|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
287-884 |
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 767942602 287 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKST 366
Cdd:PLN02759 9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 367 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 446
Cdd:PLN02759 89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 447 TQTDKALYNRLVPL-VNGVREFSEIQLARLKKLGINKTDPSTLTEEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIG 525
Cdd:PLN02759 169 TQSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 526 QGNTEKGHYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTL 605
Cdd:PLN02759 249 QGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 606 EGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMH 685
Cdd:PLN02759 329 EGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMH 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 686 GGGPSVTAGVPLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYH 765
Cdd:PLN02759 409 GGGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTH 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 766 WSVGGKGSVDLARAVREAASKRSR-FQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAK 844
Cdd:PLN02759 489 HAHGGKGAVDLGEAVQKACEGNSQpFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAK 568
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 767942602 845 THLSLSHQPDKKGVPRDFILPISDVRASIGAGFIYPLVGT 884
Cdd:PLN02759 569 TQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGT 608
|
|
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
295-884 |
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 767942602 295 PSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQA 374
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 375 LtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkaly 454
Cdd:pfam01268 81 L-NRLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 455 nrlvplvngvrefseiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHY 534
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 535 RQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHA 614
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 615 GPFANIAHGNSSVLADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGgpsvtag 694
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGG------- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 695 vPLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKrAGAFDAVPCYHWSVGGKGSV 774
Cdd:pfam01268 339 -VGKDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRELCE-AGGVDAALSEHWAKGGEGAI 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 775 DLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQP 853
Cdd:pfam01268 417 ELAEAVVEACeEEPSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
|
570 580 590
....*....|....*....|....*....|.
gi 767942602 854 DKKGVPRDFILPISDVRASIGAGFIYPLVGT 884
Cdd:pfam01268 497 KLKGAPTGFTLPVRDVRLSAGAGFIVALTGD 527
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
309-884 |
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 767942602 309 VDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALTAHLNvNSFACLR 388
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 389 QPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkalynrlvplvngvrefs 468
Cdd:cd00477 80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 469 eiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYRQAQFDIAVASEIM 548
Cdd:cd00477 139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 549 AVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSVL 628
Cdd:cd00477 189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 629 ADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGvplkkeytEENIQL 708
Cdd:cd00477 269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 709 VADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVpCYHWSVGGKGSVDLARAVREAASK-R 787
Cdd:cd00477 338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKpK 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 788 SRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQPDKKGVPRDFILPIS 867
Cdd:cd00477 417 SNFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
|
570
....*....|....*..
gi 767942602 868 DVRASIGAGFIYPLVGT 884
Cdd:cd00477 497 DVRLSAGAGFVVPLAGD 513
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
294-884 |
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 767942602 294 VPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQ 373
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 374 ALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENtqtdkal 453
Cdd:COG2759 81 AL-NRLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQGN------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 454 ynrlvplvngvrefseiqlarlkklginktdpstlteeevskfaRLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGH 533
Cdd:COG2759 153 --------------------------------------------ELNIDPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 534 YRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVH 613
Cdd:COG2759 189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 614 AGPFANIAHGNSSVLADKIALKLvGEegFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPsvta 693
Cdd:COG2759 269 GGPFANIAHGCNSVIATKLALKL-AD--YVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 694 gvplKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAfDAVPCYHWSVGGKGS 773
Cdd:COG2759 342 ----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEGA 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 774 VDLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQ 852
Cdd:COG2759 417 EELAEAVVEACeEGPSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSDD 496
|
570 580 590
....*....|....*....|....*....|..
gi 767942602 853 PDKKGVPRDFILPISDVRASIGAGFIYPLVGT 884
Cdd:COG2759 497 PKLLGAPTGFTLTVREVRLSAGAGFIVALTGD 528
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
127-270 |
1.60e-65 |
|
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: 215.83 E-value: 1.60e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 127 GDAHECFVSPVAKAVIELLEKSvGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGS 206
Cdd:cd05212 1 GPCTPLFVSPVAKAVKELLNKE-GVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGS 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767942602 207 PKPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSPRIHFGGLIeedDVILLAAALRIQNMVSSGR 270
Cdd:cd05212 80 PKPEKVPTEWIKPGATVINCSPTKLSGDDVKESASLYVPMTG---GVGKLTVAMRMQNMVRSVR 140
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
117-273 |
7.28e-34 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 127.58 E-value: 7.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 117 TDINLGKLVRGdaHECFVSPVAKAVIELLEKSvGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKL 196
Cdd:pfam02882 1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRY-GIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEIT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 197 HEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSprIHF--------------GGlieeddVILLAAALRI 262
Cdd:pfam02882 78 READIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGD--VDFenvkekasaitpvpGG------VGPMTVAMLL 149
|
170
....*....|.
gi 767942602 263 QNMVSSGRRWL 273
Cdd:pfam02882 150 QNTVEAAKRQL 160
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
31-224 |
7.33e-32 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 125.90 E-value: 7.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 31 KPVLAIIQAGDD--------NLmqeinQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ------ISE 96
Cdd:COG0190 32 TPGLAVVLVGDDpasqvyvrNK-----HKACEEVGIESELIRLPADTTQEELLALIDELNADPSVHGILVQlplpkhIDE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 97 NlfsnKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEkSVGVNLDGKKILVVGAhgSLE-----AAL 171
Cdd:COG0190 107 E----AVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLE-RYGIDLAGKHAVVVGR--SNIvgkplALL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767942602 172 qcLFQRKGSMTM--SiqwKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVL 224
Cdd:COG0190 178 --LLRRNATVTVchS---RTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVI 227
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
32-225 |
3.55e-24 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 103.75 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 32 PVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNA 106
Cdd:PRK14187 33 PCLIVILVGDDPASQlyvRNKQRKAEMLGLRSETILLPSTISESSLIEKINELNNDDSVHGILVQlpVPNHIDKNLIINT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 107 LKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLeKSVGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQ 186
Cdd:PRK14187 113 IDPEKDVDGFHNENVGRLFTGQKKNCLIPCTPKGCLYLI-KTITRNLSGSDAVVIGRSNIVGKPMACLLLGENCTVTTVH 191
|
170 180 190
....*....|....*....|....*....|....*....
