|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
349-975 |
0e+00 |
|
Formate--tetrahydrofolate ligase
Pssm-ID: 178359 Cd Length: 637 Bit Score: 1015.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 349 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKST 428
Cdd:PLN02759 9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 429 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 508
Cdd:PLN02759 89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 509 TQTDKALYNRLVPS-VNGVREFSEIQLARLKKLGINKTDPSALTEEEMGKFARLNIDPSTITWQRVLDTNDRFLRKITIG 587
Cdd:PLN02759 169 TQSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 588 QASTEKGYSRQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTL 667
Cdd:PLN02759 249 QGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 668 EGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMH 747
Cdd:PLN02759 329 EGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMH 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 748 GGGPSVIPGVPLKKEYTEENIQLVADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYH 827
Cdd:PLN02759 409 GGGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTH 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 828 WSVGGKGSVDLARAVREAANTNS-HFQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAK 906
Cdd:PLN02759 489 HAHGGKGAVDLGEAVQKACEGNSqPFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAK 568
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2327289797 907 THLSLSHQPDKKGVPRDFVLPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVQGLF 975
Cdd:PLN02759 569 TQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTETGKVLGLS 637
|
|
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
357-975 |
0e+00 |
|
Formate--tetrahydrofolate ligase;
Pssm-ID: 460143 Cd Length: 555 Bit Score: 989.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 357 PSDIEISRGQTPKAVDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQA 436
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 437 LtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkaly 516
Cdd:pfam01268 81 L-NRLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 517 nrlvpsvngvrefseiqlarlkklginktdpsalteeemgkfarLNIDPSTITWQRVLDTNDRFLRKITIGQASTEKGYS 596
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 597 RQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHA 676
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 677 GPFANIAHGNSSVLADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMHGGgpsvipg 756
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGG------- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 757 vPLKKEYTEENIQLVADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKrAGAFDAVPCYHWSVGGKGSV 836
Cdd:pfam01268 339 -VGKDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRELCE-AGGVDAALSEHWAKGGEGAI 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 837 DLARAVREAANTN-SHFQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAKTHLSLSHQP 915
Cdd:pfam01268 417 ELAEAVVEACEEEpSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 916 DKKGVPRDFVLPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTEtEQVQGLF 975
Cdd:pfam01268 497 KLKGAPTGFTLPVRDVRLSAGAGFIVALTGDIMTMPGLPKRPAAENIDVDED-GKITGLF 555
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
371-974 |
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: 932.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 371 VDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALTAHLNvNSFACLR 450
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 451 QPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkalynrlvpsvngvrefs 530
Cdd:cd00477 80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 531 eiqlarlkklginktdpsalteeemgkfarLNIDPSTITWQRVLDTNDRFLRKITIGQASTEKGYSRQAQFDIAVASEIM 610
Cdd:cd00477 139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 611 AVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSVL 690
Cdd:cd00477 189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 691 ADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMHGGGPSVIPGvplkkeytEENIQL 770
Cdd:cd00477 269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 771 VADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVpCYHWSVGGKGSVDLARAVREAANTNS 850
Cdd:cd00477 338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKPK 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 851 H-FQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAKTHLSLSHQPDKKGVPRDFVLPIS 929
Cdd:cd00477 417 SnFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 2327289797 930 DVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDtETEQVQGL 974
Cdd:cd00477 497 DVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDID-DTGKIEGL 540
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
356-975 |
0e+00 |
|
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
Pssm-ID: 442046 Cd Length: 556 Bit Score: 882.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 356 VPSDIEISRGQTPKAVDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQ 435
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 436 ALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENtqtdkal 515
Cdd:COG2759 81 AL-NRLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQGN------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 516 ynrlvpsvngvrefseiqlarlkklginktdpsalteeemgkfaRLNIDPSTITWQRVLDTNDRFLRKITIGQASTEKGY 595
Cdd:COG2759 153 --------------------------------------------ELNIDPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 596 SRQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVH 675
Cdd:COG2759 189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 676 AGPFANIAHGNSSVLADKIALKLvGEegFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMHGGGPsvip 755
Cdd:COG2759 269 GGPFANIAHGCNSVIATKLALKL-AD--YVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 756 gvplKKEYTEENIQLVADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKRAGAfDAVPCYHWSVGGKGS 835
Cdd:COG2759 342 ----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEGA 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 836 VDLARAVREAANTN-SHFQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAKTHLSLSHQ 914
Cdd:COG2759 417 EELAEAVVEACEEGpSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSDD 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2327289797 915 PDKKGVPRDFVLPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDtETEQVQGLF 975
Cdd:COG2759 497 PKLLGAPTGFTLTVREVRLSAGAGFIVALTGDIMTMPGLPKVPAAERIDID-EDGKITGLF 556
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
190-332 |
7.64e-55 |
|
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: 186.56 E-value: 7.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 190 GDAHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSP 269
Cdd:cd05212 1 GPCTPLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2327289797 270 KPEKIPVAWIRPGTTVLNCFHSFMSEKLGCGSHGVHCGGSIaedDVSLLAAALRIQNMVSSGR 332
Cdd:cd05212 81 KPEKVPTEWIKPGATVINCSPTKLSGDDVKESASLYVPMTG---GVGKLTVAMRMQNMVRSVR 140
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
180-335 |
2.94e-37 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 137.21 E-value: 2.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 180 TDVNLGKLVRGdaHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMSSQWKTPQLESKLQ 259
Cdd:pfam02882 1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 260 EADIVILGSPKPEKIPVAWIRPGTTVLNCFHSFMSEKLGCGshGVHcGGSIAE---------DDVSLLAAALRIQNMVSS 330
Cdd:pfam02882 79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVG--DVD-FENVKEkasaitpvpGGVGPMTVAMLLQNTVEA 155
|
....*
gi 2327289797 331 GRRWL 335
Cdd:pfam02882 156 AKRQL 160
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
94-286 |
7.32e-36 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 137.45 E-value: 7.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 94 KPVLAVIQAGDDnllqE-----VN--QNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQVPensL---- 162
Cdd:COG0190 32 TPGLAVVLVGDD----PasqvyVRnkHKACEEVGIESELIRLPADTTQEELLALIDELNADPSVHGILVQLP---Lpkhi 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 163 -SSKVLNALKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLGaHG-----PLeaALqcL 236
Cdd:COG0190 105 dEEAVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLERYGIDLAGKHAVVVG-RSnivgkPL--AL--L 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2327289797 237 FQRKD---SMTMSsqwKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVL 286
Cdd:COG0190 178 LLRRNatvTVCHS---RTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVI 227
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
80-287 |
2.24e-29 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 118.96 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 80 KEVLSLlqeKNPAFKPVLAVIQAGDDNLLQ---EVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ 156
Cdd:PRK14190 21 EEVVKL---KEQGIVPGLAVILVGDDPASHsyvRGKKKAAEKVGIYSELYEFPADITEEELLALIDRLNADPRINGILVQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 157 --VPENSLSSKVLNALKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQ 234
Cdd:PRK14190 98 lpLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQ--DTFLPCTPHGILELLKEYNIDISGKHVVVVGRSNIVGKPVG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2327289797 235 CLFQRKD-SMTMSSQwKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14190 176 QLLLNENaTVTYCHS-KTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVID 228
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
95-287 |
8.85e-26 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 108.83 E-value: 8.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 95 PVLAVIQAG---DDNLLQEVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQVP--ENSLSSKVLNA 169
Cdd:PLN02516 40 PGLAVVIVGsrkDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISKVHELNANPDVHGILVQLPlpKHINEEKILNE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 170 LKPEKDVDGVTDVNLGKLVRGDAHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMSSQW 249
Cdd:PLN02516 120 ISLEKDVDGFHPLNIGKLAMKGREPLFLPCTPKGCLELLSRSGIPIKGKKAVVVGRSNIVGLPVSLLLLKADATVTVVHS 199
|
170 180 190
....*....|....*....|....*....|....*...
