|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
310-935 |
0e+00 |
|
Formate--tetrahydrofolate ligase
Pssm-ID: 178359 Cd Length: 637 Bit Score: 1047.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 310 LTLKMPVPSDIEISRSCIPKPIDQVAKEAGLLPDEVELYGQTKAKVQLSALRRLQDQPNGKYVVVTGITPTPLGEGKSTT 389
Cdd:PLN02759 10 LEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKSTT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 390 TIGLVQALGAHLHQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAVDARIFHELT 469
Cdd:PLN02759 90 TIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEAT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 470 QTDQALYNRLVPP-VNGVRKFSDIQIRRLQKLGINKTDPAALTKEEINVFVRLDIDPATITWQRVLDTNDRFLRRITIGQ 548
Cdd:PLN02759 170 QSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVGQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 549 SPTEKGFSRTAQFDITVASEIMAVLALADGLDDMRMRLGRMVVASSKKGEPVTADDLGVTGALAVLMKDAVKPNLMQTLE 628
Cdd:PLN02759 250 GPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTLE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 629 GTPVFVHAGPFANIAHGNSSVLADKIALKLVGKDGFVVTEAGFGADIGMEKFFNIKCRYSGLRPHVVVLVATVRALKMHG 708
Cdd:PLN02759 330 GTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMHG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 709 GGPAVAAGVPLPKEYTEENLQLLTKGCSNLSKQIQNAQIFGVPVVVAVNAFKTDTKAELALVVQLAKTAGAFDAVECTHW 788
Cdd:PLN02759 410 GGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTHH 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 789 AEGGKGAVALAQAVQRASQAPS-NFKFLYNVELPVTDKIRLIAQQIYGASDIELFPEAQEKVTLYTKQGFGNLPICMAKT 867
Cdd:PLN02759 490 AHGGKGAVDLGEAVQKACEGNSqPFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAKT 569
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444535382 868 HLSLSHDPEQKGAPTGFILPIRDVRASVGAGFLYPLVGTMSTMPGLPTRPCFFDIDLDPVSGEVNGLF 935
Cdd:PLN02759 570 QYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTETGKVLGLS 637
|
|
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
317-935 |
0e+00 |
|
Formate--tetrahydrofolate ligase;
Pssm-ID: 460143 Cd Length: 555 Bit Score: 998.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 317 PSDIEISRSCIPKPIDQVAKEAGLLPDEVELYGQTKAKVQLSALRRLQDQPNGKYVVVTGITPTPLGEGKSTTTIGLVQA 396
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 397 LGaHLHQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAVDARIFHELTqtdqaly 476
Cdd:pfam01268 81 LN-RLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 477 nrlvppvngvrkfsdiqirrlqklginktdpaaltkeeinvfvrLDIDPATITWQRVLDTNDRFLRRITIGQSPTEKGFS 556
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 557 RTAQFDITVASEIMAVLALADGLDDMRMRLGRMVVASSKKGEPVTADDLGVTGALAVLMKDAVKPNLMQTLEGTPVFVHA 636
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 637 GPFANIAHGNSSVLADKIALKLvgkDGFVVTEAGFGADIGMEKFFNIKCRYSGLRPHVVVLVATVRALKMHGGGPAvaag 716
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGGVGK---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 717 vplpKEYTEENLQLLTKGCSNLSKQIQNAQIFGVPVVVAVNAFKTDTKAELALVVQLAKtAGAFDAVECTHWAEGGKGAV 796
Cdd:pfam01268 342 ----DELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRELCE-AGGVDAALSEHWAKGGEGAI 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 797 ALAQAVQRA-SQAPSNFKFLYNVELPVTDKIRLIAQQIYGASDIELFPEAQEKVTLYTKQGFGNLPICMAKTHLSLSHDP 875
Cdd:pfam01268 417 ELAEAVVEAcEEEPSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 876 EQKGAPTGFILPIRDVRASVGAGFLYPLVGTMSTMPGLPTRPCFFDIDLDPvSGEVNGLF 935
Cdd:pfam01268 497 KLKGAPTGFTLPVRDVRLSAGAGFIVALTGDIMTMPGLPKRPAAENIDVDE-DGKITGLF 555
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
331-934 |
0e+00 |
|
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ATP-dependent activation of formate ion via its addition to the N10 position of tetrahydrofolate. FTHFS is a highly expressed key enzyme in both the Wood-Ljungdahl pathway of autotrophic CO2 fixation (acetogenesis) and the glycine synthase/reductase pathways of purinolysis. The key physiological role of this enzyme in acetogens is to catalyze the formylation of tetrahydrofolate, an initial step in the reduction of carbon dioxide and other one-carbon precursors to acetate. In purinolytic organisms, the enzymatic reaction is reversed, liberating formate from 10-formyltetrahydrofolate with concurrent production of ATP.
Pssm-ID: 349750 Cd Length: 540 Bit Score: 958.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 331 IDQVAKEAGLLPDEVELYGQTKAKVQLSALRRLQDQPNGKYVVVTGITPTPLGEGKSTTTIGLVQALGAHLhQNVFACVR 410
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALG-KKAIAALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 411 QPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAVDARIFHELTqtdqalynrlvppvngvrkfs 490
Cdd:cd00477 80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 491 diqirrlqklginktdpaaltkeeinvfvrLDIDPATITWQRVLDTNDRFLRRITIGQSPTEKGFSRTAQFDITVASEIM 570
Cdd:cd00477 139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 571 AVLALADGLDDMRMRLGRMVVASSKKGEPVTADDLGVTGALAVLMKDAVKPNLMQTLEGTPVFVHAGPFANIAHGNSSVL 650
Cdd:cd00477 189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 651 ADKIALKLvgkDGFVVTEAGFGADIGMEKFFNIKCRYSGLRPHVVVLVATVRALKMHGGGPAVAAGvplpkeytEENLQL 730
Cdd:cd00477 269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 731 LTKGCSNLSKQIQNAQIFGVPVVVAVNAFKTDTKAELALVVQLAKTAGAFDAVeCTHWAEGGKGAVALAQAVQRASQAP- 809
Cdd:cd00477 338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKPk 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 810 SNFKFLYNVELPVTDKIRLIAQQIYGASDIELFPEAQEKVTLYTKQGFGNLPICMAKTHLSLSHDPEQKGAPTGFILPIR 889
Cdd:cd00477 417 SNFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1444535382 890 DVRASVGAGFLYPLVGTMSTMPGLPTRPCFFDIDLDPvSGEVNGL 934
Cdd:cd00477 497 DVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDIDD-TGKIEGL 540
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
316-935 |
0e+00 |
|
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
Pssm-ID: 442046 Cd Length: 556 Bit Score: 889.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 316 VPSDIEISRSCIPKPIDQVAKEAGLLPDEVELYGQTKAKVQLSALRRLQDQPNGKYVVVTGITPTPLGEGKSTTTIGLVQ 395
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 396 ALGaHLHQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAVDARIFHEltqtdqal 475
Cdd:COG2759 81 ALN-RLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQG-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 476 ynrlvppvngvrkfsdiqirrlqklginktdpaaltkeeiNvfvRLDIDPATITWQRVLDTNDRFLRRITIGQSPTEKGF 555
Cdd:COG2759 152 ----------------------------------------N---ELNIDPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 556 SRTAQFDITVASEIMAVLALADGLDDMRMRLGRMVVASSKKGEPVTADDLGVTGALAVLMKDAVKPNLMQTLEGTPVFVH 635
Cdd:COG2759 189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 636 AGPFANIAHGNSSVLADKIALKLVgkDgFVVTEAGFGADIGMEKFFNIKCRYSGLRPHVVVLVATVRALKMHGGGPavaa 715
Cdd:COG2759 269 GGPFANIAHGCNSVIATKLALKLA--D-YVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 716 gvplPKEYTEENLQLLTKGCSNLSKQIQNAQIFGVPVVVAVNAFKTDTKAELALVVQLAKTAGAfDAVECTHWAEGGKGA 795
Cdd:COG2759 342 ----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEGA 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 796 VALAQAVQRAS-QAPSNFKFLYNVELPVTDKIRLIAQQIYGASDIELFPEAQEKVTLYTKQGFGNLPICMAKTHLSLSHD 874
Cdd:COG2759 417 EELAEAVVEACeEGPSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSDD 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1444535382 875 PEQKGAPTGFILPIRDVRASVGAGFLYPLVGTMSTMPGLPTRPCFFDIDLDpVSGEVNGLF 935
Cdd:COG2759 497 PKLLGAPTGFTLTVREVRLSAGAGFIVALTGDIMTMPGLPKVPAAERIDID-EDGKITGLF 556
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
3-293 |
3.74e-143 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 426.74 E-value: 3.74e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 3 PAEVLSGKIVSAQVRERLKKQVAEMKEKfpGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVL 82
Cdd:COG0190 2 MAQILDGKAVAAEIREELKERVAALKAK--GITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 83 KCIASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDlgDCFIPCTPKGCMELIRQTGIQ 162
Cdd:COG0190 80 ALIDELNADPSVHGILVQLPLP--KHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLERYGID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 163 VAGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVP 242
Cdd:COG0190 156 LAGKHAVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1444535382 243 DStkasgkRVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:COG0190 236 DG------KLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-293 |
2.85e-111 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 343.92 E-value: 2.85e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 4 AEVLSGKIVSAQVRERLKKQVAEMKEKfpGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLK 83
Cdd:PRK14190 3 AVIIDGKEVAKEKREQLKEEVVKLKEQ--GIVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 84 CIASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDlgDCFIPCTPKGCMELIRQTGIQV 163
Cdd:PRK14190 81 LIDRLNADPRINGILVQLPLP--KHIDEKAVIERISPEKDVDGFHPINVGRMMLGQ--DTFLPCTPHGILELLKEYNIDI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 164 AGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVpd 243
Cdd:PRK14190 157 SGKHVVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRL-- 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1444535382 244 stkASGKrVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PRK14190 235 ---ENGK-LCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKR 280
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
120-292 |
8.20e-94 |
|
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding domain of the Methylene-Tetrahydrofolate Dehydrogenase/cyclohydrolase (m-THF DH/cyclohydrolase) bifunctional enzyme. Tetrahydrofolate is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofucntional DH, as well as bifunctional m-THF m-THF DHm-THF DHDH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains the bifunctional DH/cyclohydrolase. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains.
