|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
286-883 |
0e+00 |
|
Formate--tetrahydrofolate ligase
Pssm-ID: 178359 Cd Length: 637 Bit Score: 969.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 286 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKST 365
Cdd:PLN02759 9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 366 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 445
Cdd:PLN02759 89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 446 TQTDKALYNRLVPL-VNGVREFSEIQLARLKKLGINKTDPSTLTEEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIG 524
Cdd:PLN02759 169 TQSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 525 QGNTEKGHYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTL 604
Cdd:PLN02759 249 QGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 605 EGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMH 684
Cdd:PLN02759 329 EGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMH 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 685 GGGPSVTAGVPLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYH 764
Cdd:PLN02759 409 GGGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTH 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 765 WSVGGKGSVDLARAVREAASKRSR-FQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAK 843
Cdd:PLN02759 489 HAHGGKGAVDLGEAVQKACEGNSQpFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAK 568
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 767942604 844 THLSLSHQPDKKGVPRDFILPISDVRASIGAGFIYPLVGT 883
Cdd:PLN02759 569 TQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGT 608
|
|
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
294-883 |
0e+00 |
|
Formate--tetrahydrofolate ligase;
Pssm-ID: 460143 Cd Length: 555 Bit Score: 934.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 294 PSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQA 373
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 374 LtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkaly 453
Cdd:pfam01268 81 L-NRLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 454 nrlvplvngvrefseiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHY 533
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 534 RQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHA 613
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 614 GPFANIAHGNSSVLADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGgpsvtag 693
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGG------- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 694 vPLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKrAGAFDAVPCYHWSVGGKGSV 773
Cdd:pfam01268 339 -VGKDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRELCE-AGGVDAALSEHWAKGGEGAI 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 774 DLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQP 852
Cdd:pfam01268 417 ELAEAVVEACeEEPSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
|
570 580 590
....*....|....*....|....*....|.
gi 767942604 853 DKKGVPRDFILPISDVRASIGAGFIYPLVGT 883
Cdd:pfam01268 497 KLKGAPTGFTLPVRDVRLSAGAGFIVALTGD 527
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
308-883 |
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: 883.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 308 VDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALTAHLNvNSFACLR 387
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 388 QPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkalynrlvplvngvrefs 467
Cdd:cd00477 80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 468 eiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYRQAQFDIAVASEIM 547
Cdd:cd00477 139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 548 AVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSVL 627
Cdd:cd00477 189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 628 ADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGvplkkeytEENIQL 707
Cdd:cd00477 269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 708 VADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVpCYHWSVGGKGSVDLARAVREAASK-R 786
Cdd:cd00477 338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKpK 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 787 SRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQPDKKGVPRDFILPIS 866
Cdd:cd00477 417 SNFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
|
570
....*....|....*..
gi 767942604 867 DVRASIGAGFIYPLVGT 883
Cdd:cd00477 497 DVRLSAGAGFVVPLAGD 513
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
293-883 |
0e+00 |
|
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
Pssm-ID: 442046 Cd Length: 556 Bit Score: 834.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 293 VPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQ 372
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 373 ALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENtqtdkal 452
Cdd:COG2759 81 AL-NRLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQGN------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 453 ynrlvplvngvrefseiqlarlkklginktdpstlteeevskfaRLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGH 532
Cdd:COG2759 153 --------------------------------------------ELNIDPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 533 YRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVH 612
Cdd:COG2759 189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 613 AGPFANIAHGNSSVLADKIALKLvGEegFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPsvta 692
Cdd:COG2759 269 GGPFANIAHGCNSVIATKLALKL-AD--YVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 693 gvplKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAfDAVPCYHWSVGGKGS 772
Cdd:COG2759 342 ----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEGA 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 773 VDLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQ 851
Cdd:COG2759 417 EELAEAVVEACeEGPSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSDD 496
|
570 580 590
....*....|....*....|....*....|..
gi 767942604 852 PDKKGVPRDFILPISDVRASIGAGFIYPLVGT 883
Cdd:COG2759 497 PKLLGAPTGFTLTVREVRLSAGAGFIVALTGD 528
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
127-269 |
2.81e-67 |
|
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: 220.84 E-value: 2.81e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 127 GDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSP 206
Cdd:cd05212 1 GPCTPLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767942604 207 KPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSPRIHFGGLIeedDVILLAAALRIQNMVSSGR 269
Cdd:cd05212 81 KPEKVPTEWIKPGATVINCSPTKLSGDDVKESASLYVPMTG---GVGKLTVAMRMQNMVRSVR 140
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
117-272 |
1.60e-35 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 132.20 E-value: 1.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 117 TDINLGKLVRGdaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLH 196
Cdd:pfam02882 1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 197 EADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSprIHF--------------GGlieeddVILLAAALRIQ 262
Cdd:pfam02882 79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGD--VDFenvkekasaitpvpGG------VGPMTVAMLLQ 150
|
170
....*....|
gi 767942604 263 NMVSSGRRWL 272
Cdd:pfam02882 151 NTVEAAKRQL 160
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
31-223 |
3.14e-33 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 129.75 E-value: 3.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 31 KPVLAIIQAGDD--------NLmqeinQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ------ISE 96
Cdd:COG0190 32 TPGLAVVLVGDDpasqvyvrNK-----HKACEEVGIESELIRLPADTTQEELLALIDELNADPSVHGILVQlplpkhIDE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 97 NlfsnKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAhgSLE-----AALq 171
Cdd:COG0190 107 E----AVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLERYGIDLAGKHAVVVGR--SNIvgkplALL- 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767942604 172 cLFQRKGSMTM--SiqwKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVL 223
Cdd:COG0190 178 -LLRRNATVTVchS---RTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVI 227
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
32-224 |
2.41e-25 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 108.51 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 32 PVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNA 106
Cdd:PLN02897 87 PGLAVVLVGQQRDSQTYVRNkikACEETGIKSLLAELPEDCTEGQILSALRKFNEDTSIHGILVQLPlpQHLDESKILNM 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 107 LKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQW 186
Cdd:PLN02897 167 VRLEKDVDGFHPLNVGNLAMRGREPLFVSCTPKGCVELLIRSGVEIAGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHA 246
|
170 180 190
....*....|....*....|....*....|....*...
