLACE 280
Cdd:PRK14173 237 RdiLTGDVHPEVA-EVAGALTPVPGGVGPMTVAMLMANTVIAAL 279
PRK14182 PRK14182
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
6-276 9.84e-97

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


Pssm-ID: 172670 [Multi-domain]  Cd Length: 282  Bit Score: 286.15  E-value: 9.84e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   6 IDGTLISQTVRSEVAARVKARVAAGLrAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLALIDE 85
Cdd:PRK14182   4 IDGKQIAAKVKGEVATEVRALAARGV-QTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIAR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  86 LNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKL-RSCTPKGIITLLDRYNIELRGKHAVV 164
Cdd:PRK14182  83 LNADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGVpRPCTPAGVMRMLDEARVDPKGKRALV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 165 VGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSGKLVGDV 244
Cdd:PRK14182 163 VGRSNIVGKPMAMMLLERHATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLADGKLVGDV 242
                        250       260       270
                 ....*....|....*....|....*....|..
gi 491602985 245 EYDKARESASFITPVPGGVGPMTVASLIENTM 276
Cdd:PRK14182 243 EFAAAAARASAITPVPGGVGPMTRAMLLVNTV 274
PRK14169 PRK14169
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
3-283 1.30e-96

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184550 [Multi-domain]  Cd Length: 282  Bit Score: 285.69  E-value: 1.30e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   3 AQNIDGTLISQTVRSEVAARVKARVAAGLrAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLAL 82
Cdd:PRK14169   1 ATRLDGRAVSKKILADLKQTVAKLAQQDV-TPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  83 IDELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGKHA 162
Cdd:PRK14169  80 VAELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 163 VVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSGKLVG 242
Cdd:PRK14169 160 VIVGRSNIVGRPLAGLMVNHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRGADGKLLG 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 491602985 243 DVEYDKARESASFITPVPGGVGPMTVASLIENTM-LACEQFH 283
Cdd:PRK14169 240 DVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVtLAKRRAN 281
PLN02616 PLN02616
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
3-286 2.13e-96

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 215332 [Multi-domain]  Cd Length: 364  Bit Score: 288.06  E-value: 2.13e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   3 AQNIDGTLISQTVRSEVAARVKARVAAGLRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLAL 82
Cdd:PLN02616  73 AKVIDGKAVAKKIRDEITIEVSRMKESIGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKF 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  83 IDELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQR--IPKLRSCTPKGIITLLDRYNIELRGK 160
Cdd:PLN02616 153 ISGFNNDPSVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMRgrEPLFVPCTPKGCIELLHRYNVEIKGK 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSG-- 238
Cdd:PLN02616 233 RAVVIGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPVEDAss 312
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491602985 239 ----KLVGDVEYDKARESASFITPVPGGVGPMTVASLIENTMLACEQFHTEQ 286
Cdd:PLN02616 313 prgyRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKRIHNFQ 364
PRK14185 PRK14185
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
4-278 2.34e-96

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184556 [Multi-domain]  Cd Length: 293  Bit Score: 285.18  E-value: 2.34e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   4 QNIDGTLISQTVRSEVAARVKARVAAGLRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLALI 83
Cdd:PRK14185   2 QLIDGKAISAQIKQEIAAEVAEIVAKGGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  84 DELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGKHAV 163
Cdd:PRK14185  82 RELNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 164 VVGASNIVGRPMTLELLLAG----CTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRL---- 235
Cdd:PRK14185 162 VLGRSNIVGKPMAQLMMQKAypgdCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTRVpdat 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 491602985 236 -DSG-KLVGDVEYDKARESASFITPVPGGVGPMTVASLIENTMLA 278
Cdd:PRK14185 242 rKSGfKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLA 286
PRK14192 PRK14192
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-281 4.34e-96

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184561 [Multi-domain]  Cd Length: 283  Bit Score: 284.43  E-value: 4.34e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   1 MTAQNIDGTLISQTVRSEVAARVKARVAAGLRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELL 80
Cdd:PRK14192   1 MMALVLDGKALAKQIEEELSVRVEALKAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  81 ALIDELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGK 160
Cdd:PRK14192  81 AKIEELNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSGKl 240
Cdd:PRK14192 161 HAVVVGRSAILGKPMAMMLLNANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFHPRDGGG- 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 491602985 241 VGDVEYDKARESASFITPVPGGVGPMTVASLIENTMLACEQ 281
Cdd:PRK14192 240 VGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEK 280
PLN02516 PLN02516
methylenetetrahydrofolate dehydrogenase (NADP+)
2-276 2.12e-95

methylenetetrahydrofolate dehydrogenase (NADP+)