gi 767942602 187 WKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 225
Cdd:PRK14187 192 SATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVID 230
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-225 |
6.30e-24 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 102.78 E-value: 6.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 6 ARPRREviQNSKEVLSLlqeKNPAFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKIN 82
Cdd:PRK14190 12 AKEKRE--QLKEEVVKL---KEQGIVPGLAVILVGDDPASHsyvRGKKKAAEKVGIYSELYEFPADITEEELLALIDRLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 83 EDTRVHGLALQ------ISENlfsnKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLeKSVGVNLDGK 156
Cdd:PRK14190 87 ADPRINGILVQlplpkhIDEK----AVIERISPEKDVDGFHPINVGRMMLGQ--DTFLPCTPHGILELL-KEYNIDISGK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767942602 157 KILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 225
Cdd:PRK14190 160 HVVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVID 228
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
24-114 |
1.66e-17 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 78.99 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 24 QEKNPAFKPVLAIIQAGDD---NLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENL 98
Cdd:pfam00763 20 ALKAGGRKPGLAVILVGDDpasQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKLNADPSVHGILVQlpLPKHI 99
|
90
....*....|....*.
gi 767942602 99 FSNKVLNALKPEKDVD 114
Cdd:pfam00763 100 DEEKVLEAIDPEKDVD 115
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
287-884 |
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 767942602 287 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKST 366
Cdd:PLN02759 9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 367 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 446
Cdd:PLN02759 89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 447 TQTDKALYNRLVPL-VNGVREFSEIQLARLKKLGINKTDPSTLTEEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIG 525
Cdd:PLN02759 169 TQSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 526 QGNTEKGHYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTL 605
Cdd:PLN02759 249 QGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 606 EGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMH 685
Cdd:PLN02759 329 EGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMH 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 686 GGGPSVTAGVPLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYH 765
Cdd:PLN02759 409 GGGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTH 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 766 WSVGGKGSVDLARAVREAASKRSR-FQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAK 844
Cdd:PLN02759 489 HAHGGKGAVDLGEAVQKACEGNSQpFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAK 568
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 767942602 845 THLSLSHQPDKKGVPRDFILPISDVRASIGAGFIYPLVGT 884
Cdd:PLN02759 569 TQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGT 608
|
|
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
295-884 |
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 767942602 295 PSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQA 374
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 375 LtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkaly 454
Cdd:pfam01268 81 L-NRLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 455 nrlvplvngvrefseiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHY 534
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 535 RQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHA 614
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 615 GPFANIAHGNSSVLADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGgpsvtag 694
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGG------- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 695 vPLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKrAGAFDAVPCYHWSVGGKGSV 774
Cdd:pfam01268 339 -VGKDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRELCE-AGGVDAALSEHWAKGGEGAI 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 775 DLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQP 853
Cdd:pfam01268 417 ELAEAVVEACeEEPSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
|
570 580 590
....*....|....*....|....*....|.
gi 767942602 854 DKKGVPRDFILPISDVRASIGAGFIYPLVGT 884
Cdd:pfam01268 497 KLKGAPTGFTLPVRDVRLSAGAGFIVALTGD 527
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
309-884 |
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 767942602 309 VDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALTAHLNvNSFACLR 388
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 389 QPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkalynrlvplvngvrefs 468
Cdd:cd00477 80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 469 eiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYRQAQFDIAVASEIM 548
Cdd:cd00477 139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 549 AVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSVL 628
Cdd:cd00477 189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 629 ADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGvplkkeytEENIQL 708
Cdd:cd00477 269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 709 VADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVpCYHWSVGGKGSVDLARAVREAASK-R 787
Cdd:cd00477 338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKpK 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 788 SRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQPDKKGVPRDFILPIS 867
Cdd:cd00477 417 SNFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
|
570
....*....|....*..
gi 767942602 868 DVRASIGAGFIYPLVGT 884
Cdd:cd00477 497 DVRLSAGAGFVVPLAGD 513
|
|
| PTZ00386 |
PTZ00386 |
formyl tetrahydrofolate synthetase; Provisional |
287-883 |
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 767942602 287 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKST 366
Cdd:PTZ00386 8 KLSCQWPVPSDIDIAQSVKPQPITSVAESAGILLSELDPYGSTRAKVKLSVLKRLENSPNGKYVVVAGMNPTPLGEGKST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 367 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 446
Cdd:PTZ00386 88 TTIGLAQSLGAHLHRKTFACIRQPSQGPTFGIKGGAAGGGYSQVIPMEDFNLHGTGDIHAITAANNLLAAALDTRIFHER 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 447 TQTDKALYNRLVplvNGVREFSEIQLARLKKLGINKTDPSTLTEEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIGQ 526
Cdd:PTZ00386 168 TQSDAALYRRLT---DELKKFTPIMLKRLEKLGISKTDPKQLTEEERVRFARLDIDPDTISWRRVTDVNDRMLREITIGQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 527 GNTEKGHYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLE 606
Cdd:PTZ00386 245 GKEEKGITRKTGFDISVASEVMAILALATDLADMRQRLGAIVVAKSKSGEPVTAEDLGCAGAMTVLMKDTIEPTLMQTLE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 607 GTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHG 686
Cdd:PTZ00386 325 GTPVLVHAGPFGNIAHGNSSIVADQIALKLAGQDGFVLTEAGFGADIGCEKFFNIKCRTSGLKPDAAVLVATVRALKFHG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 687 GGPSVTAGvplkkeytEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELA-KRAGAFDAVPCYH 765
Cdd:PTZ00386 405 GVEPVVAG--------KENLEAVRKGLSNLQRHIQNIRKFGVPVVVALNKFSTDTDAELELVKELAlQEGGAADVVVTDH 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 766 WSVGGKGSVDLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAK 844
Cdd:PTZ00386 477 WAKGGAGAVDLAQALIRVTeNVPSNFKLLYPLDASLKEKIETICKEIYGAAGVEYLNDADEKLEDFERMGYGKFPVCMAK 556
|
570 580 590
....*....|....*....|....*....|....*....
