|
Name |
Accession |
Description |
Interval |
E-value |
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
36-329 |
5.54e-156 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 438.68 E-value: 5.54e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 36 AVVISGRKLAQQIKQEVRQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 115
Cdd:COG0190 3 AQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 116 IRTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKNV 195
Cdd:COG0190 82 IDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 196 VVAGRSKNVGMPIAMLLhtdgAHErpggDATVTISHRHTPkeQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGI 275
Cdd:COG0190 162 VVVGRSNIVGKPLALLL----LRR----NATVTVCHSRTK--DLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGI 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 157820897 276 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 329
Cdd:COG0190 232 NRVED-----GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
36-329 |
1.32e-128 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 369.34 E-value: 1.32e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 36 AVVISGRKLAQQIKQEVRQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 115
Cdd:PRK14190 3 AVIIDGKEVAKEKREQLKEEVVKLKEQG-IVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 116 IRTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKNV 195
Cdd:PRK14190 82 IDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGKHV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 196 VVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRHTPkeQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGI 275
Cdd:PRK14190 162 VVVGRSNIVGKPVGQLLLNE--------NATVTYCHSKTK--NLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGV 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 157820897 276 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 329
Cdd:PRK14190 232 NRLEN-----GKLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKR 280
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
36-329 |
1.12e-119 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 346.90 E-value: 1.12e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 36 AVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 115
Cdd:PRK10792 3 AKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELLAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 116 IRTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKNV 195
Cdd:PRK10792 83 IDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGLNA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 196 VVAGRSKNVGMPIAMLLHTDGaherpggdATVTISHRHTPkeQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGI 275
Cdd:PRK10792 163 VVVGASNIVGRPMSLELLLAG--------CTVTVCHRFTK--NLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 157820897 276 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 329
Cdd:PRK10792 233 NRLED-----GKLVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEE 281
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
36-333 |
6.56e-111 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 324.72 E-value: 6.56e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 36 AVVISGRKLAQQIKQEVRQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 115
Cdd:PRK14189 3 AQLIDGNALSKQLRAEAAQRAAALTARG-HQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 116 IRTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKNV 195
Cdd:PRK14189 82 IDELNRDPKIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGAHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 196 VVAGRSKNVGMPIAMLLHTDGaherpggdATVTISHRHTPkeQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGI 275
Cdd:PRK14189 162 VVIGRSNIVGKPMAMLLLQAG--------ATVTICHSKTR--DLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGM 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 157820897 276 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRP 333
Cdd:PRK14189 232 NRDDA-----GKLCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAERAAAA 284
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
36-329 |
6.05e-110 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 322.40 E-value: 6.05e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 36 AVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 115
Cdd:PRK14186 2 ALILDGKALAAEIEQRLQAQIESNLPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 116 IRTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKNV 195
Cdd:PRK14186 82 IAQLNQDERVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 196 VVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRHTPkeQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGI 275
Cdd:PRK14186 162 VVVGRSILVGKPLALMLLA--------ANATVTIAHSRTQ--DLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGI 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 157820897 276 NRVQDPvTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 329
Cdd:PRK14186 232 HRLPSS-DGKTRLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSWQK 284
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
37-332 |
2.54e-106 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 312.86 E-value: 2.54e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 37 VVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSI 116
Cdd:PRK14191 2 VLLDGKALSYKIEKDLKNKIQILTAQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 117 RTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKNVV 196
Cdd:PRK14191 82 KDLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 197 VAGRSKNVGMPIAMLLHTDGaherpggdATVTISHRHTpkEQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGIN 276
Cdd:PRK14191 162 IIGASNIVGKPLAMLMLNAG--------ASVSVCHILT--KDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGIN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 157820897 277 RVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 332
Cdd:PRK14191 232 RLND-----GRLVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEKRQR 282
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
35-329 |
1.08e-104 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 309.20 E-value: 1.08e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 35 EAVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLN 114
Cdd:PRK14188 1 MATIIDGKAFAADVRATVAAEVARLKAAHGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 115 SIRTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKN 194