Pssm-ID: 133448 Cd Length: 168 Bit Score: 293.31 E-value: 8.20e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 120 PEKDVDGLSSINAGKLSRGDlgDCFIPCTPKGCMELIRQTGIQVAGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKT 199
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGR--PGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 200 STLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVPDstkASGKRVVGDVAYSTAKEKASYITPVPGGVGPMT 279
Cdd:cd01080 79 KNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPD---KSGGKLVGDVDFESAKEKASAITPVPGGVGPMT 155
|
170
....*....|...
gi 1444535382 280 VAMLMQSTVESAQ 292
Cdd:cd01080 156 VAMLMKNTVEAAK 168
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
128-295 |
6.09e-85 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 269.34 E-value: 6.09e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 128 SSINAGKLSRGdlGDCFIPCTPKGCMELIRQTGIQVAGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVA 207
Cdd:pfam02882 1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 208 KADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVpdstkaSGKRVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQST 287
Cdd:pfam02882 79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRV------GNGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNT 152
|
....*...
gi 1444535382 288 VESAQRFL 295
Cdd:pfam02882 153 VEAAKRQL 160
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
189-235 |
4.67e-03 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 38.64 E-value: 4.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1444535382 189 HATVTTCHSKTSTLAEEVAKADILVVAA---GK-------AEMVKGewIKPGAVVID 235
Cdd:smart01002 64 GARFTTLYSQAELLEEAVKEADLVIGAVlipGAkapklvtREMVKS--MKPGSVIVD 118
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
310-935 |
0e+00 |
|
Formate--tetrahydrofolate ligase
Pssm-ID: 178359 Cd Length: 637 Bit Score: 1047.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 310 LTLKMPVPSDIEISRSCIPKPIDQVAKEAGLLPDEVELYGQTKAKVQLSALRRLQDQPNGKYVVVTGITPTPLGEGKSTT 389
Cdd:PLN02759 10 LEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKSTT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 390 TIGLVQALGAHLHQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAVDARIFHELT 469
Cdd:PLN02759 90 TIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEAT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 470 QTDQALYNRLVPP-VNGVRKFSDIQIRRLQKLGINKTDPAALTKEEINVFVRLDIDPATITWQRVLDTNDRFLRRITIGQ 548
Cdd:PLN02759 170 QSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVGQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 549 SPTEKGFSRTAQFDITVASEIMAVLALADGLDDMRMRLGRMVVASSKKGEPVTADDLGVTGALAVLMKDAVKPNLMQTLE 628
Cdd:PLN02759 250 GPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTLE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 629 GTPVFVHAGPFANIAHGNSSVLADKIALKLVGKDGFVVTEAGFGADIGMEKFFNIKCRYSGLRPHVVVLVATVRALKMHG 708
Cdd:PLN02759 330 GTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMHG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 709 GGPAVAAGVPLPKEYTEENLQLLTKGCSNLSKQIQNAQIFGVPVVVAVNAFKTDTKAELALVVQLAKTAGAFDAVECTHW 788
Cdd:PLN02759 410 GGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTHH 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 789 AEGGKGAVALAQAVQRASQAPS-NFKFLYNVELPVTDKIRLIAQQIYGASDIELFPEAQEKVTLYTKQGFGNLPICMAKT 867
Cdd:PLN02759 490 AHGGKGAVDLGEAVQKACEGNSqPFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAKT 569
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444535382 868 HLSLSHDPEQKGAPTGFILPIRDVRASVGAGFLYPLVGTMSTMPGLPTRPCFFDIDLDPVSGEVNGLF 935
Cdd:PLN02759 570 QYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTETGKVLGLS 637
|
|
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
317-935 |
0e+00 |
|
Formate--tetrahydrofolate ligase;
Pssm-ID: 460143 Cd Length: 555 Bit Score: 998.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 317 PSDIEISRSCIPKPIDQVAKEAGLLPDEVELYGQTKAKVQLSALRRLQDQPNGKYVVVTGITPTPLGEGKSTTTIGLVQA 396
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 397 LGaHLHQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAVDARIFHELTqtdqaly 476
Cdd:pfam01268 81 LN-RLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 477 nrlvppvngvrkfsdiqirrlqklginktdpaaltkeeinvfvrLDIDPATITWQRVLDTNDRFLRRITIGQSPTEKGFS 556
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 557 RTAQFDITVASEIMAVLALADGLDDMRMRLGRMVVASSKKGEPVTADDLGVTGALAVLMKDAVKPNLMQTLEGTPVFVHA 636
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 637 GPFANIAHGNSSVLADKIALKLvgkDGFVVTEAGFGADIGMEKFFNIKCRYSGLRPHVVVLVATVRALKMHGGGPAvaag 716
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGGVGK---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 717 vplpKEYTEENLQLLTKGCSNLSKQIQNAQIFGVPVVVAVNAFKTDTKAELALVVQLAKtAGAFDAVECTHWAEGGKGAV 796
Cdd:pfam01268 342 ----DELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRELCE-AGGVDAALSEHWAKGGEGAI 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 797 ALAQAVQRA-SQAPSNFKFLYNVELPVTDKIRLIAQQIYGASDIELFPEAQEKVTLYTKQGFGNLPICMAKTHLSLSHDP 875
Cdd:pfam01268 417 ELAEAVVEAcEEEPSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 876 EQKGAPTGFILPIRDVRASVGAGFLYPLVGTMSTMPGLPTRPCFFDIDLDPvSGEVNGLF 935
Cdd:pfam01268 497 KLKGAPTGFTLPVRDVRLSAGAGFIVALTGDIMTMPGLPKRPAAENIDVDE-DGKITGLF 555
|
|
| PTZ00386 |
PTZ00386 |
formyl tetrahydrofolate synthetase; Provisional |
307-934 |
0e+00 |
|
formyl tetrahydrofolate synthetase; Provisional
Pssm-ID: 240394 Cd Length: 625 Bit Score: 960.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 307 YNQLTLKMPVPSDIEISRSCIPKPIDQVAKEAGLLPDEVELYGQTKAKVQLSALRRLQDQPNGKYVVVTGITPTPLGEGK 386
Cdd:PTZ00386 6 TRKLSCQWPVPSDIDIAQSVKPQPITSVAESAGILLSELDPYGSTRAKVKLSVLKRLENSPNGKYVVVAGMNPTPLGEGK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 387 STTTIGLVQALGAHLHQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAVDARIFH 466
Cdd:PTZ00386 86 STTTIGLAQSLGAHLHRKTFACIRQPSQGPTFGIKGGAAGGGYSQVIPMEDFNLHGTGDIHAITAANNLLAAALDTRIFH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 467 ELTQTDQALYNRLVppvNGVRKFSDIQIRRLQKLGINKTDPAALTKEEINVFVRLDIDPATITWQRVLDTNDRFLRRITI 546
Cdd:PTZ00386 166 ERTQSDAALYRRLT---DELKKFTPIMLKRLEKLGISKTDPKQLTEEERVRFARLDIDPDTISWRRVTDVNDRMLREITI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 547 GQSPTEKGFSRTAQFDITVASEIMAVLALADGLDDMRMRLGRMVVASSKKGEPVTADDLGVTGALAVLMKDAVKPNLMQT 626
Cdd:PTZ00386 243 GQGKEEKGITRKTGFDISVASEVMAILALATDLADMRQRLGAIVVAKSKSGEPVTAEDLGCAGAMTVLMKDTIEPTLMQT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 627 LEGTPVFVHAGPFANIAHGNSSVLADKIALKLVGKDGFVVTEAGFGADIGMEKFFNIKCRYSGLRPHVVVLVATVRALKM 706
Cdd:PTZ00386 323 LEGTPVLVHAGPFGNIAHGNSSIVADQIALKLAGQDGFVLTEAGFGADIGCEKFFNIKCRTSGLKPDAAVLVATVRALKF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 707 HGGGPAVAAGvplpkeytEENLQLLTKGCSNLSKQIQNAQIFGVPVVVAVNAFKTDTKAELALVVQLA-KTAGAFDAVEC 785
Cdd:PTZ00386 403 HGGVEPVVAG--------KENLEAVRKGLSNLQRHIQNIRKFGVPVVVALNKFSTDTDAELELVKELAlQEGGAADVVVT 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 786 THWAEGGKGAVALAQAVQRASQ-APSNFKFLYNVELPVTDKIRLIAQQIYGASDIELFPEAQEKVTLYTKQGFGNLPICM 864
Cdd:PTZ00386 475 DHWAKGGAGAVDLAQALIRVTEnVPSNFKLLYPLDASLKEKIETICKEIYGAAGVEYLNDADEKLEDFERMGYGKFPVCM 554
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 865 AKTHLSLSHDPEQKGAPTGFILPIRDVRASVGAGFLYPLVGTMSTMPGLPTRPCFFDIDLDPVSGEVNGL 934
Cdd:PTZ00386 555 AKTQYSFSHDPELRGAPTGFTVPIRDVRVNCGAGFVFPLLGDISTMPGLPTRPAFYNIDIDCETGKIVGL 624
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
331-934 |
0e+00 |
|
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ATP-dependent activation of formate ion via its addition to the N10 position of tetrahydrofolate. FTHFS is a highly expressed key enzyme in both the Wood-Ljungdahl pathway of autotrophic CO2 fixation (acetogenesis) and the glycine synthase/reductase pathways of purinolysis. The key physiological role of this enzyme in acetogens is to catalyze the formylation of tetrahydrofolate, an initial step in the reduction of carbon dioxide and other one-carbon precursors to acetate. In purinolytic organisms, the enzymatic reaction is reversed, liberating formate from 10-formyltetrahydrofolate with concurrent production of ATP.