gi 767942602 845 THLSLSHQPDKKGVPRDFILPISDVRASIGAGFIYPLVG 883
Cdd:PTZ00386 557 TQYSFSHDPELRGAPTGFTVPIRDVRVNCGAGFVFPLLG 595
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
294-884 |
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 767942602 294 VPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQ 373
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 374 ALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENtqtdkal 453
Cdd:COG2759 81 AL-NRLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQGN------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 454 ynrlvplvngvrefseiqlarlkklginktdpstlteeevskfaRLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGH 533
Cdd:COG2759 153 --------------------------------------------ELNIDPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 534 YRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVH 613
Cdd:COG2759 189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 614 AGPFANIAHGNSSVLADKIALKLvGEegFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPsvta 693
Cdd:COG2759 269 GGPFANIAHGCNSVIATKLALKL-AD--YVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 694 gvplKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAfDAVPCYHWSVGGKGS 773
Cdd:COG2759 342 ----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEGA 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 774 VDLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQ 852
Cdd:COG2759 417 EELAEAVVEACeEGPSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSDD 496
|
570 580 590
....*....|....*....|....*....|..
gi 767942602 853 PDKKGVPRDFILPISDVRASIGAGFIYPLVGT 884
Cdd:COG2759 497 PKLLGAPTGFTLTVREVRLSAGAGFIVALTGD 528
|
|
| PRK13505 |
PRK13505 |
formate--tetrahydrofolate ligase; Provisional |
293-883 |
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 767942602 293 PVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLV 372
Cdd:PRK13505 1 TMKSDIEIAQEATLKPITEIAAKLGIPEDDLEPYGKYKAKISLDKIKALKDKKDGKLILVTAINPTPAGEGKSTVTVGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 373 QALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdka 452
Cdd:PRK13505 81 DAL-NKIGKKTVIALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITSANNLLAALIDNHIHQGNE----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 453 lynrlvplvngvrefseiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKG 532
Cdd:PRK13505 155 ----------------------------------------------LGIDPRRITWKRVLDMNDRALRNIVVGLGGPANG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 533 HYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFV 612
Cdd:PRK13505 189 VPREDGFDITVASEIMAILCLATDLKDLKERLGRIVVGYTYDGKPVTVKDLKVEGAMALLLKDAIKPNLVQTLEGTPAFV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 613 HAGPFANIAHGNSSVLADKIALKLvGEegFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPsvt 692
Cdd:PRK13505 269 HGGPFANIAHGCNSVLATKTALKL-AD--YVVTEAGFGADLGAEKFLDIKCRKAGLKPDAVVIVATVRALKMHGGVA--- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 693 agvplKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAfDAVPCYHWSVGGKG 772
Cdd:PRK13505 343 -----KDDLKEENVEALKKGFANLERHIENIRKFGVPVVVAINKFVTDTDAEIAALKELCEELGV-EVALSEVWAKGGEG 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 773 SVDLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSH 851
Cdd:PRK13505 417 GVELAEKVVELIeEGESNFKPLYDDEDSLEEKIEKIATKIYGAKGVEFSPKAKKQLKQIEKNGWDKLPVCMAKTQYSFSD 496
|
570 580 590
....*....|....*....|....*....|..
gi 767942602 852 QPDKKGVPRDFILPISDVRASIGAGFIYPLVG 883
Cdd:PRK13505 497 DPKLLGAPTGFTITVRELRPSAGAGFIVALTG 528
|
|
| PRK13506 |
PRK13506 |
formate--tetrahydrofolate ligase; Provisional |
296-883 |
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 767942602 296 SDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQAL 375
Cdd:PRK13506 3 SDIEISRQAPLKPIAEIAAKLGLLPDELSPFGHTKAKVSLSVLKRLADKPKGKLVLVTAITPTPLGEGKTVTTIGLTQGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 376 tAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENtqtdkalyn 455
Cdd:PRK13506 83 -NALGQKVCACIRQPSMGPVFGVKGGAAGGGYAQVVPMEELNLHLTGDIHAVSAAHNLAAAAIDARLFHEQ--------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 456 RLvplvnGVREFseiqlarlkklginktdpstlteEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYR 535
Cdd:PRK13506 153 RL-----GYDAF-----------------------EAQSGLPALDIDPEQILWKRVVDHNDRALRMITVGLGENGNGPER 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 536 QAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAG 615
Cdd:PRK13506 205 EDGFDITAASELMAILALSRDLKDMRQRIGRLVLAYNLQGQPITAEDLGVAGAMTVIMKDAIEPTLMQTLEGVPCLIHAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 616 PFANIAHGNSSVLADKIALKLVGeegFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGV 695
Cdd:PRK13506 285 PFANIAHGNSSIIADRIALKLAD---YVVTEGGFGSDMGFEKFCNIKARQSGKAPDCAVLVATLRALKANSGLYDLRPGQ 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 696 PLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYHWSVGGKGSVD 775
Cdd:PRK13506 362 ALPDSINAPDQARLEAGFANLKWHINNVAQYGLPVVVAINRFPTDTDEELEWLKEAVLLTGAFGCEISEAFAQGGEGATA 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 776 LARAVREAASKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQPDK 855
Cdd:PRK13506 442 LAQAVVRACEQPSQFKLLYPDEMSLEAKLMTLAEVGYGAAGVSLSDKAKQQLAQLTALGYDHLPVCMAKTPLSISHDPAL 521
|
570 580
....*....|....*....|....*...
