|
Name |
Accession |
Description |
Interval |
E-value |
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
347-965 |
0e+00 |
|
Formate--tetrahydrofolate ligase;
Pssm-ID: 460143 Cd Length: 555 Bit Score: 934.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 347 PSDIVIARAQKPKDIAVLAKEIGLEAREVSLYGNKKAKISLSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTTLMGLVQA 426
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 427 LGaHKLRNTMAALRQPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHENTqkdkaly 506
Cdd:pfam01268 81 LN-RLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 507 drlvpaikgqrkfspiqlrrlqklgitktdpdtltadeygpfarLDIDPDTIMWERVVDINDRYLRTITVGQSPTEKGIS 586
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 587 RETRFSISVASEIMAVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLEGTPVLVHA 666
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 667 GPFANIAHGCNSIIADEVGLKLvgkNGFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHGGgapvtPG 746
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGG-----VG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 747 AplnKQYTEENLELVQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKaALEAGAFAAVVSTHWADGGAGAV 826
Cdd:pfam01268 341 K---DELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRE-LCEAGGVDAALSEHWAKGGEGAI 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 827 QLADAVIKACEQG-NQFRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRLTDAGFGNLPICMSKVSGSFTGDA 905
Cdd:pfam01268 417 ELAEAVVEACEEEpSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 906 KIKGAPKGFTLDVEDVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNTEtGEIEGLF 965
Cdd:pfam01268 497 KLKGAPTGFTLPVRDVRLSAGAGFIVALTGDIMTMPGLPKRPAAENIDVDED-GKITGLF 555
|
|
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
340-965 |
0e+00 |
|
Formate--tetrahydrofolate ligase
Pssm-ID: 178359 Cd Length: 637 Bit Score: 913.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 340 LKPQRPVPSDIVIARAQKPKDIAVLAKEIGLEAREVSLYGNKKAKISLSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTT 419
Cdd:PLN02759 10 LEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKSTT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 420 LMGLVQALGAHKLRNTMAALRQPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHENT 499
Cdd:PLN02759 90 TIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEAT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 500 QKDKALYDRLVPAIK-GQRKFSPIQLRRLQKLGITKTDPDTLTADEYGPFARLDIDPDTIMWERVVDINDRYLRTITVGQ 578
Cdd:PLN02759 170 QSDKALFNRLCPANKeGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVGQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 579 SPTEKGISRETRFSISVASEIMAVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLE 658
Cdd:PLN02759 250 GPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTLE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 659 GTPVLVHAGPFANIAHGCNSIIADEVGLKLVGKNGFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHG 738
Cdd:PLN02759 330 GTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMHG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 739 GGAPVTPGAPLNKQYTEENLELVQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKAALEAGAFAAVVSTHW 818
Cdd:PLN02759 410 GGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTHH 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 819 ADGGAGAVQLADAVIKACEQGNQ-FRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRLTDAGFGNLPICMSKV 897
Cdd:PLN02759 490 AHGGKGAVDLGEAVQKACEGNSQpFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAKT 569
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386765496 898 SGSFTGDAKIKGAPKGFTLDVEDVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNTETGEIEGLF 965
Cdd:PLN02759 570 QYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTETGKVLGLS 637
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
361-964 |
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: 888.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 361 IAVLAKEIGLEAREVSLYGNKKAKISLSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTTLMGLVQALGAHkLRNTMAALR 440
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGAL-GKKAIAALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 441 QPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHENTqkdkalydrlvpaikgqrkfs 520
Cdd:cd00477 80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 521 piqlrrlqklgitktdpdtltadeygpfarLDIDPDTIMWERVVDINDRYLRTITVGQSPTEKGISRETRFSISVASEIM 600
Cdd:cd00477 139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 601 AVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLEGTPVLVHAGPFANIAHGCNSII 680
Cdd:cd00477 189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 681 ADEVGLKLvgkNGFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHGGGAPVTPGaplnkqytEENLEL 760
Cdd:cd00477 269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 761 VQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKaALEAGAFAAVVSTHWADGGAGAVQLADAVIKACEQ-G 839
Cdd:cd00477 338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRE-LAEEAGAEVAVSEHWAKGGKGALELAEAVIEACEKpK 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 840 NQFRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRLTDAGFGNLPICMSKVSGSFTGDAKIKGAPKGFTLDVE 919
Cdd:cd00477 417 SNFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 386765496 920 DVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNtETGEIEGL 964
Cdd:cd00477 497 DVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDID-DTGKIEGL 540
|
|
| PTZ00386 |
PTZ00386 |
formyl tetrahydrofolate synthetase; Provisional |
343-964 |
0e+00 |
|
formyl tetrahydrofolate synthetase; Provisional
Pssm-ID: 240394 Cd Length: 625 Bit Score: 863.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 343 QRPVPSDIVIARAQKPKDIAVLAKEIGLEAREVSLYGNKKAKISLSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTTLMG 422
Cdd:PTZ00386 12 QWPVPSDIDIAQSVKPQPITSVAESAGILLSELDPYGSTRAKVKLSVLKRLENSPNGKYVVVAGMNPTPLGEGKSTTTIG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 423 LVQALGAHKLRNTMAALRQPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHENTQKD 502
Cdd:PTZ00386 92 LAQSLGAHLHRKTFACIRQPSQGPTFGIKGGAAGGGYSQVIPMEDFNLHGTGDIHAITAANNLLAAALDTRIFHERTQSD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 503 KALYDRLVpaiKGQRKFSPIQLRRLQKLGITKTDPDTLTADEYGPFARLDIDPDTIMWERVVDINDRYLRTITVGQSPTE 582
