|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
351-977 |
0e+00 |
|
Formate--tetrahydrofolate ligase
Pssm-ID: 178359 Cd Length: 637 Bit Score: 1021.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 351 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSLLERLKDQTDGKYVLVAGITPTPLGEGKST 430
Cdd:PLN02759 9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 431 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRIFHES 510
Cdd:PLN02759 89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 511 TQTDKALYNRLVPL-VNGVRKFSEIQLSRLKKLGIHKTDPTALTEEEVRKFTRLNIDPSTITWQRVLDTNDRFLRKITIG 589
Cdd:PLN02759 169 TQSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 590 QGSTEKGYSRQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTL 669
Cdd:PLN02759 249 QGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 670 EGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMH 749
Cdd:PLN02759 329 EGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMH 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 750 GGGPSVTAGVPLKKEYTEENIQLVADGCCNLQKQIQIAQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYH 829
Cdd:PLN02759 409 GGGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTH 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 830 WSAGGKGSVDLARAVREAANKRSR-FRFLYDVQLPIVAKIRVIAQTVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAK 908
Cdd:PLN02759 489 HAHGGKGAVDLGEAVQKACEGNSQpFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAK 568
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313151179 909 THLSLSHEPDKKGVPRDFILPISDVRASIGAGFIYPLVGMMSTMPGLPTRPCFYDIDLDTETEQVKGLF 977
Cdd:PLN02759 569 TQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTETGKVLGLS 637
|
|
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
359-977 |
0e+00 |
|
Formate--tetrahydrofolate ligase;
Pssm-ID: 460143 Cd Length: 555 Bit Score: 990.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 359 PSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSLLERLKDQTDGKYVLVAGITPTPLGEGKSTVTIGLVQA 438
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 439 LtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRIFHESTqtdkaly 518
Cdd:pfam01268 81 L-NRLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 519 nrlvplvngvrkfseiqlsrlkklgihktdptalteeevrkftrLNIDPSTITWQRVLDTNDRFLRKITIGQGSTEKGYS 598
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 599 RQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHA 678
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 679 GPFANIAHGNSSVLADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGgpsvtag 758
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGG------- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 759 vPLKKEYTEENIQLVADGCCNLQKQIQIAQLFGVPVVVALNVFKTDTRAEIDLVCELAKrAGAFDAVPCYHWSAGGKGSV 838
Cdd:pfam01268 339 -VGKDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRELCE-AGGVDAALSEHWAKGGEGAI 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 839 DLARAVREAANKR-SRFRFLYDVQLPIVAKIRVIAQTVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHEP 917
Cdd:pfam01268 417 ELAEAVVEACEEEpSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 918 DKKGVPRDFILPISDVRASIGAGFIYPLVGMMSTMPGLPTRPCFYDIDLDTEtEQVKGLF 977
Cdd:pfam01268 497 KLKGAPTGFTLPVRDVRLSAGAGFIVALTGDIMTMPGLPKRPAAENIDVDED-GKITGLF 555
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
373-976 |
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: 937.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 373 VDVLAKEIGLLADEIEIYGKSKAKVRLSLLERLKDQTDGKYVLVAGITPTPLGEGKSTVTIGLVQALTAHLNvNSFACLR 452
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 453 QPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRIFHESTqtdkalynrlvplvngvrkfs 532
Cdd:cd00477 80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 533 eiqlsrlkklgihktdptalteeevrkftrLNIDPSTITWQRVLDTNDRFLRKITIGQGSTEKGYSRQAQFDIAVASEIM 612
Cdd:cd00477 139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 613 AVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSVL 692
Cdd:cd00477 189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 693 ADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGvplkkeytEENIQL 772
Cdd:cd00477 269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 773 VADGCCNLQKQIQIAQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVpCYHWSAGGKGSVDLARAVREAANK-R 851
Cdd:cd00477 338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKpK 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 852 SRFRFLYDVQLPIVAKIRVIAQTVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHEPDKKGVPRDFILPIS 931
Cdd:cd00477 417 SNFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 313151179 932 DVRASIGAGFIYPLVGMMSTMPGLPTRPCFYDIDLDtETEQVKGL 976
Cdd:cd00477 497 DVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDID-DTGKIEGL 540
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
358-977 |
0e+00 |
|
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
Pssm-ID: 442046 Cd Length: 556 Bit Score: 882.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 358 VPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSLLERLKDQTDGKYVLVAGITPTPLGEGKSTVTIGLVQ 437
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 438 ALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRIFHEStqtdkal 517
Cdd:COG2759 81 AL-NRLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQGN------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 518 ynrlvplvngvrkfseiqlsrlkklgihktdptalteeevrkftRLNIDPSTITWQRVLDTNDRFLRKITIGQGSTEKGY 597
Cdd:COG2759 153 --------------------------------------------ELNIDPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 598 SRQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVH 677
Cdd:COG2759 189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 678 AGPFANIAHGNSSVLADKIALKLvGEegFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPsvta 757
Cdd:COG2759 269 GGPFANIAHGCNSVIATKLALKL-AD--YVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 758 gvplKKEYTEENIQLVADGCCNLQKQIQIAQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAfDAVPCYHWSAGGKGS 837
Cdd:COG2759 342 ----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEGA 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 838 VDLARAVREAANKR-SRFRFLYDVQLPIVAKIRVIAQTVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHE 916
Cdd:COG2759 417 EELAEAVVEACEEGpSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSDD 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 313151179 917 PDKKGVPRDFILPISDVRASIGAGFIYPLVGMMSTMPGLPTRPCFYDIDLDtETEQVKGLF 977
Cdd:COG2759 497 PKLLGAPTGFTLTVREVRLSAGAGFIVALTGDIMTMPGLPKVPAAERIDID-EDGKITGLF 556
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
192-334 |
3.28e-46 |
|
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: 162.29 E-value: 3.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 192 GDAPECFVSPLARAAVELIEKSGITLDGKKVLVIGAHGPLEAALQCLFQRKGSMTMSSPWITPQLQDKLREADIVVLGSP 271
Cdd:cd05212 1 GPCTPLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313151179 272 KPDEIPAAWIPSGATMLNCFHDFLSGKLRGGSPGVPMNRLIAdesVSLLAAALRVQNMVNSGR 334
Cdd:cd05212 81 KPEKVPTEWIKPGATVINCSPTKLSGDDVKESASLYVPMTGG---VGKLTVAMRMQNMVRSVR 140
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
182-337 |
4.35e-40 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 145.30 E-value: 4.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 182 TDVNLGKLVRGdaPECFVSPLARAAVELIEKSGITLDGKKVLVIGAHGPLEAALQCLFQRKGSMTMSSPWITPQLQDKLR 261
Cdd:pfam02882 1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 262 EADIVVLGSPKPDEIPAAWIPSGATMLNCFHDFLS-GKLRGGSPGVPMNRLIA-----DESVSLLAAALRVQNMVNSGRR 335
Cdd:pfam02882 79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRVGnGKLVGDVDFENVKEKASaitpvPGGVGPMTVAMLLQNTVEAAKR 158
|
..