Cdd:PRK14188 81 LIARLNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 195 VVVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRHTpkEQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVG 274
Cdd:PRK14188 161 AVVIGRSNLVGKPMAQLLLAA--------NATVTIAHSRT--RDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVG 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 157820897 275 INRVQDPVTA--KPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 329
Cdd:PRK14188 231 INRIPAPEKGegKTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACR 287
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
38-331 |
1.07e-101 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 301.36 E-value: 1.07e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 38 VISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 117
Cdd:PRK14185 3 LIDGKAISAQIKQEIAAEVAEIVAKGGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 118 TLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKNVVV 197
Cdd:PRK14185 83 ELNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 198 AGRSKNVGMPIAMLLHTDGAherpGGDATVTISHRHTPkeQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGINR 277
Cdd:PRK14185 163 LGRSNIVGKPMAQLMMQKAY----PGDCTVTVCHSRSK--NLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 157820897 278 VQDPVTAKP-KLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVL 331
Cdd:PRK14185 237 VPDATRKSGfKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKKAI 291
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
38-329 |
1.12e-99 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 295.92 E-value: 1.12e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 38 VISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 117
Cdd:PRK14184 3 LLDGKATAATIREELKTEVAALTARHGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 118 TLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKNVVV 197
Cdd:PRK14184 83 ELNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 198 AGRSKNVGMPIAMLLHTDGaherPGGDATVTISHRHTPkeQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGINR 277
Cdd:PRK14184 163 VGRSNIVGKPLALMLGAPG----KFANATVTVCHSRTP--DLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 157820897 278 VQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 329
Cdd:PRK14184 237 TDD------GLVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQSWKE 282
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
37-324 |
1.84e-99 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 295.96 E-value: 1.84e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 37 VVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSI 116
Cdd:PRK14174 2 LIIDGKKVSLDLKNELKTRVEAYRAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 117 RTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYS--MLPATPWGVWEILKRTGIPTLGKN 194
Cdd:PRK14174 82 EDLNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGHLDkcFVSCTPYGILELLGRYNIETKGKH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 195 VVVAGRSKNVGMPIAMLLhtdgAHERPGGDATVTISHRHTPkeQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVG 274
Cdd:PRK14174 162 CVVVGRSNIVGKPMANLM----LQKLKESNCTVTICHSATK--DIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 157820897 275 INRVQDPVT-AKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTI 324
Cdd:PRK14174 236 INRIEDPSTkSGYRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTL 286
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
38-328 |
4.43e-99 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 294.43 E-value: 4.43e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 38 VISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 117
Cdd:PRK14183 3 ILDGKALSDKIKENVKKEVDELKLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 118 TLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKNVVV 197
Cdd:PRK14183 83 MMNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVCV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 198 AGRSKNVGMPIAMLLHTDGaherpggdATVTISHRHTpkEQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGINR 277
Cdd:PRK14183 163 VGASNIVGKPMAALLLNAN--------ATVDICHIFT--KDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINR 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 157820897 278 VQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 328
Cdd:PRK14183 233 TED-----GRLVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAK 278
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
35-331 |
1.28e-97 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 290.94 E-value: 1.28e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 35 EAVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLN 114
Cdd:PRK14176 7 ESRIIDGKALAKKIEAEVRSGVERLKSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 115 SIRTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKN 194
Cdd:PRK14176 87 LIDSLNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGKN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 195 VVVAGRSKNVGMPIA-MLLHTdgaherpggDATVTISHRHTpkEQLKKHTILADIVISAAGIPNLITADMIKEGATVIDV 273
Cdd:PRK14176 167 AVIVGHSNVVGKPMAaMLLNR---------NATVSVCHVFT--DDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 157820897 274 GINRVQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVL 331
Cdd:PRK14176 236 GITKEED------KVYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEKSL 287
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
36-329 |
4.93e-95 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 283.95 E-value: 4.93e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 36 AVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 115
Cdd:PRK14179 2 TEIIDGKALAQKMQAELAEKVAKLKEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 116 IRTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKNV 195
Cdd:PRK14179 82 IERYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 196 VVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRHTpkEQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGI 275
Cdd:PRK14179 162 VVIGRSNIVGKPMAQLLLDK--------NATVTLTHSRT--RNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGM 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 157820897 276 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 329
Cdd:PRK14179 232 NRDEN-----GKLIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALR 280
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
36-328 |