Cdd:PTZ00386 172 AALYRRLT---DELKKFTPIMLKRLEKLGISKTDPKQLTEEERVRFARLDIDPDTISWRRVTDVNDRMLREITIGQGKEE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 583 KGISRETRFSISVASEIMAVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLEGTPV 662
Cdd:PTZ00386 249 KGITRKTGFDISVASEVMAILALATDLADMRQRLGAIVVAKSKSGEPVTAEDLGCAGAMTVLMKDTIEPTLMQTLEGTPV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 663 LVHAGPFANIAHGCNSIIADEVGLKLVGKNGFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHGGGAP 742
Cdd:PTZ00386 329 LVHAGPFGNIAHGNSSIVADQIALKLAGQDGFVLTEAGFGADIGCEKFFNIKCRTSGLKPDAAVLVATVRALKFHGGVEP 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 743 VTPGaplnkqytEENLELVQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKAALEAG-AFAAVVSTHWADG 821
Cdd:PTZ00386 409 VVAG--------KENLEAVRKGLSNLQRHIQNIRKFGVPVVVALNKFSTDTDAELELVKELALQEGgAADVVVTDHWAKG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 822 GAGAVQLADAVIKACEQG-NQFRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRLTDAGFGNLPICMSKVSGS 900
Cdd:PTZ00386 481 GAGAVDLAQALIRVTENVpSNFKLLYPLDASLKEKIETICKEIYGAAGVEYLNDADEKLEDFERMGYGKFPVCMAKTQYS 560
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386765496 901 FTGDAKIKGAPKGFTLDVEDVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNTETGEIEGL 964
Cdd:PTZ00386 561 FSHDPELRGAPTGFTVPIRDVRVNCGAGFVFPLLGDISTMPGLPTRPAFYNIDIDCETGKIVGL 624
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
346-965 |
0e+00 |
|
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
Pssm-ID: 442046 Cd Length: 556 Bit Score: 845.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 346 VPSDIVIARAQKPKDIAVLAKEIGLEAREVSLYGNKKAKISLSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTTLMGLVQ 425
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 426 ALGahKL-RNTMAALRQPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHENtqkdka 504
Cdd:COG2759 81 ALN--RLgKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQGN------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 505 lydrlvpaikgqrkfspiqlrrlqklgitktdpdtltadeygpfaRLDIDPDTIMWERVVDINDRYLRTITVGQSPTEKG 584
Cdd:COG2759 153 ---------------------------------------------ELNIDPRRITWKRVLDMNDRALRNIVIGLGGKANG 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 585 ISRETRFSISVASEIMAVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLEGTPVLV 664
Cdd:COG2759 188 VPREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFV 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 665 HAGPFANIAHGCNSIIADEVGLKLvgkNGFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHGGGApvt 744
Cdd:COG2759 268 HGGPFANIAHGCNSVIATKLALKL---ADYVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA--- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 745 pgaplNKQYTEENLELVQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKaALEAGAFAAVVSTHWADGGAG 824
Cdd:COG2759 342 -----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRE-LCEELGVRVALSEVWAKGGEG 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 825 AVQLADAVIKACEQG-NQFRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRLTDAGFGNLPICMSKVSGSFTG 903
Cdd:COG2759 416 AEELAEAVVEACEEGpSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSD 495
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386765496 904 DAKIKGAPKGFTLDVEDVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNtETGEIEGLF 965
Cdd:COG2759 496 DPKLLGAPTGFTLTVREVRLSAGAGFIVALTGDIMTMPGLPKVPAAERIDID-EDGKITGLF 556
|
|
| PRK13505 |
PRK13505 |
formate--tetrahydrofolate ligase; Provisional |
345-965 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237403 Cd Length: 557 Bit Score: 733.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 345 PVPSDIVIARAQKPKDIAVLAKEIGLEAREVSLYGNKKAKISLSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTTLMGLV 424
Cdd:PRK13505 1 TMKSDIEIAQEATLKPITEIAAKLGIPEDDLEPYGKYKAKISLDKIKALKDKKDGKLILVTAINPTPAGEGKSTVTVGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 425 QALgAHKLRNTMAALRQPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHENTqkdka 504
Cdd:PRK13505 81 DAL-NKIGKKTVIALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITSANNLLAALIDNHIHQGNE----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 505 lydrlvpaikgqrkfspiqlrrlqklgitktdpdtltadeygpfarLDIDPDTIMWERVVDINDRYLRTITVGQSPTEKG 584
Cdd:PRK13505 155 ----------------------------------------------LGIDPRRITWKRVLDMNDRALRNIVVGLGGPANG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 585 ISRETRFSISVASEIMAVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLEGTPVLV 664
Cdd:PRK13505 189 VPREDGFDITVASEIMAILCLATDLKDLKERLGRIVVGYTYDGKPVTVKDLKVEGAMALLLKDAIKPNLVQTLEGTPAFV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 665 HAGPFANIAHGCNSIIADEVGLKLvgkNGFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHGGGApvt 744
Cdd:PRK13505 269 HGGPFANIAHGCNSVLATKTALKL---ADYVVTEAGFGADLGAEKFLDIKCRKAGLKPDAVVIVATVRALKMHGGVA--- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 745 pgaplNKQYTEENLELVQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKaALEAGAFAAVVSTHWADGGAG 824
Cdd:PRK13505 343 -----KDDLKEENVEALKKGFANLERHIENIRKFGVPVVVAINKFVTDTDAEIAALKE-LCEELGVEVALSEVWAKGGEG 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 825 AVQLADAVIKACEQG-NQFRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRLTDAGFGNLPICMSKVSGSFTG 903
Cdd:PRK13505 417 GVELAEKVVELIEEGeSNFKPLYDDEDSLEEKIEKIATKIYGAKGVEFSPKAKKQLKQIEKNGWDKLPVCMAKTQYSFSD 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386765496 904 DAKIKGAPKGFTLDVEDVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNtETGEIEGLF 965
Cdd:PRK13505 497 DPKLLGAPTGFTITVRELRPSAGAGFIVALTGDIMTMPGLPKVPAALNIDVD-EDGNIVGLF 557
|
|
| PRK13506 |
PRK13506 |
formate--tetrahydrofolate ligase; Provisional |
348-964 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237404 Cd Length: 578 Bit Score: 674.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 348 SDIVIARAQKPKDIAVLAKEIGLEAREVSLYGNKKAKISLSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTTLMGLVQAL 427
Cdd:PRK13506 3 SDIEISRQAPLKPIAEIAAKLGLLPDELSPFGHTKAKVSLSVLKRLADKPKGKLVLVTAITPTPLGEGKTVTTIGLTQGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 428 gAHKLRNTMAALRQPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHEntqkdkalyd 507
Cdd:PRK13506 83 -NALGQKVCACIRQPSMGPVFGVKGGAAGGGYAQVVPMEELNLHLTGDIHAVSAAHNLAAAAIDARLFHE---------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 508 rlvpaikgqrkfspiqlrrlQKLGitktdpdtltADEYGP---FARLDIDPDTIMWERVVDINDRYLRTITVGQSPTEKG 584
Cdd:PRK13506 152 --------------------QRLG----------YDAFEAqsgLPALDIDPEQILWKRVVDHNDRALRMITVGLGENGNG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 585 ISRETRFSISVASEIMAVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLEGTPVLV 664