gi 767942604 187 KTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 224
Cdd:PLN02897 247 FTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVID 284
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-224 |
3.73e-25 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 106.25 E-value: 3.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 6 ARPRREviQNSKEVLSLlqeKNPAFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKIN 82
Cdd:PRK14190 12 AKEKRE--QLKEEVVKL---KEQGIVPGLAVILVGDDPASHsyvRGKKKAAEKVGIYSELYEFPADITEEELLALIDRLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 83 EDTRVHGLALQ------ISENlfsnKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKK 156
Cdd:PRK14190 87 ADPRINGILVQlplpkhIDEK----AVIERISPEKDVDGFHPINVGRMMLGQ--DTFLPCTPHGILELLKEYNIDISGKH 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767942604 157 ILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 224
Cdd:PRK14190 161 VVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVID 228
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
24-114 |
1.62e-17 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 78.99 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 24 QEKNPAFKPVLAIIQAGDD---NLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENL 98
Cdd:pfam00763 20 ALKAGGRKPGLAVILVGDDpasQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKLNADPSVHGILVQlpLPKHI 99
|
90
....*....|....*.
gi 767942604 99 FSNKVLNALKPEKDVD 114
Cdd:pfam00763 100 DEEKVLEAIDPEKDVD 115
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
286-883 |
0e+00 |
|
Formate--tetrahydrofolate ligase
Pssm-ID: 178359 Cd Length: 637 Bit Score: 969.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 286 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKST 365
Cdd:PLN02759 9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 366 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 445
Cdd:PLN02759 89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 446 TQTDKALYNRLVPL-VNGVREFSEIQLARLKKLGINKTDPSTLTEEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIG 524
Cdd:PLN02759 169 TQSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 525 QGNTEKGHYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTL 604
Cdd:PLN02759 249 QGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 605 EGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMH 684
Cdd:PLN02759 329 EGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMH 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 685 GGGPSVTAGVPLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYH 764
Cdd:PLN02759 409 GGGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTH 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 765 WSVGGKGSVDLARAVREAASKRSR-FQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAK 843
Cdd:PLN02759 489 HAHGGKGAVDLGEAVQKACEGNSQpFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAK 568
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 767942604 844 THLSLSHQPDKKGVPRDFILPISDVRASIGAGFIYPLVGT 883
Cdd:PLN02759 569 TQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGT 608
|
|
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
294-883 |
0e+00 |
|
Formate--tetrahydrofolate ligase;
Pssm-ID: 460143 Cd Length: 555 Bit Score: 934.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 294 PSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQA 373
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 374 LtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkaly 453
Cdd:pfam01268 81 L-NRLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 454 nrlvplvngvrefseiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHY 533
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 534 RQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHA 613
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 614 GPFANIAHGNSSVLADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGgpsvtag 693
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGG------- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 694 vPLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKrAGAFDAVPCYHWSVGGKGSV 773
Cdd:pfam01268 339 -VGKDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRELCE-AGGVDAALSEHWAKGGEGAI 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 774 DLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQP 852
Cdd:pfam01268 417 ELAEAVVEACeEEPSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
|
570 580 590
....*....|....*....|....*....|.
gi 767942604 853 DKKGVPRDFILPISDVRASIGAGFIYPLVGT 883
Cdd:pfam01268 497 KLKGAPTGFTLPVRDVRLSAGAGFIVALTGD 527
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
308-883 |
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: 883.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 308 VDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALTAHLNvNSFACLR 387
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 388 QPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkalynrlvplvngvrefs 467
Cdd:cd00477 80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 468 eiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYRQAQFDIAVASEIM 547
Cdd:cd00477 139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 548 AVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSVL 627
Cdd:cd00477 189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 628 ADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGvplkkeytEENIQL 707
Cdd:cd00477 269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 708 VADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVpCYHWSVGGKGSVDLARAVREAASK-R 786
Cdd:cd00477 338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKpK 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 787 SRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQPDKKGVPRDFILPIS 866
Cdd:cd00477 417 SNFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
|
570
....*....|....*..
