|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
347-974 |
0e+00 |
|
Formate--tetrahydrofolate ligase
Pssm-ID: 178359 Cd Length: 637 Bit Score: 1034.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 347 KLQPLTPVPSDIEISRAQTPKPVDQLAEEIGLLPEELEAYGRSKAKVRLSLLDRLHAQPDGKYVLVAGITPTPLGEGKST 426
Cdd:PLN02759 9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 427 VTIGLVQALSAHLKLNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARMLHEA 506
Cdd:PLN02759 89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 507 TQSDKALFSRLVPS-VNGVRRFSPIQISRLNRLGINKTDPASLTPEEISTFVRLDLDPSKITWQRVLDTNDRFLRKITVG 585
Cdd:PLN02759 169 TQSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 586 QASTEKGQIRETGFDIAVASEIMAILALADSLEDMKNRLARMVVGTSRSGEPVTAEDLGVSGALAVLMKDAIKPTLMQTL 665
Cdd:PLN02759 249 QGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 666 EGTPVFVHAGPFANIAHGNSSVLADKLALKLVGRDGFVVTEAGFGADIGMEKFFNIKCRASGLRPNVVVLVATVRALKMH 745
Cdd:PLN02759 329 EGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMH 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 746 GGGPNVSAGAPLPREYIDENLSLVAGGChSNLRKQIQIAHLFGVPVVVALNVFRTDTQAEIDLVCQLAKECGASDAVPCH 825
Cdd:PLN02759 409 GGGPAVVAGKPLDHAYTTENVELVEAGC-VNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCT 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 826 HWAQGGRGSLELAQAVNEAASRPS-NFQFLYNKEMPIVEKIRTIAKKVYGADDIKLSPEAEAKIDYYSQQGYGSLPICMA 904
Cdd:PLN02759 488 HHAHGGKGAVDLGEAVQKACEGNSqPFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMA 567
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 905 KTHLSLSHMPDKKGAPTGFVLPIRDVRASIGAGFVYPLVGTMSTMPGLPTRPCFYDIDLDPVTEEITGLF 974
Cdd:PLN02759 568 KTQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTETGKVLGLS 637
|
|
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
355-974 |
0e+00 |
|
Formate--tetrahydrofolate ligase;
Pssm-ID: 460143 Cd Length: 555 Bit Score: 1020.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 355 PSDIEISRAQTPKPVDQLAEEIGLLPEELEAYGRSKAKVRLSLLDRLHAQPDGKYVLVAGITPTPLGEGKSTVTIGLVQA 434
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 435 LsAHLKLNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARMLHEATqsdkalf 514
Cdd:pfam01268 81 L-NRLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 515 srlvpsvngvrrfspiqisrlnrlginktdpasltpeeistfvrLDLDPSKITWQRVLDTNDRFLRKITVGQASTEKGQI 594
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 595 RETGFDIAVASEIMAILALADSLEDMKNRLARMVVGTSRSGEPVTAEDLGVSGALAVLMKDAIKPTLMQTLEGTPVFVHA 674
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 675 GPFANIAHGNSSVLADKLALKLvgrDGFVVTEAGFGADIGMEKFFNIKCRASGLRPNVVVLVATVRALKMHGGgpnvsAG 754
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGG-----VG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 755 APlprEYIDENLSLVAGGChSNLRKQIQIAHLFGVPVVVALNVFRTDTQAEIDLVCQLAKEcGASDAVPCHHWAQGGRGS 834
Cdd:pfam01268 341 KD---ELTEENLEALEKGL-ANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRELCEA-GGVDAALSEHWAKGGEGA 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 835 LELAQAVNEAA-SRPSNFQFLYNKEMPIVEKIRTIAKKVYGADDIKLSPEAEAKIDYYSQQGYGSLPICMAKTHLSLSHM 913
Cdd:pfam01268 416 IELAEAVVEACeEEPSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDD 495
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1724746110 914 PDKKGAPTGFVLPIRDVRASIGAGFVYPLVGTMSTMPGLPTRPCFYDIDLDPvTEEITGLF 974
Cdd:pfam01268 496 PKLKGAPTGFTLPVRDVRLSAGAGFIVALTGDIMTMPGLPKRPAAENIDVDE-DGKITGLF 555
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
369-973 |
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: 956.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 369 VDQLAEEIGLLPEELEAYGRSKAKVRLSLLDRLHAQPDGKYVLVAGITPTPLGEGKSTVTIGLVQALSAHLKlNSFACLR 448
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 449 QPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARMLHEATqsdkalfsrlvpsvngvrrfs 528
Cdd:cd00477 80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 529 piqisrlnrlginktdpasltpeeistfvrLDLDPSKITWQRVLDTNDRFLRKITVGQASTEKGQIRETGFDIAVASEIM 608
Cdd:cd00477 139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 609 AILALADSLEDMKNRLARMVVGTSRSGEPVTAEDLGVSGALAVLMKDAIKPTLMQTLEGTPVFVHAGPFANIAHGNSSVL 688
Cdd:cd00477 189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 689 ADKLALKLvgrDGFVVTEAGFGADIGMEKFFNIKCRASGLRPNVVVLVATVRALKMHGGGPNVSAGaplpreyiDENLSL 768
Cdd:cd00477 269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 769 VAGGChSNLRKQIQIAHLFGVPVVVALNVFRTDTQAEIDLVCQLAKECGASDAVpCHHWAQGGRGSLELAQAVNEAASRP 848
Cdd:cd00477 338 LKKGC-ANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKP 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 849 -SNFQFLYNKEMPIVEKIRTIAKKVYGADDIKLSPEAEAKIDYYSQQGYGSLPICMAKTHLSLSHMPDKKGAPTGFVLPI 927
Cdd:cd00477 416 kSNFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPI 495
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1724746110 928 RDVRASIGAGFVYPLVGTMSTMPGLPTRPCFYDIDLDPvTEEITGL 973
Cdd:cd00477 496 RDVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDIDD-TGKIEGL 540
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
354-974 |
0e+00 |
|
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
Pssm-ID: 442046 Cd Length: 556 Bit Score: 916.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 354 VPSDIEISRAQTPKPVDQLAEEIGLLPEELEAYGRSKAKVRLSLLDRLHAQPDGKYVLVAGITPTPLGEGKSTVTIGLVQ 433
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 434 ALsAHLKLNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARMLHEatqsdkal 513
Cdd:COG2759 81 AL-NRLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQG-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 514 fsrlvpsvngvrrfspiqisrlNRLGInktdpasltpeeistfvrldlDPSKITWQRVLDTNDRFLRKITVGQASTEKGQ 593
Cdd:COG2759 152 ----------------------NELNI---------------------DPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 594 IRETGFDIAVASEIMAILALADSLEDMKNRLARMVVGTSRSGEPVTAEDLGVSGALAVLMKDAIKPTLMQTLEGTPVFVH 673
Cdd:COG2759 189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 674 AGPFANIAHGNSSVLADKLALKLVgrDgFVVTEAGFGADIGMEKFFNIKCRASGLRPNVVVLVATVRALKMHGGGPNVsa 753
Cdd:COG2759 269 GGPFANIAHGCNSVIATKLALKLA--D-YVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVAKD-- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 754 gaplprEYIDENLSLVAGGChSNLRKQIQIAHLFGVPVVVALNVFRTDTQAEIDLVCQLAKECGAsDAVPCHHWAQGGRG 833
Cdd:COG2759 344 ------ELTEENLEALEKGL-ANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEG 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 834 SLELAQAVNEAA-SRPSNFQFLYNKEMPIVEKIRTIAKKVYGADDIKLSPEAEAKIDYYSQQGYGSLPICMAKTHLSLSH 912