Cdd:PRK13506 202 PEREDGFDITAASELMAILALSRDLKDMRQRIGRLVLAYNLQGQPITAEDLGVAGAMTVIMKDAIEPTLMQTLEGVPCLI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 665 HAGPFANIAHGCNSIIADEVGLKLVGkngFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHGGGAPVT 744
Cdd:PRK13506 282 HAGPFANIAHGNSSIIADRIALKLAD---YVVTEGGFGSDMGFEKFCNIKARQSGKAPDCAVLVATLRALKANSGLYDLR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 745 PGAPLNKQYTEENLELVQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKAALEAGAFAAVVSTHWADGGAG 824
Cdd:PRK13506 359 PGQALPDSINAPDQARLEAGFANLKWHINNVAQYGLPVVVAINRFPTDTDEELEWLKEAVLLTGAFGCEISEAFAQGGEG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 825 AVQLADAVIKACEQGNQFRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRLTDAGFGNLPICMSKVSGSFTGD 904
Cdd:PRK13506 439 ATALAQAVVRACEQPSQFKLLYPDEMSLEAKLMTLAEVGYGAAGVSLSDKAKQQLAQLTALGYDHLPVCMAKTPLSISHD 518
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 905 AKIKGAPKGFTLDVEDVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNtETGEIEGL 964
Cdd:PRK13506 519 PALKGAPTDFEVPIRELRLCAGAGFITALVGNVMTMPGLGLKPGYLNIDID-ADGEIVGL 577
|
|
| PRK13507 |
PRK13507 |
formate--tetrahydrofolate ligase; Provisional |
349-965 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 184098 Cd Length: 587 Bit Score: 622.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 349 DIVIA-RAQKP-KDIAVLAKEIGLEAREVSLYGNKKAKIS-LSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTTLMGLVQ 425
Cdd:PRK13507 10 DWEIAeEAEKFmKPVEELAEELGLTKEELLPYGHYIAKVDfRKVLDRLKDRPDGKYIDVTAITPTPLGEGKSTTTMGLVQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 426 ALGAhKLRNTMAALRQPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHENTQKDKAL 505
Cdd:PRK13507 90 GLGK-RGKKVSGAIRQPSGGPTMNIKGSAAGGGLSQCIPLTPFSLGLTGDINAIMNAHNLAMVALTARMQHERNYTDEQL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 506 YDRlvpaikGQRkfspiqlrrlqklgitktdpdtltadeygpfaRLDIDPDTIMWERVVDINDRYLRTITVGQSPTEKGI 585
Cdd:PRK13507 169 ARR------GLK--------------------------------RLDIDPTRVEMGWIIDFCAQALRNIIIGIGGKTDGY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 586 SRETRFSISVASEIMAVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLEGTPVLVH 665
Cdd:PRK13507 211 MMQSGFGIAVSSEVMAILSVATDLKDLRERIGKIVVAYDKNGKPVTTADLEVDGAMTAWMVRAINPNLLQTIEGQPVFVH 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 666 AGPFANIAHGCNSIIADEVGLKLvgkNGFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHGGGAPVTP 745
Cdd:PRK13507 291 AGPFANIAIGQSSIIADRVGLKL---ADYHVTESGFGADIGFEKFWNLKCRLSGLKPDCAVIVATIRALKMHGGGPKVVP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 746 GAPLNKQYTEENLELVQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKAALEAGAFAAvVSTHWADGGAGA 825
Cdd:PRK13507 368 GKPLPEEYTKENVGLVEKGCANLLHHIGTVKKSGINPVVCINAFYTDTHAEIAIVRRLAEQAGARVA-VSRHWEKGGEGA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 826 VQLADAVIKACEQGNQFRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRL-TDAGFGNLPICMSKVSGSFTGD 904
Cdd:PRK13507 447 LELADAVIDACNEPNDFKFLYPLEMPLRERIETIAREVYGADGVSYTPEAEAKLKRLeSDPETADFGTCMVKTHLSLSHD 526
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386765496 905 AKIKGAPKGFTLDVEDVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNTETGEIEGLF 965
Cdd:PRK13507 527 PALKGVPKGWTLPIRDILTYGGAGFVVPVAGDISLMPGTGSDPAFRRIDVDTQTGKVKGLF 587
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
32-323 |
1.37e-144 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 431.36 E-value: 1.37e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 32 MSgAKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVE 111
Cdd:COG0190 1 MM-AQILDGKAVAAEIREELKERVAALKAK--GITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 112 LLDKINDLNEDPRVHGIIVQMPLdcdtP--IDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRS 189
Cdd:COG0190 78 LLALIDELNADPSVHGILVQLPL----PkhIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGE-PGFVPCTPAGIMELLERY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 190 GVEIAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGIN 269
Cdd:COG0190 153 GIDLAGKHAVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGIN 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 386765496 270 VKPDaskasgSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 323
Cdd:COG0190 233 RVED------GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
35-323 |
1.29e-108 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 338.09 E-value: 1.29e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 35 AKIISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 114
Cdd:PRK14188 2 ATIIDGKAFAADVRATVAAEVARLKAA-HGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 115 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIA 194
Cdd:PRK14188 81 LIARLNADPAIHGILVQLPLP--KHLDSEAVIQAIDPEKDVDGLHVVNAGRLATG-ETALVPCTPLGCMMLLRRVHGDLS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 195 GARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDA 274
Cdd:PRK14188 158 GLNAVVIGRSNLVGKPMAQLLLAANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIPAP 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 386765496 275 SKASG-SKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 323
Cdd:PRK14188 238 EKGEGkTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACR 287
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
8-323 |
2.62e-108 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 340.06 E-value: 2.62e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 8 QLEPEKFILSHGLNGEWTAEPAIKMS-------GAKIISGTAVAKSIREELRNEVTAMSKQLAdFVPGLRIVQVGGREDS 80
Cdd:PLN02616 39 PLRVRTTASGRGCCINSSSSPSPVINadtgsegGAKVIDGKAVAKKIRDEITIEVSRMKESIG-VVPGLAVILVGDRKDS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 81 NVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHT 160
Cdd:PLN02616 118 ATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKFISGFNNDPSVHGILVQLPLP--SHMDEQNILNAVSIEKDVDGFHP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 161 VNEGRLAI-GDLGGFLPCTPWGCLELIRRSGVEIAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSA 239
Cdd:PLN02616 196 LNIGRLAMrGREPLFVPCTPKGCIELLHRYNVEIKGKRAVVIGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 240 DILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVR 319
Cdd:PLN02616 276 DIIISAVGQPNMVRGSWIKPGAVVIDVGINPVEDASSPRGYRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLT 355
|
....