gi 767942604 867 DVRASIGAGFIYPLVGT 883
Cdd:cd00477 497 DVRLSAGAGFVVPLAGD 513
|
|
| PTZ00386 |
PTZ00386 |
formyl tetrahydrofolate synthetase; Provisional |
286-882 |
0e+00 |
|
formyl tetrahydrofolate synthetase; Provisional
Pssm-ID: 240394 Cd Length: 625 Bit Score: 875.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 286 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKST 365
Cdd:PTZ00386 8 KLSCQWPVPSDIDIAQSVKPQPITSVAESAGILLSELDPYGSTRAKVKLSVLKRLENSPNGKYVVVAGMNPTPLGEGKST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 366 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 445
Cdd:PTZ00386 88 TTIGLAQSLGAHLHRKTFACIRQPSQGPTFGIKGGAAGGGYSQVIPMEDFNLHGTGDIHAITAANNLLAAALDTRIFHER 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 446 TQTDKALYNRLVplvNGVREFSEIQLARLKKLGINKTDPSTLTEEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIGQ 525
Cdd:PTZ00386 168 TQSDAALYRRLT---DELKKFTPIMLKRLEKLGISKTDPKQLTEEERVRFARLDIDPDTISWRRVTDVNDRMLREITIGQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 526 GNTEKGHYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLE 605
Cdd:PTZ00386 245 GKEEKGITRKTGFDISVASEVMAILALATDLADMRQRLGAIVVAKSKSGEPVTAEDLGCAGAMTVLMKDTIEPTLMQTLE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 606 GTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHG 685
Cdd:PTZ00386 325 GTPVLVHAGPFGNIAHGNSSIVADQIALKLAGQDGFVLTEAGFGADIGCEKFFNIKCRTSGLKPDAAVLVATVRALKFHG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 686 GGPSVTAGvplkkeytEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELA-KRAGAFDAVPCYH 764
Cdd:PTZ00386 405 GVEPVVAG--------KENLEAVRKGLSNLQRHIQNIRKFGVPVVVALNKFSTDTDAELELVKELAlQEGGAADVVVTDH 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 765 WSVGGKGSVDLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAK 843
Cdd:PTZ00386 477 WAKGGAGAVDLAQALIRVTeNVPSNFKLLYPLDASLKEKIETICKEIYGAAGVEYLNDADEKLEDFERMGYGKFPVCMAK 556
|
570 580 590
....*....|....*....|....*....|....*....
gi 767942604 844 THLSLSHQPDKKGVPRDFILPISDVRASIGAGFIYPLVG 882
Cdd:PTZ00386 557 TQYSFSHDPELRGAPTGFTVPIRDVRVNCGAGFVFPLLG 595
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
293-883 |
0e+00 |
|
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
Pssm-ID: 442046 Cd Length: 556 Bit Score: 834.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 293 VPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQ 372
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 373 ALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENtqtdkal 452
Cdd:COG2759 81 AL-NRLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQGN------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 453 ynrlvplvngvrefseiqlarlkklginktdpstlteeevskfaRLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGH 532
Cdd:COG2759 153 --------------------------------------------ELNIDPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 533 YRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVH 612
Cdd:COG2759 189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 613 AGPFANIAHGNSSVLADKIALKLvGEegFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPsvta 692
Cdd:COG2759 269 GGPFANIAHGCNSVIATKLALKL-AD--YVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 693 gvplKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAfDAVPCYHWSVGGKGS 772
Cdd:COG2759 342 ----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEGA 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 773 VDLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQ 851
Cdd:COG2759 417 EELAEAVVEACeEGPSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSDD 496
|
570 580 590
....*....|....*....|....*....|..
gi 767942604 852 PDKKGVPRDFILPISDVRASIGAGFIYPLVGT 883
Cdd:COG2759 497 PKLLGAPTGFTLTVREVRLSAGAGFIVALTGD 528
|
|
| PRK13505 |
PRK13505 |
formate--tetrahydrofolate ligase; Provisional |
292-882 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237403 Cd Length: 557 Bit Score: 715.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 292 PVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLV 371
Cdd:PRK13505 1 TMKSDIEIAQEATLKPITEIAAKLGIPEDDLEPYGKYKAKISLDKIKALKDKKDGKLILVTAINPTPAGEGKSTVTVGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 372 QALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdka 451
Cdd:PRK13505 81 DAL-NKIGKKTVIALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITSANNLLAALIDNHIHQGNE----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 452 lynrlvplvngvrefseiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKG 531
Cdd:PRK13505 155 ----------------------------------------------LGIDPRRITWKRVLDMNDRALRNIVVGLGGPANG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 532 HYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFV 611
Cdd:PRK13505 189 VPREDGFDITVASEIMAILCLATDLKDLKERLGRIVVGYTYDGKPVTVKDLKVEGAMALLLKDAIKPNLVQTLEGTPAFV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 612 HAGPFANIAHGNSSVLADKIALKLvGEegFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPsvt 691
Cdd:PRK13505 269 HGGPFANIAHGCNSVLATKTALKL-AD--YVVTEAGFGADLGAEKFLDIKCRKAGLKPDAVVIVATVRALKMHGGVA--- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 692 agvplKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAfDAVPCYHWSVGGKG 771
Cdd:PRK13505 343 -----KDDLKEENVEALKKGFANLERHIENIRKFGVPVVVAINKFVTDTDAEIAALKELCEELGV-EVALSEVWAKGGEG 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 772 SVDLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSH 850
Cdd:PRK13505 417 GVELAEKVVELIeEGESNFKPLYDDEDSLEEKIEKIATKIYGAKGVEFSPKAKKQLKQIEKNGWDKLPVCMAKTQYSFSD 496
|
570 580 590
....*....|....*....|....*....|..