gi 313151179 336 WL 337
Cdd:pfam02882 159 QL 160
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
96-286 |
2.47e-32 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 127.44 E-value: 2.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 96 KPVLAVIQAGDD---HLMQNVNQNLAKEAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGLALQ------ISEdslcN 166
Cdd:COG0190 32 TPGLAVVLVGDDpasQVYVRNKHKACEEVGIESELIRLPADTTQEELLALIDELNADPSVHGILVQlplpkhIDE----E 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 167 KVLNALKPEKDVDGVTDVNLGKLVRGDapECFVSPLARAAVELIEKSGITLDGKKVLVIGaHG-----PLeAALqcLFQR 241
Cdd:COG0190 108 AVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLERYGIDLAGKHAVVVG-RSnivgkPL-ALL--LLRR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 313151179 242 KGSMTM--SSpwiTPQLQDKLREADIVVLGSPKPDEIPAAWIPSGAT 286
Cdd:COG0190 182 NATVTVchSR---TKDLAEHTRQADILVAAVGKPGLITADMVKPGAV 225
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
77-301 |
4.75e-27 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 112.03 E-value: 4.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 77 VIHNSKEVLNLLQE---------KNPAFKPVLAVIQAGDD---HLMQNVNQNLAKEAGLDITHICLPPDSGEDEIIDEIL 144
Cdd:PRK14190 4 VIIDGKEVAKEKREqlkeevvklKEQGIVPGLAVILVGDDpasHSYVRGKKKAAEKVGIYSELYEFPADITEEELLALID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 145 KINEDPRVHGLALQ------ISEDslcnKVLNALKPEKDVDGVTDVNLGKLVRGDapECFVSPLARAAVELIEKSGITLD 218
Cdd:PRK14190 84 RLNADPRINGILVQlplpkhIDEK----AVIERISPEKDVDGFHPINVGRMMLGQ--DTFLPCTPHGILELLKEYNIDIS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 219 GKKVLVIGAHGPLEAALQCLFQRK-GSMTMSSPWiTPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATML----NCFHD 293
Cdd:PRK14190 158 GKHVVVVGRSNIVGKPVGQLLLNEnATVTYCHSK-TKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIdvgvNRLEN 236
|
....*...
gi 313151179 294 flsGKLRG 301
Cdd:PRK14190 237 ---GKLCG 241
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
97-289 |
4.33e-23 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 101.96 E-value: 4.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 97 PVLAVIQAGDDHLMQNVNQNLAK---EAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGLALQISEDSLCN--KVLNA 171
Cdd:PLN02897 87 PGLAVVLVGQQRDSQTYVRNKIKaceETGIKSLLAELPEDCTEGQILSALRKFNEDTSIHGILVQLPLPQHLDesKILNM 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 172 LKPEKDVDGVTDVNLGKL-VRGDAPeCFVSPLARAAVELIEKSGITLDGKKVLVIGAHGPLEAALQCLFQRKGSMTMSSP 250
Cdd:PLN02897 167 VRLEKDVDGFHPLNVGNLaMRGREP-LFVSCTPKGCVELLIRSGVEIAGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVH 245
|
170 180 190
....*....|....*....|....*....|....*....
gi 313151179 251 WITPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLN 289
Cdd:PLN02897 246 AFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVID 284
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
81-179 |
2.81e-17 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 78.60 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 81 SKEVLNLLQE-----KNPAFKPVLAVIQAGDD---HLMQNVNQNLAKEAGLDITHICLPPDSGEDEIIDEILKINEDPRV 152
Cdd:pfam00763 7 AKKIREELKEevaalKAGGRKPGLAVILVGDDpasQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKLNADPSV 86
|
90 100 110
....*....|....*....|....*....|...
gi 313151179 153 HGLALQ------ISEdslcNKVLNALKPEKDVD 179
Cdd:pfam00763 87 HGILVQlplpkhIDE----EKVLEAIDPEKDVD 115
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
351-977 |
0e+00 |
|
Formate--tetrahydrofolate ligase
Pssm-ID: 178359 Cd Length: 637 Bit Score: 1021.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 351 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSLLERLKDQTDGKYVLVAGITPTPLGEGKST 430
Cdd:PLN02759 9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 431 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRIFHES 510
Cdd:PLN02759 89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 511 TQTDKALYNRLVPL-VNGVRKFSEIQLSRLKKLGIHKTDPTALTEEEVRKFTRLNIDPSTITWQRVLDTNDRFLRKITIG 589
Cdd:PLN02759 169 TQSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 590 QGSTEKGYSRQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTL 669
Cdd:PLN02759 249 QGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 670 EGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMH 749
Cdd:PLN02759 329 EGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMH 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 750 GGGPSVTAGVPLKKEYTEENIQLVADGCCNLQKQIQIAQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYH 829
Cdd:PLN02759 409 GGGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTH 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 830 WSAGGKGSVDLARAVREAANKRSR-FRFLYDVQLPIVAKIRVIAQTVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAK 908
Cdd:PLN02759 489 HAHGGKGAVDLGEAVQKACEGNSQpFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAK 568
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313151179 909 THLSLSHEPDKKGVPRDFILPISDVRASIGAGFIYPLVGMMSTMPGLPTRPCFYDIDLDTETEQVKGLF 977
Cdd:PLN02759 569 TQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTETGKVLGLS 637
|
|
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
359-977 |
0e+00 |
|
Formate--tetrahydrofolate ligase;
Pssm-ID: 460143 Cd Length: 555 Bit Score: 990.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 359 PSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSLLERLKDQTDGKYVLVAGITPTPLGEGKSTVTIGLVQA 438
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 439 LtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRIFHESTqtdkaly 518
Cdd:pfam01268 81 L-NRLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 519 nrlvplvngvrkfseiqlsrlkklgihktdptalteeevrkftrLNIDPSTITWQRVLDTNDRFLRKITIGQGSTEKGYS 598
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 599 RQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHA 678
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 679 GPFANIAHGNSSVLADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGgpsvtag 758
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGG------- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 759 vPLKKEYTEENIQLVADGCCNLQKQIQIAQLFGVPVVVALNVFKTDTRAEIDLVCELAKrAGAFDAVPCYHWSAGGKGSV 838
Cdd:pfam01268 339 -VGKDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRELCE-AGGVDAALSEHWAKGGEGAI 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 839 DLARAVREAANKR-SRFRFLYDVQLPIVAKIRVIAQTVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHEP 917
Cdd:pfam01268 417 ELAEAVVEACEEEpSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 918 DKKGVPRDFILPISDVRASIGAGFIYPLVGMMSTMPGLPTRPCFYDIDLDTEtEQVKGLF 977
Cdd:pfam01268 497 KLKGAPTGFTLPVRDVRLSAGAGFIVALTGDIMTMPGLPKRPAAENIDVDED-GKITGLF 555
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
373-976 |
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: 937.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 373 VDVLAKEIGLLADEIEIYGKSKAKVRLSLLERLKDQTDGKYVLVAGITPTPLGEGKSTVTIGLVQALTAHLNvNSFACLR 452
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 453 QPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRIFHESTqtdkalynrlvplvngvrkfs 532