gi 767942602 856 KGVPRDFILPISDVRASIGAGFIYPLVG 883
Cdd:PRK13506 522 KGAPTDFEVPIRELRLCAGAGFITALVG 549
|
|
| PRK13507 |
PRK13507 |
formate--tetrahydrofolate ligase; Provisional |
307-888 |
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 767942602 307 KAVDVLAKEIGLLADEIEIYGKSKAKVR-LSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALtAHLNVNSFA 385
Cdd:PRK13507 22 KPVEELAEELGLTKEELLPYGHYIAKVDfRKVLDRLKDRPDGKYIDVTAITPTPLGEGKSTTTMGLVQGL-GKRGKKVSG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 386 CLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTQTDKalynrlvplvngvr 465
Cdd:PRK13507 101 AIRQPSGGPTMNIKGSAAGGGLSQCIPLTPFSLGLTGDINAIMNAHNLAMVALTARMQHERNYTDE-------------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 466 efseiQLARlkklginktdpstlteeevSKFARLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYRQAQFDIAVAS 545
Cdd:PRK13507 167 -----QLAR-------------------RGLKRLDIDPTRVEMGWIIDFCAQALRNIIIGIGGKTDGYMMQSGFGIAVSS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 546 EIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNS 625
Cdd:PRK13507 223 EVMAILSVATDLKDLRERIGKIVVAYDKNGKPVTTADLEVDGAMTAWMVRAINPNLLQTIEGQPVFVHAGPFANIAIGQS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 626 SVLADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGVPLKKEYTEEN 705
Cdd:PRK13507 303 SIIADRVGLKL---ADYHVTESGFGADIGFEKFWNLKCRLSGLKPDCAVIVATIRALKMHGGGPKVVPGKPLPEEYTKEN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 706 IQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPcYHWSVGGKGSVDLARAVREAAS 785
Cdd:PRK13507 380 VGLVEKGCANLLHHIGTVKKSGINPVVCINAFYTDTHAEIAIVRRLAEQAGARVAVS-RHWEKGGEGALELADAVIDACN 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 786 KRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQG-FGNLPICMAKTHLSLSHQPDKKGVPRDFIL 864
Cdd:PRK13507 459 EPNDFKFLYPLEMPLRERIETIAREVYGADGVSYTPEAEAKLKRLESDPeTADFGTCMVKTHLSLSHDPALKGVPKGWTL 538
|
570 580
....*....|....*....|....
gi 767942602 865 PISDVRASIGAGFIYPLVGTANLL 888
Cdd:PRK13507 539 PIRDILTYGGAGFVVPVAGDISLM 562
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
127-270 |
1.60e-65 |
|
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: 215.83 E-value: 1.60e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 127 GDAHECFVSPVAKAVIELLEKSvGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGS 206
Cdd:cd05212 1 GPCTPLFVSPVAKAVKELLNKE-GVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGS 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767942602 207 PKPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSPRIHFGGLIeedDVILLAAALRIQNMVSSGR 270
Cdd:cd05212 80 PKPEKVPTEWIKPGATVINCSPTKLSGDDVKESASLYVPMTG---GVGKLTVAMRMQNMVRSVR 140
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
117-273 |
7.28e-34 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 127.58 E-value: 7.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 117 TDINLGKLVRGdaHECFVSPVAKAVIELLEKSvGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKL 196
Cdd:pfam02882 1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRY-GIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEIT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 197 HEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSprIHF--------------GGlieeddVILLAAALRI 262
Cdd:pfam02882 78 READIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGD--VDFenvkekasaitpvpGG------VGPMTVAMLL 149
|
170
....*....|.
gi 767942602 263 QNMVSSGRRWL 273
Cdd:pfam02882 150 QNTVEAAKRQL 160
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
31-224 |
7.33e-32 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 125.90 E-value: 7.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 31 KPVLAIIQAGDD--------NLmqeinQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ------ISE 96
Cdd:COG0190 32 TPGLAVVLVGDDpasqvyvrNK-----HKACEEVGIESELIRLPADTTQEELLALIDELNADPSVHGILVQlplpkhIDE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 97 NlfsnKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEkSVGVNLDGKKILVVGAhgSLE-----AAL 171
Cdd:COG0190 107 E----AVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLE-RYGIDLAGKHAVVVGR--SNIvgkplALL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767942602 172 qcLFQRKGSMTM--SiqwKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVL 224
Cdd:COG0190 178 --LLRRNATVTVchS---RTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVI 227
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
32-225 |
3.55e-24 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 103.75 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 32 PVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNA 106
Cdd:PRK14187 33 PCLIVILVGDDPASQlyvRNKQRKAEMLGLRSETILLPSTISESSLIEKINELNNDDSVHGILVQlpVPNHIDKNLIINT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 107 LKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLeKSVGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQ 186
Cdd:PRK14187 113 IDPEKDVDGFHNENVGRLFTGQKKNCLIPCTPKGCLYLI-KTITRNLSGSDAVVIGRSNIVGKPMACLLLGENCTVTTVH 191
|
170 180 190
....*....|....*....|....*....|....*....