gi 767942604 851 QPDKKGVPRDFILPISDVRASIGAGFIYPLVG 882
Cdd:PRK13505 497 DPKLLGAPTGFTITVRELRPSAGAGFIVALTG 528
|
|
| PRK13506 |
PRK13506 |
formate--tetrahydrofolate ligase; Provisional |
295-882 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237404 Cd Length: 578 Bit Score: 686.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 295 SDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQAL 374
Cdd:PRK13506 3 SDIEISRQAPLKPIAEIAAKLGLLPDELSPFGHTKAKVSLSVLKRLADKPKGKLVLVTAITPTPLGEGKTVTTIGLTQGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 375 tAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENtqtdkalyn 454
Cdd:PRK13506 83 -NALGQKVCACIRQPSMGPVFGVKGGAAGGGYAQVVPMEELNLHLTGDIHAVSAAHNLAAAAIDARLFHEQ--------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 455 RLvplvnGVREFseiqlarlkklginktdpstlteEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYR 534
Cdd:PRK13506 153 RL-----GYDAF-----------------------EAQSGLPALDIDPEQILWKRVVDHNDRALRMITVGLGENGNGPER 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 535 QAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAG 614
Cdd:PRK13506 205 EDGFDITAASELMAILALSRDLKDMRQRIGRLVLAYNLQGQPITAEDLGVAGAMTVIMKDAIEPTLMQTLEGVPCLIHAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 615 PFANIAHGNSSVLADKIALKLVGeegFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGV 694
Cdd:PRK13506 285 PFANIAHGNSSIIADRIALKLAD---YVVTEGGFGSDMGFEKFCNIKARQSGKAPDCAVLVATLRALKANSGLYDLRPGQ 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 695 PLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYHWSVGGKGSVD 774
Cdd:PRK13506 362 ALPDSINAPDQARLEAGFANLKWHINNVAQYGLPVVVAINRFPTDTDEELEWLKEAVLLTGAFGCEISEAFAQGGEGATA 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 775 LARAVREAASKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQPDK 854
Cdd:PRK13506 442 LAQAVVRACEQPSQFKLLYPDEMSLEAKLMTLAEVGYGAAGVSLSDKAKQQLAQLTALGYDHLPVCMAKTPLSISHDPAL 521
|
570 580
....*....|....*....|....*...
gi 767942604 855 KGVPRDFILPISDVRASIGAGFIYPLVG 882
Cdd:PRK13506 522 KGAPTDFEVPIRELRLCAGAGFITALVG 549
|
|
| PRK13507 |
PRK13507 |
formate--tetrahydrofolate ligase; Provisional |
306-887 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 184098 Cd Length: 587 Bit Score: 628.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 306 KAVDVLAKEIGLLADEIEIYGKSKAKVR-LSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALtAHLNVNSFA 384
Cdd:PRK13507 22 KPVEELAEELGLTKEELLPYGHYIAKVDfRKVLDRLKDRPDGKYIDVTAITPTPLGEGKSTTTMGLVQGL-GKRGKKVSG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 385 CLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTQTDKalynrlvplvngvr 464
Cdd:PRK13507 101 AIRQPSGGPTMNIKGSAAGGGLSQCIPLTPFSLGLTGDINAIMNAHNLAMVALTARMQHERNYTDE-------------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 465 efseiQLARlkklginktdpstlteeevSKFARLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYRQAQFDIAVAS 544
Cdd:PRK13507 167 -----QLAR-------------------RGLKRLDIDPTRVEMGWIIDFCAQALRNIIIGIGGKTDGYMMQSGFGIAVSS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 545 EIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNS 624
Cdd:PRK13507 223 EVMAILSVATDLKDLRERIGKIVVAYDKNGKPVTTADLEVDGAMTAWMVRAINPNLLQTIEGQPVFVHAGPFANIAIGQS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 625 SVLADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGVPLKKEYTEEN 704
Cdd:PRK13507 303 SIIADRVGLKL---ADYHVTESGFGADIGFEKFWNLKCRLSGLKPDCAVIVATIRALKMHGGGPKVVPGKPLPEEYTKEN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 705 IQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPcYHWSVGGKGSVDLARAVREAAS 784
Cdd:PRK13507 380 VGLVEKGCANLLHHIGTVKKSGINPVVCINAFYTDTHAEIAIVRRLAEQAGARVAVS-RHWEKGGEGALELADAVIDACN 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 785 KRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQG-FGNLPICMAKTHLSLSHQPDKKGVPRDFIL 863
Cdd:PRK13507 459 EPNDFKFLYPLEMPLRERIETIAREVYGADGVSYTPEAEAKLKRLESDPeTADFGTCMVKTHLSLSHDPALKGVPKGWTL 538
|
570 580
....*....|....*....|....
gi 767942604 864 PISDVRASIGAGFIYPLVGTANLL 887
Cdd:PRK13507 539 PIRDILTYGGAGFVVPVAGDISLM 562
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
127-269 |
2.81e-67 |
|
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: 220.84 E-value: 2.81e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 127 GDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSP 206
Cdd:cd05212 1 GPCTPLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767942604 207 KPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSPRIHFGGLIeedDVILLAAALRIQNMVSSGR 269
Cdd:cd05212 81 KPEKVPTEWIKPGATVINCSPTKLSGDDVKESASLYVPMTG---GVGKLTVAMRMQNMVRSVR 140
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
117-272 |
1.60e-35 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 132.20 E-value: 1.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 117 TDINLGKLVRGdaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLH 196
Cdd:pfam02882 1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 197 EADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSprIHF--------------GGlieeddVILLAAALRIQ 262
Cdd:pfam02882 79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGD--VDFenvkekasaitpvpGG------VGPMTVAMLLQ 150
|
170
....*....|
gi 767942604 263 NMVSSGRRWL 272
Cdd:pfam02882 151 NTVEAAKRQL 160
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
31-223 |
3.14e-33 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 129.75 E-value: 3.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 31 KPVLAIIQAGDD--------NLmqeinQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ------ISE 96
Cdd:COG0190 32 TPGLAVVLVGDDpasqvyvrNK-----HKACEEVGIESELIRLPADTTQEELLALIDELNADPSVHGILVQlplpkhIDE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 97 NlfsnKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAhgSLE-----AALq 171
Cdd:COG0190 107 E----AVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLERYGIDLAGKHAVVVGR--SNIvgkplALL- 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767942604 172 cLFQRKGSMTM--SiqwKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVL 223
Cdd:COG0190 178 -LLRRNATVTVchS---RTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVI 227
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
32-224 |
2.41e-25 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 108.51 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 32 PVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNA 106
Cdd:PLN02897 87 PGLAVVLVGQQRDSQTYVRNkikACEETGIKSLLAELPEDCTEGQILSALRKFNEDTSIHGILVQLPlpQHLDESKILNM 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 107 LKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQW 186
Cdd:PLN02897 167 VRLEKDVDGFHPLNVGNLAMRGREPLFVSCTPKGCVELLIRSGVEIAGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHA 246
|
170 180 190
....*....|....*....|....*....|....*...