Cdd:COG2759 416 AEELAEAVVEACeEGPSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSD 495
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1724746110 913 MPDKKGAPTGFVLPIRDVRASIGAGFVYPLVGTMSTMPGLPTRPCFYDIDLDpVTEEITGLF 974
Cdd:COG2759 496 DPKLLGAPTGFTLTVREVRLSAGAGFIVALTGDIMTMPGLPKVPAAERIDID-EDGKITGLF 556
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
196-330 |
5.42e-37 |
|
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: 135.71 E-value: 5.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 196 GDLSKGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDGPLGVALQCLIERSGMVALKSQWRSKSLQTQVMQADAVVLLGA 275
Cdd:cd05212 1 GPCTPLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 276 GNMDVPPTWVRPGAAVIRCEPTLETDEPTIEMSS-----KSGFRYLTAAYRSQNVVRSGR 330
Cdd:cd05212 81 KPEKVPTEWIKPGATVINCSPTKLSGDDVKESASlyvpmTGGVGKLTVAMRMQNMVRSVR 140
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
80-292 |
8.58e-29 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 117.04 E-value: 8.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 80 EIVQSAKEAMAALQKRNpaLQPMLAIIQAGED-DSLLEIN--KKMAGRIGLNITQICLAKECSEDEIVEELLKLNEDPRV 156
Cdd:COG0190 14 EIREELKERVAALKAKG--ITPGLAVVLVGDDpASQVYVRnkHKACEEVGIESELIRLPADTTQEELLALIDELNADPSV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 157 HGVYLHLP-PASL-TSRVLNTLKPEKDVNGISDLNMGRLVRGDlsKGFVPPVASAVLDLLENHDAPLGGKSVLLVGedgp 234
Cdd:COG0190 92 HGILVQLPlPKHIdEEAVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLERYGIDLAGKHAVVVG---- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1724746110 235 lgvalqclieRS-------GMVALK---------SqwRSKSLQTQVMQADAVVL-LGAGNMdVPPTWVRPGAAVI 292
Cdd:COG0190 166 ----------RSnivgkplALLLLRrnatvtvchS--RTKDLAEHTRQADILVAaVGKPGL-ITADMVKPGAVVI 227
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
4-292 |
1.46e-25 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 109.71 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 4 SLVRSACGSLRIHPARPGSRV------SLLSRRCppVGPTNSRLIL--RTASATSSGGASTKIAVDFGKQSQKD--EGFE 73
Cdd:PLN02616 3 SLMFTDCSSSTTSRLIHFNRIstpfngTFLLRRC--VGPLRVRTTAsgRGCCINSSSSPSPVINADTGSEGGAKviDGKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 74 CDSSLREIVQSAKEAMaalqKRNPALQPMLAIIQAGE--DDSLLEINKKMA-GRIGLNITQICLAKECSEDEIVEELLKL 150
Cdd:PLN02616 81 VAKKIRDEITIEVSRM----KESIGVVPGLAVILVGDrkDSATYVRNKKKAcDSVGINSFEVRLPEDSTEQEVLKFISGF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 151 NEDPRVHGVYLHLP-PASLTSR-VLNTLKPEKDVNGISDLNMGRLVRGDLSKGFVPPVASAVLDLLENHDAPLGGKSVLL 228
Cdd:PLN02616 157 NNDPSVHGILVQLPlPSHMDEQnILNAVSIEKDVDGFHPLNIGRLAMRGREPLFVPCTPKGCIELLHRYNVEIKGKRAVV 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1724746110 229 VGEDGPLGVALQCLIERSGMVALKSQWRSKSLQTQVMQADAVV-LLGAGNMdVPPTWVRPGAAVI 292
Cdd:PLN02616 237 IGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREADIIIsAVGQPNM-VRGSWIKPGAVVI 300
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
81-314 |
1.10e-21 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 96.50 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 81 IVQSAKEAMAALQKRNpALQPMLAIIQAGE---DDSLLEINKKMAGRIGLNITQICLAKECSEDEIVEELLKLNEDPRVH 157
Cdd:PLN02516 21 IRSEIAEEVAQLSEKH-GKVPGLAVVIVGSrkdSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISKVHELNANPDVH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 158 GVYLHLP-PASLTS-RVLNTLKPEKDVNGISDLNMGRLVRGDLSKGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDGPL 235
Cdd:PLN02516 100 GILVQLPlPKHINEeKILNEISLEKDVDGFHPLNIGKLAMKGREPLFLPCTPKGCLELLSRSGIPIKGKKAVVVGRSNIV 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1724746110 236 GVALQCLIERSGMVALKSQWRSKSLQTQVMQADAVVLLGAGNMDVPPTWVRPGAAVIRCEpTLETDEPtiemSSKSGFR 314
Cdd:PLN02516 180 GLPVSLLLLKADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVG-TNAVSDP----SKKSGYR 253
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
79-182 |
5.43e-19 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 83.22 E-value: 5.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 79 REIVQSAKEAMAALQKRNpaLQPMLAIIQAGED-DSLLEIN--KKMAGRIGLNITQICLAKECSEDEIVEELLKLNEDPR 155
Cdd:pfam00763 8 KKIREELKEEVAALKAGG--RKPGLAVILVGDDpASQVYVRnkKKACEEVGIESELIRLPEDTTEEELLALIDKLNADPS 85
|
90 100
....*....|....*....|....*....
gi 1724746110 156 VHGVYLHLP-PASL-TSRVLNTLKPEKDV 182
Cdd:pfam00763 86 VHGILVQLPlPKHIdEEKVLEAIDPEKDV 114
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
186-333 |
2.63e-13 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 68.65 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 186 SDLNMGRLVRGDlsKGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDGPLGVALQCLIERSG-MVALkSQWRSKSLQTQV 264
Cdd:pfam02882 1 HPYNLGRLVLGK--PCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANaTVTV-CHSKTKDLAEIT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 265 MQADAVVL-LGAGNMdVPPTWVRPGAAVIRC------EPTLETDEPTIEMSSKSGFRY--------LTAAYRSQNVVRSG 329
Cdd:pfam02882 78 READIVVVaVGKPEL-IKADWIKPGAVVIDVginrvgNGKLVGDVDFENVKEKASAITpvpggvgpMTVAMLLQNTVEAA 156
|
....
gi 1724746110 330 RRWL 333
Cdd:pfam02882 157 KRQL 160
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
347-974 |
0e+00 |
|
Formate--tetrahydrofolate ligase
Pssm-ID: 178359 Cd Length: 637 Bit Score: 1034.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 347 KLQPLTPVPSDIEISRAQTPKPVDQLAEEIGLLPEELEAYGRSKAKVRLSLLDRLHAQPDGKYVLVAGITPTPLGEGKST 426
Cdd:PLN02759 9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 427 VTIGLVQALSAHLKLNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARMLHEA 506
Cdd:PLN02759 89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 507 TQSDKALFSRLVPS-VNGVRRFSPIQISRLNRLGINKTDPASLTPEEISTFVRLDLDPSKITWQRVLDTNDRFLRKITVG 585
Cdd:PLN02759 169 TQSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 586 QASTEKGQIRETGFDIAVASEIMAILALADSLEDMKNRLARMVVGTSRSGEPVTAEDLGVSGALAVLMKDAIKPTLMQTL 665
Cdd:PLN02759 249 QGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 666 EGTPVFVHAGPFANIAHGNSSVLADKLALKLVGRDGFVVTEAGFGADIGMEKFFNIKCRASGLRPNVVVLVATVRALKMH 745
Cdd:PLN02759 329 EGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMH 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 746 GGGPNVSAGAPLPREYIDENLSLVAGGChSNLRKQIQIAHLFGVPVVVALNVFRTDTQAEIDLVCQLAKECGASDAVPCH 825
Cdd:PLN02759 409 GGGPAVVAGKPLDHAYTTENVELVEAGC-VNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCT 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 826 HWAQGGRGSLELAQAVNEAASRPS-NFQFLYNKEMPIVEKIRTIAKKVYGADDIKLSPEAEAKIDYYSQQGYGSLPICMA 904
Cdd:PLN02759 488 HHAHGGKGAVDLGEAVQKACEGNSqPFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMA 567