gi 386765496 320 SAAR 323
Cdd:PLN02616 356 SAKR 359
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
35-327 |
9.71e-108 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 335.06 E-value: 9.71e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 35 AKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 114
Cdd:PRK14190 3 AVIIDGKEVAKEKREQLKEEVVKLKEQ--GIVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 115 KINDLNEDPRVHGIIVQMPLdcdtP--IDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVE 192
Cdd:PRK14190 81 LIDRLNADPRINGILVQLPL----PkhIDEKAVIERISPEKDVDGFHPINVGRMMLGQ-DTFLPCTPHGILELLKEYNID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 193 IAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkp 272
Cdd:PRK14190 156 ISGKHVVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVN--- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 386765496 273 dasKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARFLER 327
Cdd:PRK14190 233 ---RLENGKLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKRAGGR 284
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
35-323 |
1.49e-105 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 329.93 E-value: 1.49e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 35 AKIISGTAVAKSIREELRNEVTAMSKQLADfVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 114
Cdd:PLN02516 9 AQIIDGKAIAKAIRSEIAEEVAQLSEKHGK-VPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELIS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 115 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAI-GDLGGFLPCTPWGCLELIRRSGVEI 193
Cdd:PLN02516 88 KVHELNANPDVHGILVQLPLP--KHINEEKILNEISLEKDVDGFHPLNIGKLAMkGREPLFLPCTPKGCLELLSRSGIPI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 194 AGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPD 273
Cdd:PLN02516 166 KGKKAVVVGRSNIVGLPVSLLLLKADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVSD 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 386765496 274 ASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 323
Cdd:PLN02516 246 PSKKSGYRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKR 295
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
35-323 |
5.09e-102 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 320.10 E-value: 5.09e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 35 AKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 114
Cdd:PRK14189 3 AQLIDGNALSKQLRAEAAQRAAALTAR--GHQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 115 KINDLNEDPRVHGIIVQMPLdcdtP--IDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVE 192
Cdd:PRK14189 81 RIDELNRDPKIHGILVQLPL----PkhIDSHKVIEAIAPEKDVDGFHVANAGALMTG-QPLFRPCTPYGVMKMLESIGIP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 193 IAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvKP 272
Cdd:PRK14189 156 LRGAHAVVIGRSNIVGKPMAMLLLQAGATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMN-RD 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 386765496 273 DAskasgSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 323
Cdd:PRK14189 235 DA-----GKLCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAER 280
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
35-327 |
1.28e-96 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 305.69 E-value: 1.28e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 35 AKIISGTAVAKSIREELRNEVTAMsKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 114
Cdd:PRK10792 3 AKIIDGKTIAQQVRSEVAQKVQAR-VAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 115 KINDLNEDPRVHGIIVQMPLdcdtP--IDSHRITDAVSPEKDVDGLHTVNEGRLAIgDLGGFLPCTPWGCLELIRRSGVE 192
Cdd:PRK10792 82 LIDELNADPTIDGILVQLPL----PahIDNVKVLERIHPDKDVDGFHPYNVGRLAQ-RIPLLRPCTPRGIMTLLERYGID 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 193 IAGARAVVLGRSKIVGTPAA-ELLkWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvk 271
Cdd:PRK10792 157 TYGLNAVVVGASNIVGRPMSlELL-LAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGIN-- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 386765496 272 pdasKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARFLER 327
Cdd:PRK10792 234 ----RLEDGKLVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEEYHDP 285
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
37-324 |
2.41e-94 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 300.20 E-value: 2.41e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 37 IISGTAVAKSIREELRNEVTAMsKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 116
Cdd:PRK14174 3 IIDGKKVSLDLKNELKTRVEAY-RAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 117 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGG-FLPCTPWGCLELIRRSGVEIAG 195
Cdd:PRK14174 82 EDLNNDPDVHGILVQQPLP--KQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGHLDKcFVSCTPYGILELLGRYNIETKG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 196 ARAVVLGRSKIVGTPAAEL----LKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVK 271
Cdd:PRK14174 160 KHCVVVGRSNIVGKPMANLmlqkLKESNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 386765496 272 PDASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARF 324
Cdd:PRK14174 240 EDPSTKSGYRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTLQSFERV 292
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
35-323 |
8.76e-94 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 300.72 E-value: 8.76e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 35 AKIISGTAVAKSIREELRNEVTAMSKQLADfVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 114
Cdd:PLN02897 56 TVVIDGNVIAEEIRTKIASEVRKMKKAVGK-VPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 115 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAI-GDLGGFLPCTPWGCLELIRRSGVEI 193
Cdd:PLN02897 135 ALRKFNEDTSIHGILVQLPLP--QHLDESKILNMVRLEKDVDGFHPLNVGNLAMrGREPLFVSCTPKGCVELLIRSGVEI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 194 AGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPD 273
Cdd:PLN02897 213 AGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPVED 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 386765496 274 ASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 323
Cdd:PLN02897 293 SSCEFGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKR 342
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
151-321 |
2.51e-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: 289.84 E-value: 2.51e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 151 PEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTR 230
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGR-PGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKTK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 231 NLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDASKasgSKLVGDVDYAEALQVAGHLTPVPGGVGPMTV 310
Cdd:cd01080 80 NLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDKSG---GKLVGDVDFESAKEKASAITPVPGGVGPMTV 156
|
170
....*....|.