Pssm-ID: 178131 [Multi-domain]  Cd Length: 299  Bit Score: 283.32  E-value: 2.12e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   2 TAQNIDGTLISQTVRSEVAARVKARVAAGLRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLA 81
Cdd:PLN02516   8 VAQIIDGKAIAKAIRSEIAEEVAQLSEKHGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELIS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  82 LIDELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQ--RIPKLRSCTPKGIITLLDRYNIELRG 159
Cdd:PLN02516  88 KVHELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMkgREPLFLPCTPKGCLELLSRSGIPIKG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 160 KHAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLD--- 236
Cdd:PLN02516 168 KKAVVVGRSNIVGLPVSLLLLKADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVSdps 247
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 491602985 237 --SG-KLVGDVEYDKARESASFITPVPGGVGPMTVASLIENTM 276
Cdd:PLN02516 248 kkSGyRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTV 290
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
116-280 1.60e-94

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: 275.97  E-value: 1.60e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 116 PEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGKHAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKD 195
Cdd:cd01080    1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKTKN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 196 LESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRL---DSGKLVGDVEYDKARESASFITPVPGGVGPMTVASLI 272
Cdd:cd01080   81 LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVpdkSGGKLVGDVDFESAKEKASAITPVPGGVGPMTVAMLM 160

                 ....*...
gi 491602985 273 ENTMLACE 280
Cdd:cd01080  161 KNTVEAAK 168
PRK14175 PRK14175
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-278 7.63e-92

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184552 [Multi-domain]  Cd Length: 286  Bit Score: 273.72  E-value: 7.63e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   1 MTAQNIDGTLISQTVRSEVAARVKARVAAGLrAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELL 80
Cdd:PRK14175   1 MVAKILDGKQIAKDYRQGLQDQVEALKEKGF-TPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  81 ALIDELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGK 160
Cdd:PRK14175  80 NELNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSGKL 240
Cdd:PRK14175 160 NAVVIGRSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVGNTPDENGKL 239
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 491602985 241 VGDVEYDKARESASFITPVPGGVGPMTVASLIENTMLA 278
Cdd:PRK14175 240 KGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLA 277
PRK14177 PRK14177
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
6-282 1.00e-90

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172665 [Multi-domain]  Cd Length: 284  Bit Score: 270.69  E-value: 1.00e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   6 IDGTLISQTVRSEVAARVKARVAAGLRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLALIDE 85
Cdd:PRK14177   6 LDGKKLSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLGVIDK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  86 LNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGKHAVVV 165
Cdd:PRK14177  86 LNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGKNAVVV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 166 GASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDsgklVGDVE 245
Cdd:PRK14177 166 GRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYNPGN----VGDIE 241
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 491602985 246 YDKARESASFITPVPGGVGPMTVASLIENTML-ACEQF 282
Cdd:PRK14177 242 ISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYsFKEHF 279
PRK14187 PRK14187
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
34-281 6.82e-90

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172675 [Multi-domain]  Cd Length: 294  Bit Score: 269.00  E-value: 6.82e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  34 PGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLALIDELNNDNEIDGILVQLPLPAGIDTTHVLER 113
Cdd:PRK14187  33 PCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKINELNNDDSVHGILVQLPVPNHIDKNLIINT 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 114 IHPEKDVDGFHPYNVGRL--AQRIPKLRSCTPKGIITLLDRYNIELRGKHAVVVGASNIVGRPMTLELLLAGCTTTTCHR 191
Cdd:PRK14187 113 IDPEKDVDGFHNENVGRLftGQKKNCLIPCTPKGCLYLIKTITRNLSGSDAVVIGRSNIVGKPMACLLLGENCTVTTVHS 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 192 FTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSG---KLVGDVEYDKARESASFITPVPGGVGPMTV 268
Cdd:PRK14187 193 ATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSIEEGgvkKFVGDVDFAEVKKKASAITPVPGGVGPMTI 272
                        250
                 ....*....|....
gi 491602985 269 ASLIENTML-ACEQ 281
Cdd:PRK14187 273 AFLMVNTVIaACNQ 286
PRK14172 PRK14172
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
4-282 2.87e-88

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


Pssm-ID: 172660 [Multi-domain]  Cd Length: 278  Bit Score: 264.34  E-value: 2.87e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   4 QNIDGTLISQTVRSEVAARVKARVAAGLRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLALI 83
Cdd:PRK14172   3 QIINGKEVALKIKEEIKNFVEERKENGLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  84 DELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGKHAV 163
Cdd:PRK14172  83 EELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 164 VVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDsGKLVGD 243
Cdd:PRK14172 163 VIGRSNIVGKPVAQLLLNENATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSVN-GKITGD 241
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 491602985 244 VEYDKARESASFITPVPGGVGPMTVASLIENtmlACEQF 282
Cdd:PRK14172 242 VNFDKVIDKASYITPVPGGVGSLTTTLLIKN---VCEAL 277
PLN02897 PLN02897
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
2-276 3.90e-88