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 905 KTHLSLSHMPDKKGAPTGFVLPIRDVRASIGAGFVYPLVGTMSTMPGLPTRPCFYDIDLDPVTEEITGLF 974
Cdd:PLN02759 568 KTQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTETGKVLGLS 637
|
|
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
355-974 |
0e+00 |
|
Formate--tetrahydrofolate ligase;
Pssm-ID: 460143 Cd Length: 555 Bit Score: 1020.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 355 PSDIEISRAQTPKPVDQLAEEIGLLPEELEAYGRSKAKVRLSLLDRLHAQPDGKYVLVAGITPTPLGEGKSTVTIGLVQA 434
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 435 LsAHLKLNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARMLHEATqsdkalf 514
Cdd:pfam01268 81 L-NRLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 515 srlvpsvngvrrfspiqisrlnrlginktdpasltpeeistfvrLDLDPSKITWQRVLDTNDRFLRKITVGQASTEKGQI 594
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 595 RETGFDIAVASEIMAILALADSLEDMKNRLARMVVGTSRSGEPVTAEDLGVSGALAVLMKDAIKPTLMQTLEGTPVFVHA 674
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 675 GPFANIAHGNSSVLADKLALKLvgrDGFVVTEAGFGADIGMEKFFNIKCRASGLRPNVVVLVATVRALKMHGGgpnvsAG 754
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGG-----VG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 755 APlprEYIDENLSLVAGGChSNLRKQIQIAHLFGVPVVVALNVFRTDTQAEIDLVCQLAKEcGASDAVPCHHWAQGGRGS 834
Cdd:pfam01268 341 KD---ELTEENLEALEKGL-ANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRELCEA-GGVDAALSEHWAKGGEGA 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 835 LELAQAVNEAA-SRPSNFQFLYNKEMPIVEKIRTIAKKVYGADDIKLSPEAEAKIDYYSQQGYGSLPICMAKTHLSLSHM 913
Cdd:pfam01268 416 IELAEAVVEACeEEPSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDD 495
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1724746110 914 PDKKGAPTGFVLPIRDVRASIGAGFVYPLVGTMSTMPGLPTRPCFYDIDLDPvTEEITGLF 974
Cdd:pfam01268 496 PKLKGAPTGFTLPVRDVRLSAGAGFIVALTGDIMTMPGLPKRPAAENIDVDE-DGKITGLF 555
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
369-973 |
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: 956.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 369 VDQLAEEIGLLPEELEAYGRSKAKVRLSLLDRLHAQPDGKYVLVAGITPTPLGEGKSTVTIGLVQALSAHLKlNSFACLR 448
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 449 QPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARMLHEATqsdkalfsrlvpsvngvrrfs 528
Cdd:cd00477 80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 529 piqisrlnrlginktdpasltpeeistfvrLDLDPSKITWQRVLDTNDRFLRKITVGQASTEKGQIRETGFDIAVASEIM 608
Cdd:cd00477 139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 609 AILALADSLEDMKNRLARMVVGTSRSGEPVTAEDLGVSGALAVLMKDAIKPTLMQTLEGTPVFVHAGPFANIAHGNSSVL 688
Cdd:cd00477 189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 689 ADKLALKLvgrDGFVVTEAGFGADIGMEKFFNIKCRASGLRPNVVVLVATVRALKMHGGGPNVSAGaplpreyiDENLSL 768
Cdd:cd00477 269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 769 VAGGChSNLRKQIQIAHLFGVPVVVALNVFRTDTQAEIDLVCQLAKECGASDAVpCHHWAQGGRGSLELAQAVNEAASRP 848
Cdd:cd00477 338 LKKGC-ANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKP 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 849 -SNFQFLYNKEMPIVEKIRTIAKKVYGADDIKLSPEAEAKIDYYSQQGYGSLPICMAKTHLSLSHMPDKKGAPTGFVLPI 927
Cdd:cd00477 416 kSNFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPI 495
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1724746110 928 RDVRASIGAGFVYPLVGTMSTMPGLPTRPCFYDIDLDPvTEEITGL 973
Cdd:cd00477 496 RDVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDIDD-TGKIEGL 540
|
|
| PTZ00386 |
PTZ00386 |
formyl tetrahydrofolate synthetase; Provisional |
347-973 |
0e+00 |
|
formyl tetrahydrofolate synthetase; Provisional
Pssm-ID: 240394 Cd Length: 625 Bit Score: 946.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 347 KLQPLTPVPSDIEISRAQTPKPVDQLAEEIGLLPEELEAYGRSKAKVRLSLLDRLHAQPDGKYVLVAGITPTPLGEGKST 426
Cdd:PTZ00386 8 KLSCQWPVPSDIDIAQSVKPQPITSVAESAGILLSELDPYGSTRAKVKLSVLKRLENSPNGKYVVVAGMNPTPLGEGKST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 427 VTIGLVQALSAHLKLNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARMLHEA 506
Cdd:PTZ00386 88 TTIGLAQSLGAHLHRKTFACIRQPSQGPTFGIKGGAAGGGYSQVIPMEDFNLHGTGDIHAITAANNLLAAALDTRIFHER 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 507 TQSDKALFSRLVpsvNGVRRFSPIQISRLNRLGINKTDPASLTPEEISTFVRLDLDPSKITWQRVLDTNDRFLRKITVGQ 586
Cdd:PTZ00386 168 TQSDAALYRRLT---DELKKFTPIMLKRLEKLGISKTDPKQLTEEERVRFARLDIDPDTISWRRVTDVNDRMLREITIGQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 587 ASTEKGQIRETGFDIAVASEIMAILALADSLEDMKNRLARMVVGTSRSGEPVTAEDLGVSGALAVLMKDAIKPTLMQTLE 666
Cdd:PTZ00386 245 GKEEKGITRKTGFDISVASEVMAILALATDLADMRQRLGAIVVAKSKSGEPVTAEDLGCAGAMTVLMKDTIEPTLMQTLE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 667 GTPVFVHAGPFANIAHGNSSVLADKLALKLVGRDGFVVTEAGFGADIGMEKFFNIKCRASGLRPNVVVLVATVRALKMHG 746
Cdd:PTZ00386 325 GTPVLVHAGPFGNIAHGNSSIVADQIALKLAGQDGFVLTEAGFGADIGCEKFFNIKCRTSGLKPDAAVLVATVRALKFHG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 747 GGPNVSAGAplpreyidENLSLVAGGChSNLRKQIQIAHLFGVPVVVALNVFRTDTQAEIDLVCQLA-KECGASDAVPCH 825
Cdd:PTZ00386 405 GVEPVVAGK--------ENLEAVRKGL-SNLQRHIQNIRKFGVPVVVALNKFSTDTDAELELVKELAlQEGGAADVVVTD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 826 HWAQGGRGSLELAQAVNEAA-SRPSNFQFLYNKEMPIVEKIRTIAKKVYGADDIKLSPEAEAKIDYYSQQGYGSLPICMA 904
Cdd:PTZ00386 476 HWAKGGAGAVDLAQALIRVTeNVPSNFKLLYPLDASLKEKIETICKEIYGAAGVEYLNDADEKLEDFERMGYGKFPVCMA 555
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1724746110 905 KTHLSLSHMPDKKGAPTGFVLPIRDVRASIGAGFVYPLVGTMSTMPGLPTRPCFYDIDLDPVTEEITGL 973
Cdd:PTZ00386 556 KTQYSFSHDPELRGAPTGFTVPIRDVRVNCGAGFVFPLLGDISTMPGLPTRPAFYNIDIDCETGKIVGL 624
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
354-974 |
0e+00 |
|
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
Pssm-ID: 442046 Cd Length: 556 Bit Score: 916.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 354 VPSDIEISRAQTPKPVDQLAEEIGLLPEELEAYGRSKAKVRLSLLDRLHAQPDGKYVLVAGITPTPLGEGKSTVTIGLVQ 433
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 434 ALsAHLKLNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARMLHEatqsdkal 513
Cdd:COG2759 81 AL-NRLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQG-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 514 fsrlvpsvngvrrfspiqisrlNRLGInktdpasltpeeistfvrldlDPSKITWQRVLDTNDRFLRKITVGQASTEKGQ 593
Cdd:COG2759 152 ----------------------NELNI---------------------DPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 594 IRETGFDIAVASEIMAILALADSLEDMKNRLARMVVGTSRSGEPVTAEDLGVSGALAVLMKDAIKPTLMQTLEGTPVFVH 673
Cdd:COG2759 189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 674 AGPFANIAHGNSSVLADKLALKLVgrDgFVVTEAGFGADIGMEKFFNIKCRASGLRPNVVVLVATVRALKMHGGGPNVsa 753
