|
Name |
Accession |
Description |
Interval |
E-value |
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
350-968 |
0e+00 |
|
Formate--tetrahydrofolate ligase;
Pssm-ID: 460143 Cd Length: 555 Bit Score: 935.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 350 PSDIVIARAQKPKDIAVLAKEIGLEAREVSLYGNKKAKISLSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTTLMGLVQA 429
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 430 LGaHKLRNTMAALRQPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHENTqkdkaly 509
Cdd:pfam01268 81 LN-RLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 510 drlvpaikgqrkfspiqlrrlqklgitktdpdtltadeygpfarLDIDPDTIMWERVVDINDRYLRTITVGQSPTEKGIS 589
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 590 RETRFSISVASEIMAVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLEGTPVLVHA 669
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 670 GPFANIAHGCNSIIADEVGLKLvgkNGFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHGGgapvtPG 749
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGG-----VG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 750 AplnKQYTEENLELVQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKaALEAGAFAAVVSTHWADGGAGAV 829
Cdd:pfam01268 341 K---DELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRE-LCEAGGVDAALSEHWAKGGEGAI 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 830 QLADAVIKACEQG-NQFRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRLTDAGFGNLPICMSKVSGSFTGDA 908
Cdd:pfam01268 417 ELAEAVVEACEEEpSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 909 KIKGAPKGFTLDVEDVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNTEtGEIEGLF 968
Cdd:pfam01268 497 KLKGAPTGFTLPVRDVRLSAGAGFIVALTGDIMTMPGLPKRPAAENIDVDED-GKITGLF 555
|
|
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
343-968 |
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 62472483 343 LKPQRPVPSDIVIARAQKPKDIAVLAKEIGLEAREVSLYGNKKAKISLSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTT 422
Cdd:PLN02759 10 LEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKSTT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 423 LMGLVQALGAHKLRNTMAALRQPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHENT 502
Cdd:PLN02759 90 TIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEAT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 503 QKDKALYDRLVPAIK-GQRKFSPIQLRRLQKLGITKTDPDTLTADEYGPFARLDIDPDTIMWERVVDINDRYLRTITVGQ 581
Cdd:PLN02759 170 QSDKALFNRLCPANKeGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVGQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 582 SPTEKGISRETRFSISVASEIMAVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLE 661
Cdd:PLN02759 250 GPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTLE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 662 GTPVLVHAGPFANIAHGCNSIIADEVGLKLVGKNGFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHG 741
Cdd:PLN02759 330 GTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMHG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 742 GGAPVTPGAPLNKQYTEENLELVQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKAALEAGAFAAVVSTHW 821
Cdd:PLN02759 410 GGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTHH 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 822 ADGGAGAVQLADAVIKACEQGNQ-FRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRLTDAGFGNLPICMSKV 900
Cdd:PLN02759 490 AHGGKGAVDLGEAVQKACEGNSQpFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAKT 569
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62472483 901 SGSFTGDAKIKGAPKGFTLDVEDVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNTETGEIEGLF 968
Cdd:PLN02759 570 QYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTETGKVLGLS 637
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
364-967 |
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: 889.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 364 IAVLAKEIGLEAREVSLYGNKKAKISLSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTTLMGLVQALGAHkLRNTMAALR 443
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGAL-GKKAIAALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 444 QPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHENTqkdkalydrlvpaikgqrkfs 523
Cdd:cd00477 80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 524 piqlrrlqklgitktdpdtltadeygpfarLDIDPDTIMWERVVDINDRYLRTITVGQSPTEKGISRETRFSISVASEIM 603
Cdd:cd00477 139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 604 AVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLEGTPVLVHAGPFANIAHGCNSII 683
Cdd:cd00477 189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 684 ADEVGLKLvgkNGFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHGGGAPVTPGaplnkqytEENLEL 763
Cdd:cd00477 269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 764 VQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKaALEAGAFAAVVSTHWADGGAGAVQLADAVIKACEQ-G 842
Cdd:cd00477 338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRE-LAEEAGAEVAVSEHWAKGGKGALELAEAVIEACEKpK 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 843 NQFRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRLTDAGFGNLPICMSKVSGSFTGDAKIKGAPKGFTLDVE 922
Cdd:cd00477 417 SNFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 62472483 923 DVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNtETGEIEGL 967
Cdd:cd00477 497 DVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDID-DTGKIEGL 540
|
|
| PTZ00386 |
PTZ00386 |
formyl tetrahydrofolate synthetase; Provisional |
346-967 |
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 62472483 346 QRPVPSDIVIARAQKPKDIAVLAKEIGLEAREVSLYGNKKAKISLSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTTLMG 425
Cdd:PTZ00386 12 QWPVPSDIDIAQSVKPQPITSVAESAGILLSELDPYGSTRAKVKLSVLKRLENSPNGKYVVVAGMNPTPLGEGKSTTTIG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 426 LVQALGAHKLRNTMAALRQPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHENTQKD 505
Cdd:PTZ00386 92 LAQSLGAHLHRKTFACIRQPSQGPTFGIKGGAAGGGYSQVIPMEDFNLHGTGDIHAITAANNLLAAALDTRIFHERTQSD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 506 KALYDRLVpaiKGQRKFSPIQLRRLQKLGITKTDPDTLTADEYGPFARLDIDPDTIMWERVVDINDRYLRTITVGQSPTE 585
Cdd:PTZ00386 172 AALYRRLT---DELKKFTPIMLKRLEKLGISKTDPKQLTEEERVRFARLDIDPDTISWRRVTDVNDRMLREITIGQGKEE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 586 KGISRETRFSISVASEIMAVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLEGTPV 665
Cdd:PTZ00386 249 KGITRKTGFDISVASEVMAILALATDLADMRQRLGAIVVAKSKSGEPVTAEDLGCAGAMTVLMKDTIEPTLMQTLEGTPV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 666 LVHAGPFANIAHGCNSIIADEVGLKLVGKNGFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHGGGAP 745
Cdd:PTZ00386 329 LVHAGPFGNIAHGNSSIVADQIALKLAGQDGFVLTEAGFGADIGCEKFFNIKCRTSGLKPDAAVLVATVRALKFHGGVEP 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 746 VTPGaplnkqytEENLELVQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKAALEAG-AFAAVVSTHWADG 824
Cdd:PTZ00386 409 VVAG--------KENLEAVRKGLSNLQRHIQNIRKFGVPVVVALNKFSTDTDAELELVKELALQEGgAADVVVTDHWAKG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 825 GAGAVQLADAVIKACEQG-NQFRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRLTDAGFGNLPICMSKVSGS 903
Cdd:PTZ00386 481 GAGAVDLAQALIRVTENVpSNFKLLYPLDASLKEKIETICKEIYGAAGVEYLNDADEKLEDFERMGYGKFPVCMAKTQYS 560
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62472483 904 FTGDAKIKGAPKGFTLDVEDVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNTETGEIEGL 967
Cdd:PTZ00386 561 FSHDPELRGAPTGFTVPIRDVRVNCGAGFVFPLLGDISTMPGLPTRPAFYNIDIDCETGKIVGL 624
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
349-968 |
0e+00 |
|
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
Pssm-ID: 442046 Cd Length: 556 Bit Score: 847.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 349 VPSDIVIARAQKPKDIAVLAKEIGLEAREVSLYGNKKAKISLSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTTLMGLVQ 428
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 429 ALGahKL-RNTMAALRQPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHENtqkdka 507
Cdd:COG2759 81 ALN--RLgKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQGN------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 508 lydrlvpaikgqrkfspiqlrrlqklgitktdpdtltadeygpfaRLDIDPDTIMWERVVDINDRYLRTITVGQSPTEKG 587
Cdd:COG2759 153 ---------------------------------------------ELNIDPRRITWKRVLDMNDRALRNIVIGLGGKANG 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 588 ISRETRFSISVASEIMAVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLEGTPVLV 667
Cdd:COG2759 188 VPREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFV 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 668 HAGPFANIAHGCNSIIADEVGLKLvgkNGFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHGGGApvt 747
Cdd:COG2759 268 HGGPFANIAHGCNSVIATKLALKL---ADYVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA--- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 748 pgaplNKQYTEENLELVQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKaALEAGAFAAVVSTHWADGGAG 827
Cdd:COG2759 342 -----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRE-LCEELGVRVALSEVWAKGGEG 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 828 AVQLADAVIKACEQG-NQFRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRLTDAGFGNLPICMSKVSGSFTG 906
Cdd:COG2759 416 AEELAEAVVEACEEGpSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSD 495
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62472483 907 DAKIKGAPKGFTLDVEDVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNtETGEIEGLF 968
Cdd:COG2759 496 DPKLLGAPTGFTLTVREVRLSAGAGFIVALTGDIMTMPGLPKVPAAERIDID-EDGKITGLF 556
|
|
| PRK13505 |
PRK13505 |
formate--tetrahydrofolate ligase; Provisional |
348-968 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237403 Cd Length: 557 Bit Score: 735.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 348 PVPSDIVIARAQKPKDIAVLAKEIGLEAREVSLYGNKKAKISLSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTTLMGLV 427
Cdd:PRK13505 1 TMKSDIEIAQEATLKPITEIAAKLGIPEDDLEPYGKYKAKISLDKIKALKDKKDGKLILVTAINPTPAGEGKSTVTVGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 428 QALgAHKLRNTMAALRQPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHENTqkdka 507
Cdd:PRK13505 81 DAL-NKIGKKTVIALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITSANNLLAALIDNHIHQGNE----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 508 lydrlvpaikgqrkfspiqlrrlqklgitktdpdtltadeygpfarLDIDPDTIMWERVVDINDRYLRTITVGQSPTEKG 587
Cdd:PRK13505 155 ----------------------------------------------LGIDPRRITWKRVLDMNDRALRNIVVGLGGPANG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 588 ISRETRFSISVASEIMAVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLEGTPVLV 667
Cdd:PRK13505 189 VPREDGFDITVASEIMAILCLATDLKDLKERLGRIVVGYTYDGKPVTVKDLKVEGAMALLLKDAIKPNLVQTLEGTPAFV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 668 HAGPFANIAHGCNSIIADEVGLKLvgkNGFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHGGGApvt 747
Cdd:PRK13505 269 HGGPFANIAHGCNSVLATKTALKL---ADYVVTEAGFGADLGAEKFLDIKCRKAGLKPDAVVIVATVRALKMHGGVA--- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 748 pgaplNKQYTEENLELVQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKaALEAGAFAAVVSTHWADGGAG 827
Cdd:PRK13505 343 -----KDDLKEENVEALKKGFANLERHIENIRKFGVPVVVAINKFVTDTDAEIAALKE-LCEELGVEVALSEVWAKGGEG 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 828 AVQLADAVIKACEQG-NQFRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRLTDAGFGNLPICMSKVSGSFTG 906
Cdd:PRK13505 417 GVELAEKVVELIEEGeSNFKPLYDDEDSLEEKIEKIATKIYGAKGVEFSPKAKKQLKQIEKNGWDKLPVCMAKTQYSFSD 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62472483 907 DAKIKGAPKGFTLDVEDVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNtETGEIEGLF 968
Cdd:PRK13505 497 DPKLLGAPTGFTITVRELRPSAGAGFIVALTGDIMTMPGLPKVPAALNIDVD-EDGNIVGLF 557
|
|
| PRK13506 |
PRK13506 |
formate--tetrahydrofolate ligase; Provisional |
351-967 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237404 Cd Length: 578 Bit Score: 674.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 351 SDIVIARAQKPKDIAVLAKEIGLEAREVSLYGNKKAKISLSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTTLMGLVQAL 430
Cdd:PRK13506 3 SDIEISRQAPLKPIAEIAAKLGLLPDELSPFGHTKAKVSLSVLKRLADKPKGKLVLVTAITPTPLGEGKTVTTIGLTQGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 431 gAHKLRNTMAALRQPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHEntqkdkalyd 510
Cdd:PRK13506 83 -NALGQKVCACIRQPSMGPVFGVKGGAAGGGYAQVVPMEELNLHLTGDIHAVSAAHNLAAAAIDARLFHE---------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 511 rlvpaikgqrkfspiqlrrlQKLGitktdpdtltADEYGP---FARLDIDPDTIMWERVVDINDRYLRTITVGQSPTEKG 587
Cdd:PRK13506 152 --------------------QRLG----------YDAFEAqsgLPALDIDPEQILWKRVVDHNDRALRMITVGLGENGNG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 588 ISRETRFSISVASEIMAVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLEGTPVLV 667
Cdd:PRK13506 202 PEREDGFDITAASELMAILALSRDLKDMRQRIGRLVLAYNLQGQPITAEDLGVAGAMTVIMKDAIEPTLMQTLEGVPCLI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 668 HAGPFANIAHGCNSIIADEVGLKLVGkngFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHGGGAPVT 747
Cdd:PRK13506 282 HAGPFANIAHGNSSIIADRIALKLAD---YVVTEGGFGSDMGFEKFCNIKARQSGKAPDCAVLVATLRALKANSGLYDLR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 748 PGAPLNKQYTEENLELVQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKAALEAGAFAAVVSTHWADGGAG 827
Cdd:PRK13506 359 PGQALPDSINAPDQARLEAGFANLKWHINNVAQYGLPVVVAINRFPTDTDEELEWLKEAVLLTGAFGCEISEAFAQGGEG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 828 AVQLADAVIKACEQGNQFRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRLTDAGFGNLPICMSKVSGSFTGD 907
Cdd:PRK13506 439 ATALAQAVVRACEQPSQFKLLYPDEMSLEAKLMTLAEVGYGAAGVSLSDKAKQQLAQLTALGYDHLPVCMAKTPLSISHD 518
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 908 AKIKGAPKGFTLDVEDVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNtETGEIEGL 967
Cdd:PRK13506 519 PALKGAPTDFEVPIRELRLCAGAGFITALVGNVMTMPGLGLKPGYLNIDID-ADGEIVGL 577
|
|
| PRK13507 |
PRK13507 |
formate--tetrahydrofolate ligase; Provisional |
352-968 |
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 62472483 352 DIVIA-RAQKP-KDIAVLAKEIGLEAREVSLYGNKKAKIS-LSVLERLKDKEVGHYVVVAGMTPTPLGEGKTTTLMGLVQ 428
Cdd:PRK13507 10 DWEIAeEAEKFmKPVEELAEELGLTKEELLPYGHYIAKVDfRKVLDRLKDRPDGKYIDVTAITPTPLGEGKSTTTMGLVQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 429 ALGAhKLRNTMAALRQPSQGPTFGIKGGAAGGGYAQVIPMEEFNLHLTGDIHAVSAANNLLAAQLDTRIFHENTQKDKAL 508
Cdd:PRK13507 90 GLGK-RGKKVSGAIRQPSGGPTMNIKGSAAGGGLSQCIPLTPFSLGLTGDINAIMNAHNLAMVALTARMQHERNYTDEQL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 509 YDRlvpaikGQRkfspiqlrrlqklgitktdpdtltadeygpfaRLDIDPDTIMWERVVDINDRYLRTITVGQSPTEKGI 588
Cdd:PRK13507 169 ARR------GLK--------------------------------RLDIDPTRVEMGWIIDFCAQALRNIIIGIGGKTDGY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 589 SRETRFSISVASEIMAVLALSRSLEDMKQRLADMVVAFDKRGKPVTADDLGVTGALAVLLKDALEPNLMQSLEGTPVLVH 668
Cdd:PRK13507 211 MMQSGFGIAVSSEVMAILSVATDLKDLRERIGKIVVAYDKNGKPVTTADLEVDGAMTAWMVRAINPNLLQTIEGQPVFVH 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 669 AGPFANIAHGCNSIIADEVGLKLvgkNGFVCTEAGFGSDIGMEKFCNIKCRTSGRKPNAMVLVATVRAIKMHGGGAPVTP 748
Cdd:PRK13507 291 AGPFANIAIGQSSIIADRVGLKL---ADYHVTESGFGADIGFEKFWNLKCRLSGLKPDCAVIVATIRALKMHGGGPKVVP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 749 GAPLNKQYTEENLELVQKGLPNLLQHIENGKAFGMPVVVSLNAHSADTPAEHELVKKAALEAGAFAAvVSTHWADGGAGA 828
Cdd:PRK13507 368 GKPLPEEYTKENVGLVEKGCANLLHHIGTVKKSGINPVVCINAFYTDTHAEIAIVRRLAEQAGARVA-VSRHWEKGGEGA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 829 VQLADAVIKACEQGNQFRLLYDLELPLVDKMNKIATTMYGAGKVVLSPAAEEKVKRL-TDAGFGNLPICMSKVSGSFTGD 907
Cdd:PRK13507 447 LELADAVIDACNEPNDFKFLYPLEMPLRERIETIAREVYGADGVSYTPEAEAKLKRLeSDPETADFGTCMVKTHLSLSHD 526
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62472483 908 AKIKGAPKGFTLDVEDVYVSAGAGFVVAMCGEVTKMPGLPTRPAIYDIDLNTETGEIEGLF 968
Cdd:PRK13507 527 PALKGVPKGWTLPIRDILTYGGAGFVVPVAGDISLMPGTGSDPAFRRIDVDTQTGKVKGLF 587
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
35-326 |
1.35e-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: 1.35e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 35 MSgAKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVE 114
Cdd:COG0190 1 MM-AQILDGKAVAAEIREELKERVAALKAK--GITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 115 LLDKINDLNEDPRVHGIIVQMPLdcdtP--IDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRS 192
Cdd:COG0190 78 LLALIDELNADPSVHGILVQLPL----PkhIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGE-PGFVPCTPAGIMELLERY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 193 GVEIAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGIN 272
Cdd:COG0190 153 GIDLAGKHAVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGIN 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 62472483 273 VKPDaskasgSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 326
Cdd:COG0190 233 RVED------GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
38-326 |
1.26e-108 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 338.09 E-value: 1.26e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 38 AKIISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 117
Cdd:PRK14188 2 ATIIDGKAFAADVRATVAAEVARLKAA-HGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 118 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIA 197
Cdd:PRK14188 81 LIARLNADPAIHGILVQLPLP--KHLDSEAVIQAIDPEKDVDGLHVVNAGRLATG-ETALVPCTPLGCMMLLRRVHGDLS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 198 GARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDA 277
Cdd:PRK14188 158 GLNAVVIGRSNLVGKPMAQLLLAANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIPAP 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 62472483 278 SKASG-SKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 326
Cdd:PRK14188 238 EKGEGkTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACR 287
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
36-326 |
8.85e-108 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 338.52 E-value: 8.85e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 36 SGAKIISGTAVAKSIREELRNEVTAMSKQLAdFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVEL 115
Cdd:PLN02616 71 GGAKVIDGKAVAKKIRDEITIEVSRMKESIG-VVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 116 LDKINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAI-GDLGGFLPCTPWGCLELIRRSGV 194
Cdd:PLN02616 150 LKFISGFNNDPSVHGILVQLPLP--SHMDEQNILNAVSIEKDVDGFHPLNIGRLAMrGREPLFVPCTPKGCIELLHRYNV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 195 EIAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVK 274
Cdd:PLN02616 228 EIKGKRAVVIGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPV 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 62472483 275 PDASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 326
Cdd:PLN02616 308 EDASSPRGYRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKR 359
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
38-330 |
9.87e-108 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 335.44 E-value: 9.87e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 38 AKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 117
Cdd:PRK14190 3 AVIIDGKEVAKEKREQLKEEVVKLKEQ--GIVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 118 KINDLNEDPRVHGIIVQMPLdcdtP--IDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVE 195
Cdd:PRK14190 81 LIDRLNADPRINGILVQLPL----PkhIDEKAVIERISPEKDVDGFHPINVGRMMLGQ-DTFLPCTPHGILELLKEYNID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 196 IAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkp 275
Cdd:PRK14190 156 ISGKHVVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVN--- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 62472483 276 dasKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARFLER 330
Cdd:PRK14190 233 ---RLENGKLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKRAGGR 284
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
38-326 |
1.85e-105 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 329.93 E-value: 1.85e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 38 AKIISGTAVAKSIREELRNEVTAMSKQLADfVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 117
Cdd:PLN02516 9 AQIIDGKAIAKAIRSEIAEEVAQLSEKHGK-VPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELIS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 118 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAI-GDLGGFLPCTPWGCLELIRRSGVEI 196
Cdd:PLN02516 88 KVHELNANPDVHGILVQLPLP--KHINEEKILNEISLEKDVDGFHPLNIGKLAMkGREPLFLPCTPKGCLELLSRSGIPI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 197 AGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPD 276
Cdd:PLN02516 166 KGKKAVVVGRSNIVGLPVSLLLLKADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVSD 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 62472483 277 ASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 326
Cdd:PLN02516 246 PSKKSGYRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKR 295
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
38-326 |
4.40e-102 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 320.48 E-value: 4.40e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 38 AKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 117
Cdd:PRK14189 3 AQLIDGNALSKQLRAEAAQRAAALTAR--GHQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 118 KINDLNEDPRVHGIIVQMPLdcdtP--IDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVE 195
Cdd:PRK14189 81 RIDELNRDPKIHGILVQLPL----PkhIDSHKVIEAIAPEKDVDGFHVANAGALMTG-QPLFRPCTPYGVMKMLESIGIP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 196 IAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvKP 275
Cdd:PRK14189 156 LRGAHAVVIGRSNIVGKPMAMLLLQAGATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMN-RD 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 62472483 276 DAskasgSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 326
Cdd:PRK14189 235 DA-----GKLCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAER 280
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
38-330 |
1.29e-96 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 306.07 E-value: 1.29e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 38 AKIISGTAVAKSIREELRNEVTAMsKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 117
Cdd:PRK10792 3 AKIIDGKTIAQQVRSEVAQKVQAR-VAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 118 KINDLNEDPRVHGIIVQMPLdcdtP--IDSHRITDAVSPEKDVDGLHTVNEGRLAIgDLGGFLPCTPWGCLELIRRSGVE 195
Cdd:PRK10792 82 LIDELNADPTIDGILVQLPL----PahIDNVKVLERIHPDKDVDGFHPYNVGRLAQ-RIPLLRPCTPRGIMTLLERYGID 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 196 IAGARAVVLGRSKIVGTPAA-ELLkWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvk 274
Cdd:PRK10792 157 TYGLNAVVVGASNIVGRPMSlELL-LAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGIN-- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 62472483 275 pdasKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARFLER 330
Cdd:PRK10792 234 ----RLEDGKLVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEEYHDP 285
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
40-327 |
2.33e-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: 2.33e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 40 IISGTAVAKSIREELRNEVTAMsKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 119
Cdd:PRK14174 3 IIDGKKVSLDLKNELKTRVEAY-RAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 120 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGG-FLPCTPWGCLELIRRSGVEIAG 198
Cdd:PRK14174 82 EDLNNDPDVHGILVQQPLP--KQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGHLDKcFVSCTPYGILELLGRYNIETKG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 199 ARAVVLGRSKIVGTPAAEL----LKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVK 274
Cdd:PRK14174 160 KHCVVVGRSNIVGKPMANLmlqkLKESNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 62472483 275 PDASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARF 327
Cdd:PRK14174 240 EDPSTKSGYRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTLQSFERV 292
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
38-326 |
1.00e-93 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 300.72 E-value: 1.00e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 38 AKIISGTAVAKSIREELRNEVTAMSKQLADfVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 117
Cdd:PLN02897 56 TVVIDGNVIAEEIRTKIASEVRKMKKAVGK-VPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 118 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAI-GDLGGFLPCTPWGCLELIRRSGVEI 196
Cdd:PLN02897 135 ALRKFNEDTSIHGILVQLPLP--QHLDESKILNMVRLEKDVDGFHPLNVGNLAMrGREPLFVSCTPKGCVELLIRSGVEI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 197 AGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPD 276
Cdd:PLN02897 213 AGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPVED 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 62472483 277 ASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 326
Cdd:PLN02897 293 SSCEFGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKR 342
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
154-324 |
2.60e-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: 2.60e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 154 PEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTR 233
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGR-PGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKTK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 234 NLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDASKasgSKLVGDVDYAEALQVAGHLTPVPGGVGPMTV 313
Cdd:cd01080 80 NLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDKSG---GKLVGDVDFESAKEKASAITPVPGGVGPMTV 156
|
170
....*....|.
gi 62472483 314 AMLMKNTVRSA 324
Cdd:cd01080 157 AMLMKNTVEAA 167
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
38-323 |
4.02e-92 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 294.28 E-value: 4.02e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 38 AKIISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 117
Cdd:PRK14186 2 ALILDGKALAAEIEQRLQAQIESNLPK-AGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 118 KINDLNEDPRVHGIIVQMPLdcdtP--IDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVE 195
Cdd:PRK14186 81 LIAQLNQDERVDGILLQLPL----PkhLDEVPLLHAIDPDKDADGLHPLNLGRLVKGE-PGLRSCTPAGVMRLLRSQQID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 196 IAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKP 275
Cdd:PRK14186 156 IAGKKAVVVGRSILVGKPLALMLLAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHRLP 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 62472483 276 DASKAsgSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRS 323
Cdd:PRK14186 236 SSDGK--TRLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLS 281
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
39-331 |
4.90e-92 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 293.98 E-value: 4.90e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 39 KIISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDK 118
Cdd:PRK14191 2 VLLDGKALSYKIEKDLKNKIQILTAQ-TGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 119 INDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIAG 198
Cdd:PRK14191 81 IKDLNTDQNIDGILVQLPLP--RHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQ-LDGFVPATPMGVMRLLKHYHIEIKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 199 ARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDAs 278
Cdd:PRK14191 158 KDVVIIGASNIVGKPLAMLMLNAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLNDG- 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 62472483 279 kasgsKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARFLERL 331
Cdd:PRK14191 237 -----RLVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEKRQRKG 284
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
40-323 |
8.34e-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: 8.34e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 40 IISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 119
Cdd:PRK14184 3 LLDGKATAATIREELKTEVAALTAR-HGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 120 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIAGA 199
Cdd:PRK14184 82 AELNARPDIDGILLQLPLP--KGLDSQRCLELIDPAKDVDGFHPENMGRLALG-LPGFRPCTPAGVMTLLERYGLSPAGK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 200 RAVVLGRSKIVGTPAAELL----KWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKP 275
Cdd:PRK14184 159 KAVVVGRSNIVGKPLALMLgapgKFANATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRTD 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 62472483 276 DAskasgskLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRS 323
Cdd:PRK14184 239 DG-------LVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQS 279
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
38-330 |
9.47e-89 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 285.11 E-value: 9.47e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 38 AKIISGTAVAKSIREELRNEVTAMsKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 117
Cdd:PRK14179 2 TEIIDGKALAQKMQAELAEKVAKL-KEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 118 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIA 197
Cdd:PRK14179 81 LIERYNQDPTWHGILVQLPLP--KHINEEKILLAIDPKKDVDGFHPMNTGHLWSGR-PVMIPCTPAGIMEMFREYNVELE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 198 GARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpda 277
Cdd:PRK14179 158 GKHAVVIGRSNIVGKPMAQLLLDKNATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMN----- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 62472483 278 sKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARFLER 330
Cdd:PRK14179 233 -RDENGKLIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALRSLHK 284
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
37-326 |
1.02e-85 |
|
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: 1.02e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 37 GAKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELL 116
Cdd:PRK14193 2 TAIILDGKATADEIKADLAERVAALKEK--GITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 117 DKINDLNEDPRVHGIIVQMPLdcdtP--IDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGfLPCTPWGCLELIRRSGV 194
Cdd:PRK14193 80 AVIDELNADPACTGYIVQLPL----PkhLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAP-LPCTPRGIVHLLRRYDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 195 EIAGARAVVLGRSKIVGTPAAELL--KWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGIn 272
Cdd:PRK14193 155 ELAGAHVVVIGRGVTVGRPIGLLLtrRSENATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGV- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 62472483 273 vkpdaSKASGSKLVGDVDyAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 326
Cdd:PRK14193 234 -----SRAGDGKLVGDVH-PDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAER 281
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
38-324 |
6.82e-84 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 272.52 E-value: 6.82e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 38 AKIISGTAVAKSIREELRNEVTAMsKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 117
Cdd:PRK14168 3 AKIIKGTEIREEILEEIRGEVAEL-KEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 118 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIG-DLGGFLPCTPWGCLELIRRSGVEI 196
Cdd:PRK14168 82 LIDKYNNDDSIHGILVQLPLP--KHINEKKVLNAIDPDKDVDGFHPVNVGRLMIGgDEVKFLPCTPAGIQEMLVRSGVET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 197 AGARAVVLGRSKIVGTPAAELLKW----ANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGIN 272
Cdd:PRK14168 160 SGAEVVVVGRSNIVGKPIANMMTQkgpgANATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVN 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 62472483 273 ---VKPDASKASgskLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSA 324
Cdd:PRK14168 240 rvgTNESTGKAI---LSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSA 291
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
38-325 |
9.84e-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: 9.84e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 38 AKIISGTAVAKSIREELRNEVTAMSKqlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 117
Cdd:PRK14167 2 TEIIDGNAVAAQIRDDLTDAIETLED--AGVTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 118 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIA 197
Cdd:PRK14167 80 TIDELNADEDVHGILVQMPVP--DHVDDREVLRRIDPAKDVDGFHPENVGRLVAGD-ARFKPCTPHGIQKLLAAAGVDTE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 198 GARAVVLGRSKIVGTPAAELL----KWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINv 273
Cdd:PRK14167 157 GADVVVVGRSDIVGKPMANLLiqkaDGGNATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGIN- 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 62472483 274 KPDASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAA 325
Cdd:PRK14167 236 RVDADTEKGYELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAAS 287
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
162-328 |
1.03e-82 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 263.94 E-value: 1.03e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 162 HTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRS 241
Cdd:pfam02882 1 HPYNLGRLVLG-KPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 242 ADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpdasKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTV 321
Cdd:pfam02882 80 ADIVVVAVGKPELIKADWIKPGAVVIDVGIN------RVGNGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNTV 153
|
....*..
gi 62472483 322 RSAARFL 328
Cdd:pfam02882 154 EAAKRQL 160
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
37-326 |
3.77e-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: 3.77e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 37 GAKIISGTAVAKSIREELRNEVTAMSkqladFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELL 116
Cdd:PRK14173 2 AARELSGPPAAEAVYAELRARLAKLP-----FVPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 117 DKINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEI 196
Cdd:PRK14173 77 ELIARLNADPEVDGILVQLPLP--PHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMG-GEALEPCTPAGVVRLLKHYGIPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 197 AGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGIN-VKP 275
Cdd:PRK14173 154 AGKEVVVVGRSNIVGKPLAALLLREDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINrVGG 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 62472483 276 DASKAsgsKLVGDVdYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 326
Cdd:PRK14173 234 NGGRD---ILTGDV-HPEVAEVAGALTPVPGGVGPMTVAMLMANTVIAALR 280
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
39-319 |
5.95e-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: 5.95e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 39 KIISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDK 118
Cdd:PRK14172 3 QIINGKEVALKIKEEIKNFVEERKEN-GLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 119 INDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIAG 198
Cdd:PRK14172 82 IEELNKDNNVHGIMLQLPLP--KHLDEKKITNKIDANKDIDCLTFISVGKFYKGE-KCFLPCTPNSVITLIKSLNIDIEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 199 ARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGinvkpdAS 278
Cdd:PRK14172 159 KEVVVIGRSNIVGKPVAQLLLNENATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVG------TS 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 62472483 279 KASGsKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKN 319
Cdd:PRK14172 233 SVNG-KITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKN 272
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
40-323 |
6.44e-80 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 261.43 E-value: 6.44e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 40 IISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 119
Cdd:PRK14171 4 IIDGKALANEILADLKLEIQELKSQ-TNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 120 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGFLPCTPWGCLELIRRSGVEIAGA 199
Cdd:PRK14171 83 NELNLDNEISGIIVQLPLP--SSIDKNKILSAVSPSKDIDGFHPLNVGYLHSGISQGFIPCTALGCLAVIKKYEPNLTGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 200 RAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpdasK 279
Cdd:PRK14171 161 NVVIIGRSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGIN------R 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 62472483 280 ASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRS 323
Cdd:PRK14171 235 ISGNKIIGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKA 278
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
40-324 |
1.58e-79 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 260.53 E-value: 1.58e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 40 IISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 119
Cdd:PRK14187 4 IIDGKKIANDITEILATCIDDLKRQ-HNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 120 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGFL-PCTPWGCLELIRRSGVEIAG 198
Cdd:PRK14187 83 NELNNDDSVHGILVQLPVP--NHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQKKNCLiPCTPKGCLYLIKTITRNLSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 199 ARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpDAS 278
Cdd:PRK14187 161 SDAVVIGRSNIVGKPMACLLLGENCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGIN---SIE 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 62472483 279 KASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSA 324
Cdd:PRK14187 238 EGGVKKFVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAA 283
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
35-335 |
5.22e-79 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 259.39 E-value: 5.22e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 35 MSGAKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVE 114
Cdd:PRK14194 1 LMSAKLIDGKAAAARVLAQVREDVRTLKAA--GIEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 115 LLDKINDLNEDPRVHGIIVQMPLDCDtpIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGV 194
Cdd:PRK14194 79 LLALIAELNADPSVNGILLQLPLPAH--IDEARVLQAINPLKDVDGFHSENVGGLSQGR-DVLTPCTPSGCLRLLEDTCG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 195 EIAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVK 274
Cdd:PRK14194 156 DLTGKHAVVIGRSNIVGKPMAALLLQAHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINRI 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62472483 275 PDASKasgSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVrSAARFLERLAKSQ 335
Cdd:PRK14194 236 DDDGR---SRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTV-TAARLQAHAQRSQ 292
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
40-327 |
1.77e-78 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 257.48 E-value: 1.77e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 40 IISGTAVAKSIREELRNEVTAMSKQladfvPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 119
Cdd:PRK14181 2 LLKGAPAAEHILATIKENISASSTA-----PGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 120 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGFLPCTPWGCLELIRRSGVEIAGA 199
Cdd:PRK14181 77 HRLNNDPNIHGILVQLPLP--KHLDAQAILQAISPDKDVDGLHPVNMGKLLLGETDGFIPCTPAGIIELLKYYEIPLHGR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 200 RAVVLGRSKIVGTPAAELLKW----ANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKP 275
Cdd:PRK14181 155 HVAIVGRSNIVGKPLAALLMQkhpdTNATVTLLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRVP 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 62472483 276 dASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARF 327
Cdd:PRK14181 235 -AANPKGYILVGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNTWESYLRH 285
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
38-326 |
1.98e-78 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 257.31 E-value: 1.98e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 38 AKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 117
Cdd:PRK14170 2 GEIIDGKKLAKEIQEKVTREVAELVKE--GKKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 118 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIA 197
Cdd:PRK14170 80 VVEELNEDKTIHGILVQLPLP--EHISEEKVIDTISYDKDVDGFHPVNVGNLFIGK-DSFVPCTPAGIIELIKSTGTQIE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 198 GARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpda 277
Cdd:PRK14170 157 GKRAVVIGRSNIVGKPVAQLLLNENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMD----- 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 62472483 278 sKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 326
Cdd:PRK14170 232 -RDENNKLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKR 279
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
39-324 |
2.41e-76 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 251.65 E-value: 2.41e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 39 KIISGTAVAKSIREELRNEVTAMsKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDK 118
Cdd:PRK14176 9 RIIDGKALAKKIEAEVRSGVERL-KSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 119 INDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIAG 198
Cdd:PRK14176 88 IDSLNKRKDVHGILLQLPLP--KHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGD-EGLVPCTPHGVIRALEEYGVDIEG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 199 ARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDas 278
Cdd:PRK14176 165 KNAVIVGHSNVVGKPMAAMLLNRNATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITKEED-- 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 62472483 279 kasgsKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSA 324
Cdd:PRK14176 243 -----KVYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCA 283
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
39-328 |
1.23e-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: 1.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 39 KIISGTAVAKSIREELRNEVTAMsKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDK 118
Cdd:PRK14183 2 QILDGKALSDKIKENVKKEVDEL-KLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 119 INDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIAG 198
Cdd:PRK14183 81 IAMMNNNPNIDGILVQLPLP--KHIDTTKILEAIDPKKDVDGFHPYNVGRLVTG-LDGFVPCTPLGVMELLEEYEIDVKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 199 ARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpdas 278
Cdd:PRK14183 158 KDVCVVGASNIVGKPMAALLLNANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGIN------ 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 62472483 279 KASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARFL 328
Cdd:PRK14183 232 RTEDGRLVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKNRA 281
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
38-328 |
6.25e-74 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 245.14 E-value: 6.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 38 AKIISGTAVAKSIREELRNEVTAMsKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 117
Cdd:PRK14192 3 ALVLDGKALAKQIEEELSVRVEAL-KAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 118 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIA 197
Cdd:PRK14192 82 KIEELNANPDVHGILLQHPVP--AQIDERACFDAISLAKDVDGVTCLGFGRMAMGE-AAYGSATPAGIMRLLKAYNIELA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 198 GARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDA 277
Cdd:PRK14192 159 GKHAVVVGRSAILGKPMAMMLLNANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFHPRDGG 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 62472483 278 SkasgsklVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAARFL 328
Cdd:PRK14192 239 G-------VGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKAL 282
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
40-325 |
1.32e-73 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 243.98 E-value: 1.32e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 40 IISGTAVAKSIREELRNEVTAmskqlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 119
Cdd:PRK14178 2 ILDGKAVSEKRLELLKEEIIE-----SGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 120 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIAGA 199
Cdd:PRK14178 77 RRLNEDPDINGILVQLPLP--KGVDTERVIAAILPEKDVDGFHPLNLGRLVSG-LPGFAPCTPNGIMTLLHEYKISIAGK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 200 RAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpdask 279
Cdd:PRK14178 154 RAVVVGRSIDVGRPMAALLLNADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGIN------- 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 62472483 280 ASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAA 325
Cdd:PRK14178 227 QVNGKLCGDVDFDAVKEIAGAITPVPGGVGPMTIATLMENTFDAAK 272
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
40-324 |
1.69e-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: 1.69e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 40 IISGTAVAKSIREELRNEVTAMSKQLADfvPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 119
Cdd:PRK14166 3 LLDGKALSAKIKEELKEKNQFLKSKGIE--SCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 120 NDLNEDPRVHGIIVQMPLDCDtpIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGFLPCTPWGCLELIRRSGVEIAGA 199
Cdd:PRK14166 81 NTLNHDDSVHGILVQLPLPDH--ICKDLILESIISSKDVDGFHPINVGYLNLGLESGFLPCTPLGVMKLLKAYEIDLEGK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 200 RAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpdasK 279
Cdd:PRK14166 159 DAVIIGASNIVGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGIN------R 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 62472483 280 ASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSA 324
Cdd:PRK14166 233 LESGKIVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSA 277
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
39-321 |
6.11e-73 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 242.81 E-value: 6.11e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 39 KIISGTAVAKSIREELRNEVTAMSKQlADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDK 118
Cdd:PRK14185 2 QLIDGKAISAQIKQEIAAEVAEIVAK-GGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 119 INDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIAG 198
Cdd:PRK14185 81 VRELNQDDDVDGFIVQLPLP--KHISEQKVIEAIDYRKDVDGFHPINVGRMSIG-LPCFVSATPNGILELLKRYHIETSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 199 ARAVVLGRSKIVGTPAAELL----KWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVK 274
Cdd:PRK14185 158 KKCVVLGRSNIVGKPMAQLMmqkaYPGDCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTRV 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 62472483 275 PDASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTV 321
Cdd:PRK14185 238 PDATRKSGFKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTL 284
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
38-326 |
6.61e-72 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 239.46 E-value: 6.61e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 38 AKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 117
Cdd:PRK14169 1 ATRLDGRAVSKKILADLKQTVAKLAQQ--DVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 118 KINDLNEDPRVHGIIVQMPLDCDtpIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDlGGFLPCTPWGCLELIRRSGVEIA 197
Cdd:PRK14169 79 KVAELNHDPDVDAILVQLPLPAG--LDEQAVIDAIDPDKDVDGFSPVSVGRLWANE-PTVVASTPYGIMALLDAYDIDVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 198 GARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDA 277
Cdd:PRK14169 156 GKRVVIVGRSNIVGRPLAGLMVNHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRGADG 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 62472483 278 skasgsKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 326
Cdd:PRK14169 236 ------KLLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKR 278
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
38-326 |
1.70e-70 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 235.58 E-value: 1.70e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 38 AKIISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLD 117
Cdd:PRK14175 3 AKILDGKQIAKDYRQGLQDQVEALKEK--GFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 118 KINDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIgDLGGFLPCTPWGCLELIRRSGVEIA 197
Cdd:PRK14175 81 ELNRLNNDDSVSGILVQVPLP--KQVSEQKILEAINPEKDVDGFHPINIGKLYI-DEQTFVPCTPLGIMEILKHADIDLE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 198 GARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDA 277
Cdd:PRK14175 158 GKNAVVIGRSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVGNTPDENG 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 62472483 278 skasgsKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 326
Cdd:PRK14175 238 ------KLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEKM 280
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
40-324 |
2.89e-70 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 234.87 E-value: 2.89e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 40 IISGTAVAKSIREELRNEVtAMSKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 119
Cdd:PRK14177 5 LLDGKKLSEKIRNEIRETI-EERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLGVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 120 NDLNEDPRVHGIIVQMPldcdTP--IDSHRITDAVSPEKDVDGLHTVNEGRLAIGdLGGFLPCTPWGCLELIRRSGVEIA 197
Cdd:PRK14177 84 DKLNLDPNVDGILLQHP----VPsqIDERAAFDRIALEKDVDGVTTLSFGKLSMG-VETYLPCTPYGMVLLLKEYGIDVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 198 GARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVkpda 277
Cdd:PRK14177 159 GKNAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYNP---- 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 62472483 278 skasGSklVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSA 324
Cdd:PRK14177 235 ----GN--VGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSF 275
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
40-326 |
4.58e-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: 4.58e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 40 IISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 119
Cdd:PRK14182 3 LIDGKQIAAKVKGEVATEVRALAAR--GVQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 120 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGFLPCTPWGCLELIRRSGVEIAGA 199
Cdd:PRK14182 81 ARLNADPAVHGILVQLPLP--KHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGVPRPCTPAGVMRMLDEARVDPKGK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 200 RAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDAsk 279
Cdd:PRK14182 159 RALVVGRSNIVGKPMAMMLLERHATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLADG-- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 62472483 280 asgsKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSAAR 326
Cdd:PRK14182 237 ----KLVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKR 279
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
40-324 |
1.41e-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: 1.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 40 IISGTAVAKSIREELRNEVTAMSKQLAdFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKI 119
Cdd:PRK14180 3 LIDGKSLSKDLKERLATQVQEYKHHTA-ITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 120 NDLNEDPRVHGIIVQMPLDcdTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGFLPCTPWGCLELIRRSGVEIAGA 199
Cdd:PRK14180 82 DQLNNDSSVHAILVQLPLP--AHINKNNVIYSIKPEKDVDGFHPTNVGRLQLRDKKCLESCTPKGIMTMLREYGIKTEGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 200 RAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINvkpdask 279
Cdd:PRK14180 160 YAVVVGASNVVGKPVSQLLLNAKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGIN------- 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 62472483 280 ASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSA 324
Cdd:PRK14180 233 HVDGKIVGDVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCA 277
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
41-159 |
8.30e-48 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 165.66 E-value: 8.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 41 ISGTAVAKSIREELRNEVTAMSKQlaDFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKIN 120
Cdd:pfam00763 1 IDGKAIAKKIREELKEEVAALKAG--GRKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALID 78
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 62472483 121 DLNEDPRVHGIIVQMPLdcdtP--IDSHRITDAVSPEKDVD 159
Cdd:pfam00763 79 KLNADPSVHGILVQLPL----PkhIDEEKVLEAIDPEKDVD 115
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
178-324 |
5.60e-37 |
|
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NAD(P) binding domains of methylene-tetrahydrofolate dehydrogenase (m-THF DH) and m-THF DH/cyclohydrolase bifunctional enzymes (m-THF DH/cyclohydrolase). M-THF is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, mono-functional DH, as well as bifunctional DH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express a monofunctional DH. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133451 Cd Length: 140 Bit Score: 135.71 E-value: 5.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 178 LPCTPWGCLELIR-------RSGVEIAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIG 250
Cdd:cd05212 1 GPCTPLFVSPVAKavkellnKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62472483 251 VAEMVKGSWIKPGAVVIDCGINvkpdaskasgsKLVGDvdyaEALQVAGHLTPVPGGVGPMTVAMLMKNTVRSA 324
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 ... |
154-322 |
1.78e-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: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 154 PEKDVDGLHTVN-------------EGRLAigdlgGFLPCTPWGCLELIRRSGV---------EIAGARAVVLGRSKIVG 211
Cdd:cd01079 1 PHKDVEGLSHKYifnlyhnirfldpENRKK-----SILPCTPLAIVKILEFLGIynkilpygnRLYGKTITIINRSEVVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 212 TPAAELLKWANATV---------------------TVCHSKTRNLEEITRSADILVVGIGVAEM-VKGSWIKPGAVVID- 268
Cdd:cd01079 76 RPLAALLANDGARVysvdingiqvftrgesirhekHHVTDEEAMTLDCLSQSDVVITGVPSPNYkVPTELLKDGAICINf 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 62472483 269 -CGINVKPDASKASGsklvgdvdyaealqvaghlTPVPGgVGPMTVAMLMKNTVR 322
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) ... |
180-270 |
2.90e-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: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 180 CTPWGCLELIRRSGVE----IAGARAVVLGRsKIVGTPAAELLKWA-NATVTVCHSktrnleeitrsaDILVVGIGVAEM 254
Cdd:cd05191 1 ATAAGAVALLKAAGKVtnksLKGKTVVVLGA-GEVGKGIAKLLADEgGKKVVLCDR------------DILVTATPAGVP 67
|
90
....*....|....*....
gi 62472483 255 VKG---SWIKPGAVVIDCG 270
Cdd:cd05191 68 VLEeatAKINEGAVVIDLA 86
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
196-268 |
1.93e-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: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472483 196 IAGARAVVLGrSKIVGTPAAELLKWANATVTV---------------------CHSKTRNLEEITRSADILVVGIGV--- 251
Cdd:smart01002 18 VPPAKVVVIG-AGVVGLGAAATAKGLGAEVTVldvrparlrqlesllgarfttLYSQAELLEEAVKEADLVIGAVLIpga 96
|
90 100
....*....|....*....|....
gi 62472483 252 -------AEMVKGswIKPGAVVID 268
Cdd:smart01002 97 kapklvtREMVKS--MKPGSVIVD 118
|
|
| |