Pssm-ID: 349750 Cd Length: 540 Bit Score: 958.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 331 IDQVAKEAGLLPDEVELYGQTKAKVQLSALRRLQDQPNGKYVVVTGITPTPLGEGKSTTTIGLVQALGAHLhQNVFACVR 410
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALG-KKAIAALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 411 QPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAVDARIFHELTqtdqalynrlvppvngvrkfs 490
Cdd:cd00477 80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 491 diqirrlqklginktdpaaltkeeinvfvrLDIDPATITWQRVLDTNDRFLRRITIGQSPTEKGFSRTAQFDITVASEIM 570
Cdd:cd00477 139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 571 AVLALADGLDDMRMRLGRMVVASSKKGEPVTADDLGVTGALAVLMKDAVKPNLMQTLEGTPVFVHAGPFANIAHGNSSVL 650
Cdd:cd00477 189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 651 ADKIALKLvgkDGFVVTEAGFGADIGMEKFFNIKCRYSGLRPHVVVLVATVRALKMHGGGPAVAAGvplpkeytEENLQL 730
Cdd:cd00477 269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 731 LTKGCSNLSKQIQNAQIFGVPVVVAVNAFKTDTKAELALVVQLAKTAGAFDAVeCTHWAEGGKGAVALAQAVQRASQAP- 809
Cdd:cd00477 338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKPk 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 810 SNFKFLYNVELPVTDKIRLIAQQIYGASDIELFPEAQEKVTLYTKQGFGNLPICMAKTHLSLSHDPEQKGAPTGFILPIR 889
Cdd:cd00477 417 SNFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1444535382 890 DVRASVGAGFLYPLVGTMSTMPGLPTRPCFFDIDLDPvSGEVNGL 934
Cdd:cd00477 497 DVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDIDD-TGKIEGL 540
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
316-935 |
0e+00 |
|
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
Pssm-ID: 442046 Cd Length: 556 Bit Score: 889.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 316 VPSDIEISRSCIPKPIDQVAKEAGLLPDEVELYGQTKAKVQLSALRRLQDQPNGKYVVVTGITPTPLGEGKSTTTIGLVQ 395
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 396 ALGaHLHQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAVDARIFHEltqtdqal 475
Cdd:COG2759 81 ALN-RLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQG-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 476 ynrlvppvngvrkfsdiqirrlqklginktdpaaltkeeiNvfvRLDIDPATITWQRVLDTNDRFLRRITIGQSPTEKGF 555
Cdd:COG2759 152 ----------------------------------------N---ELNIDPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 556 SRTAQFDITVASEIMAVLALADGLDDMRMRLGRMVVASSKKGEPVTADDLGVTGALAVLMKDAVKPNLMQTLEGTPVFVH 635
Cdd:COG2759 189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 636 AGPFANIAHGNSSVLADKIALKLVgkDgFVVTEAGFGADIGMEKFFNIKCRYSGLRPHVVVLVATVRALKMHGGGPavaa 715
Cdd:COG2759 269 GGPFANIAHGCNSVIATKLALKLA--D-YVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 716 gvplPKEYTEENLQLLTKGCSNLSKQIQNAQIFGVPVVVAVNAFKTDTKAELALVVQLAKTAGAfDAVECTHWAEGGKGA 795
Cdd:COG2759 342 ----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEGA 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 796 VALAQAVQRAS-QAPSNFKFLYNVELPVTDKIRLIAQQIYGASDIELFPEAQEKVTLYTKQGFGNLPICMAKTHLSLSHD 874
Cdd:COG2759 417 EELAEAVVEACeEGPSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSDD 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1444535382 875 PEQKGAPTGFILPIRDVRASVGAGFLYPLVGTMSTMPGLPTRPCFFDIDLDpVSGEVNGLF 935
Cdd:COG2759 497 PKLLGAPTGFTLTVREVRLSAGAGFIVALTGDIMTMPGLPKVPAAERIDID-EDGKITGLF 556
|
|
| PRK13505 |
PRK13505 |
formate--tetrahydrofolate ligase; Provisional |
315-935 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237403 Cd Length: 557 Bit Score: 756.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 315 PVPSDIEISRSCIPKPIDQVAKEAGLLPDEVELYGQTKAKVQLSALRRLQDQPNGKYVVVTGITPTPLGEGKSTTTIGLV 394
Cdd:PRK13505 1 TMKSDIEIAQEATLKPITEIAAKLGIPEDDLEPYGKYKAKISLDKIKALKDKKDGKLILVTAINPTPAGEGKSTVTVGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 395 QALgAHLHQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITaannlvaaavdarifheltqtdqA 474
Cdd:PRK13505 81 DAL-NKIGKKTVIALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAIT-----------------------S 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 475 LYNRLvppvngvrkfsdiqirrlqklginktdpAALTKEEINVFVRLDIDPATITWQRVLDTNDRFLRRITIGQSPTEKG 554
Cdd:PRK13505 137 ANNLL----------------------------AALIDNHIHQGNELGIDPRRITWKRVLDMNDRALRNIVVGLGGPANG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 555 FSRTAQFDITVASEIMAVLALADGLDDMRMRLGRMVVASSKKGEPVTADDLGVTGALAVLMKDAVKPNLMQTLEGTPVFV 634
Cdd:PRK13505 189 VPREDGFDITVASEIMAILCLATDLKDLKERLGRIVVGYTYDGKPVTVKDLKVEGAMALLLKDAIKPNLVQTLEGTPAFV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 635 HAGPFANIAHGNSSVLADKIALKLvgKDgFVVTEAGFGADIGMEKFFNIKCRYSGLRPHVVVLVATVRALKMHGGGPAva 714
Cdd:PRK13505 269 HGGPFANIAHGCNSVLATKTALKL--AD-YVVTEAGFGADLGAEKFLDIKCRKAGLKPDAVVIVATVRALKMHGGVAK-- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 715 agvplpKEYTEENLQLLTKGCSNLSKQIQNAQIFGVPVVVAVNAFKTDTKAELALVVQLAKTAGAfDAVECTHWAEGGKG 794
Cdd:PRK13505 344 ------DDLKEENVEALKKGFANLERHIENIRKFGVPVVVAINKFVTDTDAEIAALKELCEELGV-EVALSEVWAKGGEG 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 795 AVALAQAVQR-ASQAPSNFKFLYNVELPVTDKIRLIAQQIYGASDIELFPEAQEKVTLYTKQGFGNLPICMAKTHLSLSH 873
Cdd:PRK13505 417 GVELAEKVVElIEEGESNFKPLYDDEDSLEEKIEKIATKIYGAKGVEFSPKAKKQLKQIEKNGWDKLPVCMAKTQYSFSD 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1444535382 874 DPEQKGAPTGFILPIRDVRASVGAGFLYPLVGTMSTMPGLPTRPCFFDIDLDPvSGEVNGLF 935
Cdd:PRK13505 497 DPKLLGAPTGFTITVRELRPSAGAGFIVALTGDIMTMPGLPKVPAALNIDVDE-DGNIVGLF 557
|
|
| PRK13506 |
PRK13506 |
formate--tetrahydrofolate ligase; Provisional |
318-934 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237404 Cd Length: 578 Bit Score: 745.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 318 SDIEISRSCIPKPIDQVAKEAGLLPDEVELYGQTKAKVQLSALRRLQDQPNGKYVVVTGITPTPLGEGKSTTTIGLVQAL 397
Cdd:PRK13506 3 SDIEISRQAPLKPIAEIAAKLGLLPDELSPFGHTKAKVSLSVLKRLADKPKGKLVLVTAITPTPLGEGKTVTTIGLTQGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 398 gAHLHQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAVDARIFHEltqtdqalyN 477
Cdd:PRK13506 83 -NALGQKVCACIRQPSMGPVFGVKGGAAGGGYAQVVPMEELNLHLTGDIHAVSAAHNLAAAAIDARLFHE---------Q 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 478 RLvppvnGVRKFSdiqirrlQKLGINktdpaaltkeeinvfvRLDIDPATITWQRVLDTNDRFLRRITIGQSPTEKGFSR 557
Cdd:PRK13506 153 RL-----GYDAFE-------AQSGLP----------------ALDIDPEQILWKRVVDHNDRALRMITVGLGENGNGPER 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 558 TAQFDITVASEIMAVLALADGLDDMRMRLGRMVVASSKKGEPVTADDLGVTGALAVLMKDAVKPNLMQTLEGTPVFVHAG 637
Cdd:PRK13506 205 EDGFDITAASELMAILALSRDLKDMRQRIGRLVLAYNLQGQPITAEDLGVAGAMTVIMKDAIEPTLMQTLEGVPCLIHAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 638 PFANIAHGNSSVLADKIALKLVGkdgFVVTEAGFGADIGMEKFFNIKCRYSGLRPHVVVLVATVRALKMHGGGPAVAAGV 717
Cdd:PRK13506 285 PFANIAHGNSSIIADRIALKLAD---YVVTEGGFGSDMGFEKFCNIKARQSGKAPDCAVLVATLRALKANSGLYDLRPGQ 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 718 PLPKEYTEENLQLLTKGCSNLSKQIQNAQIFGVPVVVAVNAFKTDTKAELALVVQLAKTAGAFDAVECTHWAEGGKGAVA 797
Cdd:PRK13506 362 ALPDSINAPDQARLEAGFANLKWHINNVAQYGLPVVVAINRFPTDTDEELEWLKEAVLLTGAFGCEISEAFAQGGEGATA 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 798 LAQAVQRASQAPSNFKFLYNVELPVTDKIRLIAQQIYGASDIELFPEAQEKVTLYTKQGFGNLPICMAKTHLSLSHDPEQ 877
Cdd:PRK13506 442 LAQAVVRACEQPSQFKLLYPDEMSLEAKLMTLAEVGYGAAGVSLSDKAKQQLAQLTALGYDHLPVCMAKTPLSISHDPAL 521
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1444535382 878 KGAPTGFILPIRDVRASVGAGFLYPLVGTMSTMPGLPTRPCFFDIDLDpVSGEVNGL 934
Cdd:PRK13506 522 KGAPTDFEVPIRELRLCAGAGFITALVGNVMTMPGLGLKPGYLNIDID-ADGEIVGL 577
|
|
| PRK13507 |
PRK13507 |
formate--tetrahydrofolate ligase; Provisional |
329-935 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 184098 Cd Length: 587 Bit Score: 677.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 329 KPIDQVAKEAGLLPDEVELYGQTKAKV-QLSALRRLQDQPNGKYVVVTGITPTPLGEGKSTTTIGLVQALGAhLHQNVFA 407
