|
Name |
Accession |
Description |
Interval |
E-value |
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
7-294 |
6.42e-177 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 489.52 E-value: 6.42e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 7 ADLLDGQALSQAVRDEVKADIQAWTDDHRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLV 86
Cdd:COG0190 3 AQILDGKAVAAEIREELKERVAALKAKGITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLALI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 87 HDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDAV 166
Cdd:COG0190 83 DELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 167 IVGRSNIVGKPLANLLLRRtaNATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDDpstd 246
Cdd:COG0190 163 VVGRSNIVGKPLALLLLRR--NATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVED---- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 499723842 247 rgYRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAARLRA 294
Cdd:COG0190 237 --GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQA 282
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
7-291 |
7.82e-135 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 383.21 E-value: 7.82e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 7 ADLLDGQALSQAVRDEVKADIQAWTDDHRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLV 86
Cdd:PRK14190 3 AVIIDGKEVAKEKREQLKEEVVKLKEQGIVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLALI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 87 HDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDAV 166
Cdd:PRK14190 83 DRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGKHVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 167 IVGRSNIVGKPLANLLLRRtaNATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDDPstd 246
Cdd:PRK14190 163 VVGRSNIVGKPVGQLLLNE--NATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRLENG--- 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499723842 247 rgyRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAAR 291
Cdd:PRK14190 238 ---KLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAK 279
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
7-291 |
2.84e-127 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 363.85 E-value: 2.84e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 7 ADLLDGQALSQAVRDEVKADIQAWTDD-HRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDL 85
Cdd:PRK10792 3 AKIIDGKTIAQQVRSEVAQKVQARVAAgLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELLAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 86 VHDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDA 165
Cdd:PRK10792 83 IDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGLNA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 166 VIVGRSNIVGKPLA-NLLLrrtANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDDPs 244
Cdd:PRK10792 163 VVVGASNIVGRPMSlELLL---AGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLEDG- 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 499723842 245 tdrgyRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAAR 291
Cdd:PRK10792 239 -----KLVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACE 280
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
7-297 |
7.93e-125 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 357.85 E-value: 7.93e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 7 ADLLDGQALSQAVRDEVKADIQAWTDDHRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLV 86
Cdd:PRK14189 3 AQLIDGNALSKQLRAEAAQRAAALTARGHQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLARI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 87 HDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDAV 166
Cdd:PRK14189 83 DELNRDPKIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGAHAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 167 IVGRSNIVGKPLANLLLRrtANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDDPstd 246
Cdd:PRK14189 163 VIGRSNIVGKPMAMLLLQ--AGATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMNRDDAG--- 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499723842 247 rgyRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAARLRATSA 297
Cdd:PRK14189 238 ---KLCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAERAAAAA 285
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
9-294 |
1.45e-124 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 357.15 E-value: 1.45e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 9 LLDGQALSQAVRDEVKADIQAWTDD-HRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLVH 87
Cdd:PRK14191 3 LLDGKALSYKIEKDLKNKIQILTAQtGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLIK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 88 DLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDAVI 167
Cdd:PRK14191 83 DLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVVI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 168 VGRSNIVGKPLANLLLrrTANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDDPstdr 247
Cdd:PRK14191 163 IGASNIVGKPLAMLML--NAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLNDG---- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 499723842 248 gyRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAARLRA 294
Cdd:PRK14191 237 --RLVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEKRQ 281
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
7-294 |
8.31e-122 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 350.62 E-value: 8.31e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 7 ADLLDGQALSQAVRDEVKADIQAWTDDHRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLV 86
Cdd:PRK14167 2 TEIIDGNAVAAQIRDDLTDAIETLEDAGVTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 87 HDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDAV 166
Cdd:PRK14167 82 DELNADEDVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 167 IVGRSNIVGKPLANLLLRR--TANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDDpS 244
Cdd:PRK14167 162 VVGRSDIVGKPMANLLIQKadGGNATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINRVDA-D 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 499723842 245 TDRGYRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAARLRA 294
Cdd:PRK14167 241 TEKGYELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAASLQE 290
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
7-291 |
1.88e-121 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 349.64 E-value: 1.88e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 7 ADLLDGQALSQAVRDEVKADIQAWTDDH-RPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDL 85
Cdd:PRK14188 2 ATIIDGKAFAADVRATVAAEVARLKAAHgVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 86 VHDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDA 165
Cdd:PRK14188 82 IARLNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLNA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 166 VIVGRSNIVGKPLANLLLRrtANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDDPST 245
Cdd:PRK14188 162 VVIGRSNLVGKPMAQLLLA--ANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIPAPEK 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 499723842 246 DRG-YRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAAR 291
Cdd:PRK14188 240 GEGkTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAAC 286
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
9-289 |
2.87e-120 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 346.42 E-value: 2.87e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 9 LLDGQALSQAVRDEVKADIQAWTDD-HRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLVH 87
Cdd:PRK14174 3 IIDGKKVSLDLKNELKTRVEAYRAKtGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 88 DLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRG--TPRYIPATPYGIMEMLSRSDIDPESMDA 165
Cdd:PRK14174 83 DLNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGhlDKCFVSCTPYGILELLGRYNIETKGKHC 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 166 VIVGRSNIVGKPLANLLLR--RTANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDDP 243
Cdd:PRK14174 163 VVVGRSNIVGKPMANLMLQklKESNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRIEDP 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 499723842 244 STDRGYRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKA 289
Cdd:PRK14174 243 STKSGYRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTLQS 288
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
7-294 |
2.95e-119 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 343.97 E-value: 2.95e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 7 ADLLDGQALSQAVRDEVKADIQAW-TDDHRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDL 85
Cdd:PRK14186 2 ALILDGKALAAEIEQRLQAQIESNlPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 86 VHDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDA 165
Cdd:PRK14186 82 IAQLNQDERVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 166 VIVGRSNIVGKPLANLLLrrTANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVddPST 245
Cdd:PRK14186 162 VVVGRSILVGKPLALMLL--AANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHRL--PSS 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499723842 246 DRGYRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAARLRA 294
Cdd:PRK14186 238 DGKTRLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSWQKRH 286
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
9-293 |
7.19e-118 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 340.21 E-value: 7.19e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 9 LLDGQALSQAVRDEVKADIQAWTDDH-RPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLVH 87
Cdd:PRK14184 3 LLDGKATAATIREELKTEVAALTARHgRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 88 DLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDAVI 167
Cdd:PRK14184 83 ELNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 168 VGRSNIVGKPLANLLLR--RTANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDDPst 245
Cdd:PRK14184 163 VGRSNIVGKPLALMLGApgKFANATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRTDDG-- 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 499723842 246 drgyrLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAARLR 293
Cdd:PRK14184 241 -----LVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQSWKER 283
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
7-297 |
1.61e-111 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 324.01 E-value: 1.61e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 7 ADLLDGQALSQAVRDEVKADIQAWTDDH-RPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDL 85
Cdd:PRK14179 2 TEIIDGKALAQKMQAELAEKVAKLKEEKgIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 86 VHDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDA 165
Cdd:PRK14179 82 IERYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 166 VIVGRSNIVGKPLANLLLrrTANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRvddpst 245
Cdd:PRK14179 162 VVIGRSNIVGKPMAQLLL--DKNATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMNR------ 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 499723842 246 DRGYRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAArLRATSA 297
Cdd:PRK14179 234 DENGKLIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAA-LRSLHK 284
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-291 |
6.29e-111 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 322.53 E-value: 6.29e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 1 MPDASDADLLDGQALSQAVRDEVKADIQAWTDDHR-PPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQ 79
Cdd:PRK14176 2 MDESYESRIIDGKALAKKIEAEVRSGVERLKSNRGiTPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 80 SELLDLVHDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDID 159
Cdd:PRK14176 82 EELLELIDSLNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 160 PESMDAVIVGRSNIVGKPLANLLLRRtaNATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINR 239
Cdd:PRK14176 162 IEGKNAVIVGHSNVVGKPMAAMLLNR--NATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 499723842 240 VDDpstdrgyRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAAR 291
Cdd:PRK14176 240 EED-------KVYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAE 284
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
9-294 |
4.41e-107 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 312.53 E-value: 4.41e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 9 LLDGQALSQAVRDEVKADIQAW-TDDHRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLVH 87
Cdd:PRK14183 3 ILDGKALSDKIKENVKKEVDELkLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 88 DLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDAVI 167
Cdd:PRK14183 83 MMNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVCV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 168 VGRSNIVGKPLANLLLrrTANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDDPstdr 247
Cdd:PRK14183 163 VGASNIVGKPMAALLL--NANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINRTEDG---- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 499723842 248 gyRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAARLRA 294
Cdd:PRK14183 237 --RLVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKNRA 281
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
9-293 |
2.93e-106 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 310.80 E-value: 2.93e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 9 LLDGQALSQAVRDEVKADIQAWTDDHRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLVHD 88
Cdd:PRK14166 3 LLDGKALSAKIKEELKEKNQFLKSKGIESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALINT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 89 LNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPR-YIPATPYGIMEMLSRSDIDPESMDAVI 167
Cdd:PRK14166 83 LNHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGLESgFLPCTPLGVMKLLKAYEIDLEGKDAVI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 168 VGRSNIVGKPLANLLLrrTANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDDPstdr 247
Cdd:PRK14166 163 IGASNIVGRPMATMLL--NAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLESG---- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 499723842 248 gyRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAARLR 293
Cdd:PRK14166 237 --KIVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAKNR 280
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
7-294 |
3.87e-104 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 305.40 E-value: 3.87e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 7 ADLLDGQALSQAVRDEVKADIQAWTDDHRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLV 86
Cdd:PRK14193 3 AIILDGKATADEIKADLAERVAALKEKGITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELNAVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 87 HDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDAV 166
Cdd:PRK14193 83 DELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGAHVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 167 IVGRSNIVGKPLANLLLRRTANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDDpstd 246
Cdd:PRK14193 163 VIGRGVTVGRPIGLLLTRRSENATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSRAGD---- 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 499723842 247 rgYRLVGDVDfEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAARLRA 294
Cdd:PRK14193 239 --GKLVGDVH-PDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAERRA 283
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
9-291 |
7.24e-100 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 294.81 E-value: 7.24e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 9 LLDGQALSQAVRDEVKADIQAWTDD-HRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLVH 87
Cdd:PRK14185 3 LIDGKAISAQIKQEIAAEVAEIVAKgGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 88 DLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDAVI 167
Cdd:PRK14185 83 ELNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 168 VGRSNIVGKPLANLLLRRT--ANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDDPST 245
Cdd:PRK14185 163 LGRSNIVGKPMAQLMMQKAypGDCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTRVPDATR 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 499723842 246 DRGYRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAAR 291
Cdd:PRK14185 243 KSGFKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGK 288
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
2-291 |
1.44e-99 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 294.11 E-value: 1.44e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 2 PDASDADLLDGQALSQAVRDEVKADIQAWTDDH-RPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQS 80
Cdd:PLN02516 4 PSDHVAQIIDGKAIAKAIRSEIAEEVAQLSEKHgKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 81 ELLDLVHDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRL-MRG-TPRYIPATPYGIMEMLSRSDI 158
Cdd:PLN02516 84 ELISKVHELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLaMKGrEPLFLPCTPKGCLELLSRSGI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 159 DPESMDAVIVGRSNIVGKPLANLLLRrtANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGIN 238
Cdd:PLN02516 164 PIKGKKAVVVGRSNIVGLPVSLLLLK--ADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTN 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499723842 239 RVDDPSTDRGYRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAAR 291
Cdd:PLN02516 242 AVSDPSKKSGYRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAK 294
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
7-294 |
9.87e-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: 9.87e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 7 ADLLDGQALSQAVRDEVKADIQAWTDdhrPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLV 86
Cdd:PRK14173 3 ARELSGPPAAEAVYAELRARLAKLPF---VPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLELI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 87 HDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDAV 166
Cdd:PRK14173 80 ARLNADPEVDGILVQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGKEVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 167 IVGRSNIVGKPLANLLLRRtaNATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVddPSTD 246
Cdd:PRK14173 160 VVGRSNIVGKPLAALLLRE--DATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINRV--GGNG 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 499723842 247 RGYRLVGDVDfEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAARLRA 294
Cdd:PRK14173 236 GRDILTGDVH-PEVAEVAGALTPVPGGVGPMTVAMLMANTVIAALRRR 282
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
9-291 |
4.93e-97 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 287.30 E-value: 4.93e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 9 LLDGQALSQAVRDEVKADIQAWTDDHRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLVHD 88
Cdd:PRK14182 3 LIDGKQIAAKVKGEVATEVRALAARGVQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 89 LNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRL---MRGTPRyiPATPYGIMEMLSRSDIDPESMDA 165
Cdd:PRK14182 83 LNADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALsigIAGVPR--PCTPAGVMRMLDEARVDPKGKRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 166 VIVGRSNIVGKPLANLLLRRtaNATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDDPst 245
Cdd:PRK14182 161 LVVGRSNIVGKPMAMMLLER--HATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLADG-- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 499723842 246 drgyRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAAR 291
Cdd:PRK14182 237 ----KLVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAK 278
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
7-297 |
4.37e-95 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 282.89 E-value: 4.37e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 7 ADLLDGQALSQAVRDEVKADIQAWTDDHRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLV 86
Cdd:PRK14194 4 AKLIDGKAAAARVLAQVREDVRTLKAAGIEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLLALI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 87 HDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDAV 166
Cdd:PRK14194 84 AELNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGKHAV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 167 IVGRSNIVGKPLANLLLRrtANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDDpstD 246
Cdd:PRK14194 164 VIGRSNIVGKPMAALLLQ--AHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINRIDD---D 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499723842 247 RGYRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAARLRATSA 297
Cdd:PRK14194 239 GRSRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAARLQAHAQ 289
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
119-291 |
4.93e-95 |
|
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: 277.90 E-value: 4.93e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 119 PSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDAVIVGRSNIVGKPLANLLLRRtaNATVTVCHSRT 198
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNR--NATVTVCHSKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 199 KDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDDPStdrGYRLVGDVDFEGVRPKARRITPVPGGVGLMT 278
Cdd:cd01080 79 KNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDKS---GGKLVGDVDFESAKEKASAITPVPGGVGPMT 155
|
170
....*....|...
gi 499723842 279 RAMLLKNTLKAAR 291
Cdd:cd01080 156 VAMLMKNTVEAAK 168
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
8-289 |
1.98e-94 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 280.51 E-value: 1.98e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 8 DLLDGQALSQAVRDEVKADIQAWTDDH-RPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLV 86
Cdd:PRK14172 3 QIINGKEVALKIKEEIKNFVEERKENGlSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 87 HDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDAV 166
Cdd:PRK14172 83 EELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 167 IVGRSNIVGKPLANLLLRRtaNATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDDpstd 246
Cdd:PRK14172 163 VIGRSNIVGKPVAQLLLNE--NATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSVNG---- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 499723842 247 rgyRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKA 289
Cdd:PRK14172 237 ---KITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKNVCEA 276
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
7-293 |
2.93e-94 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 280.26 E-value: 2.93e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 7 ADLLDGQALSQAVRDEVKADIQAWTDDHRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLV 86
Cdd:PRK14175 3 AKILDGKQIAKDYRQGLQDQVEALKEKGFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLNEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 87 HDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDAV 166
Cdd:PRK14175 83 NRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGKNAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 167 IVGRSNIVGKPLANLLLRrtANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGiNRVDDPStd 246
Cdd:PRK14175 163 VIGRSHIVGQPVSKLLLQ--KNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVG-NTPDENG-- 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 499723842 247 rgyRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAARLR 293
Cdd:PRK14175 238 ---KLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEKMR 281
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
7-294 |
3.56e-94 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 279.91 E-value: 3.56e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 7 ADLLDGQALSQAVRDEVKADIQAWTDDHRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLV 86
Cdd:PRK14169 1 ATRLDGRAVSKKILADLKQTVAKLAQQDVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 87 HDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDAV 166
Cdd:PRK14169 81 AELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 167 IVGRSNIVGKPLANLLLrrTANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDDPStd 246
Cdd:PRK14169 161 IVGRSNIVGRPLAGLMV--NHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRGADGK-- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 499723842 247 rgyrLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAARLRA 294
Cdd:PRK14169 237 ----LLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKRRA 280
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
7-291 |
1.93e-93 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 281.12 E-value: 1.93e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 7 ADLLDGQALSQAVRDEVKADIQAWTDD-HRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDL 85
Cdd:PLN02616 73 AKVIDGKAVAKKIRDEITIEVSRMKESiGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 86 VHDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRL-MRG-TPRYIPATPYGIMEMLSRSDIDPESM 163
Cdd:PLN02616 153 ISGFNNDPSVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLaMRGrEPLFVPCTPKGCIELLHRYNVEIKGK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 164 DAVIVGRSNIVGKPLAnLLLRRTaNATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDDP 243
Cdd:PLN02616 233 RAVVIGRSNIVGMPAA-LLLQRE-DATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPVEDA 310
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 499723842 244 STDRGYRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAAR 291
Cdd:PLN02616 311 SSPRGYRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAK 358
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
9-293 |
2.66e-93 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 277.49 E-value: 2.66e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 9 LLDGQALSQAVRDEVKADIQawtDDHRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLVHD 88
Cdd:PRK14178 2 ILDGKAVSEKRLELLKEEII---ESGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 89 LNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDAVIV 168
Cdd:PRK14178 79 LNEDPDINGILVQLPLPKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAVVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 169 GRSNIVGKPLANLLLRrtANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDDpstdrg 248
Cdd:PRK14178 159 GRSIDVGRPMAALLLN--ADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQVNG------ 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499723842 249 yRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAARLR 293
Cdd:PRK14178 231 -KLCGDVDFDAVKEIAGAITPVPGGVGPMTIATLMENTFDAAKMR 274
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
127-294 |
3.72e-93 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 272.80 E-value: 3.72e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 127 HPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDAVIVGRSNIVGKPLANLLLRrtANATVTVCHSRTKDLAAHTR 206
Cdd:pfam02882 1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLN--ANATVTVCHSKTKDLAEITR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 207 RADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDdpstdrGYRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNT 286
Cdd:pfam02882 79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRVG------NGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNT 152
|
....*...
gi 499723842 287 LKAARLRA 294
Cdd:pfam02882 153 VEAAKRQL 160
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
7-291 |
2.15e-92 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 275.99 E-value: 2.15e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 7 ADLLDGQALSQAVRDEVKADIQAWTDDH-RPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDL 85
Cdd:PRK14168 3 AKIIKGTEIREEILEEIRGEVAELKEKYgKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 86 VHDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTP--RYIPATPYGIMEMLSRSDIDPESM 163
Cdd:PRK14168 83 IDKYNNDDSIHGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIGGDevKFLPCTPAGIQEMLVRSGVETSGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 164 DAVIVGRSNIVGKPLANLLLRRT--ANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVD 241