3.25e-94 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 282.53 E-value: 3.25e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 36 AVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 115
Cdd:PRK14168 3 AKIIKGTEIREEILEEIRGEVAELKEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 116 IRTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCL--DQYSMLPATPWGVWEILKRTGIPTLGK 193
Cdd:PRK14168 83 IDKYNNDDSIHGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIggDEVKFLPCTPAGIQEMLVRSGVETSGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 194 NVVVAGRSKNVGMPIAMLLHTDGaherPGGDATVTIShrHTPKEQLKKHTILADIVISAAGIPNLITADMIKEGATVIDV 273
Cdd:PRK14168 163 EVVVVGRSNIVGKPIANMMTQKG----PGANATVTIV--HTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 157820897 274 GINRV-QDPVTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 328
Cdd:PRK14168 237 GVNRVgTNESTGKAILSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAK 292
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
36-331 |
2.27e-93 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 280.63 E-value: 2.27e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 36 AVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 115
Cdd:PLN02516 9 AQIIDGKAIAKAIRSEIAEEVAQLSEKHGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 116 IRTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLD--QYSMLPATPWGVWEILKRTGIPTLGK 193
Cdd:PLN02516 89 VHELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMKgrEPLFLPCTPKGCLELLSRSGIPIKGK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 194 NVVVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRHTPKEQlkkhTIL--ADIVISAAGIPNLITADMIKEGATVI 271
Cdd:PLN02516 169 KAVVVGRSNIVGLPVSLLLLK--------ADATVTVVHSRTPDPE----SIVreADIVIAAAGQAMMIKGDWIKPGAAVI 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157820897 272 DVGINRVQDPVTAKP-KLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVL 331
Cdd:PLN02516 237 DVGTNAVSDPSKKSGyRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKRVF 297
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
38-327 |
3.97e-93 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 279.74 E-value: 3.97e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 38 VISGRKLAQQIKQEVRQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 117
Cdd:PRK14167 4 IIDGNAVAAQIRDDLTDAIETLEDAG-VTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 118 TLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKNVVV 197
Cdd:PRK14167 83 ELNADEDVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADVVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 198 AGRSKNVGMPIAMLLhtdgAHERPGGDATVTISHRHTpkEQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGINR 277
Cdd:PRK14167 163 VGRSDIVGKPMANLL----IQKADGGNATVTVCHSRT--DDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 157820897 278 VQDPVTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAA 327
Cdd:PRK14167 237 VDADTEKGYELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAA 286
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
36-332 |
5.72e-92 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 276.12 E-value: 5.72e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 36 AVVISGRKLAQQIKQEVRQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 115
Cdd:PRK14193 3 AIILDGKATADEIKADLAERVAALKEKG-ITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELNAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 116 IRTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKNV 195
Cdd:PRK14193 82 IDELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGAHV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 196 VVAGRSKNVGMPIAMLLhtdgahERPGGDATVTISHRHTpkEQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGI 275
Cdd:PRK14193 162 VVIGRGVTVGRPIGLLL------TRRSENATVTLCHTGT--RDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGV 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 157820897 276 NRVqdpvtAKPKLVGDVDfEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 332
Cdd:PRK14193 234 SRA-----GDGKLVGDVH-PDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAERRAG 284
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
38-332 |
8.36e-91 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 273.44 E-value: 8.36e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 38 VISGRKLAQQIKQEVRQEVEEwVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 117
Cdd:PRK14166 3 LLDGKALSAKIKEELKEKNQF-LKSKGIESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 118 TLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLD-QYSMLPATPWGVWEILKRTGIPTLGKNVV 196
Cdd:PRK14166 82 TLNHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGlESGFLPCTPLGVMKLLKAYEIDLEGKDAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 197 VAGRSKNVGMPIAMLLHTDGaherpggdATVTISHRHTpkEQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGIN 276
Cdd:PRK14166 162 IIGASNIVGRPMATMLLNAG--------ATVSVCHIKT--KDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGIN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 157820897 277 RVQdpvtaKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 332
Cdd:PRK14166 232 RLE-----SGKIVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAKNRLN 282
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
36-330 |
1.41e-89 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 273.03 E-value: 1.41e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 36 AVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 115
Cdd:PLN02616 73 AKVIDGKAVAKKIRDEITIEVSRMKESIGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 116 IRTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSML--PATPWGVWEILKRTGIPTLGK 193
Cdd:PLN02616 153 ISGFNNDPSVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMRGREPLfvPCTPKGCIELLHRYNVEIKGK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 194 NVVVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRHTPK-EQLKKHtilADIVISAAGIPNLITADMIKEGATVID 272
Cdd:PLN02616 233 RAVVIGRSNIVGMPAALLLQRE--------DATVSIVHSRTKNpEEITRE---ADIIISAVGQPNMVRGSWIKPGAVVID 301
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 157820897 273 VGINRVQDPVTAKP-KLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKV 330
Cdd:PLN02616 302 VGINPVEDASSPRGyRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKRI 360
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
36-327 |
2.61e-89 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 269.78 E-value: 2.61e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 36 AVVISGRKLAQQIKQEVRQEVEEWVAsgnkRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 115
