|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-292 |
0e+00 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 527.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 1 MQKIDGKATAAAIKAKIAEEVRQLVAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKC 80
Cdd:PRK14185 1 MQLIDGKAISAQIKQEIAAEVAEIVAKGGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 81 VDKLNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKC 160
Cdd:PRK14185 81 VRELNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 161 VILGRSNIVGKPMAQLMMQKAY-GNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDG 239
Cdd:PRK14185 161 VVLGRSNIVGKPMAQLMMQKAYpGDCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTRVPDA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 495401438 240 TRKSGFRLNGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGKKEYYR 292
Cdd:PRK14185 241 TRKSGFKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKKAIYK 293
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
19-288 |
2.71e-168 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 467.57 E-value: 2.71e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 19 EEVRQLVAKGgKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCVDKLNHDDNVDGFIVQLP 98
Cdd:COG0190 21 ERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLALIDELNADPSVHGILVQLP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 99 LPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKCVILGRSNIVGKPMAQLMM 178
Cdd:COG0190 100 LPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHAVVVGRSNIVGKPLALLLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 179 QKaygNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDGtrksgfRLNGDVKFDEVAP 258
Cdd:COG0190 180 RR---NATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVEDG------KLVGDVDFESVAE 250
|
250 260 270
....*....|....*....|....*....|
gi 495401438 259 KCSYITPVPGGVGPMTICSLMTNTLAAGKK 288
Cdd:COG0190 251 KASAITPVPGGVGPMTIAMLLENTLKAAER 280
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-288 |
3.72e-126 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 360.87 E-value: 3.72e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 4 IDGKATAAAIKAKIAEEVRQLVAKGgKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCVDK 83
Cdd:PRK14190 6 IDGKEVAKEKREQLKEEVVKLKEQG-IVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLALIDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 84 LNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKCVIL 163
Cdd:PRK14190 85 LNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGKHVVVV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 164 GRSNIVGKPMAQLMMQKaygNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDGtrks 243
Cdd:PRK14190 165 GRSNIVGKPVGQLLLNE---NATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRLENG---- 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 495401438 244 gfRLNGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGKK 288
Cdd:PRK14190 238 --KLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKR 280
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-288 |
5.12e-124 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 355.61 E-value: 5.12e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 1 MQKIDGKATAAAIKAKIAEEVRQLVAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKC 80
Cdd:PRK14191 1 MVLLDGKALSYKIEKDLKNKIQILTAQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 81 VDKLNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKC 160
Cdd:PRK14191 81 IKDLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 161 VILGRSNIVGKPMAQLMMQkayGNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDGt 240
Cdd:PRK14191 161 VIIGASNIVGKPLAMLMLN---AGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLNDG- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 495401438 241 rksgfRLNGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGKK 288
Cdd:PRK14191 237 -----RLVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEK 279
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-288 |
1.21e-123 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 354.47 E-value: 1.21e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 1 MQKIDGKATAAAIKAKIAEEVRQLVAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKC 80
Cdd:PRK14184 1 MLLLDGKATAATIREELKTEVAALTARHGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 81 VDKLNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKC 160
Cdd:PRK14184 81 IAELNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 161 VILGRSNIVGKPMAQLMMQKA-YGNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDG 239
Cdd:PRK14184 161 VVVGRSNIVGKPLALMLGAPGkFANATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRTDDG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 495401438 240 trksgfrLNGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGKK 288
Cdd:PRK14184 241 -------LVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQSWKE 282
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-283 |
1.58e-120 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 347.19 E-value: 1.58e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 1 MQKIDGKATAAAIKAKIAEEVRQLVAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKC 80
Cdd:PRK14174 1 MLIIDGKKVSLDLKNELKTRVEAYRAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 81 VDKLNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGL--PCFISATPLGIMTLLQHYNIDTNGK 158
Cdd:PRK14174 81 IEDLNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGHldKCFVSCTPYGILELLGRYNIETKGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 159 KCVILGRSNIVGKPMAQLMMQK-AYGNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVP 237