gi 2327289797 250 KTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PLN02516 200 RTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVID 237
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
87-177 |
6.99e-18 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 80.14 E-value: 6.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 87 QEKNPAFKPVLAVIQAGDD--------NLlqevnQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ-- 156
Cdd:pfam00763 20 ALKAGGRKPGLAVILVGDDpasqvyvrNK-----KKACEEVGIESELIRLPEDTTEEELLALIDKLNADPSVHGILVQlp 94
|
90 100
....*....|....*....|.
gi 2327289797 157 VPENSLSSKVLNALKPEKDVD 177
Cdd:pfam00763 95 LPKHIDEEKVLEAIDPEKDVD 115
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
349-975 |
0e+00 |
|
Formate--tetrahydrofolate ligase
Pssm-ID: 178359 Cd Length: 637 Bit Score: 1015.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 349 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKST 428
Cdd:PLN02759 9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 429 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 508
Cdd:PLN02759 89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 509 TQTDKALYNRLVPS-VNGVREFSEIQLARLKKLGINKTDPSALTEEEMGKFARLNIDPSTITWQRVLDTNDRFLRKITIG 587
Cdd:PLN02759 169 TQSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 588 QASTEKGYSRQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTL 667
Cdd:PLN02759 249 QGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 668 EGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMH 747
Cdd:PLN02759 329 EGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMH 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 748 GGGPSVIPGVPLKKEYTEENIQLVADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYH 827
Cdd:PLN02759 409 GGGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTH 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 828 WSVGGKGSVDLARAVREAANTNS-HFQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAK 906
Cdd:PLN02759 489 HAHGGKGAVDLGEAVQKACEGNSqPFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAK 568
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2327289797 907 THLSLSHQPDKKGVPRDFVLPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVQGLF 975
Cdd:PLN02759 569 TQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTETGKVLGLS 637
|
|
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
357-975 |
0e+00 |
|
Formate--tetrahydrofolate ligase;
Pssm-ID: 460143 Cd Length: 555 Bit Score: 989.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 357 PSDIEISRGQTPKAVDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQA 436
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 437 LtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkaly 516
Cdd:pfam01268 81 L-NRLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 517 nrlvpsvngvrefseiqlarlkklginktdpsalteeemgkfarLNIDPSTITWQRVLDTNDRFLRKITIGQASTEKGYS 596
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 597 RQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHA 676
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 677 GPFANIAHGNSSVLADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMHGGgpsvipg 756
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGG------- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 757 vPLKKEYTEENIQLVADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKrAGAFDAVPCYHWSVGGKGSV 836
Cdd:pfam01268 339 -VGKDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRELCE-AGGVDAALSEHWAKGGEGAI 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 837 DLARAVREAANTN-SHFQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAKTHLSLSHQP 915
Cdd:pfam01268 417 ELAEAVVEACEEEpSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 916 DKKGVPRDFVLPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTEtEQVQGLF 975
Cdd:pfam01268 497 KLKGAPTGFTLPVRDVRLSAGAGFIVALTGDIMTMPGLPKRPAAENIDVDED-GKITGLF 555
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
371-974 |
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: 932.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 371 VDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALTAHLNvNSFACLR 450
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 451 QPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkalynrlvpsvngvrefs 530
Cdd:cd00477 80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 531 eiqlarlkklginktdpsalteeemgkfarLNIDPSTITWQRVLDTNDRFLRKITIGQASTEKGYSRQAQFDIAVASEIM 610
Cdd:cd00477 139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 611 AVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSVL 690
Cdd:cd00477 189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 691 ADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMHGGGPSVIPGvplkkeytEENIQL 770
Cdd:cd00477 269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 771 VADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVpCYHWSVGGKGSVDLARAVREAANTNS 850
Cdd:cd00477 338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKPK 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 851 H-FQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAKTHLSLSHQPDKKGVPRDFVLPIS 929
Cdd:cd00477 417 SnFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 2327289797 930 DVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDtETEQVQGL 974
Cdd:cd00477 497 DVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDID-DTGKIEGL 540
|
|
| PTZ00386 |
PTZ00386 |
formyl tetrahydrofolate synthetase; Provisional |
349-974 |
0e+00 |
|
formyl tetrahydrofolate synthetase; Provisional
Pssm-ID: 240394 Cd Length: 625 Bit Score: 922.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 349 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKST 428
Cdd:PTZ00386 8 KLSCQWPVPSDIDIAQSVKPQPITSVAESAGILLSELDPYGSTRAKVKLSVLKRLENSPNGKYVVVAGMNPTPLGEGKST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 429 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 508
Cdd:PTZ00386 88 TTIGLAQSLGAHLHRKTFACIRQPSQGPTFGIKGGAAGGGYSQVIPMEDFNLHGTGDIHAITAANNLLAAALDTRIFHER 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 509 TQTDKALYNRLVpsvNGVREFSEIQLARLKKLGINKTDPSALTEEEMGKFARLNIDPSTITWQRVLDTNDRFLRKITIGQ 588
Cdd:PTZ00386 168 TQSDAALYRRLT---DELKKFTPIMLKRLEKLGISKTDPKQLTEEERVRFARLDIDPDTISWRRVTDVNDRMLREITIGQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 589 ASTEKGYSRQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLE 668
Cdd:PTZ00386 245 GKEEKGITRKTGFDISVASEVMAILALATDLADMRQRLGAIVVAKSKSGEPVTAEDLGCAGAMTVLMKDTIEPTLMQTLE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 669 GTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMHG 748