gi 767942602 187 WKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 225
Cdd:PRK14187 192 SATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVID 230
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-225 |
6.30e-24 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 102.78 E-value: 6.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 6 ARPRREviQNSKEVLSLlqeKNPAFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKIN 82
Cdd:PRK14190 12 AKEKRE--QLKEEVVKL---KEQGIVPGLAVILVGDDPASHsyvRGKKKAAEKVGIYSELYEFPADITEEELLALIDRLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 83 EDTRVHGLALQ------ISENlfsnKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLeKSVGVNLDGK 156
Cdd:PRK14190 87 ADPRINGILVQlplpkhIDEK----AVIERISPEKDVDGFHPINVGRMMLGQ--DTFLPCTPHGILELL-KEYNIDISGK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767942602 157 KILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 225
Cdd:PRK14190 160 HVVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVID 228
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
32-225 |
8.99e-24 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 103.89 E-value: 8.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 32 PVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNA 106
Cdd:PLN02897 87 PGLAVVLVGQQRDSQTYVRNkikACEETGIKSLLAELPEDCTEGQILSALRKFNEDTSIHGILVQLPlpQHLDESKILNM 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 107 LKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSvGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQ 186
Cdd:PLN02897 167 VRLEKDVDGFHPLNVGNLAMRGREPLFVSCTPKGCVELLIRS-GVEIAGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVH 245
|
170 180 190
....*....|....*....|....*....|....*....
gi 767942602 187 WKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 225
Cdd:PLN02897 246 AFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVID 284
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
31-235 |
1.89e-23 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 101.40 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 31 KPVLAIIQAGDD--NLMQEINQN-LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLN 105
Cdd:PRK14172 32 IPKIASILVGNDggSIYYMNNQEkVANSLGIDFKKIKLDESISEEDLINEIEELNKDNNVHGIMLQlpLPKHLDEKKITN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 106 ALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLeKSVGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSI 185
Cdd:PRK14172 112 KIDANKDIDCLTFISVGKFYKGE--KCFLPCTPNSVITLI-KSLNIDIEGKEVVVIGRSNIVGKPVAQLLLNENATVTIC 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767942602 186 QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKV 235
Cdd:PRK14172 189 HSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSVNGKI 238
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
32-225 |
2.49e-23 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 102.78 E-value: 2.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 32 PVLAIIQAGD--DNLMQEINQNLA-EEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNA 106
Cdd:PLN02616 104 PGLAVILVGDrkDSATYVRNKKKAcDSVGINSFEVRLPEDSTEQEVLKFISGFNNDPSVHGILVQLPlpSHMDEQNILNA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 107 LKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKsVGVNLDGKKILVVGAHG--SLEAALqcLFQRKGSMTMS 184
Cdd:PLN02616 184 VSIEKDVDGFHPLNIGRLAMRGREPLFVPCTPKGCIELLHR-YNVEIKGKRAVVIGRSNivGMPAAL--LLQREDATVSI 260
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767942602 185 IQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 225
Cdd:PLN02616 261 VHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVID 301
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
9-225 |
2.90e-23 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 101.12 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 9 RREViqnSKEVLSLLQEKNPAfkPVLAIIQAG---DDNLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDT 85
Cdd:PLN02516 22 RSEI---AEEVAQLSEKHGKV--PGLAVVIVGsrkDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISKVHELNANP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 86 RVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSvGVNLDGKKILVVGA 163
Cdd:PLN02516 97 DVHGILVQLPlpKHINEEKILNEISLEKDVDGFHPLNIGKLAMKGREPLFLPCTPKGCLELLSRS-GIPIKGKKAVVVGR 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767942602 164 HGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 225
Cdd:PLN02516 176 SNIVGLPVSLLLLKADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVID 237
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
31-225 |
1.05e-20 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 93.69 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 31 KPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLN 105
Cdd:PRK14167 31 TPGLATVLMSDDPASEtyvSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTIDELNADEDVHGILVQmpVPDHVDDREVLR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 106 ALKPEKDVDGVTDINLGKLVRGDAHecfVSPVAKAVIELLEKSVGVNLDGKKILVVGAHGSLEAALQCLFQRK---GSMT 182
Cdd:PRK14167 111 RIDPAKDVDGFHPENVGRLVAGDAR---FKPCTPHGIQKLLAAAGVDTEGADVVVVGRSDIVGKPMANLLIQKadgGNAT 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767942602 183 MSI-QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 225
Cdd:PRK14167 188 VTVcHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVID 231
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
14-209 |
3.13e-20 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 91.90 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 14 QNSKEVLSLLQEKnpAFKPVLAIIQAGDDNLMQEI---NQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGL 90
Cdd:PRK14175 17 QGLQDQVEALKEK--GFTPKLSVILVGNDGASQSYvrsKKKAAEKIGMISEIVHLEETATEEEVLNELNRLNNDDSVSGI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 91 ALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLeKSVGVNLDGKKILVVG-AHGSL 167
Cdd:PRK14175 95 LVQVPlpKQVSEQKILEAINPEKDVDGFHPINIGKLYIDE--QTFVPCTPLGIMEIL-KHADIDLEGKNAVVIGrSHIVG 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767942602 168 EAALQCLFQRKGSMTMsIQWKTRQLQSKLHEADIVVLGSPKP 209
Cdd:PRK14175 172 QPVSKLLLQKNASVTI-LHSRSKDMASYLKDADVIVSAVGKP 212
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
16-254 |
4.45e-20 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 91.68 E-value: 4.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 16 SKEVLSLLQEKNpafKPVLAIIQAGDDNLMQEI---NQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLAL 92
Cdd:PRK14170 19 TREVAELVKEGK---KPGLAVVLVGDNQASRTYvrnKQKRTEEAGMKSVLIELPENVTEEKLLSVVEELNEDKTIHGILV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 93 Q--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLeKSVGVNLDGKKILVVGAHGSL-EA 169
Cdd:PRK14170 96 QlpLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGK--DSFVPCTPAGIIELI-KSTGTQIEGKRAVVIGRSNIVgKP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 170 ALQCLFQRKGSMTMSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSprIHFGGLIE 249
Cdd:PRK14170 173 VAQLLLNENATVTIA-HSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDRDENNKLCGD--VDFDDVVE 249
|
....*
gi 767942602 250 EDDVI 254
Cdd:PRK14170 250 EAGFI 254
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
31-224 |
1.99e-19 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 89.59 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 31 KPVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLN 105
Cdd:PRK10792 33 APGLAVVLVGSDPASQVYVASkrkACEEVGFVSRSYDLPETTSEAELLALIDELNADPTIDGILVQlpLPAHIDNVKVLE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 106 ALKPEKDVDGVTDINLGKLvrgdaheCFVSPV-----AKAVIELLEkSVGVNLDGKKILVVGAHG------SLEAALqcl 174
Cdd:PRK10792 113 RIHPDKDVDGFHPYNVGRL-------AQRIPLlrpctPRGIMTLLE-RYGIDTYGLNAVVVGASNivgrpmSLELLL--- 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767942602 175 fqrKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVL 224
Cdd:PRK10792 182 ---AGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVI 228
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
32-249 |
3.91e-19 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 88.75 E-value: 3.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 32 PVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNA 106
Cdd:PRK14192 34 PILATILVGDDPASAtyvRMKGNACRRVGMDSLKVELPQETTTEQLLAKIEELNANPDVHGILLQhpVPAQIDERACFDA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 107 LKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSvGVNLDGKKILVVGAHGSLEAAL-QCLFQRKGSMTMSi 185
Cdd:PRK14192 114 ISLAKDVDGVTCLGFGRMAMGE--AAYGSATPAGIMRLLKAY-NIELAGKHAVVVGRSAILGKPMaMMLLNANATVTIC- 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767942602 186 QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCS-HDFLSGKVGcgspRIHFGGLIE 249
Cdd:PRK14192 190 HSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGfHPRDGGGVG----DIELQGIEE 250
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
65-225 |
4.53e-19 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 88.97 E-value: 4.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 65 LPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPVakAVI 142
Cdd:PRK14186 69 LPADTSQAEVEALIAQLNQDERVDGILLQlpLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPA--GVM 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 143 ELLEkSVGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTT 222
Cdd:PRK14186 147 RLLR-SQQIDIAGKKAVVVGRSILVGKPLALMLLAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAV 225
|
...
gi 767942602 223 VLN 225
Cdd:PRK14186 226 VVD 228
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-225 |
2.38e-18 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 86.82 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 5 RARPRREVIQNSKEVLSLLQEknpAFKPVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEIIDEILKI 81
Cdd:PRK14194 10 KAAAARVLAQVREDVRTLKAA---GIEPALAVILVGNDPASQVYVRNkilRAEEAGIRSLEHRLPADTSQARLLALIAEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 82 NEDTRVHGLALQ--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAhecFVSPVAKA-VIELLEKSVGvNLDGKKI 158
Cdd:PRK14194 87 NADPSVNGILLQlpLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRD---VLTPCTPSgCLRLLEDTCG-DLTGKHA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 159 LVVGAH---GSLEAALqcLFQRKGSMTMsIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 225
Cdd:PRK14194 163 VVIGRSnivGKPMAAL--LLQAHCSVTV-VHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVID 229
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
31-225 |
3.63e-18 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 85.89 E-value: 3.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 31 KPVLAIIQAGDDNLMQEINQNLA---EEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLN 105
Cdd:PRK14189 32 QPGLAVILVGDNPASQVYVRNKVkacEDNGFHSLKDRYPADLSEAELLARIDELNRDPKIHGILVQlpLPKHIDSHKVIE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 106 ALKPEKDVDGVTDINLGKLVRGdaHECFVSPVAKAVIELLEkSVGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSI 185
Cdd:PRK14189 112 AIAPEKDVDGFHVANAGALMTG--QPLFRPCTPYGVMKMLE-SIGIPLRGAHAVVIGRSNIVGKPMAMLLLQAGATVTIC 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767942602 186 QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 225
Cdd:PRK14189 189 HSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVID 228
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
29-235 |
3.81e-18 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 85.85 E-value: 3.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 29 AFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKV 103
Cdd:PRK14180 29 AITPKLVAIIVGNDPASKtyvASKEKACAQVGIDSQVITLPEHTTESELLELIDQLNNDSSVHAILVQLPlpAHINKNNV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 104 LNALKPEKDVDGVTDINLGKLVRGDaHECFVSPVAKAVIELLeKSVGVNLDGKKILVVGAHGSL-EAALQCLFQRKGSMT 182
Cdd:PRK14180 109 IYSIKPEKDVDGFHPTNVGRLQLRD-KKCLESCTPKGIMTML-REYGIKTEGAYAVVVGASNVVgKPVSQLLLNAKATVT 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767942602 183 MSIQWkTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKV 235
Cdd:PRK14180 187 TCHRF-TTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHVDGKI 238
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
31-224 |
8.80e-18 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 85.01 E-value: 8.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 31 KPVLAIIQAGDDNLMQEINQN---LAEEAGLN-ITHIcLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVL 104
Cdd:PRK14188 32 TPGLAVVLVGEDPASQVYVRSkgkQTKEAGMAsFEHK-LPADTSQAELLALIARLNADPAIHGILVQlpLPKHLDSEAVI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 105 NALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSVGvNLDGKKILVVGAH---GSLEAALqcLFQRKGSM 181
Cdd:PRK14188 111 QAIDPEKDVDGLHVVNAGRLATGE--TALVPCTPLGCMMLLRRVHG-DLSGLNAVVIGRSnlvGKPMAQL--LLAANATV 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767942602 182 TMSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVL 224
Cdd:PRK14188 186 TIA-HSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVI 227
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
32-225 |
1.30e-17 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 84.49 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 32 PVLAIIQAGDDNLMQEINQNLAE---EAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNA 106
Cdd:PRK14174 32 PGLTVIIVGEDPASQVYVRNKAKsckEIGMNSTVIELPADTTEEHLLKKIEDLNNDPDVHGILVQqpLPKQIDEFAVTLA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 107 LKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKsVGVNLDGKKILVVGAH---GSLEAALQCLFQRKGSMTM 183
Cdd:PRK14174 112 IDPAKDVDGFHPENLGRLVMGHLDKCFVSCTPYGILELLGR-YNIETKGKHCVVVGRSnivGKPMANLMLQKLKESNCTV 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767942602 184 SI-QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 225
Cdd:PRK14174 191 TIcHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVID 233
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
24-114 |
1.66e-17 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 78.99 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 24 QEKNPAFKPVLAIIQAGDD---NLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENL 98
Cdd:pfam00763 20 ALKAGGRKPGLAVILVGDDpasQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKLNADPSVHGILVQlpLPKHI 99
|
90
....*....|....*.
gi 767942602 99 FSNKVLNALKPEKDVD 114
Cdd:pfam00763 100 DEEKVLEAIDPEKDVD 115
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
11-236 |
2.90e-17 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 83.10 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 11 EVIQNskEVLSLLQEKNPAFK--PVLAIIQAGDdNLMQEINQNL----AEEAGLNITHICLPPDSSEAEIIDEILKINED 84
Cdd:PRK14177 13 EKIRN--EIRETIEERKTKNKriPKLATILVGN-NPASETYVSMkvkaCHKVGMGSEMIRLKEQTTTEELLGVIDKLNLD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 85 TRVHGLALQ--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDahECFVsPVAKAVIELLEKSVGVNLDGKKILVVG 162
Cdd:PRK14177 90 PNVDGILLQhpVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGV--ETYL-PCTPYGMVLLLKEYGIDVTGKNAVVVG 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767942602 163 AHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDflSGKVG 236
Cdd:PRK14177 167 RSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYN--PGNVG 238
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
32-225 |
1.05e-16 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 81.74 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 32 PVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNA 106
Cdd:PRK14191 32 PKLAVILVGKDPASQtyvNMKIKACERVGMDSDLHTLQENTTEAELLSLIKDLNTDQNIDGILVQLPlpRHIDTKMVLEA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 107 LKPEKDVDGVTDINLGKLVRGdaHECFVSPVAKAVIELLEKsVGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQ 186
Cdd:PRK14191 112 IDPNKDVDGFHPLNIGKLCSQ--LDGFVPATPMGVMRLLKH-YHIEIKGKDVVIIGASNIVGKPLAMLMLNAGASVSVCH 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 767942602 187 WKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 225
Cdd:PRK14191 189 ILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVD 227
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
53-225 |
1.53e-16 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 81.46 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 53 AEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAH 130
Cdd:PRK14168 58 AHRLGFHEIQDNQSVDITEEELLALIDKYNNDDSIHGILVQlpLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIGGDE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 131 ECFVSPVAKAVIELLEKSvGVNLDGKKILVVGAHGSLEAALQCLFQRKG----SMTMSIQWKTRQLQSKLHEADIVVLGS 206
Cdd:PRK14168 138 VKFLPCTPAGIQEMLVRS-GVETSGAEVVVVGRSNIVGKPIANMMTQKGpganATVTIVHTRSKNLARHCQRADILIVAA 216
|
170
....*....|....*....
gi 767942602 207 PKPEEIPLTWIQPGTTVLN 225
Cdd:PRK14168 217 GVPNLVKPEWIKPGATVID 235
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
25-225 |
3.40e-16 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 80.24 E-value: 3.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 25 EKNPAFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLF 99
Cdd:PRK14176 32 KSNRGITPGLATILVGDDPASKmyvRLKHKACERVGIRAEDQFLPADTTQEELLELIDSLNKRKDVHGILLQLPlpKHLD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 100 SNKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKsVGVNLDGKKILVVGAHGSLEAALQCLFQRKG 179
Cdd:PRK14176 112 PQEAMEAIDPAKDADGFHPYNMGKLMIGD--EGLVPCTPHGVIRALEE-YGVDIEGKNAVIVGHSNVVGKPMAAMLLNRN 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767942602 180 SMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 225
Cdd:PRK14176 189 ATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFD 234
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
9-225 |
3.54e-16 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 80.06 E-value: 3.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 9 RREVIQNSKEVLSLLQEKnpAFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDT 85
Cdd:PRK14193 12 ADEIKADLAERVAALKEK--GITPGLGTVLVGDDPGSQayvRGKHRDCAEVGITSIRRDLPADATQEELNAVIDELNADP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 86 RVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPvaKAVIELLEKSvGVNLDGKKILVVGA 163
Cdd:PRK14193 90 ACTGYIVQLPlpKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTP--RGIVHLLRRY-DVELAGAHVVVIGR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767942602 164 HGSLEAALQCLFQRKG-SMTMSI-QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 225
Cdd:PRK14193 167 GVTVGRPIGLLLTRRSeNATVTLcHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLD 230
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
109-226 |
8.15e-16 |
|
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: 76.05 E-value: 8.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 109 PEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLeKSVGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWK 188
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGR--PGFIPCTPAGILELL-KRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSK 77
|
90 100 110
....*....|....*....|....*....|....*...
gi 767942602 189 TRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNC 226
Cdd:cd01080 78 TKNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDV 115
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
16-238 |
9.96e-16 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 78.35 E-value: 9.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 16 SKEVLSLLQEK--NPAFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGL 90
Cdd:PRK14178 9 SEKRLELLKEEiiESGLYPRLATVIVGDDPASQmyvRMKHRACERVGIGSVGIELPGDATTRTVLERIRRLNEDPDINGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 91 ALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPvaKAVIELLeKSVGVNLDGKKILVVGAH---G 165
Cdd:PRK14178 89 LVQLPlpKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTP--NGIMTLL-HEYKISIAGKRAVVVGRSidvG 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767942602 166 SLEAALqcLFQRKGSMTMSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKVgCG 238
Cdd:PRK14178 166 RPMAAL--LLNADATVTIC-HSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQVNGKL-CG 234
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
17-225 |
2.35e-15 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 77.48 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 17 KEVLSLLQEKnpAFKPVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ 93
Cdd:PRK14179 20 EKVAKLKEEK--GIVPGLVVILVGDNPASQVYVRNkerSALAAGFKSEVVRLPETISQEELLDLIERYNQDPTWHGILVQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 94 --ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGdaHECFVSPVAKAVIELLeKSVGVNLDGKKILVVGAHGSLEAAL 171
Cdd:PRK14179 98 lpLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSG--RPVMIPCTPAGIMEMF-REYNVELEGKHAVVIGRSNIVGKPM 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767942602 172 -QCLFQRKGSMTMSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 225
Cdd:PRK14179 175 aQLLLDKNATVTLT-HSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVID 228
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
31-225 |
1.70e-13 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 71.98 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 31 KPVLAIIQAGDD---NLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLN 105
Cdd:PRK14182 30 QTGLTVVRVGDDpasAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIARLNADPAVHGILVQLPlpKHVDERAVLD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 106 ALKPEKDVDGVTDINLGKL---VRGDAHECfvSPVAkaVIELLEKSvGVNLDGKKILVVGAH---GSLEAALqcLFQRKG 179
Cdd:PRK14182 110 AISPAKDADGFHPFNVGALsigIAGVPRPC--TPAG--VMRMLDEA-RVDPKGKRALVVGRSnivGKPMAMM--LLERHA 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767942602 180 SMTMSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 225
Cdd:PRK14182 183 TVTIA-HSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVID 227
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
11-233 |
1.98e-12 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 68.83 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 11 EVIQNSKEVLSLLQEKNPAfKPVLAIIQAGDDN-----LMQEINQnlAEEAGLNITHICLPPDSSEAEIIDEILKINEDT 85
Cdd:PRK14171 13 EILADLKLEIQELKSQTNA-SPKLAIVLVGDNPasiiyVKNKIKN--AHKIGIDTLLVNLSTTIHTNDLISKINELNLDN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 86 RVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGdAHECFVSPVAKAVIELLEKsVGVNLDGKKILVVGA 163
Cdd:PRK14171 90 EISGIIVQLPlpSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSG-ISQGFIPCTALGCLAVIKK-YEPNLTGKNVVIIGR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 164 HGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSG 233
Cdd:PRK14171 168 SNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRISG 237
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
16-235 |
2.71e-12 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 68.51 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 16 SKEVLSLLQEKNPAFK-----PVLAIIQAGDDNLMQEINQNLA---EEAGLNITHICLPPDSSEAEIIDEILKINEDTRV 87
Cdd:PRK14166 10 SAKIKEELKEKNQFLKskgieSCLAVILVGDNPASQTYVKSKAkacEECGIKSLVYHLNENTTQNELLALINTLNHDDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 88 HGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGdAHECFVSPVAKAVIELLEkSVGVNLDGKKILVVGAHG 165
Cdd:PRK14166 90 HGILVQLPlpDHICKDLILESIISSKDVDGFHPINVGYLNLG-LESGFLPCTPLGVMKLLK-AYEIDLEGKDAVIIGASN 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767942602 166 SLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFL-SGKV 235
Cdd:PRK14166 168 IVGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLeSGKI 238
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
32-225 |
3.96e-12 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 67.96 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 32 PVLAIIQAGDDNlMQEINQNLAEEAGLNITHIC----LPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLN 105
Cdd:PRK14181 27 PGLAVVLIGNDP-ASEVYVGMKVKKATDLGMVSkahrLPSDATLSDILKLIHRLNNDPNIHGILVQLPlpKHLDAQAILQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942602 106 ALKPEKDVDGVTDINLGKLVRGDAhECFVSPVAKAVIELLeKSVGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMS- 184
Cdd:PRK14181 106 AISPDKDVDGLHPVNMGKLLLGET-DGFIPCTPAGIIELL-KYYEIPLHGRHVAIVGRSNIVGKPLAALLMQKHPDTNAt 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767942602 185 ---IQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 225
Cdd:PRK14181 184 vtlLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVD 227
|
|
| |
