|
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
|
|
|