|
Name |
Accession |
Description |
Interval |
E-value |
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
316-934 |
0e+00 |
|
Formate--tetrahydrofolate ligase;
Pssm-ID: 460143 Cd Length: 555 Bit Score: 933.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 316 PSDIVIARAQKPKDIAVLAKEIGLEAREVSLYGNKKAKISLSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTTLMGLVQA 395
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 396 LGaHKLRNTMAALRQPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHENTqkdkaly 475
Cdd:pfam01268 81 LN-RLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 476 drlvpaikgqrkfspiqlrrlqklgitktdpdtltadeygpfarLDIDPDTIMWERVVDINDRYLRTITVGQSPTEKGIS 555
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 556 RETRFSISVASEIMAVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLEGTPVLVHA 635
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 636 GPFANIAHGCNSIIADEVGLKLvgkNGFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHGGgapvtPG 715
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGG-----VG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 716 AplnKQYTEENLELVQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKaALEAGAFAAVVSTHWADGGAGAV 795
Cdd:pfam01268 341 K---DELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRE-LCEAGGVDAALSEHWAKGGEGAI 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 796 QLADAVIKACEQG-NQFRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRLTDAGFGNLPICMSKVSGSFTGDA 874
Cdd:pfam01268 417 ELAEAVVEACEEEpSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 875 KIKGAPKGFTLDVEDVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNTEtGEIEGLF 934
Cdd:pfam01268 497 KLKGAPTGFTLPVRDVRLSAGAGFIVALTGDIMTMPGLPKRPAAENIDVDED-GKITGLF 555
|
|
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
309-934 |
0e+00 |
|
Formate--tetrahydrofolate ligase
Pssm-ID: 178359 Cd Length: 637 Bit Score: 912.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 309 LKPQRPVPSDIVIARAQKPKDIAVLAKEIGLEAREVSLYGNKKAKISLSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTT 388
Cdd:PLN02759 10 LEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKSTT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 389 LMGLVQALGAHKLRNTMAALRQPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHENT 468
Cdd:PLN02759 90 TIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEAT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 469 QKDKALYDRLVPAIK-GQRKFSPIQLRRLQKLGITKTDPDTLTADEYGPFARLDIDPDTIMWERVVDINDRYLRTITVGQ 547
Cdd:PLN02759 170 QSDKALFNRLCPANKeGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVGQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 548 SPTEKGISRETRFSISVASEIMAVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLE 627
Cdd:PLN02759 250 GPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTLE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 628 GTPVLVHAGPFANIAHGCNSIIADEVGLKLVGKNGFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHG 707
Cdd:PLN02759 330 GTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMHG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 708 GGAPVTPGAPLNKQYTEENLELVQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKAALEAGAFAAVVSTHW 787
Cdd:PLN02759 410 GGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTHH 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 788 ADGGAGAVQLADAVIKACEQGNQ-FRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRLTDAGFGNLPICMSKV 866
Cdd:PLN02759 490 AHGGKGAVDLGEAVQKACEGNSQpFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAKT 569
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24645718 867 SGSFTGDAKIKGAPKGFTLDVEDVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNTETGEIEGLF 934
Cdd:PLN02759 570 QYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTETGKVLGLS 637
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
330-933 |
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: 887.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 330 IAVLAKEIGLEAREVSLYGNKKAKISLSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTTLMGLVQALGAHkLRNTMAALR 409
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGAL-GKKAIAALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 410 QPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHENTqkdkalydrlvpaikgqrkfs 489
Cdd:cd00477 80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 490 piqlrrlqklgitktdpdtltadeygpfarLDIDPDTIMWERVVDINDRYLRTITVGQSPTEKGISRETRFSISVASEIM 569
Cdd:cd00477 139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 570 AVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLEGTPVLVHAGPFANIAHGCNSII 649
Cdd:cd00477 189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 650 ADEVGLKLvgkNGFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHGGGAPVTPGaplnkqytEENLEL 729
Cdd:cd00477 269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 730 VQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKaALEAGAFAAVVSTHWADGGAGAVQLADAVIKACEQ-G 808
Cdd:cd00477 338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRE-LAEEAGAEVAVSEHWAKGGKGALELAEAVIEACEKpK 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 809 NQFRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRLTDAGFGNLPICMSKVSGSFTGDAKIKGAPKGFTLDVE 888
Cdd:cd00477 417 SNFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 24645718 889 DVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNtETGEIEGL 933
Cdd:cd00477 497 DVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDID-DTGKIEGL 540
|
|
| PTZ00386 |
PTZ00386 |
formyl tetrahydrofolate synthetase; Provisional |
312-933 |
0e+00 |
|
formyl tetrahydrofolate synthetase; Provisional
Pssm-ID: 240394 Cd Length: 625 Bit Score: 862.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 312 QRPVPSDIVIARAQKPKDIAVLAKEIGLEAREVSLYGNKKAKISLSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTTLMG 391
Cdd:PTZ00386 12 QWPVPSDIDIAQSVKPQPITSVAESAGILLSELDPYGSTRAKVKLSVLKRLENSPNGKYVVVAGMNPTPLGEGKSTTTIG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 392 LVQALGAHKLRNTMAALRQPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHENTQKD 471
Cdd:PTZ00386 92 LAQSLGAHLHRKTFACIRQPSQGPTFGIKGGAAGGGYSQVIPMEDFNLHGTGDIHAITAANNLLAAALDTRIFHERTQSD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 472 KALYDRLVpaiKGQRKFSPIQLRRLQKLGITKTDPDTLTADEYGPFARLDIDPDTIMWERVVDINDRYLRTITVGQSPTE 551
Cdd:PTZ00386 172 AALYRRLT---DELKKFTPIMLKRLEKLGISKTDPKQLTEEERVRFARLDIDPDTISWRRVTDVNDRMLREITIGQGKEE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 552 KGISRETRFSISVASEIMAVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLEGTPV 631