Cdd:PTZ00386 325 GTPVLVHAGPFGNIAHGNSSIVADQIALKLAGQDGFVLTEAGFGADIGCEKFFNIKCRTSGLKPDAAVLVATVRALKFHG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 749 GGPSVIPGvplkkeytEENIQLVADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELA-KRAGAFDAVPCYH 827
Cdd:PTZ00386 405 GVEPVVAG--------KENLEAVRKGLSNLQRHIQNIRKFGVPVVVALNKFSTDTDAELELVKELAlQEGGAADVVVTDH 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 828 WSVGGKGSVDLARAVREAANTN-SHFQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAK 906
Cdd:PTZ00386 477 WAKGGAGAVDLAQALIRVTENVpSNFKLLYPLDASLKEKIETICKEIYGAAGVEYLNDADEKLEDFERMGYGKFPVCMAK 556
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2327289797 907 THLSLSHQPDKKGVPRDFVLPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVQGL 974
Cdd:PTZ00386 557 TQYSFSHDPELRGAPTGFTVPIRDVRVNCGAGFVFPLLGDISTMPGLPTRPAFYNIDIDCETGKIVGL 624
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
356-975 |
0e+00 |
|
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
Pssm-ID: 442046 Cd Length: 556 Bit Score: 882.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 356 VPSDIEISRGQTPKAVDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQ 435
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 436 ALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENtqtdkal 515
Cdd:COG2759 81 AL-NRLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQGN------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 516 ynrlvpsvngvrefseiqlarlkklginktdpsalteeemgkfaRLNIDPSTITWQRVLDTNDRFLRKITIGQASTEKGY 595
Cdd:COG2759 153 --------------------------------------------ELNIDPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 596 SRQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVH 675
Cdd:COG2759 189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 676 AGPFANIAHGNSSVLADKIALKLvGEegFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMHGGGPsvip 755
Cdd:COG2759 269 GGPFANIAHGCNSVIATKLALKL-AD--YVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 756 gvplKKEYTEENIQLVADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKRAGAfDAVPCYHWSVGGKGS 835
Cdd:COG2759 342 ----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEGA 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 836 VDLARAVREAANTN-SHFQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAKTHLSLSHQ 914
Cdd:COG2759 417 EELAEAVVEACEEGpSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSDD 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2327289797 915 PDKKGVPRDFVLPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDtETEQVQGLF 975
Cdd:COG2759 497 PKLLGAPTGFTLTVREVRLSAGAGFIVALTGDIMTMPGLPKVPAAERIDID-EDGKITGLF 556
|
|
| PRK13505 |
PRK13505 |
formate--tetrahydrofolate ligase; Provisional |
355-975 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237403 Cd Length: 557 Bit Score: 754.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 355 PVPSDIEISRGQTPKAVDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLV 434
Cdd:PRK13505 1 TMKSDIEIAQEATLKPITEIAAKLGIPEDDLEPYGKYKAKISLDKIKALKDKKDGKLILVTAINPTPAGEGKSTVTVGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 435 QALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdka 514
Cdd:PRK13505 81 DAL-NKIGKKTVIALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITSANNLLAALIDNHIHQGNE----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 515 lynrlvpsvngvrefseiqlarlkklginktdpsalteeemgkfarLNIDPSTITWQRVLDTNDRFLRKITIGQASTEKG 594
Cdd:PRK13505 155 ----------------------------------------------LGIDPRRITWKRVLDMNDRALRNIVVGLGGPANG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 595 YSRQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFV 674
Cdd:PRK13505 189 VPREDGFDITVASEIMAILCLATDLKDLKERLGRIVVGYTYDGKPVTVKDLKVEGAMALLLKDAIKPNLVQTLEGTPAFV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 675 HAGPFANIAHGNSSVLADKIALKLvGEegFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMHGGGPsvi 754
Cdd:PRK13505 269 HGGPFANIAHGCNSVLATKTALKL-AD--YVVTEAGFGADLGAEKFLDIKCRKAGLKPDAVVIVATVRALKMHGGVA--- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 755 pgvplKKEYTEENIQLVADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKRAGAfDAVPCYHWSVGGKG 834
Cdd:PRK13505 343 -----KDDLKEENVEALKKGFANLERHIENIRKFGVPVVVAINKFVTDTDAEIAALKELCEELGV-EVALSEVWAKGGEG 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 835 SVDLARAVREAANTN-SHFQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAKTHLSLSH 913
Cdd:PRK13505 417 GVELAEKVVELIEEGeSNFKPLYDDEDSLEEKIEKIATKIYGAKGVEFSPKAKKQLKQIEKNGWDKLPVCMAKTQYSFSD 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2327289797 914 QPDKKGVPRDFVLPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDtETEQVQGLF 975
Cdd:PRK13505 497 DPKLLGAPTGFTITVRELRPSAGAGFIVALTGDIMTMPGLPKVPAALNIDVD-EDGNIVGLF 557
|
|
| PRK13506 |
PRK13506 |
formate--tetrahydrofolate ligase; Provisional |
358-974 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237404 Cd Length: 578 Bit Score: 710.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 358 SDIEISRGQTPKAVDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQAL 437
Cdd:PRK13506 3 SDIEISRQAPLKPIAEIAAKLGLLPDELSPFGHTKAKVSLSVLKRLADKPKGKLVLVTAITPTPLGEGKTVTTIGLTQGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 438 tAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEntqtdkalyN 517
Cdd:PRK13506 83 -NALGQKVCACIRQPSMGPVFGVKGGAAGGGYAQVVPMEELNLHLTGDIHAVSAAHNLAAAAIDARLFHE---------Q 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 518 RLvpsvnGVREFSEiqlarlkklginKTDpsalteeemgkFARLNIDPSTITWQRVLDTNDRFLRKITIGQASTEKGYSR 597
Cdd:PRK13506 153 RL-----GYDAFEA------------QSG-----------LPALDIDPEQILWKRVVDHNDRALRMITVGLGENGNGPER 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 598 QAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAG 677
Cdd:PRK13506 205 EDGFDITAASELMAILALSRDLKDMRQRIGRLVLAYNLQGQPITAEDLGVAGAMTVIMKDAIEPTLMQTLEGVPCLIHAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 678 PFANIAHGNSSVLADKIALKLVgeeGFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMHGGGPSVIPGV 757
Cdd:PRK13506 285 PFANIAHGNSSIIADRIALKLA---DYVVTEGGFGSDMGFEKFCNIKARQSGKAPDCAVLVATLRALKANSGLYDLRPGQ 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 758 PLKKEYTEENIQLVADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYHWSVGGKGSVD 837
Cdd:PRK13506 362 ALPDSINAPDQARLEAGFANLKWHINNVAQYGLPVVVAINRFPTDTDEELEWLKEAVLLTGAFGCEISEAFAQGGEGATA 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 838 LARAVREAANTNSHFQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAKTHLSLSHQPDK 917
Cdd:PRK13506 442 LAQAVVRACEQPSQFKLLYPDEMSLEAKLMTLAEVGYGAAGVSLSDKAKQQLAQLTALGYDHLPVCMAKTPLSISHDPAL 521
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 2327289797 918 KGVPRDFVLPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVqGL 974