Cdd:cd00477 80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 533 eiqlsrlkklgihktdptalteeevrkftrLNIDPSTITWQRVLDTNDRFLRKITIGQGSTEKGYSRQAQFDIAVASEIM 612
Cdd:cd00477 139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 613 AVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSVL 692
Cdd:cd00477 189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 693 ADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGvplkkeytEENIQL 772
Cdd:cd00477 269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 773 VADGCCNLQKQIQIAQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVpCYHWSAGGKGSVDLARAVREAANK-R 851
Cdd:cd00477 338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKpK 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 852 SRFRFLYDVQLPIVAKIRVIAQTVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHEPDKKGVPRDFILPIS 931
Cdd:cd00477 417 SNFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 313151179 932 DVRASIGAGFIYPLVGMMSTMPGLPTRPCFYDIDLDtETEQVKGL 976
Cdd:cd00477 497 DVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDID-DTGKIEGL 540
|
|
| PTZ00386 |
PTZ00386 |
formyl tetrahydrofolate synthetase; Provisional |
351-976 |
0e+00 |
|
formyl tetrahydrofolate synthetase; Provisional
Pssm-ID: 240394 Cd Length: 625 Bit Score: 920.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 351 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSLLERLKDQTDGKYVLVAGITPTPLGEGKST 430
Cdd:PTZ00386 8 KLSCQWPVPSDIDIAQSVKPQPITSVAESAGILLSELDPYGSTRAKVKLSVLKRLENSPNGKYVVVAGMNPTPLGEGKST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 431 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRIFHES 510
Cdd:PTZ00386 88 TTIGLAQSLGAHLHRKTFACIRQPSQGPTFGIKGGAAGGGYSQVIPMEDFNLHGTGDIHAITAANNLLAAALDTRIFHER 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 511 TQTDKALYNRLVplvNGVRKFSEIQLSRLKKLGIHKTDPTALTEEEVRKFTRLNIDPSTITWQRVLDTNDRFLRKITIGQ 590
Cdd:PTZ00386 168 TQSDAALYRRLT---DELKKFTPIMLKRLEKLGISKTDPKQLTEEERVRFARLDIDPDTISWRRVTDVNDRMLREITIGQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 591 GSTEKGYSRQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLE 670
Cdd:PTZ00386 245 GKEEKGITRKTGFDISVASEVMAILALATDLADMRQRLGAIVVAKSKSGEPVTAEDLGCAGAMTVLMKDTIEPTLMQTLE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 671 GTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHG 750
Cdd:PTZ00386 325 GTPVLVHAGPFGNIAHGNSSIVADQIALKLAGQDGFVLTEAGFGADIGCEKFFNIKCRTSGLKPDAAVLVATVRALKFHG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 751 GGPSVTAGvplkkeytEENIQLVADGCCNLQKQIQIAQLFGVPVVVALNVFKTDTRAEIDLVCELA-KRAGAFDAVPCYH 829
Cdd:PTZ00386 405 GVEPVVAG--------KENLEAVRKGLSNLQRHIQNIRKFGVPVVVALNKFSTDTDAELELVKELAlQEGGAADVVVTDH 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 830 WSAGGKGSVDLARAVREAA-NKRSRFRFLYDVQLPIVAKIRVIAQTVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAK 908
Cdd:PTZ00386 477 WAKGGAGAVDLAQALIRVTeNVPSNFKLLYPLDASLKEKIETICKEIYGAAGVEYLNDADEKLEDFERMGYGKFPVCMAK 556
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 313151179 909 THLSLSHEPDKKGVPRDFILPISDVRASIGAGFIYPLVGMMSTMPGLPTRPCFYDIDLDTETEQVKGL 976
Cdd:PTZ00386 557 TQYSFSHDPELRGAPTGFTVPIRDVRVNCGAGFVFPLLGDISTMPGLPTRPAFYNIDIDCETGKIVGL 624
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
358-977 |
0e+00 |
|
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
Pssm-ID: 442046 Cd Length: 556 Bit Score: 882.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 358 VPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSLLERLKDQTDGKYVLVAGITPTPLGEGKSTVTIGLVQ 437
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 438 ALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRIFHEStqtdkal 517
Cdd:COG2759 81 AL-NRLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQGN------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 518 ynrlvplvngvrkfseiqlsrlkklgihktdptalteeevrkftRLNIDPSTITWQRVLDTNDRFLRKITIGQGSTEKGY 597
Cdd:COG2759 153 --------------------------------------------ELNIDPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 598 SRQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVH 677
Cdd:COG2759 189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 678 AGPFANIAHGNSSVLADKIALKLvGEegFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPsvta 757
Cdd:COG2759 269 GGPFANIAHGCNSVIATKLALKL-AD--YVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 758 gvplKKEYTEENIQLVADGCCNLQKQIQIAQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAfDAVPCYHWSAGGKGS 837
Cdd:COG2759 342 ----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEGA 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 838 VDLARAVREAANKR-SRFRFLYDVQLPIVAKIRVIAQTVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHE 916
Cdd:COG2759 417 EELAEAVVEACEEGpSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSDD 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 313151179 917 PDKKGVPRDFILPISDVRASIGAGFIYPLVGMMSTMPGLPTRPCFYDIDLDtETEQVKGLF 977
Cdd:COG2759 497 PKLLGAPTGFTLTVREVRLSAGAGFIVALTGDIMTMPGLPKVPAAERIDID-EDGKITGLF 556
|
|
| PRK13505 |
PRK13505 |
formate--tetrahydrofolate ligase; Provisional |
357-977 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237403 Cd Length: 557 Bit Score: 753.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 357 PVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSLLERLKDQTDGKYVLVAGITPTPLGEGKSTVTIGLV 436
Cdd:PRK13505 1 TMKSDIEIAQEATLKPITEIAAKLGIPEDDLEPYGKYKAKISLDKIKALKDKKDGKLILVTAINPTPAGEGKSTVTVGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 437 QALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRIFHESTqtdka 516
Cdd:PRK13505 81 DAL-NKIGKKTVIALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITSANNLLAALIDNHIHQGNE----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 517 lynrlvplvngvrkfseiqlsrlkklgihktdptalteeevrkftrLNIDPSTITWQRVLDTNDRFLRKITIGQGSTEKG 596
Cdd:PRK13505 155 ----------------------------------------------LGIDPRRITWKRVLDMNDRALRNIVVGLGGPANG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 597 YSRQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFV 676
Cdd:PRK13505 189 VPREDGFDITVASEIMAILCLATDLKDLKERLGRIVVGYTYDGKPVTVKDLKVEGAMALLLKDAIKPNLVQTLEGTPAFV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 677 HAGPFANIAHGNSSVLADKIALKLvGEegFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPsvt 756
Cdd:PRK13505 269 HGGPFANIAHGCNSVLATKTALKL-AD--YVVTEAGFGADLGAEKFLDIKCRKAGLKPDAVVIVATVRALKMHGGVA--- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 757 agvplKKEYTEENIQLVADGCCNLQKQIQIAQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAfDAVPCYHWSAGGKG 836
Cdd:PRK13505 343 -----KDDLKEENVEALKKGFANLERHIENIRKFGVPVVVAINKFVTDTDAEIAALKELCEELGV-EVALSEVWAKGGEG 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 837 SVDLARAVREAA-NKRSRFRFLYDVQLPIVAKIRVIAQTVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSH 915
Cdd:PRK13505 417 GVELAEKVVELIeEGESNFKPLYDDEDSLEEKIEKIATKIYGAKGVEFSPKAKKQLKQIEKNGWDKLPVCMAKTQYSFSD 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 313151179 916 EPDKKGVPRDFILPISDVRASIGAGFIYPLVGMMSTMPGLPTRPCFYDIDLDtETEQVKGLF 977
Cdd:PRK13505 497 DPKLLGAPTGFTITVRELRPSAGAGFIVALTGDIMTMPGLPKVPAALNIDVD-EDGNIVGLF 557
|
|
| PRK13506 |