Cdd:PTZ00386 249 KGITRKTGFDISVASEVMAILALATDLADMRQRLGAIVVAKSKSGEPVTAEDLGCAGAMTVLMKDTIEPTLMQTLEGTPV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 632 LVHAGPFANIAHGCNSIIADEVGLKLVGKNGFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHGGGAP 711
Cdd:PTZ00386 329 LVHAGPFGNIAHGNSSIVADQIALKLAGQDGFVLTEAGFGADIGCEKFFNIKCRTSGLKPDAAVLVATVRALKFHGGVEP 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 712 VTPGaplnkqytEENLELVQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKAALEAG-AFAAVVSTHWADG 790
Cdd:PTZ00386 409 VVAG--------KENLEAVRKGLSNLQRHIQNIRKFGVPVVVALNKFSTDTDAELELVKELALQEGgAADVVVTDHWAKG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 791 GAGAVQLADAVIKACEQG-NQFRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRLTDAGFGNLPICMSKVSGS 869
Cdd:PTZ00386 481 GAGAVDLAQALIRVTENVpSNFKLLYPLDASLKEKIETICKEIYGAAGVEYLNDADEKLEDFERMGYGKFPVCMAKTQYS 560
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24645718 870 FTGDAKIKGAPKGFTLDVEDVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNTETGEIEGL 933
Cdd:PTZ00386 561 FSHDPELRGAPTGFTVPIRDVRVNCGAGFVFPLLGDISTMPGLPTRPAFYNIDIDCETGKIVGL 624
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
315-934 |
0e+00 |
|
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
Pssm-ID: 442046 Cd Length: 556 Bit Score: 844.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 315 VPSDIVIARAQKPKDIAVLAKEIGLEAREVSLYGNKKAKISLSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTTLMGLVQ 394
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 395 ALGahKL-RNTMAALRQPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHENtqkdka 473
Cdd:COG2759 81 ALN--RLgKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQGN------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 474 lydrlvpaikgqrkfspiqlrrlqklgitktdpdtltadeygpfaRLDIDPDTIMWERVVDINDRYLRTITVGQSPTEKG 553
Cdd:COG2759 153 ---------------------------------------------ELNIDPRRITWKRVLDMNDRALRNIVIGLGGKANG 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 554 ISRETRFSISVASEIMAVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLEGTPVLV 633
Cdd:COG2759 188 VPREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFV 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 634 HAGPFANIAHGCNSIIADEVGLKLvgkNGFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHGGGApvt 713
Cdd:COG2759 268 HGGPFANIAHGCNSVIATKLALKL---ADYVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA--- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 714 pgaplNKQYTEENLELVQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKaALEAGAFAAVVSTHWADGGAG 793
Cdd:COG2759 342 -----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRE-LCEELGVRVALSEVWAKGGEG 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 794 AVQLADAVIKACEQG-NQFRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRLTDAGFGNLPICMSKVSGSFTG 872
Cdd:COG2759 416 AEELAEAVVEACEEGpSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSD 495
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24645718 873 DAKIKGAPKGFTLDVEDVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNtETGEIEGLF 934
Cdd:COG2759 496 DPKLLGAPTGFTLTVREVRLSAGAGFIVALTGDIMTMPGLPKVPAAERIDID-EDGKITGLF 556
|
|
| PRK13505 |
PRK13505 |
formate--tetrahydrofolate ligase; Provisional |
314-934 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237403 Cd Length: 557 Bit Score: 733.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 314 PVPSDIVIARAQKPKDIAVLAKEIGLEAREVSLYGNKKAKISLSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTTLMGLV 393
Cdd:PRK13505 1 TMKSDIEIAQEATLKPITEIAAKLGIPEDDLEPYGKYKAKISLDKIKALKDKKDGKLILVTAINPTPAGEGKSTVTVGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 394 QALgAHKLRNTMAALRQPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHENTqkdka 473
Cdd:PRK13505 81 DAL-NKIGKKTVIALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITSANNLLAALIDNHIHQGNE----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 474 lydrlvpaikgqrkfspiqlrrlqklgitktdpdtltadeygpfarLDIDPDTIMWERVVDINDRYLRTITVGQSPTEKG 553
Cdd:PRK13505 155 ----------------------------------------------LGIDPRRITWKRVLDMNDRALRNIVVGLGGPANG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 554 ISRETRFSISVASEIMAVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLEGTPVLV 633
Cdd:PRK13505 189 VPREDGFDITVASEIMAILCLATDLKDLKERLGRIVVGYTYDGKPVTVKDLKVEGAMALLLKDAIKPNLVQTLEGTPAFV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 634 HAGPFANIAHGCNSIIADEVGLKLvgkNGFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHGGGApvt 713
Cdd:PRK13505 269 HGGPFANIAHGCNSVLATKTALKL---ADYVVTEAGFGADLGAEKFLDIKCRKAGLKPDAVVIVATVRALKMHGGVA--- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 714 pgaplNKQYTEENLELVQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKaALEAGAFAAVVSTHWADGGAG 793
Cdd:PRK13505 343 -----KDDLKEENVEALKKGFANLERHIENIRKFGVPVVVAINKFVTDTDAEIAALKE-LCEELGVEVALSEVWAKGGEG 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 794 AVQLADAVIKACEQG-NQFRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRLTDAGFGNLPICMSKVSGSFTG 872
Cdd:PRK13505 417 GVELAEKVVELIEEGeSNFKPLYDDEDSLEEKIEKIATKIYGAKGVEFSPKAKKQLKQIEKNGWDKLPVCMAKTQYSFSD 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24645718 873 DAKIKGAPKGFTLDVEDVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNtETGEIEGLF 934
Cdd:PRK13505 497 DPKLLGAPTGFTITVRELRPSAGAGFIVALTGDIMTMPGLPKVPAALNIDVD-EDGNIVGLF 557
|
|
| PRK13506 |
PRK13506 |
formate--tetrahydrofolate ligase; Provisional |
317-933 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237404 Cd Length: 578 Bit Score: 673.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 317 SDIVIARAQKPKDIAVLAKEIGLEAREVSLYGNKKAKISLSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTTLMGLVQAL 396
Cdd:PRK13506 3 SDIEISRQAPLKPIAEIAAKLGLLPDELSPFGHTKAKVSLSVLKRLADKPKGKLVLVTAITPTPLGEGKTVTTIGLTQGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 397 gAHKLRNTMAALRQPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHEntqkdkalyd 476
Cdd:PRK13506 83 -NALGQKVCACIRQPSMGPVFGVKGGAAGGGYAQVVPMEELNLHLTGDIHAVSAAHNLAAAAIDARLFHE---------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 477 rlvpaikgqrkfspiqlrrlQKLGitktdpdtltADEYGP---FARLDIDPDTIMWERVVDINDRYLRTITVGQSPTEKG 553
Cdd:PRK13506 152 --------------------QRLG----------YDAFEAqsgLPALDIDPEQILWKRVVDHNDRALRMITVGLGENGNG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 554 ISRETRFSISVASEIMAVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLEGTPVLV 633