gi 386765496 311 AMLMKNTVRSA 321
Cdd:cd01080 157 AMLMKNTVEAA 167
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
35-320 |
3.83e-92 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 294.28 E-value: 3.83e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 35 AKIISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 114
Cdd:PRK14186 2 ALILDGKALAAEIEQRLQAQIESNLPK-AGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 115 KINDLNEDPRVHGIIVQMPLdcdtP--IDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVE 192
Cdd:PRK14186 81 LIAQLNQDERVDGILLQLPL----PkhLDEVPLLHAIDPDKDADGLHPLNLGRLVKGE-PGLRSCTPAGVMRLLRSQQID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 193 IAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKP 272
Cdd:PRK14186 156 IAGKKAVVVGRSILVGKPLALMLLAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHRLP 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 386765496 273 DASKAsgSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRS 320
Cdd:PRK14186 236 SSDGK--TRLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLS 281
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
36-328 |
5.34e-92 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 293.60 E-value: 5.34e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 36 KIISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDK 115
Cdd:PRK14191 2 VLLDGKALSYKIEKDLKNKIQILTAQ-TGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 116 INDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIAG 195
Cdd:PRK14191 81 IKDLNTDQNIDGILVQLPLP--RHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQ-LDGFVPATPMGVMRLLKHYHIEIKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 196 ARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDAs 275
Cdd:PRK14191 158 KDVVIIGASNIVGKPLAMLMLNAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLNDG- 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 386765496 276 kasgsKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARFLERL 328
Cdd:PRK14191 237 -----RLVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEKRQRKG 284
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
37-320 |
7.81e-89 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 285.13 E-value: 7.81e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 37 IISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 116
Cdd:PRK14184 3 LLDGKATAATIREELKTEVAALTAR-HGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 117 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIAGA 196
Cdd:PRK14184 82 AELNARPDIDGILLQLPLP--KGLDSQRCLELIDPAKDVDGFHPENMGRLALG-LPGFRPCTPAGVMTLLERYGLSPAGK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 197 RAVVLGRSKIVGTPAAELL----KWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKP 272
Cdd:PRK14184 159 KAVVVGRSNIVGKPLALMLgapgKFANATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRTD 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 386765496 273 DAskasgskLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRS 320
Cdd:PRK14184 239 DG-------LVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQS 279
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
35-327 |
9.15e-89 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 285.11 E-value: 9.15e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 35 AKIISGTAVAKSIREELRNEVTAMsKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 114
Cdd:PRK14179 2 TEIIDGKALAQKMQAELAEKVAKL-KEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 115 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIA 194
Cdd:PRK14179 81 LIERYNQDPTWHGILVQLPLP--KHINEEKILLAIDPKKDVDGFHPMNTGHLWSGR-PVMIPCTPAGIMEMFREYNVELE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 195 GARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpda 274
Cdd:PRK14179 158 GKHAVVIGRSNIVGKPMAQLLLDKNATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMN----- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 386765496 275 sKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARFLER 327
Cdd:PRK14179 233 -RDENGKLIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALRSLHK 284
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
34-323 |
9.74e-86 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 276.89 E-value: 9.74e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 34 GAKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELL 113
Cdd:PRK14193 2 TAIILDGKATADEIKADLAERVAALKEK--GITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 114 DKINDLNEDPRVHGIIVQMPLdcdtP--IDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGfLPCTPWGCLELIRRSGV 191
Cdd:PRK14193 80 AVIDELNADPACTGYIVQLPL----PkhLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAP-LPCTPRGIVHLLRRYDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 192 EIAGARAVVLGRSKIVGTPAAELL--KWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGIn 269
Cdd:PRK14193 155 ELAGAHVVVIGRGVTVGRPIGLLLtrRSENATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGV- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 386765496 270 vkpdaSKASGSKLVGDVDyAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 323
Cdd:PRK14193 234 -----SRAGDGKLVGDVH-PDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAER 281
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
35-321 |
6.74e-84 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 272.52 E-value: 6.74e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 35 AKIISGTAVAKSIREELRNEVTAMsKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 114
Cdd:PRK14168 3 AKIIKGTEIREEILEEIRGEVAEL-KEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 115 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIG-DLGGFLPCTPWGCLELIRRSGVEI 193
Cdd:PRK14168 82 LIDKYNNDDSIHGILVQLPLP--KHINEKKVLNAIDPDKDVDGFHPVNVGRLMIGgDEVKFLPCTPAGIQEMLVRSGVET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 194 AGARAVVLGRSKIVGTPAAELLKW----ANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGIN 269
Cdd:PRK14168 160 SGAEVVVVGRSNIVGKPIANMMTQkgpgANATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVN 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 386765496 270 ---VKPDASKASgskLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSA 321
Cdd:PRK14168 240 rvgTNESTGKAI---LSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSA 291
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
35-322 |
9.44e-84 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 272.04 E-value: 9.44e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 35 AKIISGTAVAKSIREELRNEVTAMSKqlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 114
Cdd:PRK14167 2 TEIIDGNAVAAQIRDDLTDAIETLED--AGVTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 115 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIA 194
Cdd:PRK14167 80 TIDELNADEDVHGILVQMPVP--DHVDDREVLRRIDPAKDVDGFHPENVGRLVAGD-ARFKPCTPHGIQKLLAAAGVDTE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 195 GARAVVLGRSKIVGTPAAELL----KWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINv 270
Cdd:PRK14167 157 GADVVVVGRSDIVGKPMANLLiqkaDGGNATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGIN- 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 386765496 271 KPDASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAA 322
Cdd:PRK14167 236 RVDADTEKGYELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAAS 287
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
159-325 |
9.97e-83 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 263.94 E-value: 9.97e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 159 HTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRS 238
Cdd:pfam02882 1 HPYNLGRLVLG-KPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 239 ADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpdasKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTV 318
Cdd:pfam02882 80 ADIVVVAVGKPELIKADWIKPGAVVIDVGIN------RVGNGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNTV 153
|
....*..