gi 767942604 187 KTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 224
Cdd:PLN02897 247 FTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVID 284
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-224 |
3.73e-25 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 106.25 E-value: 3.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 6 ARPRREviQNSKEVLSLlqeKNPAFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKIN 82
Cdd:PRK14190 12 AKEKRE--QLKEEVVKL---KEQGIVPGLAVILVGDDPASHsyvRGKKKAAEKVGIYSELYEFPADITEEELLALIDRLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 83 EDTRVHGLALQ------ISENlfsnKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKK 156
Cdd:PRK14190 87 ADPRINGILVQlplpkhIDEK----AVIERISPEKDVDGFHPINVGRMMLGQ--DTFLPCTPHGILELLKEYNIDISGKH 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767942604 157 ILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 224
Cdd:PRK14190 161 VVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVID 228
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
9-224 |
6.82e-25 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 106.13 E-value: 6.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 9 RREViqnSKEVLSLLQEKNPAfkPVLAIIQAG---DDNLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDT 85
Cdd:PLN02516 22 RSEI---AEEVAQLSEKHGKV--PGLAVVIVGsrkDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISKVHELNANP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 86 RVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAH 163
Cdd:PLN02516 97 DVHGILVQLPlpKHINEEKILNEISLEKDVDGFHPLNIGKLAMKGREPLFLPCTPKGCLELLSRSGIPIKGKKAVVVGRS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767942604 164 GSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 224
Cdd:PLN02516 177 NIVGLPVSLLLLKADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVID 237
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
32-224 |
8.27e-25 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 107.40 E-value: 8.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 32 PVLAIIQAGD--DNLMQEINQNLA-EEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNA 106
Cdd:PLN02616 104 PGLAVILVGDrkDSATYVRNKKKAcDSVGINSFEVRLPEDSTEQEVLKFISGFNNDPSVHGILVQLPlpSHMDEQNILNA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 107 LKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHG--SLEAALqcLFQRKGSMTMSI 184
Cdd:PLN02616 184 VSIEKDVDGFHPLNIGRLAMRGREPLFVPCTPKGCIELLHRYNVEIKGKRAVVIGRSNivGMPAAL--LLQREDATVSIV 261
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767942604 185 QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 224
Cdd:PLN02616 262 HSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVID 301
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
32-224 |
1.02e-23 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 102.60 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 32 PVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNA 106
Cdd:PRK14187 33 PCLIVILVGDDPASQlyvRNKQRKAEMLGLRSETILLPSTISESSLIEKINELNNDDSVHGILVQlpVPNHIDKNLIINT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 107 LKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQW 186
Cdd:PRK14187 113 IDPEKDVDGFHNENVGRLFTGQKKNCLIPCTPKGCLYLIKTITRNLSGSDAVVIGRSNIVGKPMACLLLGENCTVTTVHS 192
|
170 180 190
....*....|....*....|....*....|....*...
gi 767942604 187 KTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 224
Cdd:PRK14187 193 ATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVID 230
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
31-234 |
2.13e-23 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 101.01 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 31 KPVLAIIQAGDD--NLMQEINQN-LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLN 105
Cdd:PRK14172 32 IPKIASILVGNDggSIYYMNNQEkVANSLGIDFKKIKLDESISEEDLINEIEELNKDNNVHGIMLQlpLPKHLDEKKITN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 106 ALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQ 185
Cdd:PRK14172 112 KIDANKDIDCLTFISVGKFYKGE--KCFLPCTPNSVITLIKSLNIDIEGKEVVVIGRSNIVGKPVAQLLLNENATVTICH 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767942604 186 WKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKV 234
Cdd:PRK14172 190 SKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSVNGKI 238
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
31-224 |
1.48e-21 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 96.00 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 31 KPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLN 105
Cdd:PRK14167 31 TPGLATVLMSDDPASEtyvSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTIDELNADEDVHGILVQmpVPDHVDDREVLR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 106 ALKPEKDVDGVTDINLGKLVRGDAHecFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRK---GSMTM 182
Cdd:PRK14167 111 RIDPAKDVDGFHPENVGRLVAGDAR--FKPCTPHGIQKLLAAAGVDTEGADVVVVGRSDIVGKPMANLLIQKadgGNATV 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767942604 183 SI-QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 224
Cdd:PRK14167 189 TVcHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVID 231
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
14-208 |
2.16e-21 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 95.37 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 14 QNSKEVLSLLQEKnpAFKPVLAIIQAGDDNLMQEI---NQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGL 90
Cdd:PRK14175 17 QGLQDQVEALKEK--GFTPKLSVILVGNDGASQSYvrsKKKAAEKIGMISEIVHLEETATEEEVLNELNRLNNDDSVSGI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 91 ALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVG-AHGSLE 167
Cdd:PRK14175 95 LVQVPlpKQVSEQKILEAINPEKDVDGFHPINIGKLYIDE--QTFVPCTPLGIMEILKHADIDLEGKNAVVIGrSHIVGQ 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767942604 168 AALQCLFQRKGSMTMsIQWKTRQLQSKLHEADIVVLGSPKP 208
Cdd:PRK14175 173 PVSKLLLQKNASVTI-LHSRSKDMASYLKDADVIVSAVGKP 212
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
16-253 |
1.01e-20 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 93.60 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 16 SKEVLSLLQEKNpafKPVLAIIQAGDDNLMQEI---NQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLAL 92
Cdd:PRK14170 19 TREVAELVKEGK---KPGLAVVLVGDNQASRTYvrnKQKRTEEAGMKSVLIELPENVTEEKLLSVVEELNEDKTIHGILV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 93 Q--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSL-EAA 169
Cdd:PRK14170 96 QlpLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGK--DSFVPCTPAGIIELIKSTGTQIEGKRAVVIGRSNIVgKPV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 170 LQCLFQRKGSMTMSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSprIHFGGLIEE 249
Cdd:PRK14170 174 AQLLLNENATVTIA-HSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDRDENNKLCGD--VDFDDVVEE 250
|
....