Cdd:PRK13506 202 PEREDGFDITAASELMAILALSRDLKDMRQRIGRLVLAYNLQGQPITAEDLGVAGAMTVIMKDAIEPTLMQTLEGVPCLI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 634 HAGPFANIAHGCNSIIADEVGLKLVGkngFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHGGGAPVT 713
Cdd:PRK13506 282 HAGPFANIAHGNSSIIADRIALKLAD---YVVTEGGFGSDMGFEKFCNIKARQSGKAPDCAVLVATLRALKANSGLYDLR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 714 PGAPLNKQYTEENLELVQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKAALEAGAFAAVVSTHWADGGAG 793
Cdd:PRK13506 359 PGQALPDSINAPDQARLEAGFANLKWHINNVAQYGLPVVVAINRFPTDTDEELEWLKEAVLLTGAFGCEISEAFAQGGEG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 794 AVQLADAVIKACEQGNQFRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRLTDAGFGNLPICMSKVSGSFTGD 873
Cdd:PRK13506 439 ATALAQAVVRACEQPSQFKLLYPDEMSLEAKLMTLAEVGYGAAGVSLSDKAKQQLAQLTALGYDHLPVCMAKTPLSISHD 518
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 874 AKIKGAPKGFTLDVEDVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNtETGEIEGL 933
Cdd:PRK13506 519 PALKGAPTDFEVPIRELRLCAGAGFITALVGNVMTMPGLGLKPGYLNIDID-ADGEIVGL 577
|
|
| PRK13507 |
PRK13507 |
formate--tetrahydrofolate ligase; Provisional |
318-934 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 184098 Cd Length: 587 Bit Score: 622.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 318 DIVIA-RAQKP-KDIAVLAKEIGLEAREVSLYGNKKAKIS-LSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTTLMGLVQ 394
Cdd:PRK13507 10 DWEIAeEAEKFmKPVEELAEELGLTKEELLPYGHYIAKVDfRKVLDRLKDRPDGKYIDVTAITPTPLGEGKSTTTMGLVQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 395 ALGAhKLRNTMAALRQPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHENTQKDKAL 474
Cdd:PRK13507 90 GLGK-RGKKVSGAIRQPSGGPTMNIKGSAAGGGLSQCIPLTPFSLGLTGDINAIMNAHNLAMVALTARMQHERNYTDEQL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 475 YDRlvpaikGQRkfspiqlrrlqklgitktdpdtltadeygpfaRLDIDPDTIMWERVVDINDRYLRTITVGQSPTEKGI 554
Cdd:PRK13507 169 ARR------GLK--------------------------------RLDIDPTRVEMGWIIDFCAQALRNIIIGIGGKTDGY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 555 SRETRFSISVASEIMAVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLEGTPVLVH 634
Cdd:PRK13507 211 MMQSGFGIAVSSEVMAILSVATDLKDLRERIGKIVVAYDKNGKPVTTADLEVDGAMTAWMVRAINPNLLQTIEGQPVFVH 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 635 AGPFANIAHGCNSIIADEVGLKLvgkNGFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHGGGAPVTP 714
Cdd:PRK13507 291 AGPFANIAIGQSSIIADRVGLKL---ADYHVTESGFGADIGFEKFWNLKCRLSGLKPDCAVIVATIRALKMHGGGPKVVP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 715 GAPLNKQYTEENLELVQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKAALEAGAFAAvVSTHWADGGAGA 794
Cdd:PRK13507 368 GKPLPEEYTKENVGLVEKGCANLLHHIGTVKKSGINPVVCINAFYTDTHAEIAIVRRLAEQAGARVA-VSRHWEKGGEGA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 795 VQLADAVIKACEQGNQFRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRL-TDAGFGNLPICMSKVSGSFTGD 873
Cdd:PRK13507 447 LELADAVIDACNEPNDFKFLYPLEMPLRERIETIAREVYGADGVSYTPEAEAKLKRLeSDPETADFGTCMVKTHLSLSHD 526
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24645718 874 AKIKGAPKGFTLDVEDVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNTETGEIEGLF 934
Cdd:PRK13507 527 PALKGVPKGWTLPIRDILTYGGAGFVVPVAGDISLMPGTGSDPAFRRIDVDTQTGKVKGLF 587
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
1-292 |
1.99e-144 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 429.82 E-value: 1.99e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 1 MSgAKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVE 80
Cdd:COG0190 1 MM-AQILDGKAVAAEIREELKERVAALKAK--GITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 81 LLDKINDLNEDPRVHGIIVQMPLdcdtP--IDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRS 158
Cdd:COG0190 78 LLALIDELNADPSVHGILVQLPL----PkhIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGE-PGFVPCTPAGIMELLERY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 159 GVEIAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGIN 238
Cdd:COG0190 153 GIDLAGKHAVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGIN 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 24645718 239 VKPDaskasgSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 292
Cdd:COG0190 233 RVED------GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-292 |
1.80e-108 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 336.93 E-value: 1.80e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 4 AKIISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 83
Cdd:PRK14188 2 ATIIDGKAFAADVRATVAAEVARLKAA-HGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 84 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIA 163
Cdd:PRK14188 81 LIARLNADPAIHGILVQLPLP--KHLDSEAVIQAIDPEKDVDGLHVVNAGRLATG-ETALVPCTPLGCMMLLRRVHGDLS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 164 GARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDA 243
Cdd:PRK14188 158 GLNAVVIGRSNLVGKPMAQLLLAANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIPAP 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 24645718 244 SKASG-SKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 292
Cdd:PRK14188 238 EKGEGkTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACR 287
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-296 |
1.04e-107 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 334.29 E-value: 1.04e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 4 AKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 83
Cdd:PRK14190 3 AVIIDGKEVAKEKREQLKEEVVKLKEQ--GIVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 84 KINDLNEDPRVHGIIVQMPLdcdtP--IDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVE 161
Cdd:PRK14190 81 LIDRLNADPRINGILVQLPL----PkhIDEKAVIERISPEKDVDGFHPINVGRMMLGQ-DTFLPCTPHGILELLKEYNID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 162 IAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkp 241
Cdd:PRK14190 156 ISGKHVVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVN--- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 24645718 242 dasKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARFLER 296
Cdd:PRK14190 233 ---RLENGKLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKRAGGR 284
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
2-292 |
1.12e-107 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 337.36 E-value: 1.12e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 2 SGAKIISGTAVAKSIREELRNEVTAMSKQLAdFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVEL 81