Cdd:COG2759 269 GGPFANIAHGCNSVIATKLALKLA--D-YVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVAKD-- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 754 gaplprEYIDENLSLVAGGChSNLRKQIQIAHLFGVPVVVALNVFRTDTQAEIDLVCQLAKECGAsDAVPCHHWAQGGRG 833
Cdd:COG2759 344 ------ELTEENLEALEKGL-ANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEG 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 834 SLELAQAVNEAA-SRPSNFQFLYNKEMPIVEKIRTIAKKVYGADDIKLSPEAEAKIDYYSQQGYGSLPICMAKTHLSLSH 912
Cdd:COG2759 416 AEELAEAVVEACeEGPSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSD 495
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1724746110 913 MPDKKGAPTGFVLPIRDVRASIGAGFVYPLVGTMSTMPGLPTRPCFYDIDLDpVTEEITGLF 974
Cdd:COG2759 496 DPKLLGAPTGFTLTVREVRLSAGAGFIVALTGDIMTMPGLPKVPAAERIDID-EDGKITGLF 556
|
|
| PRK13505 |
PRK13505 |
formate--tetrahydrofolate ligase; Provisional |
353-974 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237403 Cd Length: 557 Bit Score: 778.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 353 PVPSDIEISRAQTPKPVDQLAEEIGLLPEELEAYGRSKAKVRLSLLDRLHAQPDGKYVLVAGITPTPLGEGKSTVTIGLV 432
Cdd:PRK13505 1 TMKSDIEIAQEATLKPITEIAAKLGIPEDDLEPYGKYKAKISLDKIKALKDKKDGKLILVTAINPTPAGEGKSTVTVGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 433 QALsAHLKLNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLVAAAIDArmlHeatqsdka 512
Cdd:PRK13505 81 DAL-NKIGKKTVIALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITSANNLLAALIDN---H-------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 513 lfsrlvpsvngvrrfspiqISRLNRLGInktdpasltpeeistfvrldlDPSKITWQRVLDTNDRFLRKITVGQASTEKG 592
Cdd:PRK13505 149 -------------------IHQGNELGI---------------------DPRRITWKRVLDMNDRALRNIVVGLGGPANG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 593 QIRETGFDIAVASEIMAILALADSLEDMKNRLARMVVGTSRSGEPVTAEDLGVSGALAVLMKDAIKPTLMQTLEGTPVFV 672
Cdd:PRK13505 189 VPREDGFDITVASEIMAILCLATDLKDLKERLGRIVVGYTYDGKPVTVKDLKVEGAMALLLKDAIKPNLVQTLEGTPAFV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 673 HAGPFANIAHGNSSVLADKLALKLVgrDgFVVTEAGFGADIGMEKFFNIKCRASGLRPNVVVLVATVRALKMHGGgpnvs 752
Cdd:PRK13505 269 HGGPFANIAHGCNSVLATKTALKLA--D-YVVTEAGFGADLGAEKFLDIKCRKAGLKPDAVVIVATVRALKMHGG----- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 753 agapLPREYID-ENLSLVAGGChSNLRKQIQIAHLFGVPVVVALNVFRTDTQAEIDLVCQLAKECGAsDAVPCHHWAQGG 831
Cdd:PRK13505 341 ----VAKDDLKeENVEALKKGF-ANLERHIENIRKFGVPVVVAINKFVTDTDAEIAALKELCEELGV-EVALSEVWAKGG 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 832 RGSLELAQAVNEAA-SRPSNFQFLYNKEMPIVEKIRTIAKKVYGADDIKLSPEAEAKIDYYSQQGYGSLPICMAKTHLSL 910
Cdd:PRK13505 415 EGGVELAEKVVELIeEGESNFKPLYDDEDSLEEKIEKIATKIYGAKGVEFSPKAKKQLKQIEKNGWDKLPVCMAKTQYSF 494
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1724746110 911 SHMPDKKGAPTGFVLPIRDVRASIGAGFVYPLVGTMSTMPGLPTRPCFYDIDLDPvTEEITGLF 974
Cdd:PRK13505 495 SDDPKLLGAPTGFTITVRELRPSAGAGFIVALTGDIMTMPGLPKVPAALNIDVDE-DGNIVGLF 557
|
|
| PRK13506 |
PRK13506 |
formate--tetrahydrofolate ligase; Provisional |
356-973 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237404 Cd Length: 578 Bit Score: 741.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 356 SDIEISRAQTPKPVDQLAEEIGLLPEELEAYGRSKAKVRLSLLDRLHAQPDGKYVLVAGITPTPLGEGKSTVTIGLVQAL 435
Cdd:PRK13506 3 SDIEISRQAPLKPIAEIAAKLGLLPDELSPFGHTKAKVSLSVLKRLADKPKGKLVLVTAITPTPLGEGKTVTTIGLTQGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 436 sAHLKLNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARMLHEatqsdkalfs 515
Cdd:PRK13506 83 -NALGQKVCACIRQPSMGPVFGVKGGAAGGGYAQVVPMEELNLHLTGDIHAVSAAHNLAAAAIDARLFHE---------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 516 rlvpsvngvrrfspiqisrlNRLGINKTdpasltpEEISTFVRLDLDPSKITWQRVLDTNDRFLRKITVGQASTEKGQIR 595
Cdd:PRK13506 152 --------------------QRLGYDAF-------EAQSGLPALDIDPEQILWKRVVDHNDRALRMITVGLGENGNGPER 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 596 ETGFDIAVASEIMAILALADSLEDMKNRLARMVVGTSRSGEPVTAEDLGVSGALAVLMKDAIKPTLMQTLEGTPVFVHAG 675
Cdd:PRK13506 205 EDGFDITAASELMAILALSRDLKDMRQRIGRLVLAYNLQGQPITAEDLGVAGAMTVIMKDAIEPTLMQTLEGVPCLIHAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 676 PFANIAHGNSSVLADKLALKLVgrdGFVVTEAGFGADIGMEKFFNIKCRASGLRPNVVVLVATVRALKMHGGGPNVSAGA 755
Cdd:PRK13506 285 PFANIAHGNSSIIADRIALKLA---DYVVTEGGFGSDMGFEKFCNIKARQSGKAPDCAVLVATLRALKANSGLYDLRPGQ 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 756 PLPREYIDENLSLVAGGChSNLRKQIQIAHLFGVPVVVALNVFRTDTQAEIDLVCQLAKECGASDAVPCHHWAQGGRGSL 835
Cdd:PRK13506 362 ALPDSINAPDQARLEAGF-ANLKWHINNVAQYGLPVVVAINRFPTDTDEELEWLKEAVLLTGAFGCEISEAFAQGGEGAT 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 836 ELAQAVNEAASRPSNFQFLYNKEMPIVEKIRTIAKKVYGADDIKLSPEAEAKIDYYSQQGYGSLPICMAKTHLSLSHMPD 915
Cdd:PRK13506 441 ALAQAVVRACEQPSQFKLLYPDEMSLEAKLMTLAEVGYGAAGVSLSDKAKQQLAQLTALGYDHLPVCMAKTPLSISHDPA 520
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1724746110 916 KKGAPTGFVLPIRDVRASIGAGFVYPLVGTMSTMPGLPTRPCFYDIDLDpVTEEITGL 973
Cdd:PRK13506 521 LKGAPTDFEVPIRELRLCAGAGFITALVGNVMTMPGLGLKPGYLNIDID-ADGEIVGL 577
|
|
| PRK13507 |
PRK13507 |
formate--tetrahydrofolate ligase; Provisional |
357-974 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 184098 Cd Length: 587 Bit Score: 685.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 357 DIEISRA--QTPKPVDQLAEEIGLLPEELEAYGRSKAKVR-LSLLDRLHAQPDGKYVLVAGITPTPLGEGKSTVTIGLVQ 433
Cdd:PRK13507 10 DWEIAEEaeKFMKPVEELAEELGLTKEELLPYGHYIAKVDfRKVLDRLKDRPDGKYIDVTAITPTPLGEGKSTTTMGLVQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 434 ALsAHLKLNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARMLHEATQSDKAL 513
Cdd:PRK13507 90 GL-GKRGKKVSGAIRQPSGGPTMNIKGSAAGGGLSQCIPLTPFSLGLTGDINAIMNAHNLAMVALTARMQHERNYTDEQL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 514 FSRlvpsvnGVRRfspiqisrlnrlginktdpasltpeeistfvrLDLDPSKITWQRVLDTNDRFLRKITVGQASTEKGQ 593
Cdd:PRK13507 169 ARR------GLKR--------------------------------LDIDPTRVEMGWIIDFCAQALRNIIIGIGGKTDGY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 594 IRETGFDIAVASEIMAILALADSLEDMKNRLARMVVGTSRSGEPVTAEDLGVSGALAVLMKDAIKPTLMQTLEGTPVFVH 673
Cdd:PRK13507 211 MMQSGFGIAVSSEVMAILSVATDLKDLRERIGKIVVAYDKNGKPVTTADLEVDGAMTAWMVRAINPNLLQTIEGQPVFVH 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 674 AGPFANIAHGNSSVLADKLALKLVgrdGFVVTEAGFGADIGMEKFFNIKCRASGLRPNVVVLVATVRALKMHGGGPNVSA 753
Cdd:PRK13507 291 AGPFANIAIGQSSIIADRVGLKLA---DYHVTESGFGADIGFEKFWNLKCRLSGLKPDCAVIVATIRALKMHGGGPKVVP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 754 GAPLPREYIDENLSLVAGGChSNLRKQIQIAHLFGVPVVVALNVFRTDTQAEIDLVCQLAKECGASDAVPcHHWAQGGRG 833