Cdd:PRK14174 161 HCVVVGRSNIVGKPMANLMLQKlKESNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRIE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 495401438 238 DGTRKSGFRLNGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTL 283
Cdd:PRK14174 241 DPSTKSGYRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTL 286
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-285 |
1.70e-118 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 341.51 E-value: 1.70e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 1 MQKIDGKATAAAIKAKIAEEVRQLVAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKC 80
Cdd:PRK10792 3 AKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELLAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 81 VDKLNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKC 160
Cdd:PRK10792 83 IDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGLNA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 161 VILGRSNIVGKPMAqlmMQKAYGNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDGt 240
Cdd:PRK10792 163 VVVGASNIVGRPMS---LELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLEDG- 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 495401438 241 rksgfRLNGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTLAA 285
Cdd:PRK10792 239 -----KLVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQA 278
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-288 |
6.79e-115 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 332.69 E-value: 6.79e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 4 IDGKATAAAIKAKIAEEVRQLVAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCVDK 83
Cdd:PRK14188 5 IDGKAFAADVRATVAAEVARLKAAHGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLALIAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 84 LNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKCVIL 163
Cdd:PRK14188 85 LNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLNAVVI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 164 GRSNIVGKPMAQLMMQKaygNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDGTRKS 243
Cdd:PRK14188 165 GRSNLVGKPMAQLLLAA---NATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIPAPEKGE 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 495401438 244 G-FRLNGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGKK 288
Cdd:PRK14188 242 GkTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACR 287
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
1-288 |
3.50e-114 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 330.56 E-value: 3.50e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 1 MQKIDGKATAAAIKAKIAEEVRQLVAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKC 80
Cdd:PRK14179 2 TEIIDGKALAQKMQAELAEKVAKLKEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 81 VDKLNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKC 160
Cdd:PRK14179 82 IERYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 161 VILGRSNIVGKPMAQLMMQKaygNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDGt 240
Cdd:PRK14179 162 VVIGRSNIVGKPMAQLLLDK---NATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMNRDENG- 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 495401438 241 rksgfRLNGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGKK 288
Cdd:PRK14179 238 -----KLIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALR 280
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
19-289 |
5.09e-114 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 330.11 E-value: 5.09e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 19 EEVRQLVA---KGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCVDKLNHDDNVDGFIV 95
Cdd:PRK14189 17 AEAAQRAAaltARGHQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLARIDELNRDPKIHGILV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 96 QLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKCVILGRSNIVGKPMAQ 175
Cdd:PRK14189 97 QLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGAHAVVIGRSNIVGKPMAM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 176 LMMQKaygNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDGtrksgfRLNGDVKFDE 255
Cdd:PRK14189 177 LLLQA---GATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMNRDDAG------KLCGDVDFAG 247
|
250 260 270
....*....|....*....|....*....|....
gi 495401438 256 VAPKCSYITPVPGGVGPMTICSLMTNTLAAGKKE 289
Cdd:PRK14189 248 VKEVAGYITPVPGGVGPMTITMLLVNTIEAAERA 281
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
19-288 |
1.15e-107 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 314.31 E-value: 1.15e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 19 EEVRQLVAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCVDKLNHDDNVDGFIVQLP 98
Cdd:PRK14186 20 AQIESNLPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEALIAQLNQDERVDGILLQLP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 99 LPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKCVILGRSNIVGKPMAqLMM 178
Cdd:PRK14186 100 LPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKKAVVVGRSILVGKPLA-LML 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 179 QKAygNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDGTRKSgfRLNGDVKFDEVAP 258
Cdd:PRK14186 179 LAA--NATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHRLPSSDGKT--RLCGDVDFEEVEP 254
|
250 260 270
....*....|....*....|....*....|
gi 495401438 259 KCSYITPVPGGVGPMTICSLMTNTLAAGKK 288
Cdd:PRK14186 255 VAAAITPVPGGVGPMTVTMLLVNTVLSWQK 284
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-287 |
1.10e-103 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 303.87 E-value: 1.10e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 1 MQKIDGKATAAAIKAKIAEEVRQLVAKGgKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKC 80
Cdd:PRK14166 1 MTLLDGKALSAKIKEELKEKNQFLKSKG-IESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 81 VDKLNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLPC-FISATPLGIMTLLQHYNIDTNGKK 159
Cdd:PRK14166 80 INTLNHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGLESgFLPCTPLGVMKLLKAYEIDLEGKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 160 CVILGRSNIVGKPMAQLMMQkayGNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDG 239
Cdd:PRK14166 160 AVIIGASNIVGRPMATMLLN---AGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLESG 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 495401438 240 trksgfRLNGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGK 287
Cdd:PRK14166 237 ------KIVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAK 278
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
2-281 |
1.08e-100 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 295.92 E-value: 1.08e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 2 QKIDGKATAAAIKAKIAEEVRQLVAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCV 81
Cdd:PRK14172 3 QIINGKEVALKIKEEIKNFVEERKENGLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 82 DKLNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKCV 161
Cdd:PRK14172 83 EELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 162 ILGRSNIVGKPMAQLMMQKaygNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVpDGtr 241
Cdd:PRK14172 163 VIGRSNIVGKPVAQLLLNE---NATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSV-NG-- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 495401438 242 ksgfRLNGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTN 281
Cdd:PRK14172 237 ----KITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKN 272
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-288 |
2.05e-100 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 295.70 E-value: 2.05e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 1 MQKIDGKATAAAIKAKIAEEVRQLvAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKC 80
Cdd:PRK14169 1 ATRLDGRAVSKKILADLKQTVAKL-AQQDVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 81 VDKLNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKC 160
Cdd:PRK14169 80 VAELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 161 VILGRSNIVGKPMAQLMMQKaygNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDGt 240
Cdd:PRK14169 160 VIVGRSNIVGRPLAGLMVNH---DATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRGADG- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 495401438 241 rksgfRLNGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGKK 288
Cdd:PRK14169 236 -----KLLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKR 278
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-287 |
3.75e-100 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 294.81 E-value: 3.75e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 1 MQKIDGKATAAAIKAKIAEEVRQLVAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKC 80
Cdd:PRK14183 1 MQILDGKALSDKIKENVKKEVDELKLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 81 VDKLNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKC 160
Cdd:PRK14183 81 IAMMNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 161 VILGRSNIVGKPMAQLMMQKaygNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDGt 240
Cdd:PRK14183 161 CVVGASNIVGKPMAALLLNA---NATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINRTEDG- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 495401438 241 rksgfRLNGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGK 287
Cdd:PRK14183 237 -----RLVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAK 278
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
25-285 |
3.25e-99 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 292.84 E-value: 3.25e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 25 VAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCVDKLNHDDNVDGFIVQLPLPKHIN 104
Cdd:PRK14167 25 LEDAGVTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTIDELNADEDVHGILVQMPVPDHVD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 105 EEKIVMAVDYKKDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKCVILGRSNIVGKPMAQLMMQKAY-G 183
Cdd:PRK14167 105 DREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADVVVVGRSDIVGKPMANLLIQKADgG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 184 NATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDGTRKsGFRLNGDVKFDEVAPKCSYI 263
Cdd:PRK14167 185 NATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINRVDADTEK-GYELVGDVEFESAKEKASAI 263
|
250 260
....*....|....*....|..
gi 495401438 264 TPVPGGVGPMTICSLMTNTLAA 285
Cdd:PRK14167 264 TPVPGGVGPMTRAMLLYNTVKA 285
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
19-285 |
8.50e-98 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 289.04 E-value: 8.50e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 19 EEVRQLVAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCVDKLNHDDNVDGFIVQLP 98
Cdd:PRK14173 17 AELRARLAKLPFVPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLELIARLNADPEVDGILVQLP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 99 LPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKCVILGRSNIVGKPMAQLMM 178
Cdd:PRK14173 97 LPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGKEVVVVGRSNIVGKPLAALLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 179 QKaygNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVP-DGTRKsgfRLNGDVKfDEVA 257
Cdd:PRK14173 177 RE---DATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINRVGgNGGRD---ILTGDVH-PEVA 249
|
250 260
....*....|....*....|....*...
gi 495401438 258 PKCSYITPVPGGVGPMTICSLMTNTLAA 285
Cdd:PRK14173 250 EVAGALTPVPGGVGPMTVAMLMANTVIA 277
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-287 |
1.73e-96 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 285.66 E-value: 1.73e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 4 IDGKATAAAIKAKIAEEVRQLVAKGgKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCVDK 83
Cdd:PRK14175 6 LDGKQIAKDYRQGLQDQVEALKEKG-FTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLNELNR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 84 LNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKCVIL 163
Cdd:PRK14175 85 LNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGKNAVVI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 164 GRSNIVGKPMAQLMMQKaygNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDGtrks 243
Cdd:PRK14175 165 GRSHIVGQPVSKLLLQK---NASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVGNTPDENG---- 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 495401438 244 gfRLNGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGK 287
Cdd:PRK14175 238 --KLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEK 279
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
4-290 |
1.46e-94 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 283.00 E-value: 1.46e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 4 IDGKATAAAIKAKIAEEVRQLVAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCVDK 83
Cdd:PLN02897 59 IDGNVIAEEIRTKIASEVRKMKKAVGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILSALRK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 84 LNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSI--GLPCFISATPLGIMTLLQHYNIDTNGKKCV 161
Cdd:PLN02897 139 FNEDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMrgREPLFVSCTPKGCVELLIRSGVEIAGKNAV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 162 ILGRSNIVGKPMAqLMMQKAygNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDGTR 241
Cdd:PLN02897 219 VIGRSNIVGLPMS-LLLQRH--DATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPVEDSSC 295
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 495401438 242 KSGFRLNGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGKKEY 290
Cdd:PLN02897 296 EFGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKRIF 344
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-290 |
3.42e-94 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 279.77 E-value: 3.42e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 4 IDGKATAAAIKAKIAEEVRQLVAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCVDK 83
Cdd:PRK14176 11 IDGKALAKKIEAEVRSGVERLKSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELIDS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 84 LNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKCVIL 163
Cdd:PRK14176 91 LNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGKNAVIV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 164 GRSNIVGKPMAQLMMQKaygNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDGTRks 243
Cdd:PRK14176 171 GHSNVVGKPMAAMLLNR---NATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITKEEDKVY-- 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 495401438 244 gfrlnGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGKKEY 290
Cdd:PRK14176 246 -----GDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEKSL 287
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
4-288 |
3.60e-94 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 282.66 E-value: 3.60e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 4 IDGKATAAAIKAKIAEEVRQLVAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCVDK 83
Cdd:PLN02616 76 IDGKAVAKKIRDEITIEVSRMKESIGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKFISG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 84 LNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSI--GLPCFISATPLGIMTLLQHYNIDTNGKKCV 161
Cdd:PLN02616 156 FNNDPSVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMrgREPLFVPCTPKGCIELLHRYNVEIKGKRAV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 162 ILGRSNIVGKPmAQLMMQKAygNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDGTR 241
Cdd:PLN02616 236 VIGRSNIVGMP-AALLLQRE--DATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPVEDASS 312
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 495401438 242 KSGFRLNGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGKK 288
Cdd:PLN02616 313 PRGYRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKR 359
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
2-290 |
5.56e-94 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 279.85 E-value: 5.56e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 2 QKIDGKATAAAIKAKIAEEVRQLVAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCV 81
Cdd:PLN02516 10 QIIDGKAIAKAIRSEIAEEVAQLSEKHGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISKV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 82 DKLNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIG--LPCFISATPLGIMTLLQHYNIDTNGKK 159
Cdd:PLN02516 90 HELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMKgrEPLFLPCTPKGCLELLSRSGIPIKGKK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 160 CVILGRSNIVGKPMAQLMMQkayGNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDG 239
Cdd:PLN02516 170 AVVVGRSNIVGLPVSLLLLK---ADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVSDP 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 495401438 240 TRKSGFRLNGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGKKEY 290
Cdd:PLN02516 247 SKKSGYRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKRVF 297
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-289 |
1.58e-93 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 278.65 E-value: 1.58e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 4 IDGKATAAAIKAKIAEEVRQLVAkGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCVDK 83
Cdd:PRK14194 7 IDGKAAAARVLAQVREDVRTLKA-AGIEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLLALIAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 84 LNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKCVIL 163
Cdd:PRK14194 86 LNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGKHAVVI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 164 GRSNIVGKPMAQLMMQkayGNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDGTRKs 243
Cdd:PRK14194 166 GRSNIVGKPMAALLLQ---AHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINRIDDDGRS- 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 495401438 244 gfRLNGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGKKE 289
Cdd:PRK14194 242 --RLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAARLQ 285
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
116-287 |
3.84e-93 |
|
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: 272.89 E-value: 3.84e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 116 KDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKCVILGRSNIVGKPMAQLMMQKaygNATVTVCHSQSK 195
Cdd:cd01080 3 KDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNR---NATVTVCHSKTK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 196 NIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDgtrKSGFRLNGDVKFDEVAPKCSYITPVPGGVGPMTI 275
Cdd:cd01080 80 NLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPD---KSGGKLVGDVDFESAKEKASAITPVPGGVGPMTV 156
|
170
....*....|..