PRK13506 |
formate--tetrahydrofolate ligase; Provisional |
360-976 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237404 Cd Length: 578 Bit Score: 717.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 360 SDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSLLERLKDQTDGKYVLVAGITPTPLGEGKSTVTIGLVQAL 439
Cdd:PRK13506 3 SDIEISRQAPLKPIAEIAAKLGLLPDELSPFGHTKAKVSLSVLKRLADKPKGKLVLVTAITPTPLGEGKTVTTIGLTQGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 440 tAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRIFHEStqtdkalyn 519
Cdd:PRK13506 83 -NALGQKVCACIRQPSMGPVFGVKGGAAGGGYAQVVPMEELNLHLTGDIHAVSAAHNLAAAAIDARLFHEQ--------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 520 RLvplvnGVRKFSEiqlsrlkklgihKTDptalteeevrkFTRLNIDPSTITWQRVLDTNDRFLRKITIGQGSTEKGYSR 599
Cdd:PRK13506 153 RL-----GYDAFEA------------QSG-----------LPALDIDPEQILWKRVVDHNDRALRMITVGLGENGNGPER 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 600 QAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAG 679
Cdd:PRK13506 205 EDGFDITAASELMAILALSRDLKDMRQRIGRLVLAYNLQGQPITAEDLGVAGAMTVIMKDAIEPTLMQTLEGVPCLIHAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 680 PFANIAHGNSSVLADKIALKLVGeegFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGV 759
Cdd:PRK13506 285 PFANIAHGNSSIIADRIALKLAD---YVVTEGGFGSDMGFEKFCNIKARQSGKAPDCAVLVATLRALKANSGLYDLRPGQ 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 760 PLKKEYTEENIQLVADGCCNLQKQIQIAQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYHWSAGGKGSVD 839
Cdd:PRK13506 362 ALPDSINAPDQARLEAGFANLKWHINNVAQYGLPVVVAINRFPTDTDEELEWLKEAVLLTGAFGCEISEAFAQGGEGATA 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 840 LARAVREAANKRSRFRFLYDVQLPIVAKIRVIAQTVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHEPDK 919
Cdd:PRK13506 442 LAQAVVRACEQPSQFKLLYPDEMSLEAKLMTLAEVGYGAAGVSLSDKAKQQLAQLTALGYDHLPVCMAKTPLSISHDPAL 521
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 313151179 920 KGVPRDFILPISDVRASIGAGFIYPLVGMMSTMPGLPTRPCFYDIDLDTETEQVkGL 976
Cdd:PRK13506 522 KGAPTDFEVPIRELRLCAGAGFITALVGNVMTMPGLGLKPGYLNIDIDADGEIV-GL 577
|
|
| PRK13507 |
PRK13507 |
formate--tetrahydrofolate ligase; Provisional |
371-977 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 184098 Cd Length: 587 Bit Score: 666.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 371 KAVDVLAKEIGLLADEIEIYGKSKAKVR-LSLLERLKDQTDGKYVLVAGITPTPLGEGKSTVTIGLVQALtAHLNVNSFA 449
Cdd:PRK13507 22 KPVEELAEELGLTKEELLPYGHYIAKVDfRKVLDRLKDRPDGKYIDVTAITPTPLGEGKSTTTMGLVQGL-GKRGKKVSG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 450 CLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRIFHESTQTDKalynrlvplvngvr 529
Cdd:PRK13507 101 AIRQPSGGPTMNIKGSAAGGGLSQCIPLTPFSLGLTGDINAIMNAHNLAMVALTARMQHERNYTDE-------------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 530 kfseiQLSRlkklgihktdptalteeevRKFTRLNIDPSTITWQRVLDTNDRFLRKITIGQGSTEKGYSRQAQFDIAVAS 609
Cdd:PRK13507 167 -----QLAR-------------------RGLKRLDIDPTRVEMGWIIDFCAQALRNIIIGIGGKTDGYMMQSGFGIAVSS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 610 EIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNS 689
Cdd:PRK13507 223 EVMAILSVATDLKDLRERIGKIVVAYDKNGKPVTTADLEVDGAMTAWMVRAINPNLLQTIEGQPVFVHAGPFANIAIGQS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 690 SVLADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGVPLKKEYTEEN 769
Cdd:PRK13507 303 SIIADRVGLKL---ADYHVTESGFGADIGFEKFWNLKCRLSGLKPDCAVIVATIRALKMHGGGPKVVPGKPLPEEYTKEN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 770 IQLVADGCCNLQKQIQIAQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPcYHWSAGGKGSVDLARAVREAAN 849
Cdd:PRK13507 380 VGLVEKGCANLLHHIGTVKKSGINPVVCINAFYTDTHAEIAIVRRLAEQAGARVAVS-RHWEKGGEGALELADAVIDACN 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 850 KRSRFRFLYDVQLPIVAKIRVIAQTVYGAKDIELSPEAQAKIDRYTQQG-FGNLPICMAKTHLSLSHEPDKKGVPRDFIL 928
Cdd:PRK13507 459 EPNDFKFLYPLEMPLRERIETIAREVYGADGVSYTPEAEAKLKRLESDPeTADFGTCMVKTHLSLSHDPALKGVPKGWTL 538
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 313151179 929 PISDVRASIGAGFIYPLVGMMSTMPGLPTRPCFYDIDLDTETEQVKGLF 977
Cdd:PRK13507 539 PIRDILTYGGAGFVVPVAGDISLMPGTGSDPAFRRIDVDTQTGKVKGLF 587
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
192-334 |
3.28e-46 |
|
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: 162.29 E-value: 3.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 192 GDAPECFVSPLARAAVELIEKSGITLDGKKVLVIGAHGPLEAALQCLFQRKGSMTMSSPWITPQLQDKLREADIVVLGSP 271
Cdd:cd05212 1 GPCTPLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313151179 272 KPDEIPAAWIPSGATMLNCFHDFLSGKLRGGSPGVPMNRLIAdesVSLLAAALRVQNMVNSGR 334
Cdd:cd05212 81 KPEKVPTEWIKPGATVINCSPTKLSGDDVKESASLYVPMTGG---VGKLTVAMRMQNMVRSVR 140
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
182-337 |
4.35e-40 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 145.30 E-value: 4.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 182 TDVNLGKLVRGdaPECFVSPLARAAVELIEKSGITLDGKKVLVIGAHGPLEAALQCLFQRKGSMTMSSPWITPQLQDKLR 261
Cdd:pfam02882 1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 262 EADIVVLGSPKPDEIPAAWIPSGATMLNCFHDFLS-GKLRGGSPGVPMNRLIA-----DESVSLLAAALRVQNMVNSGRR 335
Cdd:pfam02882 79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRVGnGKLVGDVDFENVKEKASaitpvPGGVGPMTVAMLLQNTVEAAKR 158
|
..
gi 313151179 336 WL 337
Cdd:pfam02882 159 QL 160
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
96-286 |
2.47e-32 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 127.44 E-value: 2.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 96 KPVLAVIQAGDD---HLMQNVNQNLAKEAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGLALQ------ISEdslcN 166
Cdd:COG0190 32 TPGLAVVLVGDDpasQVYVRNKHKACEEVGIESELIRLPADTTQEELLALIDELNADPSVHGILVQlplpkhIDE----E 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 167 KVLNALKPEKDVDGVTDVNLGKLVRGDapECFVSPLARAAVELIEKSGITLDGKKVLVIGaHG-----PLeAALqcLFQR 241
Cdd:COG0190 108 AVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLERYGIDLAGKHAVVVG-RSnivgkPL-ALL--LLRR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 313151179 242 KGSMTM--SSpwiTPQLQDKLREADIVVLGSPKPDEIPAAWIPSGAT 286
Cdd:COG0190 182 NATVTVchSR---TKDLAEHTRQADILVAAVGKPGLITADMVKPGAV 225
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
77-301 |
4.75e-27 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 112.03 E-value: 4.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 77 VIHNSKEVLNLLQE---------KNPAFKPVLAVIQAGDD---HLMQNVNQNLAKEAGLDITHICLPPDSGEDEIIDEIL 144
Cdd:PRK14190 4 VIIDGKEVAKEKREqlkeevvklKEQGIVPGLAVILVGDDpasHSYVRGKKKAAEKVGIYSELYEFPADITEEELLALID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 145 KINEDPRVHGLALQ------ISEDslcnKVLNALKPEKDVDGVTDVNLGKLVRGDapECFVSPLARAAVELIEKSGITLD 218
Cdd:PRK14190 84 RLNADPRINGILVQlplpkhIDEK----AVIERISPEKDVDGFHPINVGRMMLGQ--DTFLPCTPHGILELLKEYNIDIS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 219 GKKVLVIGAHGPLEAALQCLFQRK-GSMTMSSPWiTPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATML----NCFHD 293
Cdd:PRK14190 158 GKHVVVVGRSNIVGKPVGQLLLNEnATVTYCHSK-TKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIdvgvNRLEN 236
|
....*...