Cdd:PLN02616 71 GGAKVIDGKAVAKKIRDEITIEVSRMKESIG-VVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 82 LDKINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAI-GDLGGFLPCTPWGCLELIRRSGV 160
Cdd:PLN02616 150 LKFISGFNNDPSVHGILVQLPLP--SHMDEQNILNAVSIEKDVDGFHPLNIGRLAMrGREPLFVPCTPKGCIELLHRYNV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 161 EIAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVK 240
Cdd:PLN02616 228 EIKGKRAVVIGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPV 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 24645718 241 PDASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 292
Cdd:PLN02616 308 EDASSPRGYRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKR 359
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
4-292 |
1.22e-105 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 329.55 E-value: 1.22e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 4 AKIISGTAVAKSIREELRNEVTAMSKQLADfVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 83
Cdd:PLN02516 9 AQIIDGKAIAKAIRSEIAEEVAQLSEKHGK-VPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELIS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 84 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAI-GDLGGFLPCTPWGCLELIRRSGVEI 162
Cdd:PLN02516 88 KVHELNANPDVHGILVQLPLP--KHINEEKILNEISLEKDVDGFHPLNIGKLAMkGREPLFLPCTPKGCLELLSRSGIPI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 163 AGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPD 242
Cdd:PLN02516 166 KGKKAVVVGRSNIVGLPVSLLLLKADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVSD 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 24645718 243 ASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 292
Cdd:PLN02516 246 PSKKSGYRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKR 295
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
4-292 |
6.15e-102 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 319.33 E-value: 6.15e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 4 AKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 83
Cdd:PRK14189 3 AQLIDGNALSKQLRAEAAQRAAALTAR--GHQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 84 KINDLNEDPRVHGIIVQMPLdcdtP--IDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVE 161
Cdd:PRK14189 81 RIDELNRDPKIHGILVQLPL----PkhIDSHKVIEAIAPEKDVDGFHVANAGALMTG-QPLFRPCTPYGVMKMLESIGIP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 162 IAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvKP 241
Cdd:PRK14189 156 LRGAHAVVIGRSNIVGKPMAMLLLQAGATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMN-RD 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 24645718 242 DAskasgSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 292
Cdd:PRK14189 235 DA-----GKLCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAER 280
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-296 |
1.79e-96 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 304.92 E-value: 1.79e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 4 AKIISGTAVAKSIREELRNEVTAMsKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 83
Cdd:PRK10792 3 AKIIDGKTIAQQVRSEVAQKVQAR-VAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 84 KINDLNEDPRVHGIIVQMPLdcdtP--IDSHRITDAVSPEKDVDGLHTVNEGRLAIgDLGGFLPCTPWGCLELIRRSGVE 161
Cdd:PRK10792 82 LIDELNADPTIDGILVQLPL----PahIDNVKVLERIHPDKDVDGFHPYNVGRLAQ-RIPLLRPCTPRGIMTLLERYGID 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 162 IAGARAVVLGRSKIVGTPAA-ELLkWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvk 240
Cdd:PRK10792 157 TYGLNAVVVGASNIVGRPMSlELL-LAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGIN-- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 24645718 241 pdasKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARFLER 296
Cdd:PRK10792 234 ----RLEDGKLVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEEYHDP 285
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-293 |
3.15e-94 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 299.43 E-value: 3.15e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 6 IISGTAVAKSIREELRNEVTAMsKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 85
Cdd:PRK14174 3 IIDGKKVSLDLKNELKTRVEAY-RAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 86 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGG-FLPCTPWGCLELIRRSGVEIAG 164
Cdd:PRK14174 82 EDLNNDPDVHGILVQQPLP--KQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGHLDKcFVSCTPYGILELLGRYNIETKG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 165 ARAVVLGRSKIVGTPAAEL----LKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVK 240
Cdd:PRK14174 160 KHCVVVGRSNIVGKPMANLmlqkLKESNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 24645718 241 PDASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARF 293
Cdd:PRK14174 240 EDPSTKSGYRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTLQSFERV 292
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
4-292 |
1.08e-93 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 299.95 E-value: 1.08e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 4 AKIISGTAVAKSIREELRNEVTAMSKQLADfVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 83
Cdd:PLN02897 56 TVVIDGNVIAEEIRTKIASEVRKMKKAVGK-VPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 84 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAI-GDLGGFLPCTPWGCLELIRRSGVEI 162
Cdd:PLN02897 135 ALRKFNEDTSIHGILVQLPLP--QHLDESKILNMVRLEKDVDGFHPLNVGNLAMrGREPLFVSCTPKGCVELLIRSGVEI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 163 AGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPD 242
Cdd:PLN02897 213 AGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPVED 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 24645718 243 ASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 292
Cdd:PLN02897 293 SSCEFGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKR 342
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
120-290 |
3.91e-92 |
|
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: 288.68 E-value: 3.91e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 120 PEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTR 199
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGR-PGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKTK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 200 NLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDASKasgSKLVGDVDYAEALQVAGHLTPVPGGVGPMTV 279
Cdd:cd01080 80 NLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDKSG---GKLVGDVDFESAKEKASAITPVPGGVGPMTV 156
|
170
....*....|.