Cdd:PRK14168 163 EVVVVGRSNIVGKPIANMMTQKGpgANATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVNRVG 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 499723842 242 DPSTDRGYRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAAR 291
Cdd:PRK14168 243 TNESTGKAILSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAK 292
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
8-289 |
5.26e-90 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 269.52 E-value: 5.26e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 8 DLLDGQALSQAVRDEVKADIQAWTDD-HRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLV 86
Cdd:PRK14171 3 NIIDGKALANEILADLKLEIQELKSQtNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 87 HDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPR-YIPATPYGIMEMLSRSDIDPESMDA 165
Cdd:PRK14171 83 NELNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSGISQgFIPCTALGCLAVIKKYEPNLTGKNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 166 VIVGRSNIVGKPLANLLLRRtaNATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDdpst 245
Cdd:PRK14171 163 VIIGRSNIVGKPLSALLLKE--NCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRIS---- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 499723842 246 drGYRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKA 289
Cdd:PRK14171 237 --GNKIIGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKA 278
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
7-294 |
2.66e-89 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 267.85 E-value: 2.66e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 7 ADLLDGQALSQAVRDEVKADIQAWTDDHR-PPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDL 85
Cdd:PRK14187 2 TNIIDGKKIANDITEILATCIDDLKRQHNlFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 86 VHDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPR--YIPATPYGIMEMLSRSDIDPESM 163
Cdd:PRK14187 82 INELNNDDSVHGILVQLPVPNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQKKncLIPCTPKGCLYLIKTITRNLSGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 164 DAVIVGRSNIVGKPLANLLLRRtaNATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVddp 243
Cdd:PRK14187 162 DAVVIGRSNIVGKPMACLLLGE--NCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSI--- 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499723842 244 STDRGYRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAARLRA 294
Cdd:PRK14187 237 EEGGVKKFVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAACNQK 287
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
9-286 |
2.54e-88 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 265.19 E-value: 2.54e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 9 LLDGQALSQAVRDEVKADIQAWTddhRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLVHD 88
Cdd:PRK14181 2 LLKGAPAAEHILATIKENISASS---TAPGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLIHR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 89 LNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRG-TPRYIPATPYGIMEMLSRSDIDPESMDAVI 167
Cdd:PRK14181 79 LNNDPNIHGILVQLPLPKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGeTDGFIPCTPAGIIELLKYYEIPLHGRHVAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 168 VGRSNIVGKPLANLLLRR--TANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVdDPST 245
Cdd:PRK14181 159 VGRSNIVGKPLAALLMQKhpDTNATVTLLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRV-PAAN 237
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 499723842 246 DRGYRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNT 286
Cdd:PRK14181 238 PKGYILVGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNT 278
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
9-291 |
9.03e-85 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 256.11 E-value: 9.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 9 LLDGQALSQAVRDEVKADIQAWTDDHR-PPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLVH 87
Cdd:PRK14180 3 LIDGKSLSKDLKERLATQVQEYKHHTAiTPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 88 DLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRL-MRGTPRYIPATPYGIMEMLSRSDIDPESMDAV 166
Cdd:PRK14180 83 QLNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLqLRDKKCLESCTPKGIMTMLREYGIKTEGAYAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 167 IVGRSNIVGKPLANLLLrrTANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDDpstd 246
Cdd:PRK14180 163 VVGASNVVGKPVSQLLL--NAKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHVDG---- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499723842 247 rgyRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAAR 291
Cdd:PRK14180 237 ---KIVGDVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQ 278
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
7-291 |
1.34e-83 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 253.07 E-value: 1.34e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 7 ADLLDGQALSQAVRDEVKADIQAWTDDHRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLV 86
Cdd:PRK14170 2 GEIIDGKKLAKEIQEKVTREVAELVKEGKKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 87 HDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDAV 166
Cdd:PRK14170 82 EELNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 167 IVGRSNIVGKPLANLLLrrTANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRvddpstD 246
Cdd:PRK14170 162 VIGRSNIVGKPVAQLLL--NENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDR------D 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499723842 247 RGYRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAAR 291
Cdd:PRK14170 234 ENNKLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAK 278
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
6-291 |
8.62e-82 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 250.65 E-value: 8.62e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 6 DADLLDGQALSQAVRDEVKADIQAWTDD-HRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLD 84
Cdd:PLN02897 55 KTVVIDGNVIAEEIRTKIASEVRKMKKAvGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 85 LVHDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRL-MRG-TPRYIPATPYGIMEMLSRSDIDPES 162
Cdd:PLN02897 135 ALRKFNEDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLaMRGrEPLFVSCTPKGCVELLIRSGVEIAG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 163 MDAVIVGRSNIVGKPLANLLLRRtaNATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINRVDD 242
Cdd:PLN02897 215 KNAVVIGRSNIVGLPMSLLLQRH--DATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPVED 292
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499723842 243 PSTDRGYRLVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAAR 291
Cdd:PLN02897 293 SSCEFGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAK 341
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
9-291 |
1.27e-79 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 242.96 E-value: 1.27e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 9 LLDGQALSQAVRDEVKADI-QAWTDDHRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLVH 87
Cdd:PRK14177 5 LLDGKKLSEKIRNEIRETIeERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLGVID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 88 DLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDAVI 167
Cdd:PRK14177 85 KLNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGKNAVV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 168 VGRSNIVGKPLANLLLRrtANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINrvddPSTdr 247
Cdd:PRK14177 165 VGRSPILGKPMAMLLTE--MNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYN----PGN-- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 499723842 248 gyrlVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAAR 291
Cdd:PRK14177 237 ----VGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFK 276
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
7-290 |
4.12e-79 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 241.67 E-value: 4.12e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 7 ADLLDGQALSQAVRDEVKADIQAWTDDH-RPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDL 85
Cdd:PRK14192 3 ALVLDGKALAKQIEEELSVRVEALKAKTgRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 86 VHDLNADASVDGILVQLPLPDHVDERTVIDAVDPSKDVDGFHPENLGRLMRGTPRYIPATPYGIMEMLSRSDIDPESMDA 165
Cdd:PRK14192 83 IEELNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 166 VIVGRSNIVGKPLANLLLrrTANATVTVCHSRTKDLAAHTRRADLLVAAAGQAAFIDADMVKEDAVVIDVGINrvddPST 245
Cdd:PRK14192 163 VVVGRSAILGKPMAMMLL--NANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFH----PRD 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499723842 246 DRGyrlVGDVDFEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAA 290
Cdd:PRK14192 237 GGG---VGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAA 278
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
10-124 |
4.04e-58 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 181.83 E-value: 4.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 10 LDGQALSQAVRDEVKADIQAWTDDHRPPFLSAVLVGDNPASKAYVRGKEKDAAEVGIETETHHLDADTSQSELLDLVHDL 89
Cdd:pfam00763 1 IDGKAIAKKIREELKEEVAALKAGGRKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKL 80
|
90 100 110
....*....|....*....|....*....|....*
gi 499723842 90 NADASVDGILVQLPLPDHVDERTVIDAVDPSKDVD 124
Cdd:pfam00763 81 NADPSVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
142-291 |
1.01e-24 |
|
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: 96.42 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 142 IPATPYGI-------MEMLSRSDIDPESMDAVIVGRSNIVGKPLANLLLRRtaNATVTVCHSRTKDLAAHTRRADLLVAA 214
Cdd:cd05212 1 GPCTPLFVspvakavKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRD--GATVYSCDWKTIQLQSKVHDADVVVVG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499723842 215 AGQAAFIDADMVKEDAVVIDVGINRVDDpstdrgyrlvgdvdfEGVRPKARRITPVPGGVGLMTRAMLLKNTLKAAR 291
Cdd:cd05212 79 SPKPEKVPTEWIKPGATVINCSPTKLSG---------------DDVKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140
|
|
| NAD_bind_m-THF_DH |
cd01079 |
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ... |
119-288 |
2.80e-06 |
|
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: 47.04 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 119 PSKDVDGFHPENLG------RLMRGTPRY---IPATPYGIMEMLSRSDIDPESM---------DAVIVGRSNIVGKPLAN 180
Cdd:cd01079 1 PHKDVEGLSHKYIFnlyhniRFLDPENRKksiLPCTPLAIVKILEFLGIYNKILpygnrlygkTITIINRSEVVGRPLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723842 181 LLlrrtANATVTV---------CHSRTKDLAAHTR--------------RADLLVAAAGQAAF-IDADMVKEDAVVIDVG 236
Cdd:cd01079 81 LL----ANDGARVysvdingiqVFTRGESIRHEKHhvtdeeamtldclsQSDVVITGVPSPNYkVPTELLKDGAICINFA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499723842 237 INRVDDPStdrgyrlvgdvdfegVRPKARRITPVpggVGLMTRAMLLKNTLK 288
Cdd:cd01079 157 SIKNFEPS---------------VKEKASIYVPS---IGKVTIAMLLRNLLR 190
|
|
| COG5322 |
COG5322 |
Predicted amino acid dehydrogenase [General function prediction only]; |
168-236 |
2.47e-03 |
|
Predicted amino acid dehydrogenase [General function prediction only];
Pssm-ID: 444114 [Multi-domain] Cd Length: 362 Bit Score: 39.05 E-value: 2.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499723842 168 VGRSNIVGKPLANLL-----LRRTANATVTVchsrTKDLAAHTRRADLLVAAAGQA-AFIDADMVKEDAVVIDVG 236
Cdd:COG5322 175 VKRLTLVARNLERLEelaeeILRNPGGKVTI----TTDIDEALREADIVVTVTSAVgAIIDPEDLKPGAVVCDVA 245
|
|
|