Cdd:PRK14173 3 ARELSGPPAAEAVYAELRARLAKLPF----VPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 116 IRTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKNV 195
Cdd:PRK14173 79 IARLNADPEVDGILVQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGKEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 196 VVAGRSKNVGMPIAMLLHtdgaherpGGDATVTISHRHTPkeQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGI 275
Cdd:PRK14173 159 VVVGRSNIVGKPLAALLL--------REDATVTLAHSKTQ--DLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGI 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 157820897 276 NRVQDPvTAKPKLVGDVDfEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAA 327
Cdd:PRK14173 229 NRVGGN-GGRDILTGDVH-PEVAEVAGALTPVPGGVGPMTVAMLMANTVIAA 278
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
35-327 |
9.29e-88 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 265.92 E-value: 9.29e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 35 EAVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLN 114
Cdd:PRK14187 1 ETNIIDGKKIANDITEILATCIDDLKRQHNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 115 SIRTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYS--MLPATPWGVWEILKRTGIPTLG 192
Cdd:PRK14187 81 KINELNNDDSVHGILVQLPVPNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQKKncLIPCTPKGCLYLIKTITRNLSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 193 KNVVVAGRSKNVGMPIAMLLHtdgaherpGGDATVTISHRHTpkEQLKKHTILADIVISAAGIPNLITADMIKEGATVID 272
Cdd:PRK14187 161 SDAVVIGRSNIVGKPMACLLL--------GENCTVTTVHSAT--RDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVID 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 157820897 273 VGINRVQdpVTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAA 327
Cdd:PRK14187 231 VGINSIE--EGGVKKFVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAA 283
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
38-322 |
1.66e-87 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 264.72 E-value: 1.66e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 38 VISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 117
Cdd:PRK14172 4 IINGKEVALKIKEEIKNFVEERKENGLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 118 TLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKNVVV 197
Cdd:PRK14172 84 ELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 198 AGRSKNVGMPIAMLLHTDgaherpggDATVTISHRHTpkEQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGINR 277
Cdd:PRK14172 164 IGRSNIVGKPVAQLLLNE--------NATVTICHSKT--KNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSS 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 157820897 278 VQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKN 322
Cdd:PRK14172 234 VNG------KITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKN 272
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
149-328 |
7.09e-87 |
|
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: 259.02 E-value: 7.09e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 149 PDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHtdgaherpGGDATVT 228
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLL--------NRNATVT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 229 ISHRHTPKeqLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGINRVQDPvtAKPKLVGDVDFEGVKKKAGYITPVP 308
Cdd:cd01080 73 VCHSKTKN--LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDK--SGGKLVGDVDFESAKEKASAITPVP 148
|
170 180
....*....|....*....|
gi 157820897 309 GGVGPMTVAMLMKNTIIAAK 328
Cdd:cd01080 149 GGVGPMTVAMLMKNTVEAAK 168
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
36-328 |
1.96e-86 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 262.16 E-value: 1.96e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 36 AVVISGRKLAQQIKQEVRQEVEEWVASGNKrPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 115
Cdd:PRK14175 3 AKILDGKQIAKDYRQGLQDQVEALKEKGFT-PKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLNE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 116 IRTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKNV 195
Cdd:PRK14175 82 LNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGKNA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 196 VVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRHTpkEQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGi 275
Cdd:PRK14175 162 VVIGRSHIVGQPVSKLLLQ--------KNASVTILHSRS--KDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVG- 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 157820897 276 nrvqDPVTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 328
Cdd:PRK14175 231 ----NTPDENGKLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEK 279
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
36-329 |
4.57e-84 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 256.03 E-value: 4.57e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 36 AVVISGRKLAQQIKQEVRQEVEEwVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 115
Cdd:PRK14169 1 ATRLDGRAVSKKILADLKQTVAK-LAQQDVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 116 IRTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKNV 195
Cdd:PRK14169 80 VAELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 196 VVAGRSKNVGMPIAMLLhtdgaherPGGDATVTISHRHTpkEQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGI 275
Cdd:PRK14169 160 VIVGRSNIVGRPLAGLM--------VNHDATVTIAHSKT--RNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGI 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 157820897 276 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 329
Cdd:PRK14169 230 SRGAD-----GKLLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKR 278
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
157-329 |
4.67e-84 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 251.62 E-value: 4.67e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 157 HVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRHTPk 236
Cdd:pfam02882 1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA--------NATVTVCHSKTK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 237 eQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGINRVQdpvtaKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTV 316
Cdd:pfam02882 72 -DLAEITREADIVVVAVGKPELIKADWIKPGAVVIDVGINRVG-----NGKLVGDVDFENVKEKASAITPVPGGVGPMTV 145
|
170
....*....|...