gi 24645718 280 AMLMKNTVRSA 290
Cdd:cd01080 157 AMLMKNTVEAA 167
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-289 |
5.08e-92 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 293.51 E-value: 5.08e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 4 AKIISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 83
Cdd:PRK14186 2 ALILDGKALAAEIEQRLQAQIESNLPK-AGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 84 KINDLNEDPRVHGIIVQMPLdcdtP--IDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVE 161
Cdd:PRK14186 81 LIAQLNQDERVDGILLQLPL----PkhLDEVPLLHAIDPDKDADGLHPLNLGRLVKGE-PGLRSCTPAGVMRLLRSQQID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 162 IAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKP 241
Cdd:PRK14186 156 IAGKKAVVVGRSILVGKPLALMLLAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHRLP 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 24645718 242 DASKAsgSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRS 289
Cdd:PRK14186 236 SSDGK--TRLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLS 281
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-297 |
6.81e-92 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 292.83 E-value: 6.81e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 5 KIISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDK 84
Cdd:PRK14191 2 VLLDGKALSYKIEKDLKNKIQILTAQ-TGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 85 INDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIAG 164
Cdd:PRK14191 81 IKDLNTDQNIDGILVQLPLP--RHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQ-LDGFVPATPMGVMRLLKHYHIEIKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 165 ARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDAs 244
Cdd:PRK14191 158 KDVVIIGASNIVGKPLAMLMLNAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLNDG- 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 24645718 245 kasgsKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARFLERL 297
Cdd:PRK14191 237 -----RLVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEKRQRKG 284
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
4-296 |
9.20e-89 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 284.34 E-value: 9.20e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 4 AKIISGTAVAKSIREELRNEVTAMsKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 83
Cdd:PRK14179 2 TEIIDGKALAQKMQAELAEKVAKL-KEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 84 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIA 163
Cdd:PRK14179 81 LIERYNQDPTWHGILVQLPLP--KHINEEKILLAIDPKKDVDGFHPMNTGHLWSGR-PVMIPCTPAGIMEMFREYNVELE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 164 GARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpda 243
Cdd:PRK14179 158 GKHAVVIGRSNIVGKPMAQLLLDKNATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMN----- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 24645718 244 sKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARFLER 296
Cdd:PRK14179 233 -RDENGKLIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALRSLHK 284
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-289 |
1.39e-88 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 283.98 E-value: 1.39e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 6 IISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 85
Cdd:PRK14184 3 LLDGKATAATIREELKTEVAALTAR-HGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 86 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIAGA 165
Cdd:PRK14184 82 AELNARPDIDGILLQLPLP--KGLDSQRCLELIDPAKDVDGFHPENMGRLALG-LPGFRPCTPAGVMTLLERYGLSPAGK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 166 RAVVLGRSKIVGTPAAELL----KWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKP 241
Cdd:PRK14184 159 KAVVVGRSNIVGKPLALMLgapgKFANATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRTD 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 24645718 242 DAskasgskLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRS 289
Cdd:PRK14184 239 DG-------LVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQS 279
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
3-292 |
1.91e-85 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 275.35 E-value: 1.91e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 3 GAKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELL 82
Cdd:PRK14193 2 TAIILDGKATADEIKADLAERVAALKEK--GITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 83 DKINDLNEDPRVHGIIVQMPLdcdtP--IDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGfLPCTPWGCLELIRRSGV 160
Cdd:PRK14193 80 AVIDELNADPACTGYIVQLPL----PkhLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAP-LPCTPRGIVHLLRRYDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 161 EIAGARAVVLGRSKIVGTPAAELL--KWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGIn 238
Cdd:PRK14193 155 ELAGAHVVVIGRGVTVGRPIGLLLtrRSENATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGV- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 24645718 239 vkpdaSKASGSKLVGDVDyAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 292
Cdd:PRK14193 234 -----SRAGDGKLVGDVH-PDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAER 281
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-290 |
8.65e-84 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 271.75 E-value: 8.65e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 4 AKIISGTAVAKSIREELRNEVTAMsKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 83
Cdd:PRK14168 3 AKIIKGTEIREEILEEIRGEVAEL-KEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 84 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIG-DLGGFLPCTPWGCLELIRRSGVEI 162
Cdd:PRK14168 82 LIDKYNNDDSIHGILVQLPLP--KHINEKKVLNAIDPDKDVDGFHPVNVGRLMIGgDEVKFLPCTPAGIQEMLVRSGVET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 163 AGARAVVLGRSKIVGTPAAELLKW----ANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGIN 238
Cdd:PRK14168 160 SGAEVVVVGRSNIVGKPIANMMTQkgpgANATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVN 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 24645718 239 ---VKPDASKASgskLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSA 290
Cdd:PRK14168 240 rvgTNESTGKAI---LSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSA 291
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-291 |
1.83e-83 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 270.88 E-value: 1.83e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 4 AKIISGTAVAKSIREELRNEVTAMSKqlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 83
Cdd:PRK14167 2 TEIIDGNAVAAQIRDDLTDAIETLED--AGVTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 84 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIA 163
Cdd:PRK14167 80 TIDELNADEDVHGILVQMPVP--DHVDDREVLRRIDPAKDVDGFHPENVGRLVAGD-ARFKPCTPHGIQKLLAAAGVDTE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 164 GARAVVLGRSKIVGTPAAELL----KWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINv 239
Cdd:PRK14167 157 GADVVVVGRSDIVGKPMANLLiqkaDGGNATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGIN- 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 24645718 240 KPDASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAA 291
Cdd:PRK14167 236 RVDADTEKGYELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAAS 287
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
128-294 |
1.60e-82 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 262.79 E-value: 1.60e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 128 HTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRS 207
Cdd:pfam02882 1 HPYNLGRLVLG-KPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 208 ADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpdasKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTV 287
Cdd:pfam02882 80 ADIVVVAVGKPELIKADWIKPGAVVIDVGIN------RVGNGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNTV 153
|
....*..
