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Conserved domains on  [gi|2327289797|ref|XP_002715037|]
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monofunctional C1-tetrahydrofolate synthase, mitochondrial [Oryctolagus cuniculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02759 PLN02759
Formate--tetrahydrofolate ligase
349-975 0e+00

Formate--tetrahydrofolate ligase


:

Pssm-ID: 178359  Cd Length: 637  Bit Score: 1015.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 349 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKST 428
Cdd:PLN02759    9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 429 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 508
Cdd:PLN02759   89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 509 TQTDKALYNRLVPS-VNGVREFSEIQLARLKKLGINKTDPSALTEEEMGKFARLNIDPSTITWQRVLDTNDRFLRKITIG 587
Cdd:PLN02759  169 TQSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVG 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 588 QASTEKGYSRQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTL 667
Cdd:PLN02759  249 QGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTL 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 668 EGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMH 747
Cdd:PLN02759  329 EGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMH 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 748 GGGPSVIPGVPLKKEYTEENIQLVADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYH 827
Cdd:PLN02759  409 GGGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTH 488
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 828 WSVGGKGSVDLARAVREAANTNS-HFQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAK 906
Cdd:PLN02759  489 HAHGGKGAVDLGEAVQKACEGNSqPFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAK 568
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2327289797 907 THLSLSHQPDKKGVPRDFVLPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVQGLF 975
Cdd:PLN02759  569 TQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTETGKVLGLS 637
NAD_bind_m-THF_DH_Cyclohyd_like cd05212
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ...
190-332 7.64e-55

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: 186.56  E-value: 7.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 190 GDAHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSP 269
Cdd:cd05212     1 GPCTPLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2327289797 270 KPEKIPVAWIRPGTTVLNCFHSFMSEKLGCGSHGVHCGGSIaedDVSLLAAALRIQNMVSSGR 332
Cdd:cd05212    81 KPEKVPTEWIKPGATVINCSPTKLSGDDVKESASLYVPMTG---GVGKLTVAMRMQNMVRSVR 140
PRK14190 super family cl32972
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
80-287 2.24e-29

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


The actual alignment was detected with superfamily member PRK14190:

Pssm-ID: 184560 [Multi-domain]  Cd Length: 284  Bit Score: 118.96  E-value: 2.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  80 KEVLSLlqeKNPAFKPVLAVIQAGDDNLLQ---EVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ 156
Cdd:PRK14190   21 EEVVKL---KEQGIVPGLAVILVGDDPASHsyvRGKKKAAEKVGIYSELYEFPADITEEELLALIDRLNADPRINGILVQ 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 157 --VPENSLSSKVLNALKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQ 234
Cdd:PRK14190   98 lpLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQ--DTFLPCTPHGILELLKEYNIDISGKHVVVVGRSNIVGKPVG 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2327289797 235 CLFQRKD-SMTMSSQwKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14190  176 QLLLNENaTVTYCHS-KTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVID 228
 
Name Accession Description Interval E-value
PLN02759 PLN02759
Formate--tetrahydrofolate ligase
349-975 0e+00

Formate--tetrahydrofolate ligase


Pssm-ID: 178359  Cd Length: 637  Bit Score: 1015.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 349 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKST 428
Cdd:PLN02759    9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 429 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 508
Cdd:PLN02759   89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 509 TQTDKALYNRLVPS-VNGVREFSEIQLARLKKLGINKTDPSALTEEEMGKFARLNIDPSTITWQRVLDTNDRFLRKITIG 587
Cdd:PLN02759  169 TQSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVG 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 588 QASTEKGYSRQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTL 667
Cdd:PLN02759  249 QGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTL 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 668 EGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMH 747
Cdd:PLN02759  329 EGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMH 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 748 GGGPSVIPGVPLKKEYTEENIQLVADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYH 827
Cdd:PLN02759  409 GGGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTH 488
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 828 WSVGGKGSVDLARAVREAANTNS-HFQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAK 906
Cdd:PLN02759  489 HAHGGKGAVDLGEAVQKACEGNSqPFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAK 568
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2327289797 907 THLSLSHQPDKKGVPRDFVLPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVQGLF 975
Cdd:PLN02759  569 TQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTETGKVLGLS 637
FTHFS pfam01268
Formate--tetrahydrofolate ligase;
357-975 0e+00

Formate--tetrahydrofolate ligase;


Pssm-ID: 460143  Cd Length: 555  Bit Score: 989.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 357 PSDIEISRGQTPKAVDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQA 436
Cdd:pfam01268   1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 437 LtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkaly 516
Cdd:pfam01268  81 L-NRLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 517 nrlvpsvngvrefseiqlarlkklginktdpsalteeemgkfarLNIDPSTITWQRVLDTNDRFLRKITIGQASTEKGYS 596
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 597 RQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHA 676
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 677 GPFANIAHGNSSVLADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMHGGgpsvipg 756
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGG------- 338
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 757 vPLKKEYTEENIQLVADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKrAGAFDAVPCYHWSVGGKGSV 836
Cdd:pfam01268 339 -VGKDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRELCE-AGGVDAALSEHWAKGGEGAI 416
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 837 DLARAVREAANTN-SHFQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAKTHLSLSHQP 915
Cdd:pfam01268 417 ELAEAVVEACEEEpSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 916 DKKGVPRDFVLPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTEtEQVQGLF 975
Cdd:pfam01268 497 KLKGAPTGFTLPVRDVRLSAGAGFIVALTGDIMTMPGLPKRPAAENIDVDED-GKITGLF 555
FTHFS cd00477
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ...
371-974 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: 932.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 371 VDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALTAHLNvNSFACLR 450
Cdd:cd00477     1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 451 QPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkalynrlvpsvngvrefs 530
Cdd:cd00477    80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 531 eiqlarlkklginktdpsalteeemgkfarLNIDPSTITWQRVLDTNDRFLRKITIGQASTEKGYSRQAQFDIAVASEIM 610
Cdd:cd00477   139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 611 AVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSVL 690
Cdd:cd00477   189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 691 ADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMHGGGPSVIPGvplkkeytEENIQL 770
Cdd:cd00477   269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 771 VADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVpCYHWSVGGKGSVDLARAVREAANTNS 850
Cdd:cd00477   338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKPK 416
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 851 H-FQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAKTHLSLSHQPDKKGVPRDFVLPIS 929
Cdd:cd00477   417 SnFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 2327289797 930 DVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDtETEQVQGL 974
Cdd:cd00477   497 DVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDID-DTGKIEGL 540
MIS1 COG2759
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
356-975 0e+00

Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];


Pssm-ID: 442046  Cd Length: 556  Bit Score: 882.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 356 VPSDIEISRGQTPKAVDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQ 435
Cdd:COG2759     1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 436 ALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENtqtdkal 515
Cdd:COG2759    81 AL-NRLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQGN------- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 516 ynrlvpsvngvrefseiqlarlkklginktdpsalteeemgkfaRLNIDPSTITWQRVLDTNDRFLRKITIGQASTEKGY 595
Cdd:COG2759   153 --------------------------------------------ELNIDPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 596 SRQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVH 675
Cdd:COG2759   189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 676 AGPFANIAHGNSSVLADKIALKLvGEegFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMHGGGPsvip 755
Cdd:COG2759   269 GGPFANIAHGCNSVIATKLALKL-AD--YVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA---- 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 756 gvplKKEYTEENIQLVADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKRAGAfDAVPCYHWSVGGKGS 835
Cdd:COG2759   342 ----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEGA 416
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 836 VDLARAVREAANTN-SHFQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAKTHLSLSHQ 914
Cdd:COG2759   417 EELAEAVVEACEEGpSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSDD 496
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2327289797 915 PDKKGVPRDFVLPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDtETEQVQGLF 975
Cdd:COG2759   497 PKLLGAPTGFTLTVREVRLSAGAGFIVALTGDIMTMPGLPKVPAAERIDID-EDGKITGLF 556
NAD_bind_m-THF_DH_Cyclohyd_like cd05212
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ...
190-332 7.64e-55

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: 186.56  E-value: 7.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 190 GDAHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSP 269
Cdd:cd05212     1 GPCTPLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2327289797 270 KPEKIPVAWIRPGTTVLNCFHSFMSEKLGCGSHGVHCGGSIaedDVSLLAAALRIQNMVSSGR 332
Cdd:cd05212    81 KPEKVPTEWIKPGATVINCSPTKLSGDDVKESASLYVPMTG---GVGKLTVAMRMQNMVRSVR 140
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
180-335 2.94e-37

Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;


Pssm-ID: 427036  Cd Length: 160  Bit Score: 137.21  E-value: 2.94e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 180 TDVNLGKLVRGdaHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMSSQWKTPQLESKLQ 259
Cdd:pfam02882   1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 260 EADIVILGSPKPEKIPVAWIRPGTTVLNCFHSFMSEKLGCGshGVHcGGSIAE---------DDVSLLAAALRIQNMVSS 330
Cdd:pfam02882  79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVG--DVD-FENVKEkasaitpvpGGVGPMTVAMLLQNTVEA 155

                  ....*
gi 2327289797 331 GRRWL 335
Cdd:pfam02882 156 AKRQL 160
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
94-286 7.32e-36

5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 137.45  E-value: 7.32e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  94 KPVLAVIQAGDDnllqE-----VN--QNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQVPensL---- 162
Cdd:COG0190    32 TPGLAVVLVGDD----PasqvyVRnkHKACEEVGIESELIRLPADTTQEELLALIDELNADPSVHGILVQLP---Lpkhi 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 163 -SSKVLNALKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLGaHG-----PLeaALqcL 236
Cdd:COG0190   105 dEEAVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLERYGIDLAGKHAVVVG-RSnivgkPL--AL--L 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2327289797 237 FQRKD---SMTMSsqwKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVL 286
Cdd:COG0190   178 LLRRNatvTVCHS---RTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVI 227
PRK14190 PRK14190
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
80-287 2.24e-29

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 184560 [Multi-domain]  Cd Length: 284  Bit Score: 118.96  E-value: 2.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  80 KEVLSLlqeKNPAFKPVLAVIQAGDDNLLQ---EVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ 156
Cdd:PRK14190   21 EEVVKL---KEQGIVPGLAVILVGDDPASHsyvRGKKKAAEKVGIYSELYEFPADITEEELLALIDRLNADPRINGILVQ 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 157 --VPENSLSSKVLNALKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQ 234
Cdd:PRK14190   98 lpLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQ--DTFLPCTPHGILELLKEYNIDISGKHVVVVGRSNIVGKPVG 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2327289797 235 CLFQRKD-SMTMSSQwKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14190  176 QLLLNENaTVTYCHS-KTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVID 228
PLN02516 PLN02516
methylenetetrahydrofolate dehydrogenase (NADP+)
95-287 8.85e-26

methylenetetrahydrofolate dehydrogenase (NADP+)


Pssm-ID: 178131 [Multi-domain]  Cd Length: 299  Bit Score: 108.83  E-value: 8.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  95 PVLAVIQAG---DDNLLQEVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQVP--ENSLSSKVLNA 169
Cdd:PLN02516   40 PGLAVVIVGsrkDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISKVHELNANPDVHGILVQLPlpKHINEEKILNE 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 170 LKPEKDVDGVTDVNLGKLVRGDAHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMSSQW 249
Cdd:PLN02516  120 ISLEKDVDGFHPLNIGKLAMKGREPLFLPCTPKGCLELLSRSGIPIKGKKAVVVGRSNIVGLPVSLLLLKADATVTVVHS 199
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2327289797 250 KTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PLN02516  200 RTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVID 237
THF_DHG_CYH pfam00763
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
87-177 6.99e-18

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;


Pssm-ID: 459930 [Multi-domain]  Cd Length: 115  Bit Score: 80.14  E-value: 6.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  87 QEKNPAFKPVLAVIQAGDD--------NLlqevnQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ-- 156
Cdd:pfam00763  20 ALKAGGRKPGLAVILVGDDpasqvyvrNK-----KKACEEVGIESELIRLPEDTTEEELLALIDKLNADPSVHGILVQlp 94
                          90       100
                  ....*....|....*....|.
gi 2327289797 157 VPENSLSSKVLNALKPEKDVD 177
Cdd:pfam00763  95 LPKHIDEEKVLEAIDPEKDVD 115
 
Name Accession Description Interval E-value
PLN02759 PLN02759
Formate--tetrahydrofolate ligase
349-975 0e+00

Formate--tetrahydrofolate ligase


Pssm-ID: 178359  Cd Length: 637  Bit Score: 1015.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 349 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKST 428
Cdd:PLN02759    9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 429 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 508
Cdd:PLN02759   89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 509 TQTDKALYNRLVPS-VNGVREFSEIQLARLKKLGINKTDPSALTEEEMGKFARLNIDPSTITWQRVLDTNDRFLRKITIG 587
Cdd:PLN02759  169 TQSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVG 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 588 QASTEKGYSRQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTL 667
Cdd:PLN02759  249 QGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTL 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 668 EGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMH 747
Cdd:PLN02759  329 EGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMH 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 748 GGGPSVIPGVPLKKEYTEENIQLVADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYH 827
Cdd:PLN02759  409 GGGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTH 488
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 828 WSVGGKGSVDLARAVREAANTNS-HFQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAK 906
Cdd:PLN02759  489 HAHGGKGAVDLGEAVQKACEGNSqPFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAK 568
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2327289797 907 THLSLSHQPDKKGVPRDFVLPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVQGLF 975
Cdd:PLN02759  569 TQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTETGKVLGLS 637
FTHFS pfam01268
Formate--tetrahydrofolate ligase;
357-975 0e+00

Formate--tetrahydrofolate ligase;


Pssm-ID: 460143  Cd Length: 555  Bit Score: 989.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 357 PSDIEISRGQTPKAVDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQA 436
Cdd:pfam01268   1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 437 LtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkaly 516
Cdd:pfam01268  81 L-NRLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 517 nrlvpsvngvrefseiqlarlkklginktdpsalteeemgkfarLNIDPSTITWQRVLDTNDRFLRKITIGQASTEKGYS 596
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 597 RQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHA 676
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 677 GPFANIAHGNSSVLADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMHGGgpsvipg 756
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGG------- 338
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 757 vPLKKEYTEENIQLVADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKrAGAFDAVPCYHWSVGGKGSV 836
Cdd:pfam01268 339 -VGKDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRELCE-AGGVDAALSEHWAKGGEGAI 416
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 837 DLARAVREAANTN-SHFQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAKTHLSLSHQP 915
Cdd:pfam01268 417 ELAEAVVEACEEEpSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 916 DKKGVPRDFVLPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTEtEQVQGLF 975
Cdd:pfam01268 497 KLKGAPTGFTLPVRDVRLSAGAGFIVALTGDIMTMPGLPKRPAAENIDVDED-GKITGLF 555
FTHFS cd00477
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ...
371-974 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: 932.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 371 VDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALTAHLNvNSFACLR 450
Cdd:cd00477     1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 451 QPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkalynrlvpsvngvrefs 530
Cdd:cd00477    80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 531 eiqlarlkklginktdpsalteeemgkfarLNIDPSTITWQRVLDTNDRFLRKITIGQASTEKGYSRQAQFDIAVASEIM 610
Cdd:cd00477   139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 611 AVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSVL 690
Cdd:cd00477   189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 691 ADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMHGGGPSVIPGvplkkeytEENIQL 770
Cdd:cd00477   269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 771 VADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVpCYHWSVGGKGSVDLARAVREAANTNS 850
Cdd:cd00477   338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKPK 416
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 851 H-FQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAKTHLSLSHQPDKKGVPRDFVLPIS 929
Cdd:cd00477   417 SnFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 2327289797 930 DVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDtETEQVQGL 974
Cdd:cd00477   497 DVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDID-DTGKIEGL 540
PTZ00386 PTZ00386
formyl tetrahydrofolate synthetase; Provisional
349-974 0e+00

formyl tetrahydrofolate synthetase; Provisional


Pssm-ID: 240394  Cd Length: 625  Bit Score: 922.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 349 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKST 428
Cdd:PTZ00386    8 KLSCQWPVPSDIDIAQSVKPQPITSVAESAGILLSELDPYGSTRAKVKLSVLKRLENSPNGKYVVVAGMNPTPLGEGKST 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 429 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 508
Cdd:PTZ00386   88 TTIGLAQSLGAHLHRKTFACIRQPSQGPTFGIKGGAAGGGYSQVIPMEDFNLHGTGDIHAITAANNLLAAALDTRIFHER 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 509 TQTDKALYNRLVpsvNGVREFSEIQLARLKKLGINKTDPSALTEEEMGKFARLNIDPSTITWQRVLDTNDRFLRKITIGQ 588
Cdd:PTZ00386  168 TQSDAALYRRLT---DELKKFTPIMLKRLEKLGISKTDPKQLTEEERVRFARLDIDPDTISWRRVTDVNDRMLREITIGQ 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 589 ASTEKGYSRQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLE 668
Cdd:PTZ00386  245 GKEEKGITRKTGFDISVASEVMAILALATDLADMRQRLGAIVVAKSKSGEPVTAEDLGCAGAMTVLMKDTIEPTLMQTLE 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 669 GTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMHG 748
Cdd:PTZ00386  325 GTPVLVHAGPFGNIAHGNSSIVADQIALKLAGQDGFVLTEAGFGADIGCEKFFNIKCRTSGLKPDAAVLVATVRALKFHG 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 749 GGPSVIPGvplkkeytEENIQLVADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELA-KRAGAFDAVPCYH 827
Cdd:PTZ00386  405 GVEPVVAG--------KENLEAVRKGLSNLQRHIQNIRKFGVPVVVALNKFSTDTDAELELVKELAlQEGGAADVVVTDH 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 828 WSVGGKGSVDLARAVREAANTN-SHFQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAK 906
Cdd:PTZ00386  477 WAKGGAGAVDLAQALIRVTENVpSNFKLLYPLDASLKEKIETICKEIYGAAGVEYLNDADEKLEDFERMGYGKFPVCMAK 556
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2327289797 907 THLSLSHQPDKKGVPRDFVLPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVQGL 974
Cdd:PTZ00386  557 TQYSFSHDPELRGAPTGFTVPIRDVRVNCGAGFVFPLLGDISTMPGLPTRPAFYNIDIDCETGKIVGL 624
MIS1 COG2759
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
356-975 0e+00

Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];


Pssm-ID: 442046  Cd Length: 556  Bit Score: 882.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 356 VPSDIEISRGQTPKAVDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQ 435
Cdd:COG2759     1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 436 ALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENtqtdkal 515
Cdd:COG2759    81 AL-NRLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQGN------- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 516 ynrlvpsvngvrefseiqlarlkklginktdpsalteeemgkfaRLNIDPSTITWQRVLDTNDRFLRKITIGQASTEKGY 595
Cdd:COG2759   153 --------------------------------------------ELNIDPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 596 SRQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVH 675
Cdd:COG2759   189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 676 AGPFANIAHGNSSVLADKIALKLvGEegFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMHGGGPsvip 755
Cdd:COG2759   269 GGPFANIAHGCNSVIATKLALKL-AD--YVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA---- 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 756 gvplKKEYTEENIQLVADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKRAGAfDAVPCYHWSVGGKGS 835
Cdd:COG2759   342 ----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEGA 416
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 836 VDLARAVREAANTN-SHFQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAKTHLSLSHQ 914
Cdd:COG2759   417 EELAEAVVEACEEGpSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSDD 496
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2327289797 915 PDKKGVPRDFVLPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDtETEQVQGLF 975
Cdd:COG2759   497 PKLLGAPTGFTLTVREVRLSAGAGFIVALTGDIMTMPGLPKVPAAERIDID-EDGKITGLF 556
PRK13505 PRK13505
formate--tetrahydrofolate ligase; Provisional
355-975 0e+00

formate--tetrahydrofolate ligase; Provisional


Pssm-ID: 237403  Cd Length: 557  Bit Score: 754.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 355 PVPSDIEISRGQTPKAVDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLV 434
Cdd:PRK13505    1 TMKSDIEIAQEATLKPITEIAAKLGIPEDDLEPYGKYKAKISLDKIKALKDKKDGKLILVTAINPTPAGEGKSTVTVGLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 435 QALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdka 514
Cdd:PRK13505   81 DAL-NKIGKKTVIALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITSANNLLAALIDNHIHQGNE----- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 515 lynrlvpsvngvrefseiqlarlkklginktdpsalteeemgkfarLNIDPSTITWQRVLDTNDRFLRKITIGQASTEKG 594
Cdd:PRK13505  155 ----------------------------------------------LGIDPRRITWKRVLDMNDRALRNIVVGLGGPANG 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 595 YSRQAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFV 674
Cdd:PRK13505  189 VPREDGFDITVASEIMAILCLATDLKDLKERLGRIVVGYTYDGKPVTVKDLKVEGAMALLLKDAIKPNLVQTLEGTPAFV 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 675 HAGPFANIAHGNSSVLADKIALKLvGEegFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMHGGGPsvi 754
Cdd:PRK13505  269 HGGPFANIAHGCNSVLATKTALKL-AD--YVVTEAGFGADLGAEKFLDIKCRKAGLKPDAVVIVATVRALKMHGGVA--- 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 755 pgvplKKEYTEENIQLVADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKRAGAfDAVPCYHWSVGGKG 834
Cdd:PRK13505  343 -----KDDLKEENVEALKKGFANLERHIENIRKFGVPVVVAINKFVTDTDAEIAALKELCEELGV-EVALSEVWAKGGEG 416
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 835 SVDLARAVREAANTN-SHFQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAKTHLSLSH 913
Cdd:PRK13505  417 GVELAEKVVELIEEGeSNFKPLYDDEDSLEEKIEKIATKIYGAKGVEFSPKAKKQLKQIEKNGWDKLPVCMAKTQYSFSD 496
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2327289797 914 QPDKKGVPRDFVLPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDtETEQVQGLF 975
Cdd:PRK13505  497 DPKLLGAPTGFTITVRELRPSAGAGFIVALTGDIMTMPGLPKVPAALNIDVD-EDGNIVGLF 557
PRK13506 PRK13506
formate--tetrahydrofolate ligase; Provisional
358-974 0e+00

formate--tetrahydrofolate ligase; Provisional


Pssm-ID: 237404  Cd Length: 578  Bit Score: 710.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 358 SDIEISRGQTPKAVDVLAKEIGLLAEEIEIYGKSKAKVRLSLLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQAL 437
Cdd:PRK13506    3 SDIEISRQAPLKPIAEIAAKLGLLPDELSPFGHTKAKVSLSVLKRLADKPKGKLVLVTAITPTPLGEGKTVTTIGLTQGL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 438 tAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEntqtdkalyN 517
Cdd:PRK13506   83 -NALGQKVCACIRQPSMGPVFGVKGGAAGGGYAQVVPMEELNLHLTGDIHAVSAAHNLAAAAIDARLFHE---------Q 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 518 RLvpsvnGVREFSEiqlarlkklginKTDpsalteeemgkFARLNIDPSTITWQRVLDTNDRFLRKITIGQASTEKGYSR 597
Cdd:PRK13506  153 RL-----GYDAFEA------------QSG-----------LPALDIDPEQILWKRVVDHNDRALRMITVGLGENGNGPER 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 598 QAQFDIAVASEIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAG 677
Cdd:PRK13506  205 EDGFDITAASELMAILALSRDLKDMRQRIGRLVLAYNLQGQPITAEDLGVAGAMTVIMKDAIEPTLMQTLEGVPCLIHAG 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 678 PFANIAHGNSSVLADKIALKLVgeeGFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMHGGGPSVIPGV 757
Cdd:PRK13506  285 PFANIAHGNSSIIADRIALKLA---DYVVTEGGFGSDMGFEKFCNIKARQSGKAPDCAVLVATLRALKANSGLYDLRPGQ 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 758 PLKKEYTEENIQLVADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYHWSVGGKGSVD 837
Cdd:PRK13506  362 ALPDSINAPDQARLEAGFANLKWHINNVAQYGLPVVVAINRFPTDTDEELEWLKEAVLLTGAFGCEISEAFAQGGEGATA 441
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 838 LARAVREAANTNSHFQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQGFGNLPICMAKTHLSLSHQPDK 917
Cdd:PRK13506  442 LAQAVVRACEQPSQFKLLYPDEMSLEAKLMTLAEVGYGAAGVSLSDKAKQQLAQLTALGYDHLPVCMAKTPLSISHDPAL 521
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2327289797 918 KGVPRDFVLPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVqGL 974
Cdd:PRK13506  522 KGAPTDFEVPIRELRLCAGAGFITALVGNVMTMPGLGLKPGYLNIDIDADGEIV-GL 577
PRK13507 PRK13507
formate--tetrahydrofolate ligase; Provisional
369-975 0e+00

formate--tetrahydrofolate ligase; Provisional


Pssm-ID: 184098  Cd Length: 587  Bit Score: 660.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 369 KAVDVLAKEIGLLAEEIEIYGKSKAKVR-LSLLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALtAHLNVNSFA 447
Cdd:PRK13507   22 KPVEELAEELGLTKEELLPYGHYIAKVDfRKVLDRLKDRPDGKYIDVTAITPTPLGEGKSTTTMGLVQGL-GKRGKKVSG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 448 CLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTQTDKALYNRlvpsvngvr 527
Cdd:PRK13507  101 AIRQPSGGPTMNIKGSAAGGGLSQCIPLTPFSLGLTGDINAIMNAHNLAMVALTARMQHERNYTDEQLARR--------- 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 528 efseiqlarlkklginktdpsalteeemgKFARLNIDPSTITWQRVLDTNDRFLRKITIGQASTEKGYSRQAQFDIAVAS 607
Cdd:PRK13507  172 -----------------------------GLKRLDIDPTRVEMGWIIDFCAQALRNIIIGIGGKTDGYMMQSGFGIAVSS 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 608 EIMAVLALTDSLADMKERLGRMVVASDKDGQPVTAEDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNS 687
Cdd:PRK13507  223 EVMAILSVATDLKDLRERIGKIVVAYDKNGKPVTTADLEVDGAMTAWMVRAINPNLLQTIEGQPVFVHAGPFANIAIGQS 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 688 SVLADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNAVVLVATVRALKMHGGGPSVIPGVPLKKEYTEEN 767
Cdd:PRK13507  303 SIIADRVGLKL---ADYHVTESGFGADIGFEKFWNLKCRLSGLKPDCAVIVATIRALKMHGGGPKVVPGKPLPEEYTKEN 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 768 IQLVADGCCNLQKQIQIAQLFEVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPcYHWSVGGKGSVDLARAVREAAN 847
Cdd:PRK13507  380 VGLVEKGCANLLHHIGTVKKSGINPVVCINAFYTDTHAEIAIVRRLAEQAGARVAVS-RHWEKGGEGALELADAVIDACN 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 848 TNSHFQFLYDVQLPIVEKIRKIAQAVYGAKDIELFPEAQSKIDRYTQQG-FGNLPICMAKTHLSLSHQPDKKGVPRDFVL 926
Cdd:PRK13507  459 EPNDFKFLYPLEMPLRERIETIAREVYGADGVSYTPEAEAKLKRLESDPeTADFGTCMVKTHLSLSHDPALKGVPKGWTL 538
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*....
gi 2327289797 927 PISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVQGLF 975
Cdd:PRK13507  539 PIRDILTYGGAGFVVPVAGDISLMPGTGSDPAFRRIDVDTQTGKVKGLF 587
NAD_bind_m-THF_DH_Cyclohyd_like cd05212
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ...
190-332 7.64e-55

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: 186.56  E-value: 7.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 190 GDAHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSP 269
Cdd:cd05212     1 GPCTPLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2327289797 270 KPEKIPVAWIRPGTTVLNCFHSFMSEKLGCGSHGVHCGGSIaedDVSLLAAALRIQNMVSSGR 332
Cdd:cd05212    81 KPEKVPTEWIKPGATVINCSPTKLSGDDVKESASLYVPMTG---GVGKLTVAMRMQNMVRSVR 140
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
180-335 2.94e-37

Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;


Pssm-ID: 427036  Cd Length: 160  Bit Score: 137.21  E-value: 2.94e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 180 TDVNLGKLVRGdaHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMSSQWKTPQLESKLQ 259
Cdd:pfam02882   1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 260 EADIVILGSPKPEKIPVAWIRPGTTVLNCFHSFMSEKLGCGshGVHcGGSIAE---------DDVSLLAAALRIQNMVSS 330
Cdd:pfam02882  79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVG--DVD-FENVKEkasaitpvpGGVGPMTVAMLLQNTVEA 155

                  ....*
gi 2327289797 331 GRRWL 335
Cdd:pfam02882 156 AKRQL 160
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
94-286 7.32e-36

5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 137.45  E-value: 7.32e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  94 KPVLAVIQAGDDnllqE-----VN--QNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQVPensL---- 162
Cdd:COG0190    32 TPGLAVVLVGDD----PasqvyVRnkHKACEEVGIESELIRLPADTTQEELLALIDELNADPSVHGILVQLP---Lpkhi 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 163 -SSKVLNALKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLGaHG-----PLeaALqcL 236
Cdd:COG0190   105 dEEAVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLERYGIDLAGKHAVVVG-RSnivgkPL--AL--L 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2327289797 237 FQRKD---SMTMSsqwKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVL 286
Cdd:COG0190   178 LLRRNatvTVCHS---RTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVI 227
PRK14190 PRK14190
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
80-287 2.24e-29

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 184560 [Multi-domain]  Cd Length: 284  Bit Score: 118.96  E-value: 2.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  80 KEVLSLlqeKNPAFKPVLAVIQAGDDNLLQ---EVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ 156
Cdd:PRK14190   21 EEVVKL---KEQGIVPGLAVILVGDDPASHsyvRGKKKAAEKVGIYSELYEFPADITEEELLALIDRLNADPRINGILVQ 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 157 --VPENSLSSKVLNALKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQ 234
Cdd:PRK14190   98 lpLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQ--DTFLPCTPHGILELLKEYNIDISGKHVVVVGRSNIVGKPVG 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2327289797 235 CLFQRKD-SMTMSSQwKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14190  176 QLLLNENaTVTYCHS-KTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVID 228
PLN02616 PLN02616
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
68-287 8.78e-27

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 215332 [Multi-domain]  Cd Length: 364  Bit Score: 113.18  E-value: 8.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  68 RDSIVREVIQnSKEVLSLLqeknpafkPVLAVIQAGD--DNLLQEVNQNLA-EEAGLNITHICLPPDSSEDEIIDEILKM 144
Cdd:PLN02616   86 RDEITIEVSR-MKESIGVV--------PGLAVILVGDrkDSATYVRNKKKAcDSVGINSFEVRLPEDSTEQEVLKFISGF 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 145 NEDARVHGLSLQVPENSL--SSKVLNALKPEