|
Name |
Accession |
Description |
Interval |
E-value |
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
18-311 |
9.48e-156 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 437.52 E-value: 9.48e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 18 AVVISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:COG0190 3 AQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:COG0190 82 IDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLhtdgAHErpggDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:COG0190 162 VVVGRSNIVGKPLALLL----LRR----NATVTVCHSRTK--DLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGI 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 568940988 258 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 311
Cdd:COG0190 232 NRVED-----GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
18-311 |
8.04e-128 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 366.64 E-value: 8.04e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 18 AVVISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK14190 3 AVIIDGKEVAKEKREQLKEEVVKLKEQG-IVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14190 82 IDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGKHV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14190 162 VVVGRSNIVGKPVGQLLLNE--------NATVTYCHSKTK--NLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGV 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 568940988 258 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 311
Cdd:PRK14190 232 NRLEN-----GKLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKR 280
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
18-311 |
1.10e-120 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 348.44 E-value: 1.10e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 18 AVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK10792 3 AKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELLAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK10792 83 IDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGLNA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLHTDGaherpggdATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK10792 163 VVVGASNIVGRPMSLELLLAG--------CTVTVCHRFTK--NLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 568940988 258 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 311
Cdd:PRK10792 233 NRLED-----GKLVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEE 281
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
18-315 |
3.51e-111 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 324.33 E-value: 3.51e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 18 AVVISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK14189 3 AQLIDGNALSKQLRAEAAQRAAALTARG-HQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14189 82 IDELNRDPKIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGAHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLHTDGaherpggdATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14189 162 VVIGRSNIVGKPMAMLLLQAG--------ATVTICHSKTR--DLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGM 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 568940988 258 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRP 315
Cdd:PRK14189 232 NRDDA-----GKLCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAERAAAA 284
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
18-311 |
1.27e-110 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 323.55 E-value: 1.27e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 18 AVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK14186 2 ALILDGKALAAEIEQRLQAQIESNLPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14186 82 IAQLNQDERVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14186 162 VVVGRSILVGKPLALMLLA--------ANATVTIAHSRTQ--DLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGI 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 568940988 258 NRVQDPvTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 311
Cdd:PRK14186 232 HRLPSS-DGKTRLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSWQK 284
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
19-314 |
1.34e-106 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 312.86 E-value: 1.34e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 19 VVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSI 98
Cdd:PRK14191 2 VLLDGKALSYKIEKDLKNKIQILTAQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 99 RKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVV 178
Cdd:PRK14191 82 KDLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 179 VAGRSKNVGMPIAMLLHTDGaherpggdATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGIN 258
Cdd:PRK14191 162 IIGASNIVGKPLAMLMLNAG--------ASVSVCHILT--KDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGIN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568940988 259 RVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 314
Cdd:PRK14191 232 RLND-----GRLVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEKRQR 282
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
17-311 |
9.81e-104 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 306.11 E-value: 9.81e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 17 EAVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLN 96
Cdd:PRK14188 1 MATIIDGKAFAADVRATVAAEVARLKAAHGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 97 SIRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKN 176
Cdd:PRK14188 81 LIARLNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 177 VVVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVG 256
Cdd:PRK14188 161 AVVIGRSNLVGKPMAQLLLAA--------NATVTIAHSRT--RDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVG 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 568940988 257 INRVQDPVTA--KPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 311
Cdd:PRK14188 231 INRIPAPEKGegKTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACR 287
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
20-313 |
3.84e-102 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 301.75 E-value: 3.84e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 20 VISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 99
Cdd:PRK14185 3 LIDGKAISAQIKQEIAAEVAEIVAKGGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 100 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVV 179
Cdd:PRK14185 83 ELNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 180 AGRSKNVGMPIAMLLHTDGAherpGGDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINR 259
Cdd:PRK14185 163 LGRSNIVGKPMAQLMMQKAY----PGDCTVTVCHSRSK--NLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568940988 260 VQDPVTAKP-KLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVL 313
Cdd:PRK14185 237 VPDATRKSGfKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKKAI 291
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
20-311 |
7.56e-100 |
|
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: 7.56e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 20 VISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 99
Cdd:PRK14184 3 LLDGKATAATIREELKTEVAALTARHGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 100 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVV 179
Cdd:PRK14184 83 ELNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 180 AGRSKNVGMPIAMLLHTDGaherPGGDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINR 259
Cdd:PRK14184 163 VGRSNIVGKPLALMLGAPG----KFANATVTVCHSRTP--DLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 568940988 260 VQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 311
Cdd:PRK14184 237 TDD------GLVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQSWKE 282
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
19-306 |
9.47e-100 |
|
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: 9.47e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 19 VVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSI 98
Cdd:PRK14174 2 LIIDGKKVSLDLKNELKTRVEAYRAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 99 RKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYS--MLPATPWGVWEIIKRTGIPTLGKN 176
Cdd:PRK14174 82 EDLNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGHLDkcFVSCTPYGILELLGRYNIETKGKH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 177 VVVAGRSKNVGMPIAMLLhtdgAHERPGGDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVG 256
Cdd:PRK14174 162 CVVVGRSNIVGKPMANLM----LQKLKESNCTVTICHSATK--DIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568940988 257 INRVQDPVT-AKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTI 306
Cdd:PRK14174 236 INRIEDPSTkSGYRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTL 286
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
20-310 |
2.15e-98 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 291.73 E-value: 2.15e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 20 VISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 99
Cdd:PRK14183 3 ILDGKALSDKIKENVKKEVDELKLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 100 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVV 179
Cdd:PRK14183 83 MMNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVCV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 180 AGRSKNVGMPIAMLLHTDGaherpggdATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINR 259
Cdd:PRK14183 163 VGASNIVGKPMAALLLNAN--------ATVDICHIFT--KDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINR 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568940988 260 VQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 310
Cdd:PRK14183 233 TED-----GRLVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAK 278
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
17-313 |
1.92e-97 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 289.78 E-value: 1.92e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 17 EAVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLN 96
Cdd:PRK14176 7 ESRIIDGKALAKKIEAEVRSGVERLKSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 97 SIRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKN 176
Cdd:PRK14176 87 LIDSLNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGKN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 177 VVVAGRSKNVGMPIA-MLLHTdgaherpggDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDV 255
Cdd:PRK14176 167 AVIVGHSNVVGKPMAaMLLNR---------NATVSVCHVFT--DDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 568940988 256 GINRVQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVL 313
Cdd:PRK14176 236 GITKEED------KVYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEKSL 287
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
18-311 |
2.85e-95 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 283.95 E-value: 2.85e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 18 AVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK14179 2 TEIIDGKALAQKMQAELAEKVAKLKEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14179 82 IERYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14179 162 VVIGRSNIVGKPMAQLLLDK--------NATVTLTHSRTR--NLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGM 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 568940988 258 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 311
Cdd:PRK14179 232 NRDEN-----GKLIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALR 280
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
18-310 |
1.23e-94 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 282.92 E-value: 1.23e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 18 AVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK14168 3 AKIIKGTEIREEILEEIRGEVAELKEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCL--DQYSMLPATPWGVWEIIKRTGIPTLGK 175
Cdd:PRK14168 83 IDKYNNDDSIHGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIggDEVKFLPCTPAGIQEMLVRSGVETSGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 176 NVVVAGRSKNVGMPIAMLLHTDGaherPGGDATVTISHryTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDV 255
Cdd:PRK14168 163 EVVVVGRSNIVGKPIANMMTQKG----PGANATVTIVH--TRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568940988 256 GINRV-QDPVTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 310
Cdd:PRK14168 237 GVNRVgTNESTGKAILSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAK 292
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
18-314 |
2.21e-93 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 279.21 E-value: 2.21e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 18 AVVISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK14193 3 AIILDGKATADEIKADLAERVAALKEKG-ITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELNAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14193 82 IDELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGAHV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLhtdgahERPGGDATVTISHryTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14193 162 VVIGRGVTVGRPIGLLL------TRRSENATVTLCH--TGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGV 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 568940988 258 NRVqdpvtAKPKLVGDVDfEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 314
Cdd:PRK14193 234 SRA-----GDGKLVGDVH-PDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAERRAG 284
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
18-313 |
2.56e-93 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 279.47 E-value: 2.56e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 18 AVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PLN02516 9 AQIIDGKAIAKAIRSEIAEEVAQLSEKHGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLD--QYSMLPATPWGVWEIIKRTGIPTLGK 175
Cdd:PLN02516 89 VHELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMKgrEPLFLPCTPKGCLELLSRSGIPIKGK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 176 NVVVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRYTPKEQlkkhTIL--ADIVISAAGIPNLITADMIKEGAAVI 253
Cdd:PLN02516 169 KAVVVGRSNIVGLPVSLLLLK--------ADATVTVVHSRTPDPE----SIVreADIVIAAAGQAMMIKGDWIKPGAAVI 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568940988 254 DVGINRVQDPVTAKP-KLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVL 313
Cdd:PLN02516 237 DVGTNAVSDPSKKSGyRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKRVF 297
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
20-309 |
8.43e-92 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 275.50 E-value: 8.43e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 20 VISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 99
Cdd:PRK14167 4 IIDGNAVAAQIRDDLTDAIETLEDAG-VTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 100 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVV 179
Cdd:PRK14167 83 ELNADEDVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADVVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 180 AGRSKNVGMPIAMLLhtdgAHERPGGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINR 259
Cdd:PRK14167 163 VGRSDIVGKPMANLL----IQKADGGNATVTVCHSRT--DDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 568940988 260 VQDPVTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAA 309
Cdd:PRK14167 237 VDADTEKGYELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAA 286
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
18-309 |
1.47e-90 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 272.09 E-value: 1.47e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 18 AVVISGRKLAQQIKQEVQQEVEEWVAsgnkRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK14173 3 ARELSGPPAAEAVYAELRARLAKLPF----VPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14173 79 IARLNADPEVDGILVQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGKEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLHtdgaherpGGDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14173 159 VVVGRSNIVGKPLAALLL--------REDATVTLAHSKTQ--DLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGI 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 568940988 258 NRVQDPvTAKPKLVGDVDfEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAA 309
Cdd:PRK14173 229 NRVGGN-GGRDILTGDVH-PEVAEVAGALTPVPGGVGPMTVAMLMANTVIAA 278
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
20-314 |
8.69e-90 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 269.97 E-value: 8.69e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 20 VISGRKLAQQIKQEVQQEVEEwVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 99
Cdd:PRK14166 3 LLDGKALSAKIKEELKEKNQF-LKSKGIESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 100 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLD-QYSMLPATPWGVWEIIKRTGIPTLGKNVV 178
Cdd:PRK14166 82 TLNHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGlESGFLPCTPLGVMKLLKAYEIDLEGKDAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 179 VAGRSKNVGMPIAMLLHTDGaherpggdATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGIN 258
Cdd:PRK14166 162 IIGASNIVGRPMATMLLNAG--------ATVSVCHIKT--KDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGIN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568940988 259 RVQdpvtaKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 314
Cdd:PRK14166 232 RLE-----SGKIVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAKNRLN 282
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
18-312 |
1.05e-89 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 272.65 E-value: 1.05e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 18 AVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PLN02616 73 AKVIDGKAVAKKIRDEITIEVSRMKESIGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSML--PATPWGVWEIIKRTGIPTLGK 175
Cdd:PLN02616 153 ISGFNNDPSVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMRGREPLfvPCTPKGCIELLHRYNVEIKGK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 176 NVVVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTPK-EQLKKHtilADIVISAAGIPNLITADMIKEGAAVID 254
Cdd:PLN02616 233 RAVVIGRSNIVGMPAALLLQRE--------DATVSIVHSRTKNpEEITRE---ADIIISAVGQPNMVRGSWIKPGAVVID 301
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 568940988 255 VGINRVQDPVTAKP-KLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKV 312
Cdd:PLN02616 302 VGINPVEDASSPRGyRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKRI 360
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
17-309 |
2.68e-88 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 266.69 E-value: 2.68e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 17 EAVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLN 96
Cdd:PRK14187 1 ETNIIDGKKIANDITEILATCIDDLKRQHNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 97 SIRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYS--MLPATPWGVWEIIKRTGIPTLG 174
Cdd:PRK14187 81 KINELNNDDSVHGILVQLPVPNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQKKncLIPCTPKGCLYLIKTITRNLSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 175 KNVVVAGRSKNVGMPIAMLLHtdgaherpGGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVID 254
Cdd:PRK14187 161 SDAVVIGRSNIVGKPMACLLL--------GENCTVTTVHSAT--RDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVID 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568940988 255 VGINRVQdpVTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAA 309
Cdd:PRK14187 231 VGINSIE--EGGVKKFVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAA 283
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
131-310 |
3.86e-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: 3.86e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 131 PDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHtdgaherpGGDATVT 210
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLL--------NRNATVT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 211 ISHRYTPKeqLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVQDPvtAKPKLVGDVDFEGVKKKAGYITPVP 290
Cdd:cd01080 73 VCHSKTKN--LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDK--SGGKLVGDVDFESAKEKASAITPVP 148
|
170 180
....*....|....*....|
gi 568940988 291 GGVGPMTVAMLMKNTIIAAK 310
Cdd:cd01080 149 GGVGPMTVAMLMKNTVEAAK 168
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
18-310 |
5.72e-87 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 262.93 E-value: 5.72e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 18 AVVISGRKLAQQIKQEVQQEVEEWVASGNKrPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK14175 3 AKILDGKQIAKDYRQGLQDQVEALKEKGFT-PKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLNE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14175 82 LNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGKNA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGi 257
Cdd:PRK14175 162 VVIGRSHIVGQPVSKLLLQ--------KNASVTILHSRS--KDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVG- 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568940988 258 nrvqDPVTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 310
Cdd:PRK14175 231 ----NTPDENGKLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEK 279
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
20-304 |
1.08e-86 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 262.02 E-value: 1.08e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 20 VISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 99
Cdd:PRK14172 4 IINGKEVALKIKEEIKNFVEERKENGLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 100 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVV 179
Cdd:PRK14172 84 ELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 180 AGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINR 259
Cdd:PRK14172 164 IGRSNIVGKPVAQLLLNE--------NATVTICHSKT--KNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSS 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 568940988 260 VQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKN 304
Cdd:PRK14172 234 VNG------KITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKN 272
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
18-311 |
1.39e-83 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 254.10 E-value: 1.39e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 18 AVVISGRKLAQQIKQEVQQEVEEwVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK14169 1 ATRLDGRAVSKKILADLKQTVAK-LAQQDVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14169 80 VAELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLhtdgaherPGGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14169 160 VIVGRSNIVGRPLAGLM--------VNHDATVTIAHSKT--RNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGI 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 568940988 258 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 311
Cdd:PRK14169 230 SRGAD-----GKLLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKR 278
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
139-311 |
5.47e-83 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 248.15 E-value: 5.47e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 139 HVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTPk 218
Cdd:pfam02882 1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA--------NATVTVCHSKTK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 219 eQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVQdpvtaKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTV 298
Cdd:pfam02882 72 -DLAEITREADIVVVAVGKPELIKADWIKPGAVVIDVGINRVG-----NGKLVGDVDFENVKEKASAITPVPGGVGPMTV 145
|
170
....*....|...
gi 568940988 299 AMLMKNTIIAAKK 311
Cdd:pfam02882 146 AMLLQNTVEAAKR 158
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
20-310 |
2.13e-81 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 248.72 E-value: 2.13e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 20 VISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 99
Cdd:PRK14171 4 IIDGKALANEILADLKLEIQELKSQTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKIN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 100 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRM--CLDQySMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14171 84 ELNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLhsGISQ-GFIPCTALGCLAVIKKYEPNLTGKNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14171 163 VIIGRSNIVGKPLSALLLKE--------NCSVTICHSKT--HNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568940988 258 NRVqdpvtAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 310
Cdd:PRK14171 233 NRI-----SGNKIIGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKAFK 280
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
19-310 |
2.20e-81 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 248.60 E-value: 2.20e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 19 VVISGRKLAQQIKQEVQQEVEEwvasGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSI 98
Cdd:PRK14178 1 MILDGKAVSEKRLELLKEEIIE----SGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 99 RKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVV 178
Cdd:PRK14178 77 RRLNEDPDINGILVQLPLPKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 179 VAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGIN 258
Cdd:PRK14178 157 VVGRSIDVGRPMAALLLN--------ADATVTICHSKT--ENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGIN 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 568940988 259 RVQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 310
Cdd:PRK14178 227 QVNG------KLCGDVDFDAVKEIAGAITPVPGGVGPMTIATLMENTFDAAK 272
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
13-312 |
3.63e-81 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 250.26 E-value: 3.63e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 13 DTRNEAVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEE 92
Cdd:PLN02897 51 ETEQKTVVIDGNVIAEEIRTKIASEVRKMKKAVGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 93 ELLNSIRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSML--PATPWGVWEIIKRTGI 170
Cdd:PLN02897 131 QILSALRKFNEDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREPLfvSCTPKGCVELLIRSGV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 171 PTLGKNVVVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYT--PKEQLKKhtilADIVISAAGIPNLITADMIKE 248
Cdd:PLN02897 211 EIAGKNAVVIGRSNIVGLPMSLLLQRH--------DATVSTVHAFTkdPEQITRK----ADIVIAAAGIPNLVRGSWLKP 278
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568940988 249 GAAVIDVGINRVQDPVTA-KPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKV 312
Cdd:PLN02897 279 GAVVIDVGTTPVEDSSCEfGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKRI 343
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
20-314 |
3.95e-81 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 248.07 E-value: 3.95e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 20 VISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 99
Cdd:PRK14170 4 IIDGKKLAKEIQEKVTREVAELVKEG-KKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSVVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 100 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVV 179
Cdd:PRK14170 83 ELNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRAVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 180 AGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINR 259
Cdd:PRK14170 163 IGRSNIVGKPVAQLLLNE--------NATVTIAHSRT--KDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDR 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568940988 260 VQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 314
Cdd:PRK14170 233 DEN-----NKLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKRIWK 282
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
19-314 |
7.42e-81 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 247.25 E-value: 7.42e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 19 VVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSI 98
Cdd:PRK14180 2 ILIDGKSLSKDLKERLATQVQEYKHHTAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 99 RKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCL-DQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14180 82 DQLNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLQLrDKKCLESCTPKGIMTMLREYGIKTEGAYA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14180 162 VVVGASNVVGKPVSQLLLN--------AKATVTTCHRFT--TDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGI 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 568940988 258 NRVQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 314
Cdd:PRK14180 232 NHVDG------KIVGDVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQELNR 282
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
16-310 |
9.05e-79 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 242.44 E-value: 9.05e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 16 NEAVVISGRKLAQQIKQEVQQEVEEWVASGNKrPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELL 95
Cdd:PRK14194 2 MSAKLIDGKAAAARVLAQVREDVRTLKAAGIE-PALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 96 NSIRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGK 175
Cdd:PRK14194 81 ALIAELNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 176 NVVVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHryTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDV 255
Cdd:PRK14194 161 HAVVIGRSNIVGKPMAALLLQ--------AHCSVTVVH--SRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDV 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568940988 256 GINRVQDpvTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 310
Cdd:PRK14194 231 GINRIDD--DGRSRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAAR 283
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
17-315 |
2.08e-78 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 241.03 E-value: 2.08e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 17 EAVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLN 96
Cdd:PRK14177 2 SPILLDGKKLSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 97 SIRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKN 176
Cdd:PRK14177 82 VIDKLNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGKN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 177 VVVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVG 256
Cdd:PRK14177 162 AVVVGRSPILGKPMAMLLTE--------MNATVTLCHSKT--QNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAG 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 568940988 257 INrvqdpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRP 315
Cdd:PRK14177 232 YN---------PGNVGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFKEHFTP 281
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
19-305 |
6.38e-77 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 237.45 E-value: 6.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 19 VVISGRKLAQQIKQEVQQEVeewvASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSI 98