gi 313151179 294 flsGKLRG 301
Cdd:PRK14190 237 ---GKLCG 241
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
97-289 |
4.33e-23 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 101.96 E-value: 4.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 97 PVLAVIQAGDDHLMQNVNQNLAK---EAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGLALQISEDSLCN--KVLNA 171
Cdd:PLN02897 87 PGLAVVLVGQQRDSQTYVRNKIKaceETGIKSLLAELPEDCTEGQILSALRKFNEDTSIHGILVQLPLPQHLDesKILNM 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 172 LKPEKDVDGVTDVNLGKL-VRGDAPeCFVSPLARAAVELIEKSGITLDGKKVLVIGAHGPLEAALQCLFQRKGSMTMSSP 250
Cdd:PLN02897 167 VRLEKDVDGFHPLNVGNLaMRGREP-LFVSCTPKGCVELLIRSGVEIAGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVH 245
|
170 180 190
....*....|....*....|....*....|....*....
gi 313151179 251 WITPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLN 289
Cdd:PLN02897 246 AFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVID 284
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
82-301 |
6.64e-23 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 99.86 E-value: 6.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 82 KEVLNLLQEKNPAfKPVLAVIQAGDDH---LMQNVNQNLAKEAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGLALQ 158
Cdd:PRK14172 19 KNFVEERKENGLS-IPKIASILVGNDGgsiYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEIEELNKDNNVHGIMLQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 159 ISEDSLCN--KVLNALKPEKDVDGVTDVNLGKLVRGDapECFVSPLARAAVELIEKSGITLDGKKVLVIGAHGPL-EAAL 235
Cdd:PRK14172 98 LPLPKHLDekKITNKIDANKDIDCLTFISVGKFYKGE--KCFLPCTPNSVITLIKSLNIDIEGKEVVVIGRSNIVgKPVA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313151179 236 QCLFQRKGSMTMSSPwITPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLNCFHDFLSGKLRG 301
Cdd:PRK14172 176 QLLLNENATVTICHS-KTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSVNGKITG 240
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
97-289 |
1.69e-22 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 100.46 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 97 PVLAVIQAGD--DHLMQNVNQNLAKEA-GLDITHICLPPDSGEDEIIDEILKINEDPRVHGLALQISEDSLCNK--VLNA 171
Cdd:PLN02616 104 PGLAVILVGDrkDSATYVRNKKKACDSvGINSFEVRLPEDSTEQEVLKFISGFNNDPSVHGILVQLPLPSHMDEqnILNA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 172 LKPEKDVDGVTDVNLGKL-VRGDAPeCFVSPLARAAVELIEKSGITLDGKKVLVIGAHGPLEAALQCLFQRKGSMTMSSP 250
Cdd:PLN02616 184 VSIEKDVDGFHPLNIGRLaMRGREP-LFVPCTPKGCIELLHRYNVEIKGKRAVVIGRSNIVGMPAALLLQREDATVSIVH 262
|
170 180 190
....*....|....*....|....*....|....*....
gi 313151179 251 WITPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLN 289
Cdd:PLN02616 263 SRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVID 301
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
97-289 |
2.19e-22 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 98.75 E-value: 2.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 97 PVLAVIQAGDD---HLMQNVNQNLAKEAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGLALQ--ISEDSLCNKVLNA 171
Cdd:PRK14187 33 PCLIVILVGDDpasQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKINELNNDDSVHGILVQlpVPNHIDKNLIINT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 172 LKPEKDVDGVTDVNLGKLVRGDAPECFVSPLARAAVELIEKSGITLDGKKVLVIGAHGPLEAALQCLFQRKGSMTMSSPW 251
Cdd:PRK14187 113 IDPEKDVDGFHNENVGRLFTGQKKNCLIPCTPKGCLYLIKTITRNLSGSDAVVIGRSNIVGKPMACLLLGENCTVTTVHS 192
|
170 180 190
....*....|....*....|....*....|....*...
gi 313151179 252 ITPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLN 289
Cdd:PRK14187 193 ATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVID 230
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
97-289 |
8.76e-22 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 96.88 E-value: 8.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 97 PVLAVIQAG---DDHLMQNVNQNLAKEAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGLALQISEDSLCN--KVLNA 171
Cdd:PLN02516 40 PGLAVVIVGsrkDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISKVHELNANPDVHGILVQLPLPKHINeeKILNE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 172 LKPEKDVDGVTDVNLGKL-VRGDAPeCFVSPLARAAVELIEKSGITLDGKKVLVIGAHGPLEAALQCLFQRKGSMTMSSP 250
Cdd:PLN02516 120 ISLEKDVDGFHPLNIGKLaMKGREP-LFLPCTPKGCLELLSRSGIPIKGKKAVVVGRSNIVGLPVSLLLLKADATVTVVH 198
|
170 180 190
....*....|....*....|....*....|....*....
gi 313151179 251 WITPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLN 289
Cdd:PLN02516 199 SRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVID 237
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
97-289 |
7.95e-19 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 87.90 E-value: 7.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 97 PVLAVIQAGDDHLMQ---NVNQNLAKEAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGLALQI----SEDSlcNKVL 169
Cdd:PRK14191 32 PKLAVILVGKDPASQtyvNMKIKACERVGMDSDLHTLQENTTEAELLSLIKDLNTDQNIDGILVQLplprHIDT--KMVL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 170 NALKPEKDVDGVTDVNLGKLVRGdaPECFVSPLARAAVELIEKSGITLDGKKVLVIGAHGPLEAALQCLFQRKGSMTMSS 249
Cdd:PRK14191 110 EAIDPNKDVDGFHPLNIGKLCSQ--LDGFVPATPMGVMRLLKHYHIEIKGKDVVIIGASNIVGKPLAMLMLNAGASVSVC 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 313151179 250 PWITPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLN 289
Cdd:PRK14191 188 HILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVD 227
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
96-301 |
1.93e-18 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 86.89 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 96 KPVLAVIQAGDDHLMQ---NVNQNLAKEAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGLALQ------ISEdslcN 166
Cdd:PRK10792 33 APGLAVVLVGSDPASQvyvASKRKACEEVGFVSRSYDLPETTSEAELLALIDELNADPTIDGILVQlplpahIDN----V 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 167 KVLNALKPEKDVDGVTDVNLGKLvrgdapeCFVSPLARAA-----VELIEKSGITLDGKKVLVIGAHG----PLeaALQC 237
Cdd:PRK10792 109 KVLERIHPDKDVDGFHPYNVGRL-------AQRIPLLRPCtprgiMTLLERYGIDTYGLNAVVVGASNivgrPM--SLEL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313151179 238 LFqrKGSMTMSSPWITPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLNC-FHDFLSGKLRG 301
Cdd:PRK10792 180 LL--AGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVgINRLEDGKLVG 242
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
81-324 |
2.09e-18 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 86.80 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 81 SKEVLNLLQEKNPAFK------PVLAVIQAGDDHLMQNVNQNLAK---EAGLDITHICLPPDSGEDEIIDEILKINEDPR 151
Cdd:PRK14174 10 SLDLKNELKTRVEAYRaktgkvPGLTVIIVGEDPASQVYVRNKAKsckEIGMNSTVIELPADTTEEHLLKKIEDLNNDPD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 152 VHGLALQ------ISEDSlcnkVLNALKPEKDVDGVTDVNLGKLVRGDAPECFVSPLARAAVELIEKSGITLDGKKVLVI 225
Cdd:PRK14174 90 VHGILVQqplpkqIDEFA----VTLAIDPAKDVDGFHPENLGRLVMGHLDKCFVSCTPYGILELLGRYNIETKGKHCVVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 226 GAHGPLEAALQCLFQRKGSMTMSSPWI----TPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLNCfhdflsGKLRG 301
Cdd:PRK14174 166 GRSNIVGKPMANLMLQKLKESNCTVTIchsaTKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDV------GINRI 239
|
250 260
....*....|....*....|....*..