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 178485 [Multi-domain]  Cd Length: 345  Bit Score: 266.44  E-value: 3.90e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   2 TAQNIDGTLISQTVRSEVAARVKARVAAGLRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLA 81
Cdd:PLN02897  55 KTVVIDGNVIAEEIRTKIASEVRKMKKAVGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILS 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  82 LIDELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQ--RIPKLRSCTPKGIITLLDRYNIELRG 159
Cdd:PLN02897 135 ALRKFNEDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMrgREPLFVSCTPKGCVELLIRSGVEIAG 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 160 KHAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSG- 238
Cdd:PLN02897 215 KNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPVEDSs 294
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 491602985 239 -----KLVGDVEYDKARESASFITPVPGGVGPMTVASLIENTM 276
Cdd:PLN02897 295 cefgyRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTL 337
PRK14168 PRK14168
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
1-283 1.48e-83

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237633 [Multi-domain]  Cd Length: 297  Bit Score: 252.87  E-value: 1.48e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   1 MTAQNIDGTLISQTVRSEVAARVKARVAAGLRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELL 80
Cdd:PRK14168   1 MSAKIIKGTEIREEILEEIRGEVAELKEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  81 ALIDELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRL--AQRIPKLRSCTPKGIITLLDRYNIELR 158
Cdd:PRK14168  81 ALIDKYNNDDSIHGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLmiGGDEVKFLPCTPAGIQEMLVRSGVETS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 159 GKHAVVVGASNIVGRPMTLELLLAG----CTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINR 234
Cdd:PRK14168 161 GAEVVVVGRSNIVGKPIANMMTQKGpganATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVNR 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491602985 235 L----DSGK--LVGDVEYDKARESASFITPVPGGVGPMTVASLIENTmLACEQFH 283
Cdd:PRK14168 241 VgtneSTGKaiLSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNT-LKSAKFH 294
PRK14171 PRK14171
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
6-278 2.62e-83

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172659 [Multi-domain]  Cd Length: 288  Bit Score: 252.19  E-value: 2.62e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   6 IDGTLISQTVRSEVAARVKARVAAGLRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLALIDE 85
Cdd:PRK14171   5 IDGKALANEILADLKLEIQELKSQTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKINE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  86 LNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPK-LRSCTPKGIITLLDRYNIELRGKHAVV 164
Cdd:PRK14171  85 LNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSGISQgFIPCTALGCLAVIKKYEPNLTGKNVVI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 165 VGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSGKLVGDV 244
Cdd:PRK14171 165 IGRSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRISGNKIIGDV 244
                        250       260       270
                 ....*....|....*....|....*....|....
gi 491602985 245 EYDKARESASFITPVPGGVGPMTVASLIENTMLA 278
Cdd:PRK14171 245 DFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKA 278
PRK14170 PRK14170
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
3-281 1.07e-78

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172658 [Multi-domain]  Cd Length: 284  Bit Score: 239.98  E-value: 1.07e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985   3 AQNIDGTLISQTVRSEVAARVKARVAAGlRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLAL 82
Cdd:PRK14170   2 GEIIDGKKLAKEIQEKVTREVAELVKEG-KKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  83 IDELNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVDGFHPYNVGRLAQRIPKLRSCTPKGIITLLDRYNIELRGKHA 162
Cdd:PRK14170  81 VEELNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 163 VVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRLDSGKLVG 242
Cdd:PRK14170 161 VVIGRSNIVGKPVAQLLLNENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDRDENNKLCG 240
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 491602985 243 DVEYDKARESASFITPVPGGVGPMTVASLIENTMLACEQ 281
Cdd:PRK14170 241 DVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKR 279
PRK14181 PRK14181
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
33-275 1.82e-78