gi 495401438 276 CSLMTNTLAAGK 287
Cdd:cd01080 157 AMLMKNTVEAAK 168
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
2-281 |
4.65e-93 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 276.89 E-value: 4.65e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 2 QKIDGKATAAAIKAKIAEEVRQLVAKGgKRPHLAAVLVGHDGGSETYVRNKVLACEECGFEStlIRYE--ENVTEEELLK 79
Cdd:PRK14193 4 IILDGKATADEIKADLAERVAALKEKG-ITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITS--IRRDlpADATQEELNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 80 CVDKLNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIG----LPCfisaTPLGIMTLLQHYNIDT 155
Cdd:PRK14193 81 VIDELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNepapLPC----TPRGIVHLLRRYDVEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 156 NGKKCVILGRSNIVGKPMAqLMMQKAYGNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTR 235
Cdd:PRK14193 157 AGAHVVVIGRGVTVGRPIG-LLLTRRSENATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSR 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 495401438 236 VPDGtrksgfRLNGDVKFDeVAPKCSYITPVPGGVGPMTICSLMTN 281
Cdd:PRK14193 236 AGDG------KLVGDVHPD-VWEVAGAVSPNPGGVGPMTRAFLLTN 274
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
19-282 |
2.78e-92 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 275.20 E-value: 2.78e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 19 EEVRQLVAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCVDKLNHDDNVDGFIVQLP 98
Cdd:PRK14181 14 ATIKENISASSTAPGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLIHRLNNDPNIHGILVQLP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 99 LPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIG-LPCFISATPLGIMTLLQHYNIDTNGKKCVILGRSNIVGKPMAQLM 177
Cdd:PRK14181 94 LPKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGeTDGFIPCTPAGIIELLKYYEIPLHGRHVAIVGRSNIVGKPLAALL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 178 MQK-AYGNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDGTRKsGFRLNGDVKFDEV 256
Cdd:PRK14181 174 MQKhPDTNATVTLLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRVPAANPK-GYILVGDVDFNNV 252
|
250 260
....*....|....*....|....*.
gi 495401438 257 APKCSYITPVPGGVGPMTICSLMTNT 282
Cdd:PRK14181 253 VPKCRAITPVPGGVGPMTVAMLMRNT 278
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
122-288 |
7.09e-92 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 269.34 E-value: 7.09e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 122 HPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKCVILGRSNIVGKPMAQLMMQKaygNATVTVCHSQSKNIKQEC 201
Cdd:pfam02882 1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA---NATVTVCHSKTKDLAEIT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 202 READIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDGtrksgfRLNGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTN 281
Cdd:pfam02882 78 READIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNG------KLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQN 151
|
....*..
gi 495401438 282 TLAAGKK 288
Cdd:pfam02882 152 TVEAAKR 158
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
2-288 |
1.21e-90 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 270.79 E-value: 1.21e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 2 QKIDGKATAAAIKAKIAEEVRQLvAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCV 81
Cdd:PRK14170 3 EIIDGKKLAKEIQEKVTREVAEL-VKEGKKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 82 DKLNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKCV 161
Cdd:PRK14170 82 EELNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 162 ILGRSNIVGKPMAQLMMQKaygNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDGtr 241
Cdd:PRK14170 162 VIGRSNIVGKPVAQLLLNE---NATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDRDENN-- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 495401438 242 ksgfRLNGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGKK 288
Cdd:PRK14170 237 ----KLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKR 279
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
19-287 |
3.08e-90 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 269.41 E-value: 3.08e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 19 EEVRQLVAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCVDKLNHDDNVDGFIVQLP 98
Cdd:PRK14178 14 ELLKEEIIESGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIRRLNEDPDINGILVQLP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 99 LPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKCVILGRSNIVGKPMAQLMM 178
Cdd:PRK14178 94 LPKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAVVVGRSIDVGRPMAALLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 179 QkayGNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVpDGtrksgfRLNGDVKFDEVAP 258
Cdd:PRK14178 174 N---ADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQV-NG------KLCGDVDFDAVKE 243
|
250 260
....*....|....*....|....*....
gi 495401438 259 KCSYITPVPGGVGPMTICSLMTNTLAAGK 287
Cdd:PRK14178 244 IAGAITPVPGGVGPMTIATLMENTFDAAK 272
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
20-287 |
1.22e-87 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 263.66 E-value: 1.22e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 20 EVRQLVAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCVDKLNHDDNVDGFIVQLPL 99
Cdd:PRK14168 22 EVAELKEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLALIDKYNNDDSIHGILVQLPL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 100 PKHINEEKIVMAVDYKKDVDGFHPINVGRMSIG------LPCfisaTPLGIMTLLQHYNIDTNGKKCVILGRSNIVGKPM 173
Cdd:PRK14168 102 PKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIGgdevkfLPC----TPAGIQEMLVRSGVETSGAEVVVVGRSNIVGKPI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 174 AQLMMQKAYG-NATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDGTRKSGFRLNGDVK 252
Cdd:PRK14168 178 ANMMTQKGPGaNATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVNRVGTNESTGKAILSGDVD 257
|
250 260 270
....*....|....*....|....*....|....*
gi 495401438 253 FDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGK 287
Cdd:PRK14168 258 FDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAK 292
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-289 |
3.75e-83 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 251.69 E-value: 3.75e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 4 IDGKATAAAIKAKIAEEVRQLVAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCVDK 83
Cdd:PRK14192 6 LDGKALAKQIEEELSVRVEALKAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLAKIEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 84 LNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKCVIL 163
Cdd:PRK14192 86 LNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGKHAVVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 164 GRSNIVGKPMAQLMMQkayGNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDGTRks 243
Cdd:PRK14192 166 GRSAILGKPMAMMLLN---ANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFHPRDGGGV-- 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 495401438 244 gfrlnGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGKKE 289
Cdd:PRK14192 241 -----GDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKA 281
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-288 |
3.76e-83 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 251.49 E-value: 3.76e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 1 MQKIDGKATAAAIKAKIAEEVRQLVAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKC 80
Cdd:PRK14180 1 MILIDGKSLSKDLKERLATQVQEYKHHTAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 81 VDKLNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSI-GLPCFISATPLGIMTLLQHYNIDTNGKK 159
Cdd:PRK14180 81 IDQLNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLQLrDKKCLESCTPKGIMTMLREYGIKTEGAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 160 CVILGRSNIVGKPMAQLMMQkayGNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVpDG 239
Cdd:PRK14180 161 AVVVGASNVVGKPVSQLLLN---AKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHV-DG 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 495401438 240 trksgfRLNGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGKK 288
Cdd:PRK14180 237 ------KIVGDVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQE 279
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-291 |
6.09e-83 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 251.41 E-value: 6.09e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 4 IDGKATAAAIKAKIAEEVRQLVAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCVDK 83
Cdd:PRK14171 5 IDGKALANEILADLKLEIQELKSQTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKINE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 84 LNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLP-CFISATPLGIMTLLQHYNIDTNGKKCVI 162
Cdd:PRK14171 85 LNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSGISqGFIPCTALGCLAVIKKYEPNLTGKNVVI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 163 LGRSNIVGKPMAQLMMQKaygNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVpdgtrk 242
Cdd:PRK14171 165 IGRSNIVGKPLSALLLKE---NCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRI------ 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 495401438 243 SGFRLNGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGKKEYY 291
Cdd:PRK14171 236 SGNKIIGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKAFKDSLY 284
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-290 |
2.65e-82 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 249.51 E-value: 2.65e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 4 IDGKATAAAIKAKIAEEVRQLVAKGGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCVDK 83
Cdd:PRK14177 6 LDGKKLSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLGVIDK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 84 LNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGLPCFISATPLGIMTLLQHYNIDTNGKKCVIL 163
Cdd:PRK14177 86 LNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGKNAVVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 164 GRSNIVGKPMAQLMMQKaygNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTrvPDGTrks 243
Cdd:PRK14177 166 GRSPILGKPMAMLLTEM---NATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYN--PGNV--- 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 495401438 244 gfrlnGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGKKEY 290
Cdd:PRK14177 238 -----GDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFKEHF 279
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-288 |
6.28e-81 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 246.09 E-value: 6.28e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 1 MQKIDGKATAAAIKAKIAEEVRQLVAKGgKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKC 80
Cdd:PRK14182 1 MNLIDGKQIAAKVKGEVATEVRALAARG-VQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 81 VDKLNHDDNVDGFIVQLPLPKHINEEKIVMAVDYKKDVDGFHPINVGRMSIGL-----PCfisaTPLGIMTLLQHYNIDT 155
Cdd:PRK14182 80 IARLNADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIagvprPC----TPAGVMRMLDEARVDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 156 NGKKCVILGRSNIVGKPMAQLMMQKaygNATVTVCHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTR 235
Cdd:PRK14182 156 KGKRALVVGRSNIVGKPMAMMLLER---HATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNR 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 495401438 236 VPDGtrksgfRLNGDVKFDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGKK 288
Cdd:PRK14182 233 LADG------KLVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKR 279
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
32-285 |
2.01e-80 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 245.12 E-value: 2.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 32 PHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCVDKLNHDDNVDGFIVQLPLPKHINEEKIVMA 111
Cdd:PRK14187 33 PCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKINELNNDDSVHGILVQLPVPNHIDKNLIINT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 112 VDYKKDVDGFHPINVGRMSIG--LPCFISATPLGIMTLLQHYNIDTNGKKCVILGRSNIVGKPMAQLMMQKaygNATVTV 189
Cdd:PRK14187 113 IDPEKDVDGFHNENVGRLFTGqkKNCLIPCTPKGCLYLIKTITRNLSGSDAVVIGRSNIVGKPMACLLLGE---NCTVTT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 190 CHSQSKNIKQECREADIIIAAIGVPNFVTADMVKEGAVVIDVGTTRVPDGTRKsgfRLNGDVKFDEVAPKCSYITPVPGG 269
Cdd:PRK14187 190 VHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSIEEGGVK---KFVGDVDFAEVKKKASAITPVPGG 266
|
250
....*....|....*.
gi 495401438 270 VGPMTICSLMTNTLAA 285
Cdd:PRK14187 267 VGPMTIAFLMVNTVIA 282
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
19-119 |
8.19e-51 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 162.96 E-value: 8.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 19 EEVRQLVAK---GGKRPHLAAVLVGHDGGSETYVRNKVLACEECGFESTLIRYEENVTEEELLKCVDKLNHDDNVDGFIV 95
Cdd:pfam00763 12 EELKEEVAAlkaGGRKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKLNADPSVHGILV 91
|
90 100
....*....|....*....|....
gi 495401438 96 QLPLPKHINEEKIVMAVDYKKDVD 119
Cdd:pfam00763 92 QLPLPKHIDEEKVLEAIDPEKDVD 115
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
134-287 |
4.47e-26 |
|
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: 99.89 E-value: 4.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 134 PCFISATPLGIMTLLQHYNIDTNGKKCVILGRSNIVGKPMAQLMMQKaygNATVTVCHSQSKNIKQECREADIIIAAIGV 213
Cdd:cd05212 5 PLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRD---GATVYSCDWKTIQLQSKVHDADVVVVGSPK 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495401438 214 PNFVTADMVKEGAVVIDVGTTRVPDgtrksgfrlngdvkfDEVAPKCSYITPVPGGVGPMTICSLMTNTLAAGK 287
Cdd:cd05212 82 PEKVPTEWIKPGATVINCSPTKLSG---------------DDVKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140
|
|
| NAD_bind_m-THF_DH |
cd01079 |
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ... |
116-283 |
5.00e-10 |
|
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: 57.82 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 116 KDVDGFHPINVGRM--------------SIgLPCfisaTPLGIMTLLQHYNIDTN---------GKKCVILGRSNIVGKP 172
Cdd:cd01079 3 KDVEGLSHKYIFNLyhnirfldpenrkkSI-LPC----TPLAIVKILEFLGIYNKilpygnrlyGKTITIINRSEVVGRP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 173 MAQLMmqkAYGNATV-------TVCHSQSKNIKQECRE--------------ADIIIAAIGVPNF-VTADMVKEGAVVID 230
Cdd:cd01079 78 LAALL---ANDGARVysvdingIQVFTRGESIRHEKHHvtdeeamtldclsqSDVVITGVPSPNYkVPTELLKDGAICIN 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495401438 231 VGTTRVPDgtrksgfrlngdvkfDEVAPKCSYITPVpggVGPMTICSLMTNTL 283
Cdd:cd01079 155 FASIKNFE---------------PSVKEKASIYVPS---IGKVTIAMLLRNLL 189
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
184-231 |
2.55e-08 |
|
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: 52.12 E-value: 2.55e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 495401438 184 NATVTVCHSQSKNIKQECREADIIIAAIGVPN-----FVTADMV---KEGAVVIDV 231
Cdd:smart01002 64 GARFTTLYSQAELLEEAVKEADLVIGAVLIPGakapkLVTREMVksmKPGSVIVDV 119
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
182-231 |
4.65e-07 |
|
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: 49.42 E-value: 4.65e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 495401438 182 YGNATVTVCHSQSKNIKQECREADIIIAAIGV-----PNFVTADMV---KEGAVVIDV 231
Cdd:pfam01262 71 LGAKFVETLYSQAELIAEAVKEADLVIGTALIpgakaPKLVTREMVksmKPGSVIVDV 128
|
|
| Ald |
COG0686 |
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ... |
187-231 |
7.42e-07 |
|
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: 50.01 E-value: 7.42e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 495401438 187 VTVCHSQSKNIKQECREADIIIAAIGVPN-----FVTADMV---KEGAVVIDV 231
Cdd:COG0686 215 VTTLYSNPANIEEALKEADLVIGAVLIPGarapkLVTREMVkrmKPGSVIVDV 267
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
187-231 |
3.53e-06 |
|
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: 47.79 E-value: 3.53e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 495401438 187 VTVCHSQSKNIKQECREADIIIAAIGVPNF-----VTADMV---KEGAVVIDV 231
Cdd:cd05305 215 VTTLYSNPANLEEALKEADLVIGAVLIPGAkapklVTEEMVktmKPGSVIVDV 267
|
|
| NAD_bind_amino_acid_DH |
cd05191 |
NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH) ... |
139-232 |
6.01e-03 |
|
NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and are found in glutamate, leucine, and phenylalanine DHs (DHs), methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate 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: 133449 [Multi-domain] Cd Length: 86 Bit Score: 35.05 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495401438 139 ATPLGIMTLLQ----HYNIDTNGKKCVILGRSNiVGKPMAQLMMQKayGNATVTVCHSqsknikqecreaDIIIAAIGVP 214
Cdd:cd05191 1 ATAAGAVALLKaagkVTNKSLKGKTVVVLGAGE-VGKGIAKLLADE--GGKKVVLCDR------------DILVTATPAG 65
|
90 100
....*....|....*....|.
gi 495401438 215 NFVTADMV---KEGAVVIDVG 232
Cdd:cd05191 66 VPVLEEATakiNEGAVVIDLA 86
|
|
| Rubrum_tdh |
cd05304 |
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ... |
193-230 |
7.64e-03 |
|
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matrix side. DI contains 2 domains in Rossmann-like folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than a classical Rossmann domain.
Pssm-ID: 240629 [Multi-domain] Cd Length: 363 Bit Score: 37.39 E-value: 7.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 495401438 193 QSKNIKQECREADIII--AAI-G--VPNFVTADMV---KEGAVVID 230
Cdd:cd05304 239 QRELLAKHIAEADIVIttALIpGrkAPKLITKEMVesmKPGSVIVD 284
|
|
| |