gi 157820897 317 AMLMKNTIIAAKK 329
Cdd:pfam02882 146 AMLLQNTVEAAKR 158
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
37-328 |
3.92e-81 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 248.60 E-value: 3.92e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 37 VVISGRKLAQQIKQEVRQEVEEwvasGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSI 116
Cdd:PRK14178 1 MILDGKAVSEKRLELLKEEIIE----SGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 117 RTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKNVV 196
Cdd:PRK14178 77 RRLNEDPDINGILVQLPLPKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 197 VAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRHTpkEQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGIN 276
Cdd:PRK14178 157 VVGRSIDVGRPMAALLLN--------ADATVTICHSKT--ENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGIN 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 157820897 277 RVQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 328
Cdd:PRK14178 227 QVNG------KLCGDVDFDAVKEIAGAITPVPGGVGPMTIATLMENTFDAAK 272
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
38-328 |
5.38e-81 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 248.33 E-value: 5.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 38 VISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 117
Cdd:PRK14171 4 IIDGKALANEILADLKLEIQELKSQTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKIN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 118 TLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRM--CLDQySMLPATPWGVWEILKRTGIPTLGKNV 195
Cdd:PRK14171 84 ELNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLhsGISQ-GFIPCTALGCLAVIKKYEPNLTGKNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 196 VVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRHTpkEQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGI 275
Cdd:PRK14171 163 VIIGRSNIVGKPLSALLLKE--------NCSVTICHSKT--HNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 157820897 276 NRVqdpvtAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 328
Cdd:PRK14171 233 NRI-----SGNKIIGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKAFK 280
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
38-332 |
5.85e-81 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 248.45 E-value: 5.85e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 38 VISGRKLAQQIKQEVRQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 117
Cdd:PRK14170 4 IIDGKKLAKEIQEKVTREVAELVKEG-KKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSVVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 118 TLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKNVVV 197
Cdd:PRK14170 83 ELNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRAVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 198 AGRSKNVGMPIAMLLHTDgaherpggDATVTISHRHTpkEQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGINR 277
Cdd:PRK14170 163 IGRSNIVGKPVAQLLLNE--------NATVTIAHSRT--KDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDR 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 157820897 278 VQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 332
Cdd:PRK14170 233 DEN-----NKLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKRIWK 282
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
35-330 |
3.42e-80 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 248.34 E-value: 3.42e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 35 EAVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLN 114
Cdd:PLN02897 55 KTVVIDGNVIAEEIRTKIASEVRKMKKAVGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 115 SIRTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSML--PATPWGVWEILKRTGIPTLG 192
Cdd:PLN02897 135 ALRKFNEDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREPLfvSCTPKGCVELLIRSGVEIAG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 193 KNVVVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRHT--PKEQLKKhtilADIVISAAGIPNLITADMIKEGATV 270
Cdd:PLN02897 215 KNAVVIGRSNIVGLPMSLLLQRH--------DATVSTVHAFTkdPEQITRK----ADIVIAAAGIPNLVRGSWLKPGAVV 282
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157820897 271 IDVGINRVQDPVTA-KPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKV 330
Cdd:PLN02897 283 IDVGTTPVEDSSCEfGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKRI 343
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
37-332 |
2.05e-79 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 244.17 E-value: 2.05e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 37 VVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSI 116
Cdd:PRK14180 2 ILIDGKSLSKDLKERLATQVQEYKHHTAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 117 RTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCL-DQYSMLPATPWGVWEILKRTGIPTLGKNV 195
Cdd:PRK14180 82 DQLNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLQLrDKKCLESCTPKGIMTMLREYGIKTEGAYA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 196 VVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRHTpkEQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGI 275
Cdd:PRK14180 162 VVVGASNVVGKPVSQLLLN--------AKATVTTCHRFT--TDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGI 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 157820897 276 NRVQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 332
Cdd:PRK14180 232 NHVDG------KIVGDVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQELNR 282
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
35-333 |
4.93e-78 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 240.65 E-value: 4.93e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 35 EAVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLN 114
Cdd:PRK14177 2 SPILLDGKKLSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 115 SIRTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKN 194
Cdd:PRK14177 82 VIDKLNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGKN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 195 VVVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRHTpkEQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVG 274
Cdd:PRK14177 162 AVVVGRSPILGKPMAMLLTE--------MNATVTLCHSKT--QNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAG 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 157820897 275 INrvqdpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRP 333
Cdd:PRK14177 232 YN---------PGNVGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFKEHFTP 281
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
34-328 |
1.09e-77 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 240.52 E-value: 1.09e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 34 NEAVVISGRKLAQQIKQEVRQEVEEWVASGNKrPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELL 113
Cdd:PRK14194 2 MSAKLIDGKAAAARVLAQVREDVRTLKAAGIE-PALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 114 NSIRTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGK 193
Cdd:PRK14194 81 ALIAELNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 194 NVVVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRHTpkEQLKKHTILADIVISAAGIPNLITADMIKEGATVIDV 273
Cdd:PRK14194 161 HAVVIGRSNIVGKPMAALLLQ--------AHCSVTVVHSRS--TDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDV 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 157820897 274 GINRVQDpvTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 328
Cdd:PRK14194 231 GINRIDD--DGRSRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAAR 283
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
37-323 |
5.77e-76 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 235.53 E-value: 5.77e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 37 VVISGRKLAQQIKQEVRQEVeewvASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSI 116
Cdd:PRK14181 1 MLLKGAPAAEHILATIKENI----SASSTAPGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 117 RTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQY-SMLPATPWGVWEILKRTGIPTLGKNV 195
Cdd:PRK14181 77 HRLNNDPNIHGILVQLPLPKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGETdGFIPCTPAGIIELLKYYEIPLHGRHV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 196 VVAGRSKNVGMPIAMLLhtdgAHERPGGDATVTISHRHTpkEQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGI 275
Cdd:PRK14181 157 AIVGRSNIVGKPLAALL----MQKHPDTNATVTLLHSQS--ENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGT 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 157820897 276 NRVQdpvTAKPK---LVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNT 323
Cdd:PRK14181 231 SRVP---AANPKgyiLVGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNT 278
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
36-332 |
8.65e-76 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 235.13 E-value: 8.65e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 36 AVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 115
Cdd:PRK14192 3 ALVLDGKALAKQIEEELSVRVEALKAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 116 IRTLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEILKRTGIPTLGKNV 195
Cdd:PRK14192 83 IEELNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 196 VVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRHTpkEQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGI 275
Cdd:PRK14192 163 VVVGRSAILGKPMAMMLLN--------ANATVTICHSRT--QNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGF 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 157820897 276 NRVQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 332