Cdd:PRK13507 22 KPVEELAEELGLTKEELLPYGHYIAKVdFRKVLDRLKDRPDGKYIDVTAITPTPLGEGKSTTTMGLVQGLGK-RGKKVSG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 408 CVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAVDARIFHELTQTDQALYNRlvppvnGVR 487
Cdd:PRK13507 101 AIRQPSGGPTMNIKGSAAGGGLSQCIPLTPFSLGLTGDINAIMNAHNLAMVALTARMQHERNYTDEQLARR------GLK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 488 kfsdiqirrlqklginktdpaaltkeeinvfvRLDIDPATITWQRVLDTNDRFLRRITIGQSPTEKGFSRTAQFDITVAS 567
Cdd:PRK13507 175 --------------------------------RLDIDPTRVEMGWIIDFCAQALRNIIIGIGGKTDGYMMQSGFGIAVSS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 568 EIMAVLALADGLDDMRMRLGRMVVASSKKGEPVTADDLGVTGALAVLMKDAVKPNLMQTLEGTPVFVHAGPFANIAHGNS 647
Cdd:PRK13507 223 EVMAILSVATDLKDLRERIGKIVVAYDKNGKPVTTADLEVDGAMTAWMVRAINPNLLQTIEGQPVFVHAGPFANIAIGQS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 648 SVLADKIALKLVgkdGFVVTEAGFGADIGMEKFFNIKCRYSGLRPHVVVLVATVRALKMHGGGPAVAAGVPLPKEYTEEN 727
Cdd:PRK13507 303 SIIADRVGLKLA---DYHVTESGFGADIGFEKFWNLKCRLSGLKPDCAVIVATIRALKMHGGGPKVVPGKPLPEEYTKEN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 728 LQLLTKGCSNLSKQIQNAQIFGVPVVVAVNAFKTDTKAELALVVQLAKTAGAFDAVEcTHWAEGGKGAVALAQAVQRASQ 807
Cdd:PRK13507 380 VGLVEKGCANLLHHIGTVKKSGINPVVCINAFYTDTHAEIAIVRRLAEQAGARVAVS-RHWEKGGEGALELADAVIDACN 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 808 APSNFKFLYNVELPVTDKIRLIAQQIYGASDIELFPEAQEKVT-LYTKQGFGNLPICMAKTHLSLSHDPEQKGAPTGFIL 886
Cdd:PRK13507 459 EPNDFKFLYPLEMPLRERIETIAREVYGADGVSYTPEAEAKLKrLESDPETADFGTCMVKTHLSLSHDPALKGVPKGWTL 538
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1444535382 887 PIRDVRASVGAGFLYPLVGTMSTMPGLPTRPCFFDIDLDPVSGEVNGLF 935
Cdd:PRK13507 539 PIRDILTYGGAGFVVPVAGDISLMPGTGSDPAFRRIDVDTQTGKVKGLF 587
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
3-293 |
3.74e-143 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 426.74 E-value: 3.74e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 3 PAEVLSGKIVSAQVRERLKKQVAEMKEKfpGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVL 82
Cdd:COG0190 2 MAQILDGKAVAAEIREELKERVAALKAK--GITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 83 KCIASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDlgDCFIPCTPKGCMELIRQTGIQ 162
Cdd:COG0190 80 ALIDELNADPSVHGILVQLPLP--KHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLERYGID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 163 VAGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVP 242
Cdd:COG0190 156 LAGKHAVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1444535382 243 DStkasgkRVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:COG0190 236 DG------KLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-293 |
2.85e-111 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 343.92 E-value: 2.85e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 4 AEVLSGKIVSAQVRERLKKQVAEMKEKfpGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLK 83
Cdd:PRK14190 3 AVIIDGKEVAKEKREQLKEEVVKLKEQ--GIVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 84 CIASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDlgDCFIPCTPKGCMELIRQTGIQV 163
Cdd:PRK14190 81 LIDRLNADPRINGILVQLPLP--KHIDEKAVIERISPEKDVDGFHPINVGRMMLGQ--DTFLPCTPHGILELLKEYNIDI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 164 AGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVpd 243
Cdd:PRK14190 157 SGKHVVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRL-- 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1444535382 244 stkASGKrVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PRK14190 235 ---ENGK-LCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKR 280
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-293 |
6.23e-110 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 340.78 E-value: 6.23e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 3 PAEVLSGKIVSAQVRERLKKQVAEMKEKFpGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVL 82
Cdd:PRK14188 1 MATIIDGKAFAADVRATVAAEVARLKAAH-GVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 83 KCIASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDlgDCFIPCTPKGCMELIRQTGIQ 162
Cdd:PRK14188 80 ALIARLNADPAIHGILVQLPLP--KHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGE--TALVPCTPLGCMMLLRRVHGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 163 VAGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVP 242
Cdd:PRK14188 156 LSGLNAVVIGRSNLVGKPMAQLLLAANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIP 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1444535382 243 DSTKASGK-RVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PRK14188 236 APEKGEGKtRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACR 287
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-297 |
1.78e-100 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 315.32 E-value: 1.78e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 3 PAEVLSGKIVSAQVRERLKKQVAEMKEKfpGFR-PGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEV 81
Cdd:PRK10792 2 TAKIIDGKTIAQQVRSEVAQKVQARVAA--GLRaPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 82 LKCIASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLS------RgdlgdcfiPCTPKGCMEL 155
Cdd:PRK10792 80 LALIDELNADPTIDGILVQLPLP--AHIDNVKVLERIHPDKDVDGFHPYNVGRLAqripllR--------PCTPRGIMTL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 156 IRQTGIQVAGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVID 235
Cdd:PRK10792 150 LERYGIDTYGLNAVVVGASNIVGRPMSLELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVID 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1444535382 236 CGINHVPDstkasGKrVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQRFLEK 297
Cdd:PRK10792 230 VGINRLED-----GK-LVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEEYHDP 285
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
4-293 |
2.13e-100 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 315.68 E-value: 2.13e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 4 AEVLSGKIVSAQVRERLKKQVAEMKEKFpGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLK 83
Cdd:PLN02516 9 AQIIDGKAIAKAIRSEIAEEVAQLSEKH-GKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELIS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 84 CIASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDLGDCFIPCTPKGCMELIRQTGIQV 163
Cdd:PLN02516 88 KVHELNANPDVHGILVQLPLP--KHINEEKILNEISLEKDVDGFHPLNIGKLAMKGREPLFLPCTPKGCLELLSRSGIPI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 164 AGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVPD 243
Cdd:PLN02516 166 KGKKAVVVGRSNIVGLPVSLLLLKADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVSD 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1444535382 244 STKASGKRVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PLN02516 246 PSKKSGYRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKR 295
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
3-293 |
1.10e-98 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 310.85 E-value: 1.10e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 3 PAEVLSGKIVSAQVRERLKKQVAEMKEKfpGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVL 82
Cdd:PRK14189 2 TAQLIDGNALSKQLRAEAAQRAAALTAR--GHQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 83 KCIASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDLGdcFIPCTPKGCMELIRQTGIQ 162
Cdd:PRK14189 80 ARIDELNRDPKIHGILVQLPLP--KHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPL--FRPCTPYGVMKMLESIGIP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 163 VAGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVP 242
Cdd:PRK14189 156 LRGAHAVVIGRSNIVGKPMAMLLLQAGATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMNRDD 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1444535382 243 DstkasGKrVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PRK14189 236 A-----GK-LCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAER 280
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
2-299 |