gi 386765496 319 RSAARFL 325
Cdd:pfam02882 154 EAAKRQL 160
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
34-323 |
3.30e-81 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 264.77 E-value: 3.30e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 34 GAKIISGTAVAKSIREELRNEVTAMSkqladFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELL 113
Cdd:PRK14173 2 AARELSGPPAAEAVYAELRARLAKLP-----FVPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 114 DKINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEI 193
Cdd:PRK14173 77 ELIARLNADPEVDGILVQLPLP--PHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMG-GEALEPCTPAGVVRLLKHYGIPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 194 AGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGIN-VKP 272
Cdd:PRK14173 154 AGKEVVVVGRSNIVGKPLAALLLREDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINrVGG 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 386765496 273 DASKAsgsKLVGDVdYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 323
Cdd:PRK14173 234 NGGRD---ILTGDV-HPEVAEVAGALTPVPGGVGPMTVAMLMANTVIAALR 280
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
36-316 |
5.91e-80 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 261.25 E-value: 5.91e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 36 KIISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDK 115
Cdd:PRK14172 3 QIINGKEVALKIKEEIKNFVEERKEN-GLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 116 INDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIAG 195
Cdd:PRK14172 82 IEELNKDNNVHGIMLQLPLP--KHLDEKKITNKIDANKDIDCLTFISVGKFYKGE-KCFLPCTPNSVITLIKSLNIDIEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 196 ARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGinvkpdAS 275
Cdd:PRK14172 159 KEVVVIGRSNIVGKPVAQLLLNENATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVG------TS 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 386765496 276 KASGsKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKN 316
Cdd:PRK14172 233 SVNG-KITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKN 272
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
37-320 |
6.33e-80 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 261.43 E-value: 6.33e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 37 IISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 116
Cdd:PRK14171 4 IIDGKALANEILADLKLEIQELKSQ-TNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 117 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGFLPCTPWGCLELIRRSGVEIAGA 196
Cdd:PRK14171 83 NELNLDNEISGIIVQLPLP--SSIDKNKILSAVSPSKDIDGFHPLNVGYLHSGISQGFIPCTALGCLAVIKKYEPNLTGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 197 RAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpdasK 276
Cdd:PRK14171 161 NVVIIGRSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGIN------R 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 386765496 277 ASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRS 320
Cdd:PRK14171 235 ISGNKIIGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKA 278
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
37-321 |
1.74e-79 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 260.53 E-value: 1.74e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 37 IISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 116
Cdd:PRK14187 4 IIDGKKIANDITEILATCIDDLKRQ-HNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 117 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGFL-PCTPWGCLELIRRSGVEIAG 195
Cdd:PRK14187 83 NELNNDDSVHGILVQLPVP--NHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQKKNCLiPCTPKGCLYLIKTITRNLSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 196 ARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpDAS 275
Cdd:PRK14187 161 SDAVVIGRSNIVGKPMACLLLGENCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGIN---SIE 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 386765496 276 KASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSA 321
Cdd:PRK14187 238 EGGVKKFVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAA 283
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
32-332 |
5.08e-79 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 259.39 E-value: 5.08e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 32 MSGAKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVE 111
Cdd:PRK14194 1 LMSAKLIDGKAAAARVLAQVREDVRTLKAA--GIEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 112 LLDKINDLNEDPRVHGIIVQMPLDCDtpIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGV 191
Cdd:PRK14194 79 LLALIAELNADPSVNGILLQLPLPAH--IDEARVLQAINPLKDVDGFHSENVGGLSQGR-DVLTPCTPSGCLRLLEDTCG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 192 EIAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVK 271
Cdd:PRK14194 156 DLTGKHAVVIGRSNIVGKPMAALLLQAHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINRI 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386765496 272 PDASKasgSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVrSAARFLERLAKSQ 332
Cdd:PRK14194 236 DDDGR---SRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTV-TAARLQAHAQRSQ 292
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
35-323 |
1.80e-78 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 257.31 E-value: 1.80e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 35 AKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 114
Cdd:PRK14170 2 GEIIDGKKLAKEIQEKVTREVAELVKE--GKKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 115 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIA 194
Cdd:PRK14170 80 VVEELNEDKTIHGILVQLPLP--EHISEEKVIDTISYDKDVDGFHPVNVGNLFIGK-DSFVPCTPAGIIELIKSTGTQIE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 195 GARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpda 274
Cdd:PRK14170 157 GKRAVVIGRSNIVGKPVAQLLLNENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMD----- 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 386765496 275 sKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 323
Cdd:PRK14170 232 -RDENNKLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKR 279
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
37-324 |
1.83e-78 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 257.48 E-value: 1.83e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 37 IISGTAVAKSIREELRNEVTAMSKQladfvPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 116
Cdd:PRK14181 2 LLKGAPAAEHILATIKENISASSTA-----PGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 117 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGFLPCTPWGCLELIRRSGVEIAGA 196
Cdd:PRK14181 77 HRLNNDPNIHGILVQLPLP--KHLDAQAILQAISPDKDVDGLHPVNMGKLLLGETDGFIPCTPAGIIELLKYYEIPLHGR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 197 RAVVLGRSKIVGTPAAELLKW----ANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKP 272
Cdd:PRK14181 155 HVAIVGRSNIVGKPLAALLMQkhpdTNATVTLLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRVP 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 386765496 273 dASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARF 324