Cdd:PRK14192 233 HPRDG------GGVGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKALG 283
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
38-332 |
9.49e-71 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 222.20 E-value: 9.49e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 38 VISGRKLAQQIKQEVRQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 117
Cdd:PRK14182 3 LIDGKQIAAKVKGEVATEVRALAARG-VQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 118 TLNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVDGFHVINVGRMCLDQYSM-LPATPWGVWEILKRTGIPTLGKNVV 196
Cdd:PRK14182 82 RLNADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGVpRPCTPAGVMRMLDEARVDPKGKRAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 197 VAGRSKNVGMPIAMLLhtdgaHERpggDATVTISHRHTpkEQLKKHTILADIVISAAGIPNLITADMIKEGATVIDVGIN 276
Cdd:PRK14182 162 VVGRSNIVGKPMAMML-----LER---HATVTIAHSRT--ADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 157820897 277 RVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 332
Cdd:PRK14182 232 RLAD-----GKLVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKRTAR 282
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
39-154 |
2.27e-59 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 186.84 E-value: 2.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 39 ISGRKLAQQIKQEVRQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIRT 118
Cdd:pfam00763 1 IDGKAIAKKIREELKEEVAALKAGG-RKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDK 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 157820897 119 LNDDENVDGLLVQLPLPEHIDERKICNAVSPDKDVD 154
Cdd:pfam00763 80 LNADPSVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
172-328 |
2.74e-21 |
|
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: 88.33 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 172 LPATPWGVWEILKRTGI-------PTLGKNVVVAGRSKNVGMPIAMLLHTDGAherpggdaTVTISHRHTPKEQLKKHTi 244
Cdd:cd05212 1 GPCTPLFVSPVAKAVKEllnkegvRLDGKKVLVVGRSGIVGAPLQCLLQRDGA--------TVYSCDWKTIQLQSKVHD- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 245 lADIVISAAGIPNLITADMIKEGATVIDVGINrvqdpvtakpKLVGDVdfegVKKKAGYITPVPGGVGPMTVAMLMKNTI 324
Cdd:cd05212 72 -ADVVVVGSPKPEKVPTEWIKPGATVINCSPT----------KLSGDD----VKESASLYVPMTGGVGKLTVAMRMQNMV 136
|
....
gi 157820897 325 IAAK 328
Cdd:cd05212 137 RSVR 140
|
|
| NAD_bind_m-THF_DH |
cd01079 |
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ... |
149-324 |
1.20e-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: 65.91 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 149 PDKDVDGFHVINVGRMC-----LD----QYSMLPATPWGVWEILKRTGI---------PTLGKNVVVAGRSKNVGMPIAM 210
Cdd:cd01079 1 PHKDVEGLSHKYIFNLYhnirfLDpenrKKSILPCTPLAIVKILEFLGIynkilpygnRLYGKTITIINRSEVVGRPLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 211 LLHTDGA-------------HERPGGDATVTisHRHTPKEQLKKHTILADIVISAAGIPNL-ITADMIKEGATVIDVGin 276
Cdd:cd01079 81 LLANDGArvysvdingiqvfTRGESIRHEKH--HVTDEEAMTLDCLSQSDVVITGVPSPNYkVPTELLKDGAICINFA-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 157820897 277 rvqdpvtakpklvGDVDFE-GVKKKAGYITPVpggVGPMTVAMLMKNTI 324
Cdd:cd01079 157 -------------SIKNFEpSVKEKASIYVPS---IGKVTIAMLLRNLL 189
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
222-275 |
3.28e-03 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 37.49 E-value: 3.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157820897 222 GGDATVTISHRHTPKEQLKKhtilADIVISAAGIPN-----LITADMI---KEGATVIDVGI 275
Cdd:smart01002 64 GARFTTLYSQAELLEEAVKE----ADLVIGAVLIPGakapkLVTREMVksmKPGSVIVDVAA 121
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
222-275 |
5.71e-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: 38.16 E-value: 5.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157820897 222 GGDATVTISHRHTPKEQLKKhtilADIVISAAGIPN-----LITADMI---KEGATVIDVGI 275
Cdd:cd05305 212 GGRVTTLYSNPANLEEALKE----ADLVIGAVLIPGakapkLVTEEMVktmKPGSVIVDVAI 269
|
|
| MDR |
cd05188 |
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
166-289 |
9.78e-03 |
|
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.
Pssm-ID: 176178 [Multi-domain] Cd Length: 271 Bit Score: 37.30 E-value: 9.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820897 166 LDQYSMLPaTPWGV-WEILKRTGIPTLGKNVVVAGRSKnVGMPIAMLLHTDGAH--------------ERPGGDATVTIS 230
Cdd:cd05188 109 LEEAALLP-EPLATaYHALRRAGVLKPGDTVLVLGAGG-VGLLAAQLAKAAGARvivtdrsdeklelaKELGADHVIDYK 186
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157820897 231 HRHTPKEQLKKHTILADIVISAAGIPNLITA--DMIKEGATVIDVGINRVQDPVTAKPKLV 289
Cdd:cd05188 187 EEDLEEELRLTGGGGADVVIDAVGGPETLAQalRLLRPGGRIVVVGGTSGGPPLDDLRRLL 247
|
|
| |