Cdd:PRK13507 368 GKPLPEEYTKENVGLVEKGC-ANLLHHIGTVKKSGINPVVCINAFYTDTHAEIAIVRRLAEQAGARVAVS-RHWEKGGEG 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 834 SLELAQAVNEAASRPSNFQFLYNKEMPIVEKIRTIAKKVYGADDIKLSPEAEAKIDYYSQQG-YGSLPICMAKTHLSLSH 912
Cdd:PRK13507 446 ALELADAVIDACNEPNDFKFLYPLEMPLRERIETIAREVYGADGVSYTPEAEAKLKRLESDPeTADFGTCMVKTHLSLSH 525
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1724746110 913 MPDKKGAPTGFVLPIRDVRASIGAGFVYPLVGTMSTMPGLPTRPCFYDIDLDPVTEEITGLF 974
Cdd:PRK13507 526 DPALKGVPKGWTLPIRDILTYGGAGFVVPVAGDISLMPGTGSDPAFRRIDVDTQTGKVKGLF 587
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
196-330 |
5.42e-37 |
|
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: 135.71 E-value: 5.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 196 GDLSKGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDGPLGVALQCLIERSGMVALKSQWRSKSLQTQVMQADAVVLLGA 275
Cdd:cd05212 1 GPCTPLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 276 GNMDVPPTWVRPGAAVIRCEPTLETDEPTIEMSS-----KSGFRYLTAAYRSQNVVRSGR 330
Cdd:cd05212 81 KPEKVPTEWIKPGATVINCSPTKLSGDDVKESASlyvpmTGGVGKLTVAMRMQNMVRSVR 140
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
80-292 |
8.58e-29 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 117.04 E-value: 8.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 80 EIVQSAKEAMAALQKRNpaLQPMLAIIQAGED-DSLLEIN--KKMAGRIGLNITQICLAKECSEDEIVEELLKLNEDPRV 156
Cdd:COG0190 14 EIREELKERVAALKAKG--ITPGLAVVLVGDDpASQVYVRnkHKACEEVGIESELIRLPADTTQEELLALIDELNADPSV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 157 HGVYLHLP-PASL-TSRVLNTLKPEKDVNGISDLNMGRLVRGDlsKGFVPPVASAVLDLLENHDAPLGGKSVLLVGedgp 234
Cdd:COG0190 92 HGILVQLPlPKHIdEEAVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLERYGIDLAGKHAVVVG---- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1724746110 235 lgvalqclieRS-------GMVALK---------SqwRSKSLQTQVMQADAVVL-LGAGNMdVPPTWVRPGAAVI 292
Cdd:COG0190 166 ----------RSnivgkplALLLLRrnatvtvchS--RTKDLAEHTRQADILVAaVGKPGL-ITADMVKPGAVVI 227
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
4-292 |
1.46e-25 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 109.71 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 4 SLVRSACGSLRIHPARPGSRV------SLLSRRCppVGPTNSRLIL--RTASATSSGGASTKIAVDFGKQSQKD--EGFE 73
Cdd:PLN02616 3 SLMFTDCSSSTTSRLIHFNRIstpfngTFLLRRC--VGPLRVRTTAsgRGCCINSSSSPSPVINADTGSEGGAKviDGKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 74 CDSSLREIVQSAKEAMaalqKRNPALQPMLAIIQAGE--DDSLLEINKKMA-GRIGLNITQICLAKECSEDEIVEELLKL 150
Cdd:PLN02616 81 VAKKIRDEITIEVSRM----KESIGVVPGLAVILVGDrkDSATYVRNKKKAcDSVGINSFEVRLPEDSTEQEVLKFISGF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 151 NEDPRVHGVYLHLP-PASLTSR-VLNTLKPEKDVNGISDLNMGRLVRGDLSKGFVPPVASAVLDLLENHDAPLGGKSVLL 228
Cdd:PLN02616 157 NNDPSVHGILVQLPlPSHMDEQnILNAVSIEKDVDGFHPLNIGRLAMRGREPLFVPCTPKGCIELLHRYNVEIKGKRAVV 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1724746110 229 VGEDGPLGVALQCLIERSGMVALKSQWRSKSLQTQVMQADAVV-LLGAGNMdVPPTWVRPGAAVI 292
Cdd:PLN02616 237 IGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREADIIIsAVGQPNM-VRGSWIKPGAVVI 300
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
81-314 |
1.10e-21 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 96.50 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 81 IVQSAKEAMAALQKRNpALQPMLAIIQAGE---DDSLLEINKKMAGRIGLNITQICLAKECSEDEIVEELLKLNEDPRVH 157
Cdd:PLN02516 21 IRSEIAEEVAQLSEKH-GKVPGLAVVIVGSrkdSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISKVHELNANPDVH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 158 GVYLHLP-PASLTS-RVLNTLKPEKDVNGISDLNMGRLVRGDLSKGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDGPL 235
Cdd:PLN02516 100 GILVQLPlPKHINEeKILNEISLEKDVDGFHPLNIGKLAMKGREPLFLPCTPKGCLELLSRSGIPIKGKKAVVVGRSNIV 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1724746110 236 GVALQCLIERSGMVALKSQWRSKSLQTQVMQADAVVLLGAGNMDVPPTWVRPGAAVIRCEpTLETDEPtiemSSKSGFR 314
Cdd:PLN02516 180 GLPVSLLLLKADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVG-TNAVSDP----SKKSGYR 253
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
94-292 |
1.66e-21 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 96.05 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 94 KRNPALQPMLAIIQAGEDDS--LLEINK-KMAGRIGLNITQICLAKECSEDEIVEELLKLNEDPRVHGVYLHLP-PASLT 169
Cdd:PRK14187 26 KRQHNLFPCLIVILVGDDPAsqLYVRNKqRKAEMLGLRSETILLPSTISESSLIEKINELNNDDSVHGILVQLPvPNHID 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 170 -SRVLNTLKPEKDVNGISDLNMGRLVRGDLSKGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDGPLGVALQCLI--ERS 246
Cdd:PRK14187 106 kNLIINTIDPEKDVDGFHNENVGRLFTGQKKNCLIPCTPKGCLYLIKTITRNLSGSDAVVIGRSNIVGKPMACLLlgENC 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1724746110 247 GMVALKSQwrSKSLQTQVMQADAVVL-LGAGNMdVPPTWVRPGAAVI 292
Cdd:PRK14187 186 TVTTVHSA--TRDLADYCSKADILVAaVGIPNF-VKYSWIKKGAIVI 229
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
101-314 |
9.40e-21 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 95.03 E-value: 9.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 101 PMLAIIQAGED-DSLLEINKKMAG--RIGLNITQICLAKECSEDEIVEELLKLNEDPRVHGVYLHLP-PASLT-SRVLNT 175
Cdd:PLN02897 87 PGLAVVLVGQQrDSQTYVRNKIKAceETGIKSLLAELPEDCTEGQILSALRKFNEDTSIHGILVQLPlPQHLDeSKILNM 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 176 LKPEKDVNGISDLNMGRLVRGDLSKGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDGPLGVALQCLIERSGMVALKSQW 255
Cdd:PLN02897 167 VRLEKDVDGFHPLNVGNLAMRGREPLFVSCTPKGCVELLIRSGVEIAGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHA 246
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 256 RSKSLQTQVMQADAVVL-LGAGNMdVPPTWVRPGAAVIRCEPTletdePTIEMSSKSGFR 314
Cdd:PLN02897 247 FTKDPEQITRKADIVIAaAGIPNL-VRGSWLKPGAVVIDVGTT-----PVEDSSCEFGYR 300
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
79-292 |
4.92e-20 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 91.38 E-value: 4.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 79 REIVQSAKEAMAAL---QKRNPALQPMLAIIQAGEDD-SLLEIN--KKMAGRIGLNITQICLAKECSEDEIVEELLKLNE 152
Cdd:PRK14172 8 KEVALKIKEEIKNFveeRKENGLSIPKIASILVGNDGgSIYYMNnqEKVANSLGIDFKKIKLDESISEEDLINEIEELNK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 153 DPRVHGVYLHLP-PASLTSR-VLNTLKPEKDVNGISDLNMGRLVRGDlsKGFVPPVASAVLDLLENHDAPLGGKSVLLVG 230
Cdd:PRK14172 88 DNNVHGIMLQLPlPKHLDEKkITNKIDANKDIDCLTFISVGKFYKGE--KCFLPCTPNSVITLIKSLNIDIEGKEVVVIG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1724746110 231 EDGPLGVAL-QCLIERSGMVALkSQWRSKSLQTQVMQADA-VVLLGAGNMdVPPTWVRPGAAVI 292