Cdd:PRK13506 522 KGAPTDFEVPIRELRLCAGAGFITALVGNVMTMPGLGLKPGYLNIDIDADGEIV-GL 577
|
|
| PRK13507 |
PRK13507 |
formate--tetrahydrofolate ligase; Provisional |
369-975 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 184098 Cd Length: 587 Bit Score: 660.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 369 KAVDVLAKEIGLLAEEIEIYGKSKAKVR-LSLLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALtAHLNVNSFA 447
Cdd:PRK13507 22 KPVEELAEELGLTKEELLPYGHYIAKVDfRKVLDRLKDRPDGKYIDVTAITPTPLGEGKSTTTMGLVQGL-GKRGKKVSG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 448 CLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTQTDKALYNRlvpsvngvr 527
Cdd:PRK13507 101 AIRQPSGGPTMNIKGSAAGGGLSQCIPLTPFSLGLTGDINAIMNAHNLAMVALTARMQHERNYTDEQLARR--------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 528 efseiqlarlkklginktdpsalteeemgKFARLNIDPSTITWQRVLDTNDRFLRKITIGQASTEKGYSRQAQFDIAVAS 607
Cdd:PRK13507 172 -----------------------------GLKRLDIDPTRVEMGWIIDFCAQALRNIIIGIGGKTDGYMMQSGFGIAVSS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 608 EIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNS 687
Cdd:PRK13507 223 EVMAILSVATDLKDLRERIGKIVVAYDKNGKPVTTADLEVDGAMTAWMVRAINPNLLQTIEGQPVFVHAGPFANIAIGQS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 688 SVLADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMHGGGPSVIPGVPLKKEYTEEN 767
Cdd:PRK13507 303 SIIADRVGLKL---ADYHVTESGFGADIGFEKFWNLKCRLSGLKPDCAVIVATIRALKMHGGGPKVVPGKPLPEEYTKEN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 768 IQLVADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPcYHWSVGGKGSVDLARAVREAAN 847
Cdd:PRK13507 380 VGLVEKGCANLLHHIGTVKKSGINPVVCINAFYTDTHAEIAIVRRLAEQAGARVAVS-RHWEKGGEGALELADAVIDACN 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 848 TNSHFQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQG-FGNLPICMAKTHLSLSHQPDKKGVPRDFVL 926
Cdd:PRK13507 459 EPNDFKFLYPLEMPLRERIETIAREVYGADGVSYTPEAEAKLKRLESDPeTADFGTCMVKTHLSLSHDPALKGVPKGWTL 538
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2327289797 927 PISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVQGLF 975
Cdd:PRK13507 539 PIRDILTYGGAGFVVPVAGDISLMPGTGSDPAFRRIDVDTQTGKVKGLF 587
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
190-332 |
7.64e-55 |
|
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: 186.56 E-value: 7.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 190 GDAHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSP 269
Cdd:cd05212 1 GPCTPLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2327289797 270 KPEKIPVAWIRPGTTVLNCFHSFMSEKLGCGSHGVHCGGSIaedDVSLLAAALRIQNMVSSGR 332
Cdd:cd05212 81 KPEKVPTEWIKPGATVINCSPTKLSGDDVKESASLYVPMTG---GVGKLTVAMRMQNMVRSVR 140
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
180-335 |
2.94e-37 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 137.21 E-value: 2.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 180 TDVNLGKLVRGdaHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMSSQWKTPQLESKLQ 259
Cdd:pfam02882 1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 260 EADIVILGSPKPEKIPVAWIRPGTTVLNCFHSFMSEKLGCGshGVHcGGSIAE---------DDVSLLAAALRIQNMVSS 330
Cdd:pfam02882 79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVG--DVD-FENVKEkasaitpvpGGVGPMTVAMLLQNTVEA 155
|
....*
gi 2327289797 331 GRRWL 335
Cdd:pfam02882 156 AKRQL 160
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
94-286 |
7.32e-36 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 137.45 E-value: 7.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 94 KPVLAVIQAGDDnllqE-----VN--QNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQVPensL---- 162
Cdd:COG0190 32 TPGLAVVLVGDD----PasqvyVRnkHKACEEVGIESELIRLPADTTQEELLALIDELNADPSVHGILVQLP---Lpkhi 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 163 -SSKVLNALKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLGaHG-----PLeaALqcL 236
Cdd:COG0190 105 dEEAVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLERYGIDLAGKHAVVVG-RSnivgkPL--AL--L 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2327289797 237 FQRKD---SMTMSsqwKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVL 286
Cdd:COG0190 178 LLRRNatvTVCHS---RTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVI 227
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
80-287 |
2.24e-29 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 118.96 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 80 KEVLSLlqeKNPAFKPVLAVIQAGDDNLLQ---EVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ 156
Cdd:PRK14190 21 EEVVKL---KEQGIVPGLAVILVGDDPASHsyvRGKKKAAEKVGIYSELYEFPADITEEELLALIDRLNADPRINGILVQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 157 --VPENSLSSKVLNALKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQ 234
Cdd:PRK14190 98 lpLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQ--DTFLPCTPHGILELLKEYNIDISGKHVVVVGRSNIVGKPVG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2327289797 235 CLFQRKD-SMTMSSQwKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14190 176 QLLLNENaTVTYCHS-KTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVID 228
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
68-287 |
8.78e-27 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 113.18 E-value: 8.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 68 RDSIVREVIQnSKEVLSLLqeknpafkPVLAVIQAGD--DNLLQEVNQNLA-EEAGLNITHICLPPDSSEDEIIDEILKM 144
Cdd:PLN02616 86 RDEITIEVSR-MKESIGVV--------PGLAVILVGDrkDSATYVRNKKKAcDSVGINSFEVRLPEDSTEQEVLKFISGF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 145 NEDARVHGLSLQVPENSL--SSKVLNALKPEKDVDGVTDVNLGKLVRGDAHECFVSPVARAVIELLEKSGVNLDGKKVLV 222
Cdd:PLN02616 157 NNDPSVHGILVQLPLPSHmdEQNILNAVSIEKDVDGFHPLNIGRLAMRGREPLFVPCTPKGCIELLHRYNVEIKGKRAVV 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2327289797 223 LGAHGPLEAALQCLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PLN02616 237 IGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVID 301
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
95-287 |
8.85e-26 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 108.83 E-value: 8.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 95 PVLAVIQAG---DDNLLQEVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQVP--ENSLSSKVLNA 169
Cdd:PLN02516 40 PGLAVVIVGsrkDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISKVHELNANPDVHGILVQLPlpKHINEEKILNE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 170 LKPEKDVDGVTDVNLGKLVRGDAHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMSSQW 249
Cdd:PLN02516 120 ISLEKDVDGFHPLNIGKLAMKGREPLFLPCTPKGCLELLSRSGIPIKGKKAVVVGRSNIVGLPVSLLLLKADATVTVVHS 199
|
170 180 190
....*....|....*....|....*....|....*...