gi 24645718 288 RSAARFL 294
Cdd:pfam02882 154 EAAKRQL 160
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
3-292 |
4.38e-81 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 264.00 E-value: 4.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 3 GAKIISGTAVAKSIREELRNEVTAMSkqladFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELL 82
Cdd:PRK14173 2 AARELSGPPAAEAVYAELRARLAKLP-----FVPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 83 DKINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEI 162
Cdd:PRK14173 77 ELIARLNADPEVDGILVQLPLP--PHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMG-GEALEPCTPAGVVRLLKHYGIPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 163 AGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGIN-VKP 241
Cdd:PRK14173 154 AGKEVVVVGRSNIVGKPLAALLLREDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINrVGG 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 24645718 242 DASKAsgsKLVGDVdYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 292
Cdd:PRK14173 234 NGGRD---ILTGDV-HPEVAEVAGALTPVPGGVGPMTVAMLMANTVIAALR 280
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-289 |
6.68e-80 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 261.04 E-value: 6.68e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 6 IISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 85
Cdd:PRK14171 4 IIDGKALANEILADLKLEIQELKSQ-TNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 86 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGFLPCTPWGCLELIRRSGVEIAGA 165
Cdd:PRK14171 83 NELNLDNEISGIIVQLPLP--SSIDKNKILSAVSPSKDIDGFHPLNVGYLHSGISQGFIPCTALGCLAVIKKYEPNLTGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 166 RAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpdasK 245
Cdd:PRK14171 161 NVVIIGRSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGIN------R 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 24645718 246 ASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRS 289
Cdd:PRK14171 235 ISGNKIIGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKA 278
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-285 |
7.68e-80 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 260.48 E-value: 7.68e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 5 KIISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDK 84
Cdd:PRK14172 3 QIINGKEVALKIKEEIKNFVEERKEN-GLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 85 INDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIAG 164
Cdd:PRK14172 82 IEELNKDNNVHGIMLQLPLP--KHLDEKKITNKIDANKDIDCLTFISVGKFYKGE-KCFLPCTPNSVITLIKSLNIDIEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 165 ARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGinvkpdAS 244
Cdd:PRK14172 159 KEVVVIGRSNIVGKPVAQLLLNENATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVG------TS 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 24645718 245 KASGsKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKN 285
Cdd:PRK14172 233 SVNG-KITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKN 272
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-290 |
1.71e-79 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 260.15 E-value: 1.71e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 6 IISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 85
Cdd:PRK14187 4 IIDGKKIANDITEILATCIDDLKRQ-HNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 86 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGFL-PCTPWGCLELIRRSGVEIAG 164
Cdd:PRK14187 83 NELNNDDSVHGILVQLPVP--NHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQKKNCLiPCTPKGCLYLIKTITRNLSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 165 ARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpDAS 244
Cdd:PRK14187 161 SDAVVIGRSNIVGKPMACLLLGENCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGIN---SIE 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 24645718 245 KASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSA 290
Cdd:PRK14187 238 EGGVKKFVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAA 283
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-301 |
6.23e-79 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 258.62 E-value: 6.23e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 1 MSGAKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVE 80
Cdd:PRK14194 1 LMSAKLIDGKAAAARVLAQVREDVRTLKAA--GIEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 81 LLDKINDLNEDPRVHGIIVQMPLDCDtpIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGV 160
Cdd:PRK14194 79 LLALIAELNADPSVNGILLQLPLPAH--IDEARVLQAINPLKDVDGFHSENVGGLSQGR-DVLTPCTPSGCLRLLEDTCG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 161 EIAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVK 240
Cdd:PRK14194 156 DLTGKHAVVIGRSNIVGKPMAALLLQAHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINRI 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24645718 241 PDASKasgSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVrSAARFLERLAKSQ 301
Cdd:PRK14194 236 DDDGR---SRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTV-TAARLQAHAQRSQ 292
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-293 |
1.56e-78 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 257.10 E-value: 1.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 6 IISGTAVAKSIREELRNEVTAMSKQladfvPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 85
Cdd:PRK14181 2 LLKGAPAAEHILATIKENISASSTA-----PGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 86 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGFLPCTPWGCLELIRRSGVEIAGA 165
Cdd:PRK14181 77 HRLNNDPNIHGILVQLPLP--KHLDAQAILQAISPDKDVDGLHPVNMGKLLLGETDGFIPCTPAGIIELLKYYEIPLHGR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 166 RAVVLGRSKIVGTPAAELLKW----ANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKP 241
Cdd:PRK14181 155 HVAIVGRSNIVGKPLAALLMQkhpdTNATVTLLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRVP 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 24645718 242 dASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARF 293
Cdd:PRK14181 235 -AANPKGYILVGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNTWESYLRH 285
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-292 |
1.74e-78 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 256.93 E-value: 1.74e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 4 AKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 83
Cdd:PRK14170 2 GEIIDGKKLAKEIQEKVTREVAELVKE--GKKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 84 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIA 163
Cdd:PRK14170 80 VVEELNEDKTIHGILVQLPLP--EHISEEKVIDTISYDKDVDGFHPVNVGNLFIGK-DSFVPCTPAGIIELIKSTGTQIE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 164 GARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpda 243
Cdd:PRK14170 157 GKRAVVIGRSNIVGKPVAQLLLNENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMD----- 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 24645718 244 sKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 292
Cdd:PRK14170 232 -RDENNKLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKR 279
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-290 |
2.78e-76 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 250.88 E-value: 2.78e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 5 KIISGTAVAKSIREELRNEVTAMsKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDK 84