Cdd:PRK14172 166 RSNIVGKPVaQLLLNENATVTI-CHSKTKNLKEVCKKADIlVVAIGRPKF-IDEEYVKEGAIVI 227
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
101-292 |
7.71e-20 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 91.04 E-value: 7.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 101 PMLAIIQAGEDD---SLLEINKKMAGRIGLNITQICLAKECSEDEIVEELLKLNEDPRVHG--VYLHLPPASLTSRVLNT 175
Cdd:PRK14173 30 PHLRVVRLGEDPasvSYVRLKDRQAKALGLRSQVEVLPESTSQEELLELIARLNADPEVDGilVQLPLPPHIDFQRVLEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 176 LKPEKDVNGISDLNMGRLVRGdlSKGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDGPLGVALQCLIERSGMVALKSQW 255
Cdd:PRK14173 110 IDPLKDVDGFHPLNVGRLWMG--GEALEPCTPAGVVRLLKHYGIPLAGKEVVVVGRSNIVGKPLAALLLREDATVTLAHS 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 1724746110 256 RSKSLQTQVMQADAVVLLGAGNMDVPPTWVRPGAAVI 292
Cdd:PRK14173 188 KTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVV 224
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
85-292 |
2.94e-19 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 89.14 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 85 AKEAMAALQKRNPALQ------PMLAIIQAGeDDSLLEINKKMAG----RIGLNITQICLAKECSEDEIVEELLKLNEDP 154
Cdd:PRK14192 12 AKQIEEELSVRVEALKaktgrtPILATILVG-DDPASATYVRMKGnacrRVGMDSLKVELPQETTTEQLLAKIEELNANP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 155 RVHGVYLHLP-PASLTSRV-LNTLKPEKDVNGISDLNMGRLVRGDLSKGFVPPvaSAVLDLLENHDAPLGGKSVLLVGED 232
Cdd:PRK14192 91 DVHGILLQHPvPAQIDERAcFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATP--AGIMRLLKAYNIELAGKHAVVVGRS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1724746110 233 GPLGVALQCLIERSGMVALKSQWRSKSLQTQVMQADAVVllgaGNMDVP----PTWVRPGAAVI 292
Cdd:PRK14192 169 AILGKPMAMMLLNANATVTICHSRTQNLPELVKQADIIV----GAVGKPelikKDWIKQGAVVV 228
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
79-182 |
5.43e-19 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 83.22 E-value: 5.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 79 REIVQSAKEAMAALQKRNpaLQPMLAIIQAGED-DSLLEIN--KKMAGRIGLNITQICLAKECSEDEIVEELLKLNEDPR 155
Cdd:pfam00763 8 KKIREELKEEVAALKAGG--RKPGLAVILVGDDpASQVYVRnkKKACEEVGIESELIRLPEDTTEEELLALIDKLNADPS 85
|
90 100
....*....|....*....|....*....
gi 1724746110 156 VHGVYLHLP-PASL-TSRVLNTLKPEKDV 182
Cdd:pfam00763 86 VHGILVQLPlPKHIdEEKVLEAIDPEKDV 114
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
80-292 |
1.56e-18 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 86.99 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 80 EIVQSAKEAMAALQKRnpALQPMLAIIQAGED-DSLLEINKKMA--GRIGLNITQICLAKECSEDEIVEELLKLNEDPRV 156
Cdd:PRK14193 14 EIKADLAERVAALKEK--GITPGLGTVLVGDDpGSQAYVRGKHRdcAEVGITSIRRDLPADATQEELNAVIDELNADPAC 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 157 HGVYLHLP-PASL-TSRVLNTLKPEKDVNGISDLNMGRLVRGDLSKgfVPPVASAVLDLLENHDAPLGGKSVLLVGEDGP 234
Cdd:PRK14193 92 TGYIVQLPlPKHLdENAVLERIDPAKDADGLHPTNLGRLVLNEPAP--LPCTPRGIVHLLRRYDVELAGAHVVVIGRGVT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1724746110 235 LGVALQCLIERSGMVALKSQW--RSKSLQTQVMQADAVVL-LGAGNMdVPPTWVRPGAAVI 292
Cdd:PRK14193 170 VGRPIGLLLTRRSENATVTLChtGTRDLAAHTRRADIIVAaAGVAHL-VTADMVKPGAAVL 229
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
94-292 |
2.82e-18 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 86.34 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 94 KRNPALQPMLAIIQAGEDDS--LLEINK-KMAGRIGLNITQICLAKECSEDEIVEELLKLNEDPRVHGVYLHLP-PASLT 169
Cdd:PRK14179 26 KEEKGIVPGLVVILVGDNPAsqVYVRNKeRSALAAGFKSEVVRLPETISQEELLDLIERYNQDPTWHGILVQLPlPKHIN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 170 S-RVLNTLKPEKDVNGISDLNMGRLVRGdlSKGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDGPLGVAL-QCLIERSG 247
Cdd:PRK14179 106 EeKILLAIDPKKDVDGFHPMNTGHLWSG--RPVMIPCTPAGIMEMFREYNVELEGKHAVVIGRSNIVGKPMaQLLLDKNA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1724746110 248 MVALkSQWRSKSLQTQVMQADA-VVLLGAGNMdVPPTWVRPGAAVI 292
Cdd:PRK14179 184 TVTL-THSRTRNLAEVARKADIlVVAIGRGHF-VTKEFVKEGAVVI 227
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
99-292 |
5.24e-18 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 85.28 E-value: 5.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 99 LQPMLAIIQAGEDD-SLLEINKKMAG--RIGLNITQICLAKECSEDEIVEELLKLNEDPRVHGVYLHLP-PASL-TSRVL 173
Cdd:PRK14178 25 LYPRLATVIVGDDPaSQMYVRMKHRAceRVGIGSVGIELPGDATTRTVLERIRRLNEDPDINGILVQLPlPKGVdTERVI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 174 NTLKPEKDVNGISDLNMGRLVRGdlSKGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDGPLGVALQCLIERSGMVALKS 253
Cdd:PRK14178 105 AAILPEKDVDGFHPLNLGRLVSG--LPGFAPCTPNGIMTLLHEYKISIAGKRAVVVGRSIDVGRPMAALLLNADATVTIC 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 1724746110 254 QWRSKSLQTQVMQADAVVLLGAGNMDVPPTWVRPGAAVI 292
Cdd:PRK14178 183 HSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVI 221
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
79-292 |
1.54e-17 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 84.54 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 79 REIVQSAKEAMAALqKRNPALQPMLAIIQAGEDD---SLLEINKKMAGRIGLNITQICLAKECSEDEIVEELLKLNEDPR 155
Cdd:PRK14168 13 EEILEEIRGEVAEL-KEKYGKVPGLVTILVGESPaslSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLALIDKYNNDDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 156 VHGVYLHLP-PASLTS-RVLNTLKPEKDVNGISDLNMGRLVRGDLSKGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDG 233
Cdd:PRK14168 92 IHGILVQLPlPKHINEkKVLNAIDPDKDVDGFHPVNVGRLMIGGDEVKFLPCTPAGIQEMLVRSGVETSGAEVVVVGRSN 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1724746110 234 PLGVALQCLIERSGMVALKS----QWRSKSLQTQVMQAD-AVVLLGAGNMdVPPTWVRPGAAVI 292
Cdd:PRK14168 172 IVGKPIANMMTQKGPGANATvtivHTRSKNLARHCQRADiLIVAAGVPNL-VKPEWIKPGATVI 234
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
78-292 |
3.14e-17 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 83.57 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 78 LREIVQSAKEAMAALQKRNPALqpmlAIIQAGED--DSLLEINKKMA-GRIGLNITQICLAKECSEDEIVEELLKLNEDP 154
Cdd:PRK14186 14 IEQRLQAQIESNLPKAGRPPGL----AVLRVGDDpaSAVYVRNKEKAcARVGIASFGKHLPADTSQAEVEALIAQLNQDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 155 RVHGVYLHLP-PASL-TSRVLNTLKPEKDVNGISDLNMGRLVRGDlsKGFVPPVASAVLDLLENHDAPLGGKSV------ 226
Cdd:PRK14186 90 RVDGILLQLPlPKHLdEVPLLHAIDPDKDADGLHPLNLGRLVKGE--PGLRSCTPAGVMRLLRSQQIDIAGKKAvvvgrs 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1724746110 227 LLVGEdgPLGVALQcliERSGMVALkSQWRSKSLQTQVMQADAVVL-LGAGNMdVPPTWVRPGAAVI 292
Cdd:PRK14186 168 ILVGK--PLALMLL---AANATVTI-AHSRTQDLASITREADILVAaAGRPNL-IGAEMVKPGAVVV 227