gi 2327289797 250 KTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PLN02516 200 RTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVID 237
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
95-287 |
1.88e-25 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 108.89 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 95 PVLAVIQAGDDNLLQEVNQN---LAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQVP--ENSLSSKVLNA 169
Cdd:PLN02897 87 PGLAVVLVGQQRDSQTYVRNkikACEETGIKSLLAELPEDCTEGQILSALRKFNEDTSIHGILVQLPlpQHLDESKILNM 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 170 LKPEKDVDGVTDVNLGKLVRGDAHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMSSQW 249
Cdd:PLN02897 167 VRLEKDVDGFHPLNVGNLAMRGREPLFVSCTPKGCVELLIRSGVEIAGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHA 246
|
170 180 190
....*....|....*....|....*....|....*...
gi 2327289797 250 KTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PLN02897 247 FTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVID 284
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
94-287 |
3.37e-25 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 106.40 E-value: 3.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 94 KPVLAVIQAGDD--NLLQEVNQN-LAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ--VPENSLSSKVLN 168
Cdd:PRK14172 32 IPKIASILVGNDggSIYYMNNQEkVANSLGIDFKKIKLDESISEEDLINEIEELNKDNNVHGIMLQlpLPKHLDEKKITN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 169 ALKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMSSQ 248
Cdd:PRK14172 112 KIDANKDIDCLTFISVGKFYKGE--KCFLPCTPNSVITLIKSLNIDIEGKEVVVIGRSNIVGKPVAQLLLNENATVTICH 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 2327289797 249 WKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14172 190 SKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVID 228
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
95-287 |
5.68e-24 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 103.37 E-value: 5.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 95 PVLAVIQAGDD---NLLQEVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ--VPENSLSSKVLNA 169
Cdd:PRK14187 33 PCLIVILVGDDpasQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKINELNNDDSVHGILVQlpVPNHIDKNLIINT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 170 LKPEKDVDGVTDVNLGKLVRGDAHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMSSQW 249
Cdd:PRK14187 113 IDPEKDVDGFHNENVGRLFTGQKKNCLIPCTPKGCLYLIKTITRNLSGSDAVVIGRSNIVGKPMACLLLGENCTVTTVHS 192
|
170 180 190
....*....|....*....|....*....|....*...
gi 2327289797 250 KTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14187 193 ATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVID 230
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
94-287 |
6.95e-22 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 97.15 E-value: 6.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 94 KPVLAVIQAGDDNLLQ---EVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ--VPENSLSSKVLN 168
Cdd:PRK14167 31 TPGLATVLMSDDPASEtyvSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTIDELNADEDVHGILVQmpVPDHVDDREVLR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 169 ALKPEKDVDGVTDVNLGKLVRGDAHecFVSPVARAVIELLEKSGVNLDGKKVLVLGAH---GPLEAALqcLFQRKD---S 242
Cdd:PRK14167 111 RIDPAKDVDGFHPENVGRLVAGDAR--FKPCTPHGIQKLLAAAGVDTEGADVVVVGRSdivGKPMANL--LIQKADggnA 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2327289797 243 MTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14167 187 TVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVID 231
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
71-287 |
8.15e-22 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 96.91 E-value: 8.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 71 IVREVIQNSKEVLSLLQEKnpAFKPVLAVIQAGDDNLLQE-VN--QNLAEEAGLNITHICLPPDSSEDEIIDEILKMNED 147
Cdd:PRK14175 11 IAKDYRQGLQDQVEALKEK--GFTPKLSVILVGNDGASQSyVRskKKAAEKIGMISEIVHLEETATEEEVLNELNRLNND 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 148 ARVHGLSLQVPENSLSS--KVLNALKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLG- 224
Cdd:PRK14175 89 DSVSGILVQVPLPKQVSeqKILEAINPEKDVDGFHPINIGKLYIDE--QTFVPCTPLGIMEILKHADIDLEGKNAVVIGr 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2327289797 225 AHGPLEAALQCLFQRKDSMTMSSQwKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14175 167 SHIVGQPVSKLLLQKNASVTILHS-RSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIID 228
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
95-287 |
2.07e-21 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 95.90 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 95 PVLAVIQAGDDNLlQEVNQNLAEEA----GLN--ITHicLPPDSSEDEIIDEILKMNEDARVHGLSLQ--VPENSLSSKV 166
Cdd:PRK14186 33 PGLAVLRVGDDPA-SAVYVRNKEKAcarvGIAsfGKH--LPADTSQAEVEALIAQLNQDERVDGILLQlpLPKHLDEVPL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 167 LNALKPEKDVDGVTDVNLGKLVRGDAHECFVSPVarAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMS 246
Cdd:PRK14186 110 LHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPA--GVMRLLRSQQIDIAGKKAVVVGRSILVGKPLALMLLAANATVTI 187
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2327289797 247 SQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14186 188 AHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVD 228
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
94-286 |
3.21e-21 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 94.98 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 94 KPVLAVIQAGDDNLLQ-EVN--QNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ--VPENSLSSKVLN 168
Cdd:PRK10792 33 APGLAVVLVGSDPASQvYVAskRKACEEVGFVSRSYDLPETTSEAELLALIDELNADPTIDGILVQlpLPAHIDNVKVLE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 169 ALKPEKDVDGVTDVNLGKLvrgdaheCFVSPVARA-----VIELLEKSGVNLDGKKVLVLGAHG----PLeaALQCLFQR 239
Cdd:PRK10792 113 RIHPDKDVDGFHPYNVGRL-------AQRIPLLRPctprgIMTLLERYGIDTYGLNAVVVGASNivgrPM--SLELLLAG 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2327289797 240 kdSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVL 286
Cdd:PRK10792 184 --CTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVI 228
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
79-287 |
2.50e-20 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 92.45 E-value: 2.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 79 SKEVLSLLQEKNpafKPVLAVIQAGDDNLLQEV---NQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSL 155
Cdd:PRK14170 19 TREVAELVKEGK---KPGLAVVLVGDNQASRTYvrnKQKRTEEAGMKSVLIELPENVTEEKLLSVVEELNEDKTIHGILV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 156 QVP--ENSLSSKVLNALKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAAL 233
Cdd:PRK14170 96 QLPlpEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGK--DSFVPCTPAGIIELIKSTGTQIEGKRAVVIGRSNIVGKPV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2327289797 234 QCLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14170 174 AQLLLNENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVID 227
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
95-290 |
4.27e-20 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 91.45 E-value: 4.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 95 PVLAVIQAGDD---NLLQEVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ--VPENSLSSKVLNA 169