Cdd:PRK14176 9 RIIDGKALAKKIEAEVRSGVERL-KSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 85 INDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIAG 164
Cdd:PRK14176 88 IDSLNKRKDVHGILLQLPLP--KHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGD-EGLVPCTPHGVIRALEEYGVDIEG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 165 ARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDas 244
Cdd:PRK14176 165 KNAVIVGHSNVVGKPMAAMLLNRNATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITKEED-- 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 24645718 245 kasgsKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSA 290
Cdd:PRK14176 243 -----KVYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCA 283
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-294 |
1.60e-75 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 248.59 E-value: 1.60e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 5 KIISGTAVAKSIREELRNEVTAMsKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDK 84
Cdd:PRK14183 2 QILDGKALSDKIKENVKKEVDEL-KLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 85 INDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIAG 164
Cdd:PRK14183 81 IAMMNNNPNIDGILVQLPLP--KHIDTTKILEAIDPKKDVDGFHPYNVGRLVTG-LDGFVPCTPLGVMELLEEYEIDVKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 165 ARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpdas 244
Cdd:PRK14183 158 KDVCVVGASNIVGKPMAALLLNANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGIN------ 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 24645718 245 KASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARFL 294
Cdd:PRK14183 232 RTEDGRLVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKNRA 281
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-294 |
7.79e-74 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 244.37 E-value: 7.79e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 4 AKIISGTAVAKSIREELRNEVTAMsKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 83
Cdd:PRK14192 3 ALVLDGKALAKQIEEELSVRVEAL-KAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 84 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIA 163
Cdd:PRK14192 82 KIEELNANPDVHGILLQHPVP--AQIDERACFDAISLAKDVDGVTCLGFGRMAMGE-AAYGSATPAGIMRLLKAYNIELA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 164 GARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDA 243
Cdd:PRK14192 159 GKHAVVVGRSAILGKPMAMMLLNANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFHPRDGG 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 24645718 244 SkasgsklVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARFL 294
Cdd:PRK14192 239 G-------VGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKAL 282
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-290 |
2.54e-73 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 243.01 E-value: 2.54e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 6 IISGTAVAKSIREELRNEVTAMSKQLADfvPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 85
Cdd:PRK14166 3 LLDGKALSAKIKEELKEKNQFLKSKGIE--SCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 86 NDLNEDPRVHGIIVQMPLDCDtpIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGFLPCTPWGCLELIRRSGVEIAGA 165
Cdd:PRK14166 81 NTLNHDDSVHGILVQLPLPDH--ICKDLILESIISSKDVDGFHPINVGYLNLGLESGFLPCTPLGVMKLLKAYEIDLEGK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 166 RAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpdasK 245
Cdd:PRK14166 159 DAVIIGASNIVGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGIN------R 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 24645718 246 ASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSA 290
Cdd:PRK14166 233 LESGKIVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSA 277
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-291 |
2.78e-73 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 242.44 E-value: 2.78e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 6 IISGTAVAKSIREELRNEVTAmskqlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 85
Cdd:PRK14178 2 ILDGKAVSEKRLELLKEEIIE-----SGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 86 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIAGA 165
Cdd:PRK14178 77 RRLNEDPDINGILVQLPLP--KGVDTERVIAAILPEKDVDGFHPLNLGRLVSG-LPGFAPCTPNGIMTLLHEYKISIAGK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 166 RAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpdask 245
Cdd:PRK14178 154 RAVVVGRSIDVGRPMAALLLNADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGIN------- 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 24645718 246 ASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAA 291
Cdd:PRK14178 227 QVNGKLCGDVDFDAVKEIAGAITPVPGGVGPMTIATLMENTFDAAK 272
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-287 |
5.88e-73 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 242.43 E-value: 5.88e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 5 KIISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDK 84
Cdd:PRK14185 2 QLIDGKAISAQIKQEIAAEVAEIVAK-GGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 85 INDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIAG 164
Cdd:PRK14185 81 VRELNQDDDVDGFIVQLPLP--KHISEQKVIEAIDYRKDVDGFHPINVGRMSIG-LPCFVSATPNGILELLKRYHIETSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 165 ARAVVLGRSKIVGTPAAELL----KWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVK 240
Cdd:PRK14185 158 KKCVVLGRSNIVGKPMAQLMmqkaYPGDCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTRV 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 24645718 241 PDASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTV 287
Cdd:PRK14185 238 PDATRKSGFKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTL 284
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-292 |
1.09e-71 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 238.31 E-value: 1.09e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 4 AKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 83
Cdd:PRK14169 1 ATRLDGRAVSKKILADLKQTVAKLAQQ--DVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 84 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIA 163
Cdd:PRK14169 79 KVAELNHDPDVDAILVQLPLP--AGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANE-PTVVASTPYGIMALLDAYDIDVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 164 GARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDA 243
Cdd:PRK14169 156 GKRVVIVGRSNIVGRPLAGLMVNHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRGADG 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 24645718 244 skasgsKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 292
Cdd:PRK14169 236 ------KLLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKR 278
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-292 |
1.70e-70 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 235.20 E-value: 1.70e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 4 AKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 83
Cdd:PRK14175 3 AKILDGKQIAKDYRQGLQDQVEALKEK--GFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 84 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIgDLGGFLPCTPWGCLELIRRSGVEIA 163
Cdd:PRK14175 81 ELNRLNNDDSVSGILVQVPLP--KQVSEQKILEAINPEKDVDGFHPINIGKLYI-DEQTFVPCTPLGIMEILKHADIDLE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 164 GARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDA 243