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
80-292 |
3.21e-17 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 83.28 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 80 EIVQSAKEAMAALqKRNPALQPMLAIIQAGEDD-SLLEINKKMAG--RIGLNITQICLAKECSEDEIVEELLKLNEDPRV 156
Cdd:PRK14191 12 KIEKDLKNKIQIL-TAQTGKRPKLAVILVGKDPaSQTYVNMKIKAceRVGMDSDLHTLQENTTEAELLSLIKDLNTDQNI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 157 HGVYLHLP-PASL-TSRVLNTLKPEKDVNGISDLNMGRLVRGdlSKGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDGP 234
Cdd:PRK14191 91 DGILVQLPlPRHIdTKMVLEAIDPNKDVDGFHPLNIGKLCSQ--LDGFVPATPMGVMRLLKHYHIEIKGKDVVIIGASNI 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1724746110 235 LGVALQCLIERSGMVALKSQWRSKSLQTQVMQADAVVlLGAGNMD-VPPTWVRPGAAVI 292
Cdd:PRK14191 169 VGKPLAMLMLNAGASVSVCHILTKDLSFYTQNADIVC-VGVGKPDlIKASMVKKGAVVV 226
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
80-292 |
3.39e-17 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 83.08 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 80 EIVQSAKEAMAALQKRNPAlQPMLAIIQAGEDD-SLLEINKKM--AGRIGLNITQICLAKECSEDEIVEELLKLNEDPRV 156
Cdd:PRK14171 13 EILADLKLEIQELKSQTNA-SPKLAIVLVGDNPaSIIYVKNKIknAHKIGIDTLLVNLSTTIHTNDLISKINELNLDNEI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 157 HGVYLHLP-PASL-TSRVLNTLKPEKDVNGISDLNMGRLVRGdLSKGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDGP 234
Cdd:PRK14171 92 SGIIVQLPlPSSIdKNKILSAVSPSKDIDGFHPLNVGYLHSG-ISQGFIPCTALGCLAVIKKYEPNLTGKNVVIIGRSNI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1724746110 235 LGVALQCLIERSGMVALKSQWRSKSLQTQVMQADAVVLLGAGNMDVPPTWVRPGAAVI 292
Cdd:PRK14171 171 VGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVI 228
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
80-292 |
2.91e-16 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 80.21 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 80 EIVQSAKEAMAALQKRNpALQPMLAIIQAGED--DSLLEINKKMA-GRIGLNITQICLAKECSEDEIVEELLKLNEDPRV 156
Cdd:PRK14184 12 TIREELKTEVAALTARH-GRAPGLAVILVGEDpaSQVYVRNKERAcEDAGIVSEAFRLPADTTQEELEDLIAELNARPDI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 157 HGVYLHLP-PASLTS-RVLNTLKPEKDVNGISDLNMGRLVRGdlSKGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDGP 234
Cdd:PRK14184 91 DGILLQLPlPKGLDSqRCLELIDPAKDVDGFHPENMGRLALG--LPGFRPCTPAGVMTLLERYGLSPAGKKAVVVGRSNI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1724746110 235 LGVALQCLIERSGMVALKS----QWRSKSLQTQVMQADAVVLLGAGNMDVPPTWVRPGAAVI 292
Cdd:PRK14184 169 VGKPLALMLGAPGKFANATvtvcHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVV 230
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
79-301 |
5.56e-16 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 79.46 E-value: 5.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 79 REIVQSAKEAMAALqKRNPALQPMLAIIQAGEDDS---LLEINKKMAGRIGLNITQICLAKECSEDEIVEELLKLNEDPR 155
Cdd:PRK14176 18 KKIEAEVRSGVERL-KSNRGITPGLATILVGDDPAskmYVRLKHKACERVGIRAEDQFLPADTTQEELLELIDSLNKRKD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 156 VHGVYLHLP-PASLTSR-VLNTLKPEKDVNGISDLNMGRLVRGDlsKGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDG 233
Cdd:PRK14176 97 VHGILLQLPlPKHLDPQeAMEAIDPAKDADGFHPYNMGKLMIGD--EGLVPCTPHGVIRALEEYGVDIEGKNAVIVGHSN 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1724746110 234 PLGVALQC-LIERSGMVALKSQWrSKSLQTQVMQADAVVLLGAGNMDVPPTWVRPGAAVIRCEPTLETD 301
Cdd:PRK14176 175 VVGKPMAAmLLNRNATVSVCHVF-TDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITKEED 242
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
94-292 |
7.88e-16 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 79.10 E-value: 7.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 94 KRNPALQPMLAIIQAGED---DSLLEINKKMAGRIGLNITQICLAKECSEDEIVEELLKLNEDPRVHGVYLHLP-PASL- 168
Cdd:PRK14183 25 KLVKNIVPGLAVILVGDDpasHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETIAMMNNNPNIDGILVQLPlPKHId 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 169 TSRVLNTLKPEKDVNGISDLNMGRLVRGdlSKGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDGPLGVALQCLIERSGM 248
Cdd:PRK14183 105 TTKILEAIDPKKDVDGFHPYNVGRLVTG--LDGFVPCTPLGVMELLEEYEIDVKGKDVCVVGASNIVGKPMAALLLNANA 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1724746110 249 VALKSQWRSKSLQTQVMQADaVVLLGAGNMD-VPPTWVRPGAAVI 292
Cdd:PRK14183 183 TVDICHIFTKDLKAHTKKAD-IVIVGVGKPNlITEDMVKEGAIVI 226
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
95-243 |
3.05e-15 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 77.21 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 95 RNPALQPMLAIIQAGEDDSLlEINKKMAGRIGLNITQICLAKECSEDEIVEELLKL----NEDPRVHGVYLHLP-PASLT 169
Cdd:PRK14181 21 SASSTAPGLAVVLIGNDPAS-EVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLihrlNNDPNIHGILVQLPlPKHLD 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1724746110 170 SR-VLNTLKPEKDVNGISDLNMGRLVRGDLSkGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDGPLGVALQCLI 243
Cdd:PRK14181 100 AQaILQAISPDKDVDGLHPVNMGKLLLGETD-GFIPCTPAGIIELLKYYEIPLHGRHVAIVGRSNIVGKPLAALL 173
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
79-292 |
5.08e-15 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 76.52 E-value: 5.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 79 REIVQSAKEAMAALQKRNpaLQPMLAIIQAGEDDS---LLEINKKMAGRIGLNITQICLAKECSEDEIVEELLKLNEDPR 155
Cdd:PRK14169 11 KKILADLKQTVAKLAQQD--VTPTLAVVLVGSDPAsevYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAKVAELNHDPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 156 VHGVYLHLP-PASLTSR-VLNTLKPEKDVNGISDLNMGRLVRGDlsKGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDG 233
Cdd:PRK14169 89 VDAILVQLPlPAGLDEQaVIDAIDPDKDVDGFSPVSVGRLWANE--PTVVASTPYGIMALLDAYDIDVAGKRVVIVGRSN 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1724746110 234 PLGVALQCLIERSGMVALKSQWRSKSLQTQVMQADAVVLLGAGNMDVPPTWVRPGAAVI 292
Cdd:PRK14169 167 IVGRPLAGLMVNHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVI 225
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
79-292 |
9.00e-15 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 75.88 E-value: 9.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 79 REIVQSAKEAMAALQKRNPalQPMLAIIQAGEDD---SLLEINKKMAGRIGLNITQICLAKECSEDEIVEELLKLNEDPR 155
Cdd:PRK14170 12 KEIQEKVTREVAELVKEGK--KPGLAVVLVGDNQasrTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSVVEELNEDKT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 156 VHGVYLHLP-PASLT-SRVLNTLKPEKDVNGISDLNMGRLVRGDLSkgFVPPVASAVLDLLENHDAPLGGKSVLLVGEDG 233
Cdd:PRK14170 90 IHGILVQLPlPEHISeEKVIDTISYDKDVDGFHPVNVGNLFIGKDS--FVPCTPAGIIELIKSTGTQIEGKRAVVIGRSN 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1724746110 234 PLG--VALQCLIERSGMVALKSqwRSKSLQTQVMQADAVVLLGAGNMDVPPTWVRPGAAVI 292
Cdd:PRK14170 168 IVGkpVAQLLLNENATVTIAHS--RTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVI 226
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
101-292 |
1.37e-13 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 72.26 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 101 PMLAIIQAGEDD-SLLEI-NKKMA-GRIGLNITQICLAKECSEDEIVEELLKLNEDPRVHGVYLHLP-PASL-TSRVLNT 175
Cdd:PRK10792 34 PGLAVVLVGSDPaSQVYVaSKRKAcEEVGFVSRSYDLPETTSEAELLALIDELNADPTIDGILVQLPlPAHIdNVKVLER 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 176 LKPEKDVNGISDLNMGRL------VRGDLSKGfvppvasaVLDLLENHDAPLGGKSVLLVGEDGPLG--VALQCLIerSG 247
Cdd:PRK10792 114 IHPDKDVDGFHPYNVGRLaqriplLRPCTPRG--------IMTLLERYGIDTYGLNAVVVGASNIVGrpMSLELLL--AG 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1724746110 248 MVALKSQWRSKSLQTQVMQAD-AVVLLGAGNMdVPPTWVRPGAAVI 292
Cdd:PRK10792 184 CTVTVCHRFTKNLRHHVRNADlLVVAVGKPGF-IPGEWIKPGAIVI 228
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
70-292 |
2.30e-13 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 71.54 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 70 EGFECDSSLREIVQSAKEAMAALQKRNPALqpmlAIIQAGED---DSLLEINKKMAGRIGLNITQICLAKECSEDEIVEE 146
Cdd:PRK14177 7 DGKKLSEKIRNEIRETIEERKTKNKRIPKL----ATILVGNNpasETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 147 LLKLNEDPRVHGVYLHLP-PASLTSR-VLNTLKPEKDVNGISDLNMGRLVRGdlSKGFVPPVASAVLDLLENHDAPLGGK 224
Cdd:PRK14177 83 IDKLNLDPNVDGILLQHPvPSQIDERaAFDRIALEKDVDGVTTLSFGKLSMG--VETYLPCTPYGMVLLLKEYGIDVTGK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 225 SVLLVGEDGPLGVALQCLIERSGMVALKSQWRSKSLQTQVMQADAVVllGA-GNMD-VPPTWVRPGAAVI 292
Cdd:PRK14177 161 NAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIV--GAvGKPEfIKADWISEGAVLL 228
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
186-333 |
2.63e-13 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 68.65 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 186 SDLNMGRLVRGDlsKGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDGPLGVALQCLIERSG-MVALkSQWRSKSLQTQV 264
Cdd:pfam02882 1 HPYNLGRLVLGK--PCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANaTVTV-CHSKTKDLAEIT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 265 MQADAVVL-LGAGNMdVPPTWVRPGAAVIRC------EPTLETDEPTIEMSSKSGFRY--------LTAAYRSQNVVRSG 329
Cdd:pfam02882 78 READIVVVaVGKPEL-IKADWIKPGAVVIDVginrvgNGKLVGDVDFENVKEKASAITpvpggvgpMTVAMLLQNTVEAA 156
|
....
gi 1724746110 330 RRWL 333
Cdd:pfam02882 157 KRQL 160
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
80-292 |
3.31e-13 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 71.21 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 80 EIVQSAKEAMAALQKRnpALQPMLAIIQAGED---DSLLEINKKMAGRIGLNITQICLAKECSEDEIVEELLKLNEDPRV 156
Cdd:PRK14166 12 KIKEELKEKNQFLKSK--GIESCLAVILVGDNpasQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALINTLNHDDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 157 HGVYLHLP-PASLTSR-VLNTLKPEKDVNGISDLNMGRLVRGdLSKGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDGP 234
Cdd:PRK14166 90 HGILVQLPlPDHICKDlILESIISSKDVDGFHPINVGYLNLG-LESGFLPCTPLGVMKLLKAYEIDLEGKDAVIIGASNI 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1724746110 235 LGVALQCLIERSGMVALKSQWRSKSLQTQVMQADaVVLLGAGNMD-VPPTWVRPGAAVI 292
Cdd:PRK14166 169 VGRPMATMLLNAGATVSVCHIKTKDLSLYTRQAD-LIIVAAGCVNlLRSDMVKEGVIVV 226
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
178-292 |
7.19e-13 |
|
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: 67.58 E-value: 7.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 178 PEKDVNGISDLNMGRLVRGDlsKGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDGPLGVAL-QCLIERSGMVALKSQwR 256
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGR--PGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLaALLLNRNATVTVCHS-K 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1724746110 257 SKSLQTQVMQADAVVL-LGAGNMdVPPTWVRPGAAVI 292
Cdd:cd01080 78 TKNLKEHTKQADIVIVaVGKPGL-VKGDMVKPGAVVI 113
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
94-292 |
3.97e-12 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 68.13 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 94 KRNPALQPMLAIIQAGED---DSLLEINKKMAGRIGLNITQICLAKECSEDEIVEELLKLNEDPRVHGVYLHLP-PASLT 169
Cdd:PRK14180 25 KHHTAITPKLVAIIVGNDpasKTYVASKEKACAQVGIDSQVITLPEHTTESELLELIDQLNNDSSVHAILVQLPlPAHIN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 170 -SRVLNTLKPEKDVNGISDLNMGRLVRGDlSKGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDGPLGVALQCLIERSGM 248
Cdd:PRK14180 105 kNNVIYSIKPEKDVDGFHPTNVGRLQLRD-KKCLESCTPKGIMTMLREYGIKTEGAYAVVVGASNVVGKPVSQLLLNAKA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1724746110 249 VALKSQWRSKSLQTQVMQADAVVLLGAGNMDVPPTWVRPGAAVI 292
Cdd:PRK14180 184 TVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVI 227
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
79-314 |
4.13e-12 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 67.93 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 79 REIVQSAKEAMAALQKRnpalqPMLAIIQAGED---DSLLEINKKMAGRIGLNITQICLAKECSEDEIVEELLKLNEDPR 155
Cdd:PRK14185 15 QEIAAEVAEIVAKGGKR-----PHLAAILVGHDggsETYVANKVKACEECGFKSSLIRYESDVTEEELLAKVRELNQDDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 156 VHG--VYLHLPPASLTSRVLNTLKPEKDVNGISDLNMGRLVRGdlSKGFVPPVASAVLDLLENHDAPLGGKSVLLVGEDG 233
Cdd:PRK14185 90 VDGfiVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIG--LPCFVSATPNGILELLKRYHIETSGKKCVVLGRSN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 234 PLGVALQCLIERSGM----VALKSQWRSKSLQTQVMQADAVVL-LGAGNMdVPPTWVRPGAAVIRCEPTLETDEptiemS 308
Cdd:PRK14185 168 IVGKPMAQLMMQKAYpgdcTVTVCHSRSKNLKKECLEADIIIAaLGQPEF-VKADMVKEGAVVIDVGTTRVPDA-----T 241
|
....*.
gi 1724746110 309 SKSGFR 314
Cdd:PRK14185 242 RKSGFK 247
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
70-230 |
4.69e-10 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 61.72 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 70 EGFECDSSLREIVQSAKEAMAalqkrNPALQPMLAIIQAGED---DSLLEINKKMAGRIGLNITQICLAKECSEDEIVEE 146
Cdd:PRK14167 6 DGNAVAAQIRDDLTDAIETLE-----DAGVTPGLATVLMSDDpasETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724746110 147 LLKLNEDPRVHGVYLHLP-PASLTSR-VLNTLKPEKDVNGISDLNMGRLVRGDLSkgFVPPVASAVLDLLENHDAPLGGK 224
Cdd:PRK14167 81 IDELNADEDVHGILVQMPvPDHVDDReVLRRIDPAKDVDGFHPENVGRLVAGDAR--FKPCTPHGIQKLLAAAGVDTEGA 158
|
....*.
gi 1724746110 225 SVLLVG 230
Cdd:PRK14167 159 DVVVVG 164
|
|
| |