3.43e-98 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 312.32 E-value: 3.43e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 2 APAEVLSGKIVSAQVRERLKKQVAEMKEKFpGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEV 81
Cdd:PLN02616 71 GGAKVIDGKAVAKKIRDEITIEVSRMKESI-GVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 82 LKCIASLNGDPAVHGFIVQLPLDSDkpINTEKITNAVAPEKDVDGLSSINAGKLSRGDLGDCFIPCTPKGCMELIRQTGI 161
Cdd:PLN02616 150 LKFISGFNNDPSVHGILVQLPLPSH--MDEQNILNAVSIEKDVDGFHPLNIGRLAMRGREPLFVPCTPKGCIELLHRYNV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 162 QVAGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHV 241
Cdd:PLN02616 228 EIKGKRAVVIGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPV 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1444535382 242 PDSTKASGKRVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQRfLEKFQ 299
Cdd:PLN02616 308 EDASSPRGYRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKR-IHNFQ 364
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
120-292 |
8.20e-94 |
|
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding domain of the Methylene-Tetrahydrofolate Dehydrogenase/cyclohydrolase (m-THF DH/cyclohydrolase) bifunctional enzyme. Tetrahydrofolate is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofucntional DH, as well as bifunctional m-THF m-THF DHm-THF DHDH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains the bifunctional DH/cyclohydrolase. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains.
Pssm-ID: 133448 Cd Length: 168 Bit Score: 293.31 E-value: 8.20e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 120 PEKDVDGLSSINAGKLSRGDlgDCFIPCTPKGCMELIRQTGIQVAGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKT 199
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGR--PGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 200 STLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVPDstkASGKRVVGDVAYSTAKEKASYITPVPGGVGPMT 279
Cdd:cd01080 79 KNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPD---KSGGKLVGDVDFESAKEKASAITPVPGGVGPMT 155
|
170
....*....|...
gi 1444535382 280 VAMLMQSTVESAQ 292
Cdd:cd01080 156 VAMLMKNTVEAAK 168
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-293 |
3.88e-93 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 296.59 E-value: 3.88e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 3 PAEVLSGKIVSAQVRERLKKQVAEMKEKFpGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVL 82
Cdd:PRK14186 1 MALILDGKALAAEIEQRLQAQIESNLPKA-GRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 83 KCIASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDLGdcFIPCTPKGCMELIRQTGIQ 162
Cdd:PRK14186 80 ALIAQLNQDERVDGILLQLPLP--KHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPG--LRSCTPAGVMRLLRSQQID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 163 VAGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVP 242
Cdd:PRK14186 156 IAGKKAVVVGRSILVGKPLALMLLAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHRLP 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1444535382 243 DSTKASgkRVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PRK14186 236 SSDGKT--RLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSWQK 284
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
4-293 |
1.30e-89 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 289.17 E-value: 1.30e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 4 AEVLSGKIVSAQVRERLKKQVAEMKEKFpGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLK 83
Cdd:PLN02897 56 TVVIDGNVIAEEIRTKIASEVRKMKKAV-GKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 84 CIASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDLGDCFIPCTPKGCMELIRQTGIQV 163
Cdd:PLN02897 135 ALRKFNEDTSIHGILVQLPLP--QHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREPLFVSCTPKGCVELLIRSGVEI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 164 AGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVPD 243
Cdd:PLN02897 213 AGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPVED 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1444535382 244 STKASGKRVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PLN02897 293 SSCEFGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKR 342
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-297 |
4.12e-89 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 285.51 E-value: 4.12e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 6 VLSGKIVSAQVRERLKKQVAEMKEKFpGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLKCI 85
Cdd:PRK14191 3 LLDGKALSYKIEKDLKNKIQILTAQT-GKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 86 ASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDlgDCFIPCTPKGCMELIRQTGIQVAG 165
Cdd:PRK14191 82 KDLNTDQNIDGILVQLPLP--RHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQL--DGFVPATPMGVMRLLKHYHIEIKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 166 KRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVPDSt 245
Cdd:PRK14191 158 KDVVIIGASNIVGKPLAMLMLNAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLNDG- 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1444535382 246 kasgkRVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQRFLEK 297
Cdd:PRK14191 237 -----RLVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEKRQRK 283
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-294 |
1.13e-88 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 284.79 E-value: 1.13e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 6 VLSGKIVSAQVRERLKKQVAEMKEKfPGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLKCI 85
Cdd:PRK14174 3 IIDGKKVSLDLKNELKTRVEAYRAK-TGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 86 ASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDLGDCFIPCTPKGCMELIRQTGIQVAG 165
Cdd:PRK14174 82 EDLNNDPDVHGILVQQPLP--KQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGHLDKCFVSCTPYGILELLGRYNIETKG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 166 KRAVVVGRSKIVGAPMHDLLL----WNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHV 241
Cdd:PRK14174 160 KHCVVVGRSNIVGKPMANLMLqklkESNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1444535382 242 PDSTKASGKRVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQRF 294
Cdd:PRK14174 240 EDPSTKSGYRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTLQSFERV 292
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
4-297 |
3.92e-88 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 282.80 E-value: 3.92e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 4 AEVLSGKIVSAQVRERLKKQVAEMKEKFpGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLK 83
Cdd:PRK14179 2 TEIIDGKALAQKMQAELAEKVAKLKEEK-GIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 84 CIASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDlgDCFIPCTPKGCMELIRQTGIQV 163
Cdd:PRK14179 81 LIERYNQDPTWHGILVQLPLP--KHINEEKILLAIDPKKDVDGFHPMNTGHLWSGR--PVMIPCTPAGIMEMFREYNVEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 164 AGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHvpd 243
Cdd:PRK14179 157 EGKHAVVIGRSNIVGKPMAQLLLDKNATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMNR--- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1444535382 244 stKASGKrVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQRFLEK 297
Cdd:PRK14179 234 --DENGK-LIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALRSLHK 284
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
128-295 |
6.09e-85 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 269.34 E-value: 6.09e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 128 SSINAGKLSRGdlGDCFIPCTPKGCMELIRQTGIQVAGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVA 207
Cdd:pfam02882 1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 208 KADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVpdstkaSGKRVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQST 287
Cdd:pfam02882 79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRV------GNGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNT 152
|
....*...