gi 313151179 302 GSPGVPMN-RLIAD---ESVSLLAAAL 324
Cdd:PRK14174 240 EDPSTKSGyRLVGDvdyEGVSAKASAI 266
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
70-297 |
2.10e-18 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 86.82 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 70 MDSIVRDVIHNSKEVLNLLQEKNPAFK------PVLAVIQAGDDHLMQN---VNQNLAKEAGLDITHICLPPDSGEDEII 140
Cdd:PRK14192 1 MMALVLDGKALAKQIEEELSVRVEALKaktgrtPILATILVGDDPASATyvrMKGNACRRVGMDSLKVELPQETTTEQLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 141 DEILKINEDPRVHGLALQ------ISEdSLCnkvLNALKPEKDVDGVTDVNLGKLVRGDapECFVSPLARAAVELIEKSG 214
Cdd:PRK14192 81 AKIEELNANPDVHGILLQhpvpaqIDE-RAC---FDAISLAKDVDGVTCLGFGRMAMGE--AAYGSATPAGIMRLLKAYN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 215 ITLDGKKVLVIGAHGPLEAAL-QCLFQRKGSMTMSSPWiTPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLNC-FH 292
Cdd:PRK14192 155 IELAGKHAVVVGRSAILGKPMaMMLLNANATVTICHSR-TQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAgFH 233
|
....*
gi 313151179 293 DFLSG 297
Cdd:PRK14192 234 PRDGG 238
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
73-301 |
2.27e-18 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 86.51 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 73 IVRDVIHNSKEVLNLLQEKnpAFKPVLAVIQAGDDHLMQ---NVNQNLAKEAGLDITHICLPPDSGEDEIIDEILKINED 149
Cdd:PRK14175 11 IAKDYRQGLQDQVEALKEK--GFTPKLSVILVGNDGASQsyvRSKKKAAEKIGMISEIVHLEETATEEEVLNELNRLNND 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 150 PRVHG------LALQISEdslcNKVLNALKPEKDVDGVTDVNLGKLVRGDapECFVSPLARAAVELIEKSGITLDGKKVL 223
Cdd:PRK14175 89 DSVSGilvqvpLPKQVSE----QKILEAINPEKDVDGFHPINIGKLYIDE--QTFVPCTPLGIMEILKHADIDLEGKNAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 224 VIG-AHGPLEAALQCLFQRKGSMTMSSPWiTPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLNCFHD-FLSGKLRG 301
Cdd:PRK14175 163 VIGrSHIVGQPVSKLLLQKNASVTILHSR-SKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVGNTpDENGKLKG 241
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
81-179 |
2.81e-17 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 78.60 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 81 SKEVLNLLQE-----KNPAFKPVLAVIQAGDD---HLMQNVNQNLAKEAGLDITHICLPPDSGEDEIIDEILKINEDPRV 152
Cdd:pfam00763 7 AKKIREELKEevaalKAGGRKPGLAVILVGDDpasQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKLNADPSV 86
|
90 100 110
....*....|....*....|....*....|...
gi 313151179 153 HGLALQ------ISEdslcNKVLNALKPEKDVD 179
Cdd:pfam00763 87 HGILVQlplpkhIDE----EKVLEAIDPEKDVD 115
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
70-289 |
3.28e-17 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 83.10 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 70 MDSIVRDVIHNSKEVLNLLQE-----KNPAFK-PVLAVIQAGDDHLMQ---NVNQNLAKEAGLDITHICLPPDSGEDEII 140
Cdd:PRK14177 1 MSPILLDGKKLSEKIRNEIREtieerKTKNKRiPKLATILVGNNPASEtyvSMKVKACHKVGMGSEMIRLKEQTTTEELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 141 DEILKINEDPRVHGLALQISEDSLCN--KVLNALKPEKDVDGVTDVNLGKLVRGdaPECFVSPLARAAVELIEKSGITLD 218
Cdd:PRK14177 81 GVIDKLNLDPNVDGILLQHPVPSQIDerAAFDRIALEKDVDGVTTLSFGKLSMG--VETYLPCTPYGMVLLLKEYGIDVT 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 313151179 219 GKKVLVIGAHGPLEAALQCLFQRKGSMTMSSPWITPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLN 289
Cdd:PRK14177 159 GKNAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLD 229
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
97-285 |
3.73e-17 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 83.19 E-value: 3.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 97 PVLAVIQAGDDH----LMQNVNQNLAKeAGLD--ITHicLPPDSGEDEIIDEILKINEDPRVHGLALQ--ISEDSLCNKV 168
Cdd:PRK14186 33 PGLAVLRVGDDPasavYVRNKEKACAR-VGIAsfGKH--LPADTSQAEVEALIAQLNQDERVDGILLQlpLPKHLDEVPL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 169 LNALKPEKDVDGVTDVNLGKLVRGDAPECFVSPLarAAVELIEKSGITLDGKKVLVIG----AHGPLEAALQCLfqrKGS 244
Cdd:PRK14186 110 LHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPA--GVMRLLRSQQIDIAGKKAVVVGrsilVGKPLALMLLAA---NAT 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 313151179 245 MTMSSPWiTPQLQDKLREADIVVLGSPKPDEIPAAWIPSGA 285
Cdd:PRK14186 185 VTIAHSR-TQDLASITREADILVAAAGRPNLIGAEMVKPGA 224
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
96-289 |
9.18e-17 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 82.13 E-value: 9.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 96 KPVLAVIQAGDDHLMQ---NVNQNLAKEAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGLALQISEDSLCNK--VLN 170
Cdd:PRK14167 31 TPGLATVLMSDDPASEtyvSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTIDELNADEDVHGILVQMPVPDHVDDreVLR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 171 ALKPEKDVDGVTDVNLGKLVRGDAPECFVSPlaRAAVELIEKSGITLDGKKVLVIGAHGPLEAALQCLFQRKGSMTMSSP 250
Cdd:PRK14167 111 RIDPAKDVDGFHPENVGRLVAGDARFKPCTP--HGIQKLLAAAGVDTEGADVVVVGRSDIVGKPMANLLIQKADGGNATV 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 313151179 251 WI----TPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLN 289
Cdd:PRK14167 189 TVchsrTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVID 231
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
94-301 |
1.61e-16 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 81.23 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 94 AFKPVLAVIQAGDDHLMQ---NVNQNLAKEAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGLALQISEDSLCNK--V 168
Cdd:PRK14180 29 AITPKLVAIIVGNDPASKtyvASKEKACAQVGIDSQVITLPEHTTESELLELIDQLNNDSSVHAILVQLPLPAHINKnnV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 169 LNALKPEKDVDGVTDVNLGKLVRGDApECFVSPLARAAVELIEKSGITLDGKKVLVIGAHGPL-EAALQCLFQRKGSMTM 247
Cdd:PRK14180 109 IYSIKPEKDVDGFHPTNVGRLQLRDK-KCLESCTPKGIMTMLREYGIKTEGAYAVVVGASNVVgKPVSQLLLNAKATVTT 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 313151179 248 SSPWiTPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLNCFHDFLSGKLRG 301
Cdd:PRK14180 188 CHRF-TTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHVDGKIVG 240
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
97-289 |
2.33e-16 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 80.44 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 97 PVLAVIQAGDDHLMQN-VNQNLAKEAGLDITHIC--LPPDSGEDEIIDEILKINEDPRVHGLALQ------ISEdslcNK 167
Cdd:PRK14193 33 PGLGTVLVGDDPGSQAyVRGKHRDCAEVGITSIRrdLPADATQEELNAVIDELNADPACTGYIVQlplpkhLDE----NA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 168 VLNALKPEKDVDGVTDVNLGKLVRGDApecfvSPL---ARAAVELIEKSGITLDGKKVLVIGAHGPLEAALQCLFQRKG- 243