Cdd:PRK14192 34 PILATILVGDDpasATYVRMKGNACRRVGMDSLKVELPQETTTEQLLAKIEELNANPDVHGILLQhpVPAQIDERACFDA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 170 LKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAAL-QCLFQRKDSMTMSSQ 248
Cdd:PRK14192 114 ISLAKDVDGVTCLGFGRMAMGE--AAYGSATPAGIMRLLKAYNIELAGKHAVVVGRSAILGKPMaMMLLNANATVTICHS 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2327289797 249 wKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLNC-FH 290
Cdd:PRK14192 192 -RTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAgFH 233
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
95-287 |
5.34e-20 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 91.42 E-value: 5.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 95 PVLAVIQAGDDNLLQEVNQNLAE---EAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ--VPENSLSSKVLNA 169
Cdd:PRK14174 32 PGLTVIIVGEDPASQVYVRNKAKsckEIGMNSTVIELPADTTEEHLLKKIEDLNNDPDVHGILVQqpLPKQIDEFAVTLA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 170 LKPEKDVDGVTDVNLGKLVRGDAHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHG----PL-EAALQCLFQRKDSMT 244
Cdd:PRK14174 112 IDPAKDVDGFHPENLGRLVMGHLDKCFVSCTPYGILELLGRYNIETKGKHCVVVGRSNivgkPMaNLMLQKLKESNCTVT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2327289797 245 MSSQwKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14174 192 ICHS-ATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVID 233
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
172-288 |
4.47e-19 |
|
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: 85.30 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 172 PEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHG----PLeAALqcLFQRKDSMTMSS 247
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGR--PGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNivgkPL-AAL--LLNRNATVTVCH 75
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2327289797 248 QwKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLNC 288
Cdd:cd01080 76 S-KTKNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDV 115
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
80-287 |
5.10e-19 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 88.35 E-value: 5.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 80 KEVLSLLQEKNpaFKPVLAVIQAGDDNLLQ---EVNQNLAEEAGL-NITHIcLPPDSSEDEIIDEILKMNEDARVHGLSL 155
Cdd:PRK14183 19 KEVDELKLVKN--IVPGLAVILVGDDPASHtyvKMKAKACDRVGIySITHE-MPSTISQKEILETIAMMNNNPNIDGILV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 156 Q--VPENSLSSKVLNALKPEKDVDGVTDVNLGKLVRGdaHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAAL 233
Cdd:PRK14183 96 QlpLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTG--LDGFVPCTPLGVMELLEEYEIDVKGKDVCVVGASNIVGKPM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2327289797 234 QCLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14183 174 AALLLNANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVID 227
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
95-287 |
2.01e-18 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 86.74 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 95 PVLAVIQAGDDNLLQE-VN--QNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQVP--ENSLSSKVLNA 169
Cdd:PRK14191 32 PKLAVILVGKDPASQTyVNmkIKACERVGMDSDLHTLQENTTEAELLSLIKDLNTDQNIDGILVQLPlpRHIDTKMVLEA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 170 LKPEKDVDGVTDVNLGKLVRGdaHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMSSQW 249
Cdd:PRK14191 112 IDPNKDVDGFHPLNIGKLCSQ--LDGFVPATPMGVMRLLKHYHIEIKGKDVVIIGASNIVGKPLAMLMLNAGASVSVCHI 189
|
170 180 190
....*....|....*....|....*....|....*...
gi 2327289797 250 KTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14191 190 LTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVD 227
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
80-287 |
2.03e-18 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 86.73 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 80 KEVLSLLQEKnpAFKPVLAVIQAGDDNLLQEVNQN---LAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ 156
Cdd:PRK14179 20 EKVAKLKEEK--GIVPGLVVILVGDNPASQVYVRNkerSALAAGFKSEVVRLPETISQEELLDLIERYNQDPTWHGILVQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 157 --VPENSLSSKVLNALKPEKDVDGVTDVNLGKLVRGdaHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQ 234
Cdd:PRK14179 98 lpLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSG--RPVMIPCTPAGIMEMFREYNVELEGKHAVVIGRSNIVGKPMA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2327289797 235 CLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14179 176 QLLLDKNATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVID 228
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
72-287 |
2.18e-18 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 86.57 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 72 VREVIQNskEVLSLLQEKNPAFK--PVLAVIQAGDdNLLQEVNQNL----AEEAGLNITHICLPPDSSEDEIIDEILKMN 145
Cdd:PRK14177 11 LSEKIRN--EIRETIEERKTKNKriPKLATILVGN-NPASETYVSMkvkaCHKVGMGSEMIRLKEQTTTEELLGVIDKLN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 146 EDARVHGLSLQ--VPENSLSSKVLNALKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVL 223
Cdd:PRK14177 88 LDPNVDGILLQhpVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGV--ETYLPCTPYGMVLLLKEYGIDVTGKNAVVV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2327289797 224 GAHGPLEAALQCLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14177 166 GRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLD 229
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
74-287 |
3.07e-18 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 86.22 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 74 EVIQNSKEVLSLLQEKnpAFKPVLAVIQAGDDNLLQE-VNQNLAEEAGLNITHIC--LPPDSSEDEIIDEILKMNEDARV 150
Cdd:PRK14193 14 EIKADLAERVAALKEK--GITPGLGTVLVGDDPGSQAyVRGKHRDCAEVGITSIRrdLPADATQEELNAVIDELNADPAC 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 151 HGLSLQVP------ENslssKVLNALKPEKDVDGVTDVNLGKLVRGDAHECFVSPvaRAVIELLEKSGVNLDGKKVLVLG 224
Cdd:PRK14193 92 TGYIVQLPlpkhldEN----AVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTP--RGIVHLLRRYDVELAGAHVVVIG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2327289797 225 AHGPLEAALQCLFQRK--DSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14193 166 RGVTVGRPIGLLLTRRseNATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLD 230
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
128-287 |
5.89e-18 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 85.70 E-value: 5.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 128 LPPDSSEDEIIDEILKMNEDARVHGLSLQ--VPENSLSSKVLNALKPEKDVDGVTDVNLGKLVRGDAHECFVSPVARAVI 205
Cdd:PRK14168 70 QSVDITEEELLALIDKYNNDDSIHGILVQlpLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIGGDEVKFLPCTPAGIQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 206 ELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRK----DSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRP 281
Cdd:PRK14168 150 EMLVRSGVETSGAEVVVVGRSNIVGKPIANMMTQKgpgaNATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKP 229
|
....*.