Cdd:PRK14181 235 -AANPKGYILVGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNTWESYLRH 285
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
36-321 |
2.97e-76 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 251.26 E-value: 2.97e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 36 KIISGTAVAKSIREELRNEVTAMsKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDK 115
Cdd:PRK14176 9 RIIDGKALAKKIEAEVRSGVERL-KSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 116 INDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIAG 195
Cdd:PRK14176 88 IDSLNKRKDVHGILLQLPLP--KHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGD-EGLVPCTPHGVIRALEEYGVDIEG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 196 ARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDas 275
Cdd:PRK14176 165 KNAVIVGHSNVVGKPMAAMLLNRNATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITKEED-- 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 386765496 276 kasgsKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSA 321
Cdd:PRK14176 243 -----KVYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCA 283
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
36-325 |
1.26e-75 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 249.36 E-value: 1.26e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 36 KIISGTAVAKSIREELRNEVTAMsKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDK 115
Cdd:PRK14183 2 QILDGKALSDKIKENVKKEVDEL-KLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 116 INDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIAG 195
Cdd:PRK14183 81 IAMMNNNPNIDGILVQLPLP--KHIDTTKILEAIDPKKDVDGFHPYNVGRLVTG-LDGFVPCTPLGVMELLEEYEIDVKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 196 ARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpdas 275
Cdd:PRK14183 158 KDVCVVGASNIVGKPMAALLLNANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGIN------ 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 386765496 276 KASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARFL 325
Cdd:PRK14183 232 RTEDGRLVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKNRA 281
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
35-325 |
6.91e-74 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 244.76 E-value: 6.91e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 35 AKIISGTAVAKSIREELRNEVTAMsKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 114
Cdd:PRK14192 3 ALVLDGKALAKQIEEELSVRVEAL-KAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 115 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIA 194
Cdd:PRK14192 82 KIEELNANPDVHGILLQHPVP--AQIDERACFDAISLAKDVDGVTCLGFGRMAMGE-AAYGSATPAGIMRLLKAYNIELA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 195 GARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDA 274
Cdd:PRK14192 159 GKHAVVVGRSAILGKPMAMMLLNANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFHPRDGG 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 386765496 275 SkasgsklVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARFL 325
Cdd:PRK14192 239 G-------VGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKAL 282
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
37-322 |
1.55e-73 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 243.60 E-value: 1.55e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 37 IISGTAVAKSIREELRNEVTAmskqlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 116
Cdd:PRK14178 2 ILDGKAVSEKRLELLKEEIIE-----SGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 117 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIAGA 196
Cdd:PRK14178 77 RRLNEDPDINGILVQLPLP--KGVDTERVIAAILPEKDVDGFHPLNLGRLVSG-LPGFAPCTPNGIMTLLHEYKISIAGK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 197 RAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpdask 276
Cdd:PRK14178 154 RAVVVGRSIDVGRPMAALLLNADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGIN------- 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 386765496 277 ASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAA 322
Cdd:PRK14178 227 QVNGKLCGDVDFDAVKEIAGAITPVPGGVGPMTIATLMENTFDAAK 272
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
37-321 |
1.87e-73 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 243.78 E-value: 1.87e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 37 IISGTAVAKSIREELRNEVTAMSKQLADfvPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 116
Cdd:PRK14166 3 LLDGKALSAKIKEELKEKNQFLKSKGIE--SCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 117 NDLNEDPRVHGIIVQMPLDCDtpIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGFLPCTPWGCLELIRRSGVEIAGA 196
Cdd:PRK14166 81 NTLNHDDSVHGILVQLPLPDH--ICKDLILESIISSKDVDGFHPINVGYLNLGLESGFLPCTPLGVMKLLKAYEIDLEGK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 197 RAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpdasK 276
Cdd:PRK14166 159 DAVIIGASNIVGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGIN------R 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 386765496 277 ASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSA 321
Cdd:PRK14166 233 LESGKIVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSA 277
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
36-318 |
5.92e-73 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 242.81 E-value: 5.92e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 36 KIISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDK 115
Cdd:PRK14185 2 QLIDGKAISAQIKQEIAAEVAEIVAK-GGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 116 INDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIAG 195
Cdd:PRK14185 81 VRELNQDDDVDGFIVQLPLP--KHISEQKVIEAIDYRKDVDGFHPINVGRMSIG-LPCFVSATPNGILELLKRYHIETSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 196 ARAVVLGRSKIVGTPAAELL----KWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVK 271
Cdd:PRK14185 158 KKCVVLGRSNIVGKPMAQLMmqkaYPGDCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTRV 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 386765496 272 PDASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTV 318
Cdd:PRK14185 238 PDATRKSGFKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTL 284
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
35-323 |
5.80e-72 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 239.46 E-value: 5.80e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 35 AKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 114
Cdd:PRK14169 1 ATRLDGRAVSKKILADLKQTVAKLAQQ--DVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 115 KINDLNEDPRVHGIIVQMPLDCDtpIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIA 194
Cdd:PRK14169 79 KVAELNHDPDVDAILVQLPLPAG--LDEQAVIDAIDPDKDVDGFSPVSVGRLWANE-PTVVASTPYGIMALLDAYDIDVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 195 GARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDA 274
Cdd:PRK14169 156 GKRVVIVGRSNIVGRPLAGLMVNHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRGADG 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 386765496 275 skasgsKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 323
Cdd:PRK14169 236 ------KLLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKR 278
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
35-323 |
1.53e-70 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 235.97 E-value: 1.53e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 35 AKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 114
Cdd:PRK14175 3 AKILDGKQIAKDYRQGLQDQVEALKEK--GFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 115 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIgDLGGFLPCTPWGCLELIRRSGVEIA 194
Cdd:PRK14175 81 ELNRLNNDDSVSGILVQVPLP--KQVSEQKILEAINPEKDVDGFHPINIGKLYI-DEQTFVPCTPLGIMEILKHADIDLE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 195 GARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDA 274
Cdd:PRK14175 158 GKNAVVIGRSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVGNTPDENG 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 386765496 275 skasgsKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 323
Cdd:PRK14175 238 ------KLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEKM 280
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
37-321 |
2.84e-70 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 234.87 E-value: 2.84e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 37 IISGTAVAKSIREELRNEVtAMSKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 116
Cdd:PRK14177 5 LLDGKKLSEKIRNEIRETI-EERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLGVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 117 NDLNEDPRVHGIIVQMPldcdTP--IDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIA 194
Cdd:PRK14177 84 DKLNLDPNVDGILLQHP----VPsqIDERAAFDRIALEKDVDGVTTLSFGKLSMG-VETYLPCTPYGMVLLLKEYGIDVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 195 GARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVkpda 274
Cdd:PRK14177 159 GKNAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYNP---- 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 386765496 275 skasGSklVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSA 321
Cdd:PRK14177 235 ----GN--VGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSF 275
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
37-323 |
4.15e-70 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 234.53 E-value: 4.15e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 37 IISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 116
Cdd:PRK14182 3 LIDGKQIAAKVKGEVATEVRALAAR--GVQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 117 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGFLPCTPWGCLELIRRSGVEIAGA 196
Cdd:PRK14182 81 ARLNADPAVHGILVQLPLP--KHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGVPRPCTPAGVMRMLDEARVDPKGK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 197 RAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDAsk 276
Cdd:PRK14182 159 RALVVGRSNIVGKPMAMMLLERHATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLADG-- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 386765496 277 asgsKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 323
Cdd:PRK14182 237 ----KLVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKR 279
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
37-321 |
1.39e-60 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 207.96 E-value: 1.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 37 IISGTAVAKSIREELRNEVTAMSKQLAdFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 116
Cdd:PRK14180 3 LIDGKSLSKDLKERLATQVQEYKHHTA-ITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 117 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGFLPCTPWGCLELIRRSGVEIAGA 196
Cdd:PRK14180 82 DQLNNDSSVHAILVQLPLP--AHINKNNVIYSIKPEKDVDGFHPTNVGRLQLRDKKCLESCTPKGIMTMLREYGIKTEGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 197 RAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpdask 276
Cdd:PRK14180 160 YAVVVGASNVVGKPVSQLLLNAKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGIN------- 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 386765496 277 ASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSA 321
Cdd:PRK14180 233 HVDGKIVGDVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCA 277
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
38-156 |
8.25e-48 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 165.66 E-value: 8.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 38 ISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKIN 117
Cdd:pfam00763 1 IDGKAIAKKIREELKEEVAALKAG--GRKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALID 78
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 386765496 118 DLNEDPRVHGIIVQMPLdcdtP--IDSHRITDAVSPEKDVD 156
Cdd:pfam00763 79 KLNADPSVHGILVQLPL----PkhIDEEKVLEAIDPEKDVD 115
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
175-321 |
4.73e-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: 136.10 E-value: 4.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 175 LPCTPWGCLELIR-------RSGVEIAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIG 247
Cdd:cd05212 1 GPCTPLFVSPVAKavkellnKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386765496 248 VAEMVKGSWIKPGAVVIDCGINvkpdaskasgsKLVGDvdyaEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSA 321
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 ... |
151-319 |
1.99e-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: 61.29 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 151 PEKDVDGLHTVN-------------EGRLAigdlgGFLPCTPWGCLELIRRSGV---------EIAGARAVVLGRSKIVG 208
Cdd:cd01079 1 PHKDVEGLSHKYifnlyhnirfldpENRKK-----SILPCTPLAIVKILEFLGIynkilpygnRLYGKTITIINRSEVVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 209 TPAAELLKWANATV---------------------TVCHSKTRNLEEITRSADILVVGIGVAEM-VKGSWIKPGAVVID- 265
Cdd:cd01079 76 RPLAALLANDGARVysvdingiqvftrgesirhekHHVTDEEAMTLDCLSQSDVVITGVPSPNYkVPTELLKDGAICINf 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 386765496 266 -CGINVKPDASKASGsklvgdvdyaealqvaghlTPVPGgVGPMTVAMLMKNTVR 319
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) ... |
177-267 |
2.83e-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: 43.52 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 177 CTPWGCLELIRRSGVE----IAGARAVVLGRsKIVGTPAAELLKWA-NATVTVCHSktrnleeitrsaDILVVGIGVAEM 251
Cdd:cd05191 1 ATAAGAVALLKAAGKVtnksLKGKTVVVLGA-GEVGKGIAKLLADEgGKKVVLCDR------------DILVTATPAGVP 67
|
90
....*....|....*....
gi 386765496 252 VKG---SWIKPGAVVIDCG 267
Cdd:cd05191 68 VLEeatAKINEGAVVIDLA 86
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
193-265 |
1.95e-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: 39.80 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765496 193 IAGARAVVLGrSKIVGTPAAELLKWANATVTV---------------------CHSKTRNLEEITRSADILVVGIGV--- 248
Cdd:smart01002 18 VPPAKVVVIG-AGVVGLGAAATAKGLGAEVTVldvrparlrqlesllgarfttLYSQAELLEEAVKEADLVIGAVLIpga 96
|
90 100
....*....|....*....|....
gi 386765496 249 -------AEMVKGswIKPGAVVID 265
Cdd:smart01002 97 kapklvtREMVKS--MKPGSVIVD 118
|
|
| |