Cdd:PRK14193 109 VLERIDPAKDADGLHPTNLGRLVLNEP-----APLpctPRGIVHLLRRYDVELAGAHVVVIGRGVTVGRPIGLLLTRRSe 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 313151179 244 --SMTMSSPWiTPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLN 289
Cdd:PRK14193 184 naTVTLCHTG-TRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLD 230
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
81-293 |
6.54e-16 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 79.35 E-value: 6.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 81 SKEVLNLLQEKNpafKPVLAVIQAGDDHLMQNVNQNLAK---EAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGLAL 157
Cdd:PRK14170 19 TREVAELVKEGK---KPGLAVVLVGDNQASRTYVRNKQKrteEAGMKSVLIELPENVTEEKLLSVVEELNEDKTIHGILV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 158 Q------ISEDslcnKVLNALKPEKDVDGVTDVNLGKLVRGDapECFVSPLARAAVELIEKSGITLDGKKVLVIGAHGPL 231
Cdd:PRK14170 96 QlplpehISEE----KVIDTISYDKDVDGFHPVNVGNLFIGK--DSFVPCTPAGIIELIKSTGTQIEGKRAVVIGRSNIV 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313151179 232 -EAALQCLFQRKGSMTMSSPWiTPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLNCFHD 293
Cdd:PRK14170 170 gKPVAQLLLNENATVTIAHSR-TKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMD 231
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
174-290 |
1.23e-15 |
|
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: 75.67 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 174 PEKDVDGVTDVNLGKLVRGDapECFVSPLARAAVELIEKSGITLDGKKVLVIGAHG----PLeAALqcLFQRKGSMTMSS 249
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGR--PGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNivgkPL-AAL--LLNRNATVTVCH 75
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 313151179 250 PWiTPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLNC 290
Cdd:cd01080 76 SK-TKNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDV 115
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
82-268 |
1.74e-15 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 77.87 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 82 KEVLNLLQEKnpAFKPVLAVIQAGDDHLMQNVNQN---LAKEAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGLALQ 158
Cdd:PRK14179 20 EKVAKLKEEK--GIVPGLVVILVGDNPASQVYVRNkerSALAAGFKSEVVRLPETISQEELLDLIERYNQDPTWHGILVQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 159 ------ISEDslcnKVLNALKPEKDVDGVTDVNLGKLVRGDaPECFVSPLArAAVELIEKSGITLDGKKVLVIGAHGPLE 232
Cdd:PRK14179 98 lplpkhINEE----KILLAIDPKKDVDGFHPMNTGHLWSGR-PVMIPCTPA-GIMEMFREYNVELEGKHAVVIGRSNIVG 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 313151179 233 AAL-QCLFQRKGSMTMSSPWiTPQLQDKLREADIVVL 268
Cdd:PRK14179 172 KPMaQLLLDKNATVTLTHSR-TRNLAEVARKADILVV 207
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
130-289 |
2.00e-15 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 77.99 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 130 LPPDSGEDEIIDEILKINEDPRVHGLALQISEDSLCN--KVLNALKPEKDVDGVTDVNLGKLVRGDAPECFVSPLARAAV 207
Cdd:PRK14168 70 QSVDITEEELLALIDKYNNDDSIHGILVQLPLPKHINekKVLNAIDPDKDVDGFHPVNVGRLMIGGDEVKFLPCTPAGIQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 208 ELIEKSGITLDGKKVLVIGAHGPLEAALQCLFQRKGSMTMSSPWI----TPQLQDKLREADIVVLGSPKPDEIPAAWIPS 283
Cdd:PRK14168 150 EMLVRSGVETSGAEVVVVGRSNIVGKPIANMMTQKGPGANATVTIvhtrSKNLARHCQRADILIVAAGVPNLVKPEWIKP 229
|
....*.
gi 313151179 284 GATMLN 289
Cdd:PRK14168 230 GATVID 235
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
96-289 |
3.17e-15 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 77.42 E-value: 3.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 96 KPVLAVIQAGDDHLMQNVNQNLAK---EAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGLALQISE----DSlcNKV 168
Cdd:PRK14189 32 QPGLAVILVGDNPASQVYVRNKVKaceDNGFHSLKDRYPADLSEAELLARIDELNRDPKIHGILVQLPLpkhiDS--HKV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 169 LNALKPEKDVDGVTDVNLGKLVRGdapecfvSPLARA-----AVELIEKSGITLDGKKVLVIGAHGPLEAALQCLFQRKG 243
Cdd:PRK14189 110 IEAIAPEKDVDGFHVANAGALMTG-------QPLFRPctpygVMKMLESIGIPLRGAHAVVIGRSNIVGKPMAMLLLQAG 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313151179 244 SMTMSSPWITPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLN 289
Cdd:PRK14189 183 ATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVID 228
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
96-286 |
5.93e-15 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 76.53 E-value: 5.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 96 KPVLAVIQAGDDHLMQNVNQN---LAKEAGL-DITHIcLPPDSGEDEIIDEILKINEDPRVHGLALQ------ISEDslc 165
Cdd:PRK14188 32 TPGLAVVLVGEDPASQVYVRSkgkQTKEAGMaSFEHK-LPADTSQAELLALIARLNADPAIHGILVQlplpkhLDSE--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 166 nKVLNALKPEKDVDGVTDVNLGKLVRGDAPECFVSPLarAAVELIEKSGITLDGKKVLVIGAH---GPLEAALqcLFQRK 242
Cdd:PRK14188 108 -AVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPL--GCMMLLRRVHGDLSGLNAVVIGRSnlvGKPMAQL--LLAAN 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 313151179 243 GSMTMSSPWiTPQLQDKLREADIVVLGSPKPDEIPAAWIPSGAT 286
Cdd:PRK14188 183 ATVTIAHSR-TRDLPAVCRRADILVAAVGRPEMVKGDWIKPGAT 225
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
81-301 |
2.06e-14 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 74.88 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 81 SKEVLNLLQEK--NPAFKPVLAVIQAGDD---HLMQNVNQNLAKEAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGL 155
Cdd:PRK14178 9 SEKRLELLKEEiiESGLYPRLATVIVGDDpasQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIRRLNEDPDINGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 156 ALQI----SEDSlcNKVLNALKPEKDVDGVTDVNLGKLVRGDAPECFVSPLarAAVELIEKSGITLDGKKVLVIGAH--- 228
Cdd:PRK14178 89 LVQLplpkGVDT--ERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTPN--GIMTLLHEYKISIAGKRAVVVGRSidv 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313151179 229 GPLEAALqcLFQRKGSMTMSSPwITPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLNCFHDFLSGKLRG 301
Cdd:PRK14178 165 GRPMAAL--LLNADATVTICHS-KTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQVNGKLCG 234
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
97-289 |
3.86e-14 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 74.04 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 97 PVLAVIQAGDDHLMQNVNQNLAK---EAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGLALQI----SEDSlcNKVL 169
Cdd:PRK14184 32 PGLAVILVGEDPASQVYVRNKERaceDAGIVSEAFRLPADTTQEELEDLIAELNARPDIDGILLQLplpkGLDS--QRCL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 170 NALKPEKDVDGVTDVNLGKLVRGdAPeCFVSPLARAAVELIEKSGITLDGKKVLVIGAHGPLEAALQCLFQRKGSMTMSS 249