Cdd:PRK14181 1 MLLKGAPAAEHILATIKENI----SASSTAPGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 99 RKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQY-SMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14181 77 HRLNNDPNIHGILVQLPLPKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGETdGFIPCTPAGIIELLKYYEIPLHGRHV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLhtdgAHERPGGDATVTISHryTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14181 157 AIVGRSNIVGKPLAALL----MQKHPDTNATVTLLH--SQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGT 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568940988 258 NRVQdpvTAKPK---LVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNT 305
Cdd:PRK14181 231 SRVP---AANPKgyiLVGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNT 278
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
18-314 |
4.09e-76 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 235.13 E-value: 4.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 18 AVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 97
Cdd:PRK14192 3 ALVLDGKALAKQIEEELSVRVEALKAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 98 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 177
Cdd:PRK14192 83 IEELNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 178 VVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 257
Cdd:PRK14192 163 VVVGRSAILGKPMAMMLLN--------ANATVTICHSRT--QNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGF 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 568940988 258 NRVQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 314
Cdd:PRK14192 233 HPRDG------GGVGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKALG 283
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
20-314 |
5.11e-72 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 224.52 E-value: 5.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 20 VISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 99
Cdd:PRK14182 3 LIDGKQIAAKVKGEVATEVRALAARG-VQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 100 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSM-LPATPWGVWEIIKRTGIPTLGKNVV 178
Cdd:PRK14182 82 RLNADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGVpRPCTPAGVMRMLDEARVDPKGKRAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 179 VAGRSKNVGMPIAMLLhtdgaHERpggDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGIN 258
Cdd:PRK14182 162 VVGRSNIVGKPMAMML-----LER---HATVTIAHSRT--ADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568940988 259 RVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 314
Cdd:PRK14182 232 RLAD-----GKLVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKRTAR 282
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
21-136 |
2.60e-60 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 188.77 E-value: 2.60e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 21 ISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIRK 100
Cdd:pfam00763 1 IDGKAIAKKIREELKEEVAALKAGG-RKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDK 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 568940988 101 LNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVD 136
Cdd:pfam00763 80 LNADPSVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
154-310 |
1.14e-20 |
|
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: 86.41 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 154 LPATPWGVWEIIKRTGI-------PTLGKNVVVAGRSKNVGMPIAMLLHTDGAherpggdaTVTISHRYTPKEQLKKHTi 226
Cdd:cd05212 1 GPCTPLFVSPVAKAVKEllnkegvRLDGKKVLVVGRSGIVGAPLQCLLQRDGA--------TVYSCDWKTIQLQSKVHD- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 227 lADIVISAAGIPNLITADMIKEGAAVIDVGINrvqdpvtakpKLVGDVdfegVKKKAGYITPVPGGVGPMTVAMLMKNTI 306
Cdd:cd05212 72 -ADVVVVGSPKPEKVPTEWIKPGATVINCSPT----------KLSGDD----VKESASLYVPMTGGVGKLTVAMRMQNMV 136
|
....
gi 568940988 307 IAAK 310
Cdd:cd05212 137 RSVR 140
|
|
| NAD_bind_m-THF_DH |
cd01079 |
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ... |
131-306 |
3.62e-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: 64.37 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 131 PDKDVDGFHVINVGRMC-----LD----QYSMLPATPWGVWEIIKRTGI---------PTLGKNVVVAGRSKNVGMPIAM 192
Cdd:cd01079 1 PHKDVEGLSHKYIFNLYhnirfLDpenrKKSILPCTPLAIVKILEFLGIynkilpygnRLYGKTITIINRSEVVGRPLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940988 193 LLHTDGAH----ERPGGDA-TVTISHRYTPK------EQLKKHTILADIVISAAGIPNL-ITADMIKEGAAVIDVGinrv 260
Cdd:cd01079 81 LLANDGARvysvDINGIQVfTRGESIRHEKHhvtdeeAMTLDCLSQSDVVITGVPSPNYkVPTELLKDGAICINFA---- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568940988 261 qdpvtakpklvGDVDFE-GVKKKAGYITPVpggVGPMTVAMLMKNTI 306
Cdd:cd01079 157 -----------SIKNFEpSVKEKASIYVPS---IGKVTIAMLLRNLL 189
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
219-257 |
2.84e-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: 2.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568940988 219 EQLKKHTILADIVISAAGIPN-----LITADMI---KEGAAVIDVGI 257
Cdd:smart01002 75 ELLEEAVKEADLVIGAVLIPGakapkLVTREMVksmKPGSVIVDVAA 121
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
204-257 |
3.13e-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: 38.93 E-value: 3.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568940988 204 GGDATVTISHRYTPKEQLKKhtilADIVISAAGIPN-----LITADMI---KEGAAVIDVGI 257
Cdd:cd05305 212 GGRVTTLYSNPANLEEALKE----ADLVIGAVLIPGakapkLVTEEMVktmKPGSVIVDVAI 269
|
|
| Ald |
COG0686 |
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ... |
200-257 |
4.59e-03 |
|
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and metabolism]; Alanine dehydrogenase (includes sporulation protein SpoVN) is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440450 [Multi-domain] Cd Length: 372 Bit Score: 38.45 E-value: 4.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568940988 200 HERPGGDATVTISHRYTPKEQLKKhtilADIVISAAGIPN-----LITADMI---KEGAAVIDVGI 257
Cdd:COG0686 208 DDIFGGRVTTLYSNPANIEEALKE----ADLVIGAVLIPGarapkLVTREMVkrmKPGSVIVDVAI 269
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
214-257 |
5.04e-03 |
|
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.
Pssm-ID: 426165 [Multi-domain] Cd Length: 213 Bit Score: 37.86 E-value: 5.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 568940988 214 RYTPKEQLKKHTILADIVISAAGI-----PNLITADMI---KEGAAVIDVGI 257
Cdd:pfam01262 79 LYSQAELIAEAVKEADLVIGTALIpgakaPKLVTREMVksmKPGSVIVDVAI 130
|
|
|