Cdd:PRK14175 158 GKNAVVIGRSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVGNTPDENG 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 24645718 244 skasgsKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 292
Cdd:PRK14175 238 ------KLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEKM 280
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-290 |
2.54e-70 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 234.87 E-value: 2.54e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 6 IISGTAVAKSIREELRNEVtAMSKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 85
Cdd:PRK14177 5 LLDGKKLSEKIRNEIRETI-EERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLGVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 86 NDLNEDPRVHGIIVQMPldcdTP--IDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIA 163
Cdd:PRK14177 84 DKLNLDPNVDGILLQHP----VPsqIDERAAFDRIALEKDVDGVTTLSFGKLSMG-VETYLPCTPYGMVLLLKEYGIDVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 164 GARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVkpda 243
Cdd:PRK14177 159 GKNAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYNP---- 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 24645718 244 skasGSklVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSA 290
Cdd:PRK14177 235 ----GN--VGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSF 275
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-292 |
4.56e-70 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 234.15 E-value: 4.56e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 6 IISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 85
Cdd:PRK14182 3 LIDGKQIAAKVKGEVATEVRALAAR--GVQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 86 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGFLPCTPWGCLELIRRSGVEIAGA 165
Cdd:PRK14182 81 ARLNADPAVHGILVQLPLP--KHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGVPRPCTPAGVMRMLDEARVDPKGK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 166 RAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDAsk 245
Cdd:PRK14182 159 RALVVGRSNIVGKPMAMMLLERHATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLADG-- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 24645718 246 asgsKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 292
Cdd:PRK14182 237 ----KLVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKR 279
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-290 |
2.43e-60 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 207.19 E-value: 2.43e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 6 IISGTAVAKSIREELRNEVTAMSKQLAdFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 85
Cdd:PRK14180 3 LIDGKSLSKDLKERLATQVQEYKHHTA-ITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 86 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGFLPCTPWGCLELIRRSGVEIAGA 165
Cdd:PRK14180 82 DQLNNDSSVHAILVQLPLP--AHINKNNVIYSIKPEKDVDGFHPTNVGRLQLRDKKCLESCTPKGIMTMLREYGIKTEGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 166 RAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpdask 245
Cdd:PRK14180 160 YAVVVGASNVVGKPVSQLLLNAKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGIN------- 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 24645718 246 ASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSA 290
Cdd:PRK14180 233 HVDGKIVGDVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCA 277
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
7-125 |
9.39e-48 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 165.27 E-value: 9.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 7 ISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKIN 86
Cdd:pfam00763 1 IDGKAIAKKIREELKEEVAALKAG--GRKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALID 78
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 24645718 87 DLNEDPRVHGIIVQMPLdcdtP--IDSHRITDAVSPEKDVD 125
Cdd:pfam00763 79 KLNADPSVHGILVQLPL----PkhIDEEKVLEAIDPEKDVD 115
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
144-290 |
6.28e-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: 6.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 144 LPCTPWGCLELIR-------RSGVEIAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIG 216
Cdd:cd05212 1 GPCTPLFVSPVAKavkellnKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24645718 217 VAEMVKGSWIKPGAVVIDCGINvkpdaskasgsKLVGDvdyaEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSA 290
Cdd:cd05212 81 KPEKVPTEWIKPGATVINCSPT-----------KLSGD----DVKESASLYVPMTGGVGKLTVAMRMQNMVRSV 139
|
|
| NAD_bind_m-THF_DH |
cd01079 |
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ... |
120-288 |
2.25e-10 |
|
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of methylene-tetrahydrofolate dehydrogenase (m-THF DH). M-THF is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. M-THF DH is a component of an unusual monofunctional enzyme; in eukaryotes, m-THF DH is typically found as part of a multifunctional protein. NADP-dependent m-THF DHs in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofunctional DH, as well as bifunctional DH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains only the monofunctional DHs from S. cerevisiae and certain bacteria. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133447 [Multi-domain] Cd Length: 197 Bit Score: 60.90 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 120 PEKDVDGLHTVN-------------EGRLAigdlgGFLPCTPWGCLELIRRSGV---------EIAGARAVVLGRSKIVG 177
Cdd:cd01079 1 PHKDVEGLSHKYifnlyhnirfldpENRKK-----SILPCTPLAIVKILEFLGIynkilpygnRLYGKTITIINRSEVVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 178 TPAAELLKWANATV---------------------TVCHSKTRNLEEITRSADILVVGIGVAEM-VKGSWIKPGAVVID- 234
Cdd:cd01079 76 RPLAALLANDGARVysvdingiqvftrgesirhekHHVTDEEAMTLDCLSQSDVVITGVPSPNYkVPTELLKDGAICINf 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24645718 235 -CGINVKPDASKASGsklvgdvdyaealqvaghlTPVPGgVGPMTVAMLMKNTVR 288
Cdd:cd01079 156 aSIKNFEPSVKEKAS-------------------IYVPS-IGKVTIAMLLRNLLR 190
|
|
| NAD_bind_amino_acid_DH |
cd05191 |
NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH) ... |
146-236 |
3.57e-05 |
|
NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and are found in glutamate, leucine, and phenylalanine DHs (DHs), methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate 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: 133449 [Multi-domain] Cd Length: 86 Bit Score: 43.13 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 146 CTPWGCLELIRRSGVE----IAGARAVVLGRsKIVGTPAAELLKWA-NATVTVCHSktrnleeitrsaDILVVGIGVAEM 220
Cdd:cd05191 1 ATAAGAVALLKAAGKVtnksLKGKTVVVLGA-GEVGKGIAKLLADEgGKKVVLCDR------------DILVTATPAGVP 67
|
90
....*....|....*....
gi 24645718 221 VKG---SWIKPGAVVIDCG 236
Cdd:cd05191 68 VLEeatAKINEGAVVIDLA 86
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
162-234 |
2.31e-03 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 39.41 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645718 162 IAGARAVVLGrSKIVGTPAAELLKWANATVTV---------------------CHSKTRNLEEITRSADILVVGIGV--- 217
Cdd:smart01002 18 VPPAKVVVIG-AGVVGLGAAATAKGLGAEVTVldvrparlrqlesllgarfttLYSQAELLEEAVKEADLVIGAVLIpga 96
|
90 100
....*....|....*....|....
gi 24645718 218 -------AEMVKGswIKPGAVVID 234
Cdd:smart01002 97 kapklvtREMVKS--MKPGSVIVD 118
|
|
| |