Cdd:PRK14184 110 ELIDPAKDVDGFHPENMGRLALG-LP-GFRPCTPAGVMTLLERYGLSPAGKKAVVVGRSNIVGKPLALMLGAPGKFANAT 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 313151179 250 PWI----TPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLN 289
Cdd:PRK14184 188 VTVchsrTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVD 231
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
91-289 |
5.14e-14 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 73.73 E-value: 5.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 91 KNPAFKPVLAVIQAGDDHLMQNVNQN---LAKEAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGLALQISEDSLCN- 166
Cdd:PRK14194 28 KAAGIEPALAVILVGNDPASQVYVRNkilRAEEAGIRSLEHRLPADTSQARLLALIAELNADPSVNGILLQLPLPAHIDe 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 167 -KVLNALKPEKDVDGVTDVNLGKLVRGDAPECFVSPlaRAAVELIEKSGITLDGKKVLVIGAH---GPLEAALqcLFQRK 242
Cdd:PRK14194 108 aRVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTP--SGCLRLLEDTCGDLTGKHAVVIGRSnivGKPMAAL--LLQAH 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 313151179 243 GSMTMSSPWITpQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLN 289
Cdd:PRK14194 184 CSVTVVHSRST-DAKALCRQADIVVAAVGRPRLIDADWLKPGAVVID 229
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
81-301 |
6.91e-13 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 70.05 E-value: 6.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 81 SKEVLNLLQEKNPAFK-----PVLAVIQAGDDHLMQNVNQNLAK---EAGLDITHICLPPDSGEDEIIDEILKINEDPRV 152
Cdd:PRK14166 10 SAKIKEELKEKNQFLKskgieSCLAVILVGDNPASQTYVKSKAKaceECGIKSLVYHLNENTTQNELLALINTLNHDDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 153 HGLALQISEDSLCNK--VLNALKPEKDVDGVTDVNLGKL---VRGDAPECfvSPLarAAVELIEKSGITLDGKKVLVIGA 227
Cdd:PRK14166 90 HGILVQLPLPDHICKdlILESIISSKDVDGFHPINVGYLnlgLESGFLPC--TPL--GVMKLLKAYEIDLEGKDAVIIGA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313151179 228 HGPLEAALQCLFQRKGSMTMSSPWITPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLNC-FHDFLSGKLRG 301
Cdd:PRK14166 166 SNIVGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVgINRLESGKIVG 240
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
96-289 |
4.26e-12 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 67.93 E-value: 4.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 96 KPVLAVIQAGDDHLMQNVNQNLAK---EAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGLALQ------ISEdslcN 166
Cdd:PRK14185 31 RPHLAAILVGHDGGSETYVANKVKaceECGFKSSLIRYESDVTEEELLAKVRELNQDDDVDGFIVQlplpkhISE----Q 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 167 KVLNALKPEKDVDGVTDVNLGKLVRGdaPECFVSPLARAAVELIEKSGITLDGKKVLVIGAHGPLEAALQCLFQRKGSMT 246
Cdd:PRK14185 107 KVIEAIDYRKDVDGFHPINVGRMSIG--LPCFVSATPNGILELLKRYHIETSGKKCVVLGRSNIVGKPMAQLMMQKAYPG 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 313151179 247 MSSPWI----TPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLN 289
Cdd:PRK14185 185 DCTVTVchsrSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVID 231
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
90-289 |
5.42e-12 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 67.52 E-value: 5.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 90 EKNPAFKPVLAVIQAGDDHLMQ---NVNQNLAKEAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGLALQISEDSLCN 166
Cdd:PRK14176 32 KSNRGITPGLATILVGDDPASKmyvRLKHKACERVGIRAEDQFLPADTTQEELLELIDSLNKRKDVHGILLQLPLPKHLD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 167 --KVLNALKPEKDVDGVTDVNLGKLVRGDapECFVSPLARAAVELIEKSGITLDGKKVLVIGaHG-----PLEAAlqcLF 239
Cdd:PRK14176 112 pqEAMEAIDPAKDADGFHPYNMGKLMIGD--EGLVPCTPHGVIRALEEYGVDIEGKNAVIVG-HSnvvgkPMAAM---LL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 313151179 240 QRKGSMTMSSPWiTPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLN 289
Cdd:PRK14176 186 NRNATVSVCHVF-TDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFD 234
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
81-271 |
6.21e-12 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 67.58 E-value: 6.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 81 SKEVLNLLQEK--NPAFKPVLAVIQAGDD---HLMQNVNQNLAKEAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGL 155
Cdd:PRK14181 9 AEHILATIKENisASSTAPGLAVVLIGNDpasEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLIHRLNNDPNIHGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 156 ALQISE----DSlcNKVLNALKPEKDVDGVTDVNLGKLVRGDApECFVSPLARAAVELIEKSGITLDGKKVLVIGAHGPL 231
Cdd:PRK14181 89 LVQLPLpkhlDA--QAILQAISPDKDVDGLHPVNMGKLLLGET-DGFIPCTPAGIIELLKYYEIPLHGRHVAIVGRSNIV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 313151179 232 EAALQCLFQRKGSMTMSSPWI----TPQLQDKLREADIVV--LGSP 271
Cdd:PRK14181 166 GKPLAALLMQKHPDTNATVTLlhsqSENLTEILKTADIIIaaIGVP 211
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
97-271 |
2.23e-11 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 65.75 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 97 PVLAVIQAGDDH----LMQNVNQNlAKEAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGLALQI----SEDSlcNKV 168
Cdd:PRK14171 33 PKLAIVLVGDNPasiiYVKNKIKN-AHKIGIDTLLVNLSTTIHTNDLISKINELNLDNEISGIIVQLplpsSIDK--NKI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 169 LNALKPEKDVDGVTDVNLGKLVRGdAPECFVSPLARAAVELIEKSGITLDGKKVLVIGAHG----PLEAalqCLFQRKGS 244
Cdd:PRK14171 110 LSAVSPSKDIDGFHPLNVGYLHSG-ISQGFIPCTALGCLAVIKKYEPNLTGKNVVIIGRSNivgkPLSA---LLLKENCS 185
|
170 180
....*....|....*....|....*....
gi 313151179 245 MTMSSPwITPQLQDKLREADIVV--LGSP 271
Cdd:PRK14171 186 VTICHS-KTHNLSSITSKADIVVaaIGSP 213
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
96-301 |
5.13e-11 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 64.66 E-value: 5.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 96 KPVLAVIQAGDD---HLMQNVNQNLAKEAGLDITHICLPPDSGEDEIIDEILKINEDPRVHGLALQISEDSLCNK--VLN 170
Cdd:PRK14182 30 QTGLTVVRVGDDpasAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIARLNADPAVHGILVQLPLPKHVDEraVLD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151179 171 ALKPEKDVDGVTDVNLGKLVRGDA--PEcfvsPLARAAV-ELIEKSGITLDGKKVLVIGAH---GPLEAALqcLFQRKGS 244
Cdd:PRK14182 110 AISPAKDADGFHPFNVGALSIGIAgvPR----PCTPAGVmRMLDEARVDPKGKRALVVGRSnivGKPMAMM--LLERHAT 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 313151179 245 MTMSSPWiTPQLQDKLREADIVVLGSPKPDEIPAAWIPSGATMLNCFHDFLS-GKLRG 301
Cdd:PRK14182 184 VTIAHSR-TADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLAdGKLVG 240
|
|
| |