gi 2327289797 282 GTTVLN 287
Cdd:PRK14168 230 GATVID 235
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
87-177 |
6.99e-18 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 80.14 E-value: 6.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 87 QEKNPAFKPVLAVIQAGDD--------NLlqevnQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ-- 156
Cdd:pfam00763 20 ALKAGGRKPGLAVILVGDDpasqvyvrNK-----KKACEEVGIESELIRLPEDTTEEELLALIDKLNADPSVHGILVQlp 94
|
90 100
....*....|....*....|.
gi 2327289797 157 VPENSLSSKVLNALKPEKDVD 177
Cdd:pfam00763 95 LPKHIDEEKVLEAIDPEKDVD 115
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
94-287 |
1.10e-17 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 84.35 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 94 KPVLAVIQAGDDNLLQEVNQNLA---EEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ--VPENSLSSKVLN 168
Cdd:PRK14189 32 QPGLAVILVGDNPASQVYVRNKVkacEDNGFHSLKDRYPADLSEAELLARIDELNRDPKIHGILVQlpLPKHIDSHKVIE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 169 ALKPEKDVDGVTDVNLGKLVRGdaHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAH---GPLEAALqcLFQRKDSMTM 245
Cdd:PRK14189 112 AIAPEKDVDGFHVANAGALMTG--QPLFRPCTPYGVMKMLESIGIPLRGAHAVVIGRSnivGKPMAML--LLQAGATVTI 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2327289797 246 SSQwKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14189 188 CHS-KTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVID 228
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
92-287 |
1.77e-17 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 83.93 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 92 AFKPVLAVIQAGDDNLLQ---EVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQVP--ENSLSSKV 166
Cdd:PRK14180 29 AITPKLVAIIVGNDPASKtyvASKEKACAQVGIDSQVITLPEHTTESELLELIDQLNNDSSVHAILVQLPlpAHINKNNV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 167 LNALKPEKDVDGVTDVNLGKLVRGDaHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPL-EAALQCLFQRKDSMTM 245
Cdd:PRK14180 109 IYSIKPEKDVDGFHPTNVGRLQLRD-KKCLESCTPKGIMTMLREYGIKTEGAYAVVVGASNVVgKPVSQLLLNAKATVTT 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2327289797 246 SSQWkTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14180 188 CHRF-TTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVID 228
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
80-287 |
2.47e-17 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 83.67 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 80 KEVLSLLQEKNPAfkPVLAVIQAGDDNLLQEVNQN---LAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ 156
Cdd:PRK14184 19 TEVAALTARHGRA--PGLAVILVGEDPASQVYVRNkerACEDAGIVSEAFRLPADTTQEELEDLIAELNARPDIDGILLQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 157 VP--ENSLSSKVLNALKPEKDVDGVTDVNLGKLVRGdaHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHG----PLE 230
Cdd:PRK14184 97 LPlpKGLDSQRCLELIDPAKDVDGFHPENMGRLALG--LPGFRPCTPAGVMTLLERYGLSPAGKKAVVVGRSNivgkPLA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2327289797 231 AALQCLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14184 175 LMLGAPGKFANATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVD 231
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
88-287 |
2.86e-17 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 83.32 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 88 EKNPAFKPVLAVIQAGDD---NLLQEVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQVP--ENSL 162
Cdd:PRK14176 32 KSNRGITPGLATILVGDDpasKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELIDSLNKRKDVHGILLQLPlpKHLD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 163 SSKVLNALKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDS 242
Cdd:PRK14176 112 PQEAMEAIDPAKDADGFHPYNMGKLMIGD--EGLVPCTPHGVIRALEEYGVDIEGKNAVIVGHSNVVGKPMAAMLLNRNA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2327289797 243 MTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14176 190 TVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFD 234
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
89-287 |
4.05e-17 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 83.36 E-value: 4.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 89 KNPAFKPVLAVIQAGDDNLLQEVNQN---LAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQVPENSL--S 163
Cdd:PRK14194 28 KAAGIEPALAVILVGNDPASQVYVRNkilRAEEAGIRSLEHRLPADTSQARLLALIAELNADPSVNGILLQLPLPAHidE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 164 SKVLNALKPEKDVDGVTDVNLGKLVRGDAHECFVSPvaRAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSM 243
Cdd:PRK14194 108 ARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTP--SGCLRLLEDTCGDLTGKHAVVIGRSNIVGKPMAALLLQAHCS 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2327289797 244 TMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14194 186 VTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVID 229
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
94-286 |
2.76e-16 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 80.77 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 94 KPVLAVIQAGDDNLLQEVNQN---LAEEAGLN-ITHIcLPPDSSEDEIIDEILKMNEDARVHGLSLQ--VPENSLSSKVL 167
Cdd:PRK14188 32 TPGLAVVLVGEDPASQVYVRSkgkQTKEAGMAsFEHK-LPADTSQAELLALIARLNADPAIHGILVQlpLPKHLDSEAVI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 168 NALKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLGAH---GPLEAALqcLFQRKDSMT 244
Cdd:PRK14188 111 QAIDPEKDVDGLHVVNAGRLATGE--TALVPCTPLGCMMLLRRVHGDLSGLNAVVIGRSnlvGKPMAQL--LLAANATVT 186
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2327289797 245 MSSQwKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVL 286
Cdd:PRK14188 187 IAHS-RTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVI 227
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
94-287 |
8.14e-16 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 79.10 E-value: 8.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 94 KPVLAVIQAGDDNLLQEVNQN---LAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQVP--ENSLSSKVLN 168