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172669 [Multi-domain]  Cd Length: 287  Bit Score: 239.76  E-value: 1.82e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985  33 APGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLALIDELNNDNEIDGILVQLPLPAGIDTTHVLE 112
Cdd:PRK14181  26 APGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLIHRLNNDPNIHGILVQLPLPKHLDAQAILQ 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 113 RIHPEKDVDGFHPYNVGR-LAQRIPKLRSCTPKGIITLLDRYNIELRGKHAVVVGASNIVGRPMTLELLL----AGCTTT 187
Cdd:PRK14181 106 AISPDKDVDGLHPVNMGKlLLGETDGFIPCTPAGIIELLKYYEIPLHGRHVAIVGRSNIVGKPLAALLMQkhpdTNATVT 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 188 TCHRFTKDLESHVRQADVVVVAVGKPNFIPGEWIKKGAVVVDVGINRL--DSGK---LVGDVEYDKARESASFITPVPGG 262
Cdd:PRK14181 186 LLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRVpaANPKgyiLVGDVDFNNVVPKCRAITPVPGG 265
                        250
                 ....*....|...
gi 491602985 263 VGPMTVASLIENT 275
Cdd:PRK14181 266 VGPMTVAMLMRNT 278
THF_DHG_CYH pfam00763
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
6-121 4.82e-57

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;


Pssm-ID: 459930 [Multi-domain]  Cd Length: 115  Bit Score: 178.75  E-value: 4.82e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985    6 IDGTLISQTVRSEVAARVKARVAAGlRAPGLAVVLVGEDPASQVYVGSKRRACEEVGFVSKSFDLPASTSEEELLALIDE 85
Cdd:pfam00763   1 IDGKAIAKKIREELKEEVAALKAGG-RKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDK 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 491602985   86 LNNDNEIDGILVQLPLPAGIDTTHVLERIHPEKDVD 121
Cdd:pfam00763  80 LNADPSVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115
NAD_bind_m-THF_DH_Cyclohyd_like cd05212
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ...
141-280 3.56e-34

NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NAD(P) binding domains of methylene-tetrahydrofolate dehydrogenase (m-THF DH) and m-THF DH/cyclohydrolase bifunctional enzymes (m-THF DH/cyclohydrolase). M-THF is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, mono-functional DH, as well as bifunctional DH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express a monofunctional DH. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133451  Cd Length: 140  Bit Score: 121.07  E-value: 3.56e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 141 CTPKGI-------ITLLDRYNIELRGKHAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLESHVRQADVVVVAVGKP 213
Cdd:cd05212    3 CTPLFVspvakavKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSPKP 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491602985 214 NFIPGEWIKKGAVVVDVGINRLdsgklvgdvEYDKARESASFITPVPGGVGPMTVASLIENTMLACE 280
Cdd:cd05212   83 EKVPTEWIKPGATVINCSPTKL---------SGDDVKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140
NAD_bind_m-THF_DH cd01079
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ...
116-274 3.58e-12

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: 63.98  E-value: 3.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 116 PEKDVDGFHPYNVGRLAQRIPKLRS---------CTPKGIITLLD---------RYNIELRGKHAVVVGASNIVGRPMTL 177
Cdd:cd01079    1 PHKDVEGLSHKYIFNLYHNIRFLDPenrkksilpCTPLAIVKILEflgiynkilPYGNRLYGKTITIINRSEVVGRPLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 178 ELLLAGCTT---------------------TTCHRFTKDLESHVRQADVVVVAVGKPNF-IPGEWIKKGAVVVDVGINRL 235
Cdd:cd01079   81 LLANDGARVysvdingiqvftrgesirhekHHVTDEEAMTLDCLSQSDVVITGVPSPNYkVPTELLKDGAICINFASIKN 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 491602985 236 DSgklvgdveyDKARESASFITPVpggVGPMTVASLIEN 274
Cdd:cd01079  161 FE---------PSVKEKASIYVPS---IGKVTIAMLLRN 187
COG5322 COG5322
Predicted amino acid dehydrogenase [General function prediction only];
150-231 1.84e-03

Predicted amino acid dehydrogenase [General function prediction only];


Pssm-ID: 444114 [Multi-domain]  Cd Length: 362  Bit Score: 39.44  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602985 150 LDRYNIELRGKHAVVVGASNIVGRPMTLELLLAGCTTTTCHR---------------------FTKDLESHVRQADVVVV 208
Cdd:COG5322  142 AERMGIDLKKATVAVVGATGSIGSVCARLLAREVKRLTLVARnlerleelaeeilrnpggkvtITTDIDEALREADIVVT 221
                         90       100
                 ....*....|....*....|....
gi 491602985 209 AVGKPNF-IPGEWIKKGAVVVDVG 231
Cdd:COG5322  222 VTSAVGAiIDPEDLKPGAVVCDVA 245
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
196-232 8.08e-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: 8.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 491602985 196 LESHVRQADVVVVAVgkpnFIPG------------EWIKKGAVVVDVGI 232
Cdd:cd05305  225 LEEALKEADLVIGAV----LIPGakapklvteemvKTMKPGSVIVDVAI 269
 
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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