gi 1444535382 288 VESAQRFL 295
Cdd:pfam02882 153 VEAAKRQL 160
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-293 |
8.01e-82 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 265.72 E-value: 8.01e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 4 AEVLSGKIVSAQVRERLKKQVAEMKEKfpGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLK 83
Cdd:PRK14193 3 AIILDGKATADEIKADLAERVAALKEK--GITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 84 CIASLNGDPAVHGFIVQLPLdsDKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDLGDcfIPCTPKGCMELIRQTGIQV 163
Cdd:PRK14193 81 VIDELNADPACTGYIVQLPL--PKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAP--LPCTPRGIVHLLRRYDVEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 164 AGKRAVVVGRSKIVGAPMHDLLLWNH--ATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHV 241
Cdd:PRK14193 157 AGAHVVVIGRGVTVGRPIGLLLTRRSenATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSRA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1444535382 242 PDStkasgkRVVGDVAySTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PRK14193 237 GDG------KLVGDVH-PDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAER 281
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-298 |
1.17e-80 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 263.23 E-value: 1.17e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 6 VLSGKIVSAQVRERLKKQVAEMKEKFPGFrPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLKCI 85
Cdd:PRK14187 4 IIDGKKIANDITEILATCIDDLKRQHNLF-PCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 86 ASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDLGDCFIPCTPKGCMELIRQTGIQVAG 165
Cdd:PRK14187 83 NELNNDDSVHGILVQLPVP--NHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQKKNCLIPCTPKGCLYLIKTITRNLSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 166 KRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVPDST 245
Cdd:PRK14187 161 SDAVVIGRSNIVGKPMACLLLGENCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSIEEGG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1444535382 246 KasgKRVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESA--QRFLEKF 298
Cdd:PRK14187 241 V---KKFVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAAcnQKGIDDF 292
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-289 |
2.02e-80 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 262.02 E-value: 2.02e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 5 EVLSGKIVSAQVRERLKKQVAEMKEKfpGFR-PGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLK 83
Cdd:PRK14172 3 QIINGKEVALKIKEEIKNFVEERKEN--GLSiPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 84 CIASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDlgDCFIPCTPKGCMELIRQTGIQV 163
Cdd:PRK14172 81 EIEELNKDNNVHGIMLQLPLP--KHLDEKKITNKIDANKDIDCLTFISVGKFYKGE--KCFLPCTPNSVITLIKSLNIDI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 164 AGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVpd 243
Cdd:PRK14172 157 EGKEVVVIGRSNIVGKPVAQLLLNENATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSV-- 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1444535382 244 stkaSGKrVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVE 289
Cdd:PRK14172 235 ----NGK-ITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKNVCE 275
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-290 |
2.57e-80 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 262.02 E-value: 2.57e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 6 VLSGKIVSAQVRERLKKQVAEMKEKfPGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLKCI 85
Cdd:PRK14184 3 LLDGKATAATIREELKTEVAALTAR-HGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 86 ASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDlgDCFIPCTPKGCMELIRQTGIQVAG 165
Cdd:PRK14184 82 AELNARPDIDGILLQLPLP--KGLDSQRCLELIDPAKDVDGFHPENMGRLALGL--PGFRPCTPAGVMTLLERYGLSPAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 166 KRAVVVGRSKIVGAPMHDLLL----WNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHV 241
Cdd:PRK14184 158 KKAVVVGRSNIVGKPLALMLGapgkFANATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRT 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1444535382 242 PDStkasgkrVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVES 290
Cdd:PRK14184 238 DDG-------LVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQS 279
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-293 |
3.84e-80 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 261.49 E-value: 3.84e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 6 VLSGKIVSAQVRERLKKQVAEMKEKfpGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLKCI 85
Cdd:PRK14182 3 LIDGKQIAAKVKGEVATEVRALAAR--GVQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 86 ASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDLGdCFIPCTPKGCMELIRQTGIQVAG 165
Cdd:PRK14182 81 ARLNADPAVHGILVQLPLP--KHVDERAVLDAISPAKDADGFHPFNVGALSIGIAG-VPRPCTPAGVMRMLDEARVDPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 166 KRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVPDSt 245
Cdd:PRK14182 158 KRALVVGRSNIVGKPMAMMLLERHATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLADG- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1444535382 246 kasgkRVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PRK14182 237 -----KLVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKR 279
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-292 |
1.69e-79 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 260.16 E-value: 1.69e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 1 MAPAEVLSGKIVSAQVRERLKKQVAEMKEKfpGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAE 80
Cdd:PRK14194 1 LMSAKLIDGKAAAARVLAQVREDVRTLKAA--GIEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 81 VLKCIASLNGDPAVHGFIVQLPLDSDkpINTEKITNAVAPEKDVDGLSSINAGKLSRGDlgDCFIPCTPKGCMELIRQTG 160
Cdd:PRK14194 79 LLALIAELNADPSVNGILLQLPLPAH--IDEARVLQAINPLKDVDGFHSENVGGLSQGR--DVLTPCTPSGCLRLLEDTC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 161 IQVAGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINH 240
Cdd:PRK14194 155 GDLTGKHAVVIGRSNIVGKPMAALLLQAHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINR 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1444535382 241 VPDSTKAsgkRVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQ 292
Cdd:PRK14194 235 IDDDGRS---RLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAAR 283
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-292 |
8.21e-79 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 257.46 E-value: 8.21e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 6 VLSGKIVSAQVRERLKKQVAEmkekfPGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLKCI 85
Cdd:PRK14178 2 ILDGKAVSEKRLELLKEEIIE-----SGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 86 ASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDLGdcFIPCTPKGCMELIRQTGIQVAG 165
Cdd:PRK14178 77 RRLNEDPDINGILVQLPLP--KGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPG--FAPCTPNGIMTLLHEYKISIAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 166 KRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVpdst 245
Cdd:PRK14178 153 KRAVVVGRSIDVGRPMAALLLNADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQV---- 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1444535382 246 kaSGKrVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQ 292
Cdd:PRK14178 229 --NGK-LCGDVDFDAVKEIAGAITPVPGGVGPMTIATLMENTFDAAK 272
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-300 |
1.15e-78 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 257.59 E-value: 1.15e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 6 VLSGKIVSAQVRERLKKQVAEMKEKfpGFR-PGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLKC 84
Cdd:PRK14177 5 LLDGKKLSEKIRNEIRETIEERKTK--NKRiPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 85 IASLNGDPAVHGFIVQLPLDSDkpINTEKITNAVAPEKDVDGLSSINAGKLSRGDlgDCFIPCTPKGCMELIRQTGIQVA 164
Cdd:PRK14177 83 IDKLNLDPNVDGILLQHPVPSQ--IDERAAFDRIALEKDVDGVTTLSFGKLSMGV--ETYLPCTPYGMVLLLKEYGIDVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 165 GKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINhvPDS 244
Cdd:PRK14177 159 GKNAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYN--PGN 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1444535382 245 tkasgkrvVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESaqrFLEKFQP 300
Cdd:PRK14177 237 --------VGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYS---FKEHFTP 281
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-291 |
2.54e-78 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 257.01 E-value: 2.54e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 4 AEVLSGKIVSAQVRERLKKQVAEMKEKfpGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLK 83