Cdd:PRK14185 31 RPHLAAILVGHDGGSETYVANkvkACEECGFKSSLIRYESDVTEEELLAKVRELNQDDDVDGFIVQLPlpKHISEQKVIE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 169 ALKPEKDVDGVTDVNLGKLVRGdaHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRK----DSMT 244
Cdd:PRK14185 111 AIDYRKDVDGFHPINVGRMSIG--LPCFVSATPNGILELLKRYHIETSGKKCVVLGRSNIVGKPMAQLMMQKaypgDCTV 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2327289797 245 MSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14185 189 TVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVID 231
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
70-287 |
1.38e-15 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 78.46 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 70 SIVREVIQNSKEVLSLLQEKNPAfKPVLAVIQAGDD--NLLQEVNQ-NLAEEAGLNITHICLPPDSSEDEIIDEILKMNE 146
Cdd:PRK14171 9 ALANEILADLKLEIQELKSQTNA-SPKLAIVLVGDNpaSIIYVKNKiKNAHKIGIDTLLVNLSTTIHTNDLISKINELNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 147 DARVHGLSLQVP-ENSL-SSKVLNALKPEKDVDGVTDVNLGKLVRGdAHECFVSPVARAVIELLEKSGVNLDGKKVLVLG 224
Cdd:PRK14171 88 DNEISGIIVQLPlPSSIdKNKILSAVSPSKDIDGFHPLNVGYLHSG-ISQGFIPCTALGCLAVIKKYEPNLTGKNVVIIG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2327289797 225 AHGPLEAALQCLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14171 167 RSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVID 229
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
79-287 |
1.51e-15 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 77.96 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 79 SKEVLSLLQEK--NPAFKPVLAVIQAGDD---NLLQEVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGL 153
Cdd:PRK14178 9 SEKRLELLKEEiiESGLYPRLATVIVGDDpasQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIRRLNEDPDINGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 154 SLQVP--ENSLSSKVLNALKPEKDVDGVTDVNLGKLVRGDAHECFVSPvaRAVIELLEKSGVNLDGKKVLVLGAHGPLEA 231
Cdd:PRK14178 89 LVQLPlpKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTP--NGIMTLLHEYKISIAGKRAVVVGRSIDVGR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2327289797 232 ALQCLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14178 167 PMAALLLNADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVID 222
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
94-287 |
6.75e-15 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 76.21 E-value: 6.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 94 KPVLAVIQAGDD---NLLQEVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQVP--ENSLSSKVLN 168
Cdd:PRK14182 30 QTGLTVVRVGDDpasAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIARLNADPAVHGILVQLPlpKHVDERAVLD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 169 ALKPEKDVDGVTDVNLGKL---VRGDAHECfvSPVAraVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTM 245
Cdd:PRK14182 110 AISPAKDADGFHPFNVGALsigIAGVPRPC--TPAG--VMRMLDEARVDPKGKRALVVGRSNIVGKPMAMMLLERHATVT 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2327289797 246 SSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14182 186 IAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVID 227
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
79-287 |
6.38e-14 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 73.14 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 79 SKEVLSLLQEKNPAFK-----PVLAVIQAGDDNLLQEVNQNLA---EEAGLNITHICLPPDSSEDEIIDEILKMNEDARV 150
Cdd:PRK14166 10 SAKIKEELKEKNQFLKskgieSCLAVILVGDNPASQTYVKSKAkacEECGIKSLVYHLNENTTQNELLALINTLNHDDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 151 HGLSLQVPENSLSSK--VLNALKPEKDVDGVTDVNLGKLVRGdAHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGP 228
Cdd:PRK14166 90 HGILVQLPLPDHICKdlILESIISSKDVDGFHPINVGYLNLG-LESGFLPCTPLGVMKLLKAYEIDLEGKDAVIIGASNI 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2327289797 229 LEAALQCLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14166 169 VGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVD 227
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
66-269 |
6.54e-13 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 70.28 E-value: 6.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 66 PARDSIVREVIQNSKevlsllqekNPAFKPVLAVIQAGDDNLlQEVNQNLAEEAGLNITHIC----LPPDSSEDEIIDEI 141
Cdd:PRK14181 7 PAAEHILATIKENIS---------ASSTAPGLAVVLIGNDPA-SEVYVGMKVKKATDLGMVSkahrLPSDATLSDILKLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 142 LKMNEDARVHGLSLQVP--ENSLSSKVLNALKPEKDVDGVTDVNLGKLVRGDAhECFVSPVARAVIELLEKSGVNLDGKK 219
Cdd:PRK14181 77 HRLNNDPNIHGILVQLPlpKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGET-DGFIPCTPAGIIELLKYYEIPLHGRH 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2327289797 220 VLVLGAHGPLEAALQCLFQRKDSMTMSS----QWKTPQLESKLQEADIVI--LGSP 269
Cdd:PRK14181 156 VAIVGRSNIVGKPLAALLMQKHPDTNATvtllHSQSENLTEILKTADIIIaaIGVP 211
|
|
| NAD_bind_m-THF_DH |
cd01079 |
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ... |
172-287 |
4.40e-03 |
|
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of methylene-tetrahydrofolate dehydrogenase (m-THF DH). M-THF is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. M-THF DH is a component of an unusual monofunctional enzyme; in eukaryotes, m-THF DH is typically found as part of a multifunctional protein. NADP-dependent m-THF DHs in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofunctional DH, as well as bifunctional DH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains only the monofunctional DHs from S. cerevisiae and certain bacteria. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133447 [Multi-domain] Cd Length: 197 Bit Score: 39.33 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 172 PEKDVDGVTDVNLGKLVrgdAHECFVSPVAR----------AVIELLEKSGV---------NLDGKKVLVLGAHG----P 228
Cdd:cd01079 1 PHKDVEGLSHKYIFNLY---HNIRFLDPENRkksilpctplAIVKILEFLGIynkilpygnRLYGKTITIINRSEvvgrP 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2327289797 229 LEAAL---------------QClFQRKDSMTMSSQW---KTPQLESKLQEADIVILGSPKPE-KIPVAWIRPGTTVLN 287
Cdd:cd01079 78 LAALLandgarvysvdingiQV-FTRGESIRHEKHHvtdEEAMTLDCLSQSDVVITGVPSPNyKVPTELLKDGAICIN 154
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