gi 767942604 250 DDVI 253
Cdd:PRK14170 251 AGFI 254
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
32-248 |
1.04e-20 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 93.37 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 32 PVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNA 106
Cdd:PRK14192 34 PILATILVGDDPASAtyvRMKGNACRRVGMDSLKVELPQETTTEQLLAKIEELNANPDVHGILLQhpVPAQIDERACFDA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 107 LKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAAL-QCLFQRKGSMTMSiQ 185
Cdd:PRK14192 114 ISLAKDVDGVTCLGFGRMAMGE--AAYGSATPAGIMRLLKAYNIELAGKHAVVVGRSAILGKPMaMMLLNANATVTIC-H 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767942604 186 WKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCS-HDFLSGKVGcgspRIHFGGLIE 248
Cdd:PRK14192 191 SRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGfHPRDGGGVG----DIELQGIEE 250
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
31-223 |
1.66e-20 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 92.67 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 31 KPVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLN 105
Cdd:PRK10792 33 APGLAVVLVGSDPASQVYVASkrkACEEVGFVSRSYDLPETTSEAELLALIDELNADPTIDGILVQlpLPAHIDNVKVLE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 106 ALKPEKDVDGVTDINLGKLvrgdaheCFVSPV-----AKAVIELLEKSGVNLDGKKILVVGAHG------SLEAALqclf 174
Cdd:PRK10792 113 RIHPDKDVDGFHPYNVGRL-------AQRIPLlrpctPRGIMTLLERYGIDTYGLNAVVVGASNivgrpmSLELLL---- 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767942604 175 qrKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVL 223
Cdd:PRK10792 182 --AGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVI 228
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
65-224 |
2.26e-20 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 92.82 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 65 LPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPVakAVI 142
Cdd:PRK14186 69 LPADTSQAEVEALIAQLNQDERVDGILLQlpLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPA--GVM 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 143 ELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTV 222
Cdd:PRK14186 147 RLLRSQQIDIAGKKAVVVGRSILVGKPLALMLLAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVV 226
|
..
gi 767942604 223 LN 224
Cdd:PRK14186 227 VD 228
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
29-234 |
2.45e-19 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 89.32 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 29 AFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKV 103
Cdd:PRK14180 29 AITPKLVAIIVGNDPASKtyvASKEKACAQVGIDSQVITLPEHTTESELLELIDQLNNDSSVHAILVQLPlpAHINKNNV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 104 LNALKPEKDVDGVTDINLGKLVRGDaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSL-EAALQCLFQRKGSMTM 182
Cdd:PRK14180 109 IYSIKPEKDVDGFHPTNVGRLQLRD-KKCLESCTPKGIMTMLREYGIKTEGAYAVVVGASNVVgKPVSQLLLNAKATVTT 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767942604 183 SIQWkTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKV 234
Cdd:PRK14180 188 CHRF-TTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHVDGKI 238
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
31-224 |
4.03e-19 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 88.59 E-value: 4.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 31 KPVLAIIQAGDDNLMQEINQNLA---EEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLN 105
Cdd:PRK14189 32 QPGLAVILVGDNPASQVYVRNKVkacEDNGFHSLKDRYPADLSEAELLARIDELNRDPKIHGILVQlpLPKHIDSHKVIE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 106 ALKPEKDVDGVTDINLGKLVRGdaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQ 185
Cdd:PRK14189 112 AIAPEKDVDGFHVANAGALMTG--QPLFRPCTPYGVMKMLESIGIPLRGAHAVVIGRSNIVGKPMAMLLLQAGATVTICH 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 767942604 186 WKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 224
Cdd:PRK14189 190 SKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVID 228
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
32-224 |
4.20e-19 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 88.72 E-value: 4.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 32 PVLAIIQAGDDNLMQEINQNLAE---EAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNA 106
Cdd:PRK14174 32 PGLTVIIVGEDPASQVYVRNKAKsckEIGMNSTVIELPADTTEEHLLKKIEDLNNDPDVHGILVQqpLPKQIDEFAVTLA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 107 LKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAH---GSLEAALQCLFQRKGSMTMS 183
Cdd:PRK14174 112 IDPAKDVDGFHPENLGRLVMGHLDKCFVSCTPYGILELLGRYNIETKGKHCVVVGRSnivGKPMANLMLQKLKESNCTVT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767942604 184 I-QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 224
Cdd:PRK14174 192 IcHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVID 233
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-224 |
2.11e-18 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 86.82 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 5 RARPRREVIQNSKEVLSLLQEknpAFKPVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEIIDEILKI 81
Cdd:PRK14194 10 KAAAARVLAQVREDVRTLKAA---GIEPALAVILVGNDPASQVYVRNkilRAEEAGIRSLEHRLPADTSQARLLALIAEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 82 NEDTRVHGLALQ--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAhecFVSPVAKA-VIELLEKSGVNLDGKKIL 158
Cdd:PRK14194 87 NADPSVNGILLQlpLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRD---VLTPCTPSgCLRLLEDTCGDLTGKHAV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767942604 159 VVGAH---GSLEAALqcLFQRKGSMTMsIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 224
Cdd:PRK14194 164 VIGRSnivGKPMAAL--LLQAHCSVTV-VHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVID 229
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
32-224 |
3.24e-18 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 85.97 E-value: 3.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 32 PVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNA 106
Cdd:PRK14191 32 PKLAVILVGKDPASQtyvNMKIKACERVGMDSDLHTLQENTTEAELLSLIKDLNTDQNIDGILVQLPlpRHIDTKMVLEA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 107 LKPEKDVDGVTDINLGKLVRGdaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQW 186
Cdd:PRK14191 112 IDPNKDVDGFHPLNIGKLCSQ--LDGFVPATPMGVMRLLKHYHIEIKGKDVVIIGASNIVGKPLAMLMLNAGASVSVCHI 189
|
170 180 190
....*....|....*....|....*....|....*...
gi 767942604 187 KTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 224
Cdd:PRK14191 190 LTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVD 227
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
53-224 |
4.17e-18 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 86.08 E-value: 4.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 53 AEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAH 130
Cdd:PRK14168 58 AHRLGFHEIQDNQSVDITEEELLALIDKYNNDDSIHGILVQlpLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIGGDE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 131 ECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKG----SMTMSIQWKTRQLQSKLHEADIVVLGSP 206
Cdd:PRK14168 138 VKFLPCTPAGIQEMLVRSGVETSGAEVVVVGRSNIVGKPIANMMTQKGpganATVTIVHTRSKNLARHCQRADILIVAAG 217
|
170
....*....|....*...
gi 767942604 207 KPEEIPLTWIQPGTTVLN 224
Cdd:PRK14168 218 VPNLVKPEWIKPGATVID 235
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
11-235 |
5.13e-18 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 85.41 E-value: 5.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 11 EVIQNskEVLSLLQEKNPAFK--PVLAIIQAGDdNLMQEINQNL----AEEAGLNITHICLPPDSSEAEIIDEILKINED 84
Cdd:PRK14177 13 EKIRN--EIRETIEERKTKNKriPKLATILVGN-NPASETYVSMkvkaCHKVGMGSEMIRLKEQTTTEELLGVIDKLNLD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 85 TRVHGLALQ--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGA 162
Cdd:PRK14177 90 PNVDGILLQhpVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGV--ETYLPCTPYGMVLLLKEYGIDVTGKNAVVVGR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767942604 163 HGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDflSGKVG 235
Cdd:PRK14177 168 SPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYN--PGNVG 238
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
9-224 |
9.57e-18 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 84.68 E-value: 9.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 9 RREVIQNSKEVLSLLQEKnpAFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDT 85
Cdd:PRK14193 12 ADEIKADLAERVAALKEK--GITPGLGTVLVGDDPGSQayvRGKHRDCAEVGITSIRRDLPADATQEELNAVIDELNADP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 86 RVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPvaKAVIELLEKSGVNLDGKKILVVGAH 163
Cdd:PRK14193 90 ACTGYIVQLPlpKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTP--RGIVHLLRRYDVELAGAHVVVIGRG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767942604 164 GSLEAALQCLFQRKG-SMTMSI-QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 224
Cdd:PRK14193 168 VTVGRPIGLLLTRRSeNATVTLcHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLD 230
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
25-224 |
1.26e-17 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 84.47 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 25 EKNPAFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLF 99
Cdd:PRK14176 32 KSNRGITPGLATILVGDDPASKmyvRLKHKACERVGIRAEDQFLPADTTQEELLELIDSLNKRKDVHGILLQLPlpKHLD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 100 SNKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGS 179
Cdd:PRK14176 112 PQEAMEAIDPAKDADGFHPYNMGKLMIGD--EGLVPCTPHGVIRALEEYGVDIEGKNAVIVGHSNVVGKPMAAMLLNRNA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767942604 180 MTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 224
Cdd:PRK14176 190 TVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFD 234
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
31-223 |
1.28e-17 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 84.62 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 31 KPVLAIIQAGDDNLMQEINQN---LAEEAGLN-ITHIcLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVL 104
Cdd:PRK14188 32 TPGLAVVLVGEDPASQVYVRSkgkQTKEAGMAsFEHK-LPADTSQAELLALIARLNADPAIHGILVQlpLPKHLDSEAVI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 105 NALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAH---GSLEAALqcLFQRKGSMT 181
Cdd:PRK14188 111 QAIDPEKDVDGLHVVNAGRLATGE--TALVPCTPLGCMMLLRRVHGDLSGLNAVVIGRSnlvGKPMAQL--LLAANATVT 186
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767942604 182 MSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVL 223
Cdd:PRK14188 187 IA-HSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVI 227
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
24-114 |
1.62e-17 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 78.99 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 24 QEKNPAFKPVLAIIQAGDD---NLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENL 98
Cdd:pfam00763 20 ALKAGGRKPGLAVILVGDDpasQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKLNADPSVHGILVQlpLPKHI 99
|
90
....*....|....*.
gi 767942604 99 FSNKVLNALKPEKDVD 114
Cdd:pfam00763 100 DEEKVLEAIDPEKDVD 115
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
16-237 |
3.27e-17 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 82.97 E-value: 3.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 16 SKEVLSLLQEK--NPAFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGL 90
Cdd:PRK14178 9 SEKRLELLKEEiiESGLYPRLATVIVGDDPASQmyvRMKHRACERVGIGSVGIELPGDATTRTVLERIRRLNEDPDINGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 91 ALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPvaKAVIELLEKSGVNLDGKKILVVGAH---GS 165
Cdd:PRK14178 89 LVQLPlpKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTP--NGIMTLLHEYKISIAGKRAVVVGRSidvGR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767942604 166 LEAALqcLFQRKGSMTMSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKVgCG 237
Cdd:PRK14178 167 PMAAL--LLNADATVTIC-HSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQVNGKL-CG 234
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
109-225 |
7.55e-17 |
|
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: 78.75 E-value: 7.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 109 PEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKT 188
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGR--PGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKT 78
|
90 100 110
....*....|....*....|....*....|....*..
gi 767942604 189 RQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNC 225
Cdd:cd01080 79 KNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDV 115
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
17-224 |
7.63e-17 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 82.11 E-value: 7.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 17 KEVLSLLQEKnpAFKPVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ 93
Cdd:PRK14179 20 EKVAKLKEEK--GIVPGLVVILVGDNPASQVYVRNkerSALAAGFKSEVVRLPETISQEELLDLIERYNQDPTWHGILVQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 94 --ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGdaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAAL- 170
Cdd:PRK14179 98 lpLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSG--RPVMIPCTPAGIMEMFREYNVELEGKHAVVIGRSNIVGKPMa 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767942604 171 QCLFQRKGSMTMSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 224
Cdd:PRK14179 176 QLLLDKNATVTLT-HSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVID 228
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
17-224 |
3.93e-16 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 79.82 E-value: 3.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 17 KEVLSLLQEKNPAfkPVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ 93
Cdd:PRK14184 19 TEVAALTARHGRA--PGLAVILVGEDPASQVYVRNkerACEDAGIVSEAFRLPADTTQEELEDLIAELNARPDIDGILLQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 94 IS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGdaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQ 171
Cdd:PRK14184 97 LPlpKGLDSQRCLELIDPAKDVDGFHPENMGRLALG--LPGFRPCTPAGVMTLLERYGLSPAGKKAVVVGRSNIVGKPLA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767942604 172 CLFQRKGSM---TMSI-QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 224
Cdd:PRK14184 175 LMLGAPGKFanaTVTVcHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVD 231
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
31-224 |
4.79e-15 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 76.60 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 31 KPVLAIIQAGDD---NLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLN 105
Cdd:PRK14182 30 QTGLTVVRVGDDpasAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIARLNADPAVHGILVQLPlpKHVDERAVLD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 106 ALKPEKDVDGVTDINLGKL---VRGDAHECfvSPVAkaVIELLEKSGVNLDGKKILVVGAH---GSLEAALqcLFQRKGS 179
Cdd:PRK14182 110 AISPAKDADGFHPFNVGALsigIAGVPRPC--TPAG--VMRMLDEARVDPKGKRALVVGRSnivGKPMAMM--LLERHAT 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767942604 180 MTMSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 224
Cdd:PRK14182 184 VTIA-HSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVID 227
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
11-232 |
5.76e-14 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 73.45 E-value: 5.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 11 EVIQNSKEVLSLLQEKNPAfKPVLAIIQAGDDN-----LMQEINQnlAEEAGLNITHICLPPDSSEAEIIDEILKINEDT 85
Cdd:PRK14171 13 EILADLKLEIQELKSQTNA-SPKLAIVLVGDNPasiiyVKNKIKN--AHKIGIDTLLVNLSTTIHTNDLISKINELNLDN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 86 RVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGdAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAH 163
Cdd:PRK14171 90 EISGIIVQLPlpSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSG-ISQGFIPCTALGCLAVIKKYEPNLTGKNVVIIGRS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767942604 164 GSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSG 232
Cdd:PRK14171 169 NIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRISG 237
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
31-224 |
1.21e-13 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 72.55 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 31 KPVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLN 105
Cdd:PRK14185 31 RPHLAAILVGHDGGSETYVANkvkACEECGFKSSLIRYESDVTEEELLAKVRELNQDDDVDGFIVQLPlpKHISEQKVIE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 106 ALKPEKDVDGVTDINLGKLVRGdaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRK---GSMTM 182
Cdd:PRK14185 111 AIDYRKDVDGFHPINVGRMSIG--LPCFVSATPNGILELLKRYHIETSGKKCVVLGRSNIVGKPMAQLMMQKaypGDCTV 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767942604 183 SI-QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 224
Cdd:PRK14185 189 TVcHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVID 231
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
16-234 |
1.29e-13 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 72.37 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 16 SKEVLSLLQEKNPAFK-----PVLAIIQAGDDNLMQEINQNLA---EEAGLNITHICLPPDSSEAEIIDEILKINEDTRV 87
Cdd:PRK14166 10 SAKIKEELKEKNQFLKskgieSCLAVILVGDNPASQTYVKSKAkacEECGIKSLVYHLNENTTQNELLALINTLNHDDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 88 HGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGdAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGS 165
Cdd:PRK14166 90 HGILVQLPlpDHICKDLILESIISSKDVDGFHPINVGYLNLG-LESGFLPCTPLGVMKLLKAYEIDLEGKDAVIIGASNI 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 166 LEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFL-SGKV 234
Cdd:PRK14166 169 VGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLeSGKI 238
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
32-224 |
3.49e-13 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 71.05 E-value: 3.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 32 PVLAIIQAGDDNlMQEINQNLAEEAGLNITHIC----LPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLN 105
Cdd:PRK14181 27 PGLAVVLIGNDP-ASEVYVGMKVKKATDLGMVSkahrLPSDATLSDILKLIHRLNNDPNIHGILVQLPlpKHLDAQAILQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942604 106 ALKPEKDVDGVTDINLGKLVRGDAhECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMS-- 183
Cdd:PRK14181 106 AISPDKDVDGLHPVNMGKLLLGET-DGFIPCTPAGIIELLKYYEIPLHGRHVAIVGRSNIVGKPLAALLMQKHPDTNAtv 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767942604 184 --IQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 224
Cdd:PRK14181 185 tlLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVD 227
|
|
| |