Cdd:PRK14167 2 TEIIDGNAVAAQIRDDLTDAIETLEDA--GVTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 84 CIASLNGDPAVHGFIVQLPLDSDkpINTEKITNAVAPEKDVDGLSSINAGKLSRGDLGdcFIPCTPKGCMELIRQTGIQV 163
Cdd:PRK14167 80 TIDELNADEDVHGILVQMPVPDH--VDDREVLRRIDPAKDVDGFHPENVGRLVAGDAR--FKPCTPHGIQKLLAAAGVDT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 164 AGKRAVVVGRSKIVGAPMHDLLLWN----HATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGIN 239
Cdd:PRK14167 156 EGADVVVVGRSDIVGKPMANLLIQKadggNATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGIN 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1444535382 240 HVPDSTKaSGKRVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESA 291
Cdd:PRK14167 236 RVDADTE-KGYELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAA 286
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-295 |
5.03e-78 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 255.52 E-value: 5.03e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 5 EVLSGKIVSAQVRERLKKQVAEMKeKFPGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLKC 84
Cdd:PRK14183 2 QILDGKALSDKIKENVKKEVDELK-LVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 85 IASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDlgDCFIPCTPKGCMELIRQTGIQVA 164
Cdd:PRK14183 81 IAMMNNNPNIDGILVQLPLP--KHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGL--DGFVPCTPLGVMELLEEYEIDVK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 165 GKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVPDS 244
Cdd:PRK14183 157 GKDVCVVGASNIVGKPMAALLLNANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINRTEDG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1444535382 245 tkasgkRVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQRFL 295
Cdd:PRK14183 237 ------RLVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKNRA 281
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-293 |
1.50e-77 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 254.37 E-value: 1.50e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 4 AEVLSGKIVSAQVRERLKKQVAemkeKFPgFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLK 83
Cdd:PRK14173 3 ARELSGPPAAEAVYAELRARLA----KLP-FVPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 84 CIASLNGDPAVHGFIVQLPLDSDKPINteKITNAVAPEKDVDGLSSINAGKLSRGdlGDCFIPCTPKGCMELIRQTGIQV 163
Cdd:PRK14173 78 LIARLNADPEVDGILVQLPLPPHIDFQ--RVLEAIDPLKDVDGFHPLNVGRLWMG--GEALEPCTPAGVVRLLKHYGIPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 164 AGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVPD 243
Cdd:PRK14173 154 AGKEVVVVGRSNIVGKPLAALLLREDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINRVGG 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1444535382 244 StkASGKRVVGDVAYSTAkEKASYITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PRK14173 234 N--GGRDILTGDVHPEVA-EVAGALTPVPGGVGPMTVAMLMANTVIAALR 280
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-297 |
4.10e-77 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 253.60 E-value: 4.10e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 5 EVLSGKIVSAQVRERLKKQVAEMKEKfPGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLKC 84
Cdd:PRK14185 2 QLIDGKAISAQIKQEIAAEVAEIVAK-GGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 85 IASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDlgDCFIPCTPKGCMELIRQTGIQVA 164
Cdd:PRK14185 81 VRELNQDDDVDGFIVQLPLP--KHISEQKVIEAIDYRKDVDGFHPINVGRMSIGL--PCFVSATPNGILELLKRYHIETS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 165 GKRAVVVGRSKIVGAPMHDLLLWNH----ATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINH 240
Cdd:PRK14185 157 GKKCVVLGRSNIVGKPMAQLMMQKAypgdCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1444535382 241 VPDSTKASGKRVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQRFLEK 297
Cdd:PRK14185 237 VPDATRKSGFKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKKAIYK 293
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-295 |
8.60e-76 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 249.72 E-value: 8.60e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 6 VLSGKIVSAQVRERLKKQVAEMKEKFpGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLKCI 85
Cdd:PRK14176 10 IIDGKALAKKIEAEVRSGVERLKSNR-GITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 86 ASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDLGdcFIPCTPKGCMELIRQTGIQVAG 165
Cdd:PRK14176 89 DSLNKRKDVHGILLQLPLP--KHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEG--LVPCTPHGVIRALEEYGVDIEG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 166 KRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGInhvpdsT 245
Cdd:PRK14176 165 KNAVIVGHSNVVGKPMAAMLLNRNATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGI------T 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1444535382 246 KASGKrVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQRFL 295
Cdd:PRK14176 239 KEEDK-VYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEKSL 287
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-297 |
1.71e-74 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 246.37 E-value: 1.71e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 3 PAEVLSGKIVSAQVRERLKKQVAEMKEKfpGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVL 82
Cdd:PRK14175 2 VAKILDGKQIAKDYRQGLQDQVEALKEK--GFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 83 KCIASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDlgDCFIPCTPKGCMELIRQTGIQ 162
Cdd:PRK14175 80 NELNRLNNDDSVSGILVQVPLP--KQVSEQKILEAINPEKDVDGFHPINIGKLYIDE--QTFVPCTPLGIMEILKHADID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 163 VAGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGinHVP 242
Cdd:PRK14175 156 LEGKNAVVIGRSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVG--NTP 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1444535382 243 DStkaSGKrVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTV--ESAQRFLEK 297
Cdd:PRK14175 234 DE---NGK-LKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLlaEKMRRGIDS 286
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-293 |
2.66e-74 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 245.76 E-value: 2.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 4 AEVLSGKIVSAQVRERLKKQVAEMKEKfpGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLK 83
Cdd:PRK14170 2 GEIIDGKKLAKEIQEKVTREVAELVKE--GKKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 84 CIASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDlgDCFIPCTPKGCMELIRQTGIQV 163
Cdd:PRK14170 80 VVEELNEDKTIHGILVQLPLP--EHISEEKVIDTISYDKDVDGFHPVNVGNLFIGK--DSFVPCTPAGIIELIKSTGTQI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 164 AGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINhvpd 243
Cdd:PRK14170 156 EGKRAVVIGRSNIVGKPVAQLLLNENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMD---- 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1444535382 244 stKASGKRVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PRK14170 232 --RDENNKLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKR 279
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-292 |
4.48e-74 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 244.94 E-value: 4.48e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 6 VLSGKIVSAQVRERLKKQVAEMKEKfpGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLKCI 85
Cdd:PRK14166 3 LLDGKALSAKIKEELKEKNQFLKSK--GIESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 86 ASLNGDPAVHGFIVQLPLDSDkpINTEKITNAVAPEKDVDGLSSINAGKLSRGdLGDCFIPCTPKGCMELIRQTGIQVAG 165
Cdd:PRK14166 81 NTLNHDDSVHGILVQLPLPDH--ICKDLILESIISSKDVDGFHPINVGYLNLG-LESGFLPCTPLGVMKLLKAYEIDLEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 166 KRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVpdst 245
Cdd:PRK14166 158 KDAVIIGASNIVGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRL---- 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1444535382 246 kASGKrVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQ 292
Cdd:PRK14166 234 -ESGK-IVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAK 278
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-291 |
8.40e-74 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 244.78 E-value: 8.40e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 4 AEVLSGKIVSAQVRERLKKQVAEMKEKFpGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLK 83
Cdd:PRK14168 3 AKIIKGTEIREEILEEIRGEVAELKEKY-GKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 84 CIASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDLGDCFIPCTPKGCMELIRQTGIQV 163
Cdd:PRK14168 82 LIDKYNNDDSIHGILVQLPLP--KHINEKKVLNAIDPDKDVDGFHPVNVGRLMIGGDEVKFLPCTPAGIQEMLVRSGVET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 164 AGKRAVVVGRSKIVGAPMHDLLLWN----HATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGIN 239
Cdd:PRK14168 160 SGAEVVVVGRSNIVGKPIANMMTQKgpgaNATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVN 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1444535382 240 HVPDSTKASGKRVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESA 291
Cdd:PRK14168 240 RVGTNESTGKAILSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSA 291
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-290 |
4.16e-73 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 242.56 E-value: 4.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 6 VLSGKIVSAQVRERLKKQVAEMKEKfPGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLKCI 85
Cdd:PRK14171 4 IIDGKALANEILADLKLEIQELKSQ-TNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 86 ASLNGDPAVHGFIVQLPLDSDkpINTEKITNAVAPEKDVDGLSSINAGKLSRGdLGDCFIPCTPKGCMELIRQTGIQVAG 165
Cdd:PRK14171 83 NELNLDNEISGIIVQLPLPSS--IDKNKILSAVSPSKDIDGFHPLNVGYLHSG-ISQGFIPCTALGCLAVIKKYEPNLTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 166 KRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVpdst 245
Cdd:PRK14171 160 KNVVIIGRSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRI---- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1444535382 246 kaSGKRVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVES 290
Cdd:PRK14171 236 --SGNKIIGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKA 278
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-295 |
1.40e-72 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 240.90 E-value: 1.40e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 4 AEVLSGKIVSAQVRERLKKQVAEMKEKfPGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLK 83
Cdd:PRK14192 3 ALVLDGKALAKQIEEELSVRVEALKAK-TGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 84 CIASLNGDPAVHGFIVQLPLDSDkpINTEKITNAVAPEKDVDGLSSINAGKLSRGDlgDCFIPCTPKGCMELIRQTGIQV 163
Cdd:PRK14192 82 KIEELNANPDVHGILLQHPVPAQ--IDERACFDAISLAKDVDGVTCLGFGRMAMGE--AAYGSATPAGIMRLLKAYNIEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 164 AGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINhvpd 243
Cdd:PRK14192 158 AGKHAVVVGRSAILGKPMAMMLLNANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFH---- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1444535382 244 STKASGkrvVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQRFL 295
Cdd:PRK14192 234 PRDGGG---VGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKAL 282
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-294 |
1.25e-71 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 238.61 E-value: 1.25e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 6 VLSGKIVSAQVRERLKKQVAEMKEkfpgfRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLKCI 85
Cdd:PRK14181 2 LLKGAPAAEHILATIKENISASST-----APGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 86 ASLNGDPAVHGFIVQLPLdsDKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDLGDcFIPCTPKGCMELIRQTGIQVAG 165
Cdd:PRK14181 77 HRLNNDPNIHGILVQLPL--PKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGETDG-FIPCTPAGIIELLKYYEIPLHG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 166 KRAVVVGRSKIVGAPMHDLLLWNH----ATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHV 241
Cdd:PRK14181 154 RHVAIVGRSNIVGKPLAALLMQKHpdtnATVTLLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRV 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1444535382 242 PdSTKASGKRVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQRF 294
Cdd:PRK14181 234 P-AANPKGYILVGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNTWESYLRH 285
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-294 |
1.33e-69 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 232.61 E-value: 1.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 6 VLSGKIVSAQVRERLKKQVAEMKEKfPGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLKCI 85
Cdd:PRK14180 3 LIDGKSLSKDLKERLATQVQEYKHH-TAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 86 ASLNGDPAVHGFIVQLPLDSDkpINTEKITNAVAPEKDVDGLSSINAGKLSRGDlGDCFIPCTPKGCMELIRQTGIQVAG 165
Cdd:PRK14180 82 DQLNNDSSVHAILVQLPLPAH--INKNNVIYSIKPEKDVDGFHPTNVGRLQLRD-KKCLESCTPKGIMTMLREYGIKTEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 166 KRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVpdst 245
Cdd:PRK14180 159 AYAVVVGASNVVGKPVSQLLLNAKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHV---- 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1444535382 246 kaSGKrVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQRF 294
Cdd:PRK14180 235 --DGK-IVGDVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQEL 280
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-293 |
7.00e-69 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 230.60 E-value: 7.00e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 4 AEVLSGKIVSAQVRERLKKQVAEMKEKfpGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLK 83
Cdd:PRK14169 1 ATRLDGRAVSKKILADLKQTVAKLAQQ--DVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 84 CIASLNGDPAVHGFIVQLPLDsdKPINTEKITNAVAPEKDVDGLSSINAGKLSRGDLGdcFIPCTPKGCMELIRQTGIQV 163
Cdd:PRK14169 79 KVAELNHDPDVDAILVQLPLP--AGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPT--VVASTPYGIMALLDAYDIDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 164 AGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAGKAEMVKGEWIKPGAVVIDCGINHVPD 243
Cdd:PRK14169 155 AGKRVVIVGRSNIVGRPLAGLMVNHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRGAD 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1444535382 244 StkasgkRVVGDVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PRK14169 235 G------KLLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKR 278
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
7-125 |
1.33e-48 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 167.97 E-value: 1.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 7 LSGKIVSAQVRERLKKQVAEMKEkfPGFRPGLAILQVGNRDDSNLYINMKLKAAAEIGISANHIKLPNTATEAEVLKCIA 86
Cdd:pfam00763 1 IDGKAIAKKIREELKEEVAALKA--GGRKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALID 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 1444535382 87 SLNGDPAVHGFIVQLPLdsDKPINTEKITNAVAPEKDVD 125
Cdd:pfam00763 79 KLNADPSVHGILVQLPL--PKHIDEEKVLEAIDPEKDVD 115
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
138-291 |
4.02e-47 |
|
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: 164.60 E-value: 4.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 138 GDLGDCFIPCTPKGCMELIRQTGIQVAGKRAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTSTLAEEVAKADILVVAAG 217
Cdd:cd05212 1 GPCTPLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1444535382 218 KAEMVKGEWIKPGAVVIDCGINHvpdstkasgkrvvgdVAYSTAKEKASYITPVPGGVGPMTVAMLMQSTVESA 291
Cdd:cd05212 81 KPEKVPTEWIKPGATVINCSPTK---------------LSGDDVKESASLYVPMTGGVGKLTVAMRMQNMVRSV 139
|
|
| NAD_bind_m-THF_DH |
cd01079 |
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ... |
120-288 |
5.45e-13 |
|
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: 68.61 E-value: 5.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 120 PEKDVDGLSSINAGKL---SRGDLGD----CFIPCTPKGCMELIRQTGI---------QVAGKRAVVVGRSKIVGAPMHD 183
Cdd:cd01079 1 PHKDVEGLSHKYIFNLyhnIRFLDPEnrkkSILPCTPLAIVKILEFLGIynkilpygnRLYGKTITIINRSEVVGRPLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 184 LLLWNHATV---------------------TTCHSKTSTLAEEVAKADILVVAAGKAEM-VKGEWIKPGAVVID-CGINH 240
Cdd:cd01079 81 LLANDGARVysvdingiqvftrgesirhekHHVTDEEAMTLDCLSQSDVVITGVPSPNYkVPTELLKDGAICINfASIKN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1444535382 241 VPDStkasgkrvvgdvaystAKEKASYITPVpggVGPMTVAMLMQSTV 288
Cdd:cd01079 161 FEPS----------------VKEKASIYVPS---IGKVTIAMLLRNLL 189
|
|
| NAD_bind_amino_acid_DH |
cd05191 |
NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH) ... |
147-237 |
3.26e-06 |
|
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: 46.22 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444535382 147 CTPKGCMELI----RQTGIQVAGKRAVVVGRsKIVGAPMHDLLLWNH-ATVTTCHSktstlaeevakaDILVVAAGKAEM 221
Cdd:cd05191 1 ATAAGAVALLkaagKVTNKSLKGKTVVVLGA-GEVGKGIAKLLADEGgKKVVLCDR------------DILVTATPAGVP 67
|
90
....*....|....*....
gi 1444535382 222 VKGE---WIKPGAVVIDCG 237
Cdd:cd05191 68 VLEEataKINEGAVVIDLA 86
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
192-235 |
2.18e-03 |
|
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.
Pssm-ID: 240630 [Multi-domain] Cd Length: 359 Bit Score: 41.24 E-value: 2.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1444535382 192 VTTCHSKTSTLAEEVAKADILVVAA----GKA------EMVKgeWIKPGAVVID 235
Cdd:cd05305 215 VTTLYSNPANLEEALKEADLVIGAVlipgAKApklvteEMVK--TMKPGSVIVD 266
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
189-235 |
4.67e-03 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 38.64 E-value: 4.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1444535382 189 HATVTTCHSKTSTLAEEVAKADILVVAA---GK-------AEMVKGewIKPGAVVID 235
Cdd:smart01002 64 GARFTTLYSQAELLEEAVKEADLVIGAVlipGAkapklvtREMVKS--MKPGSVIVD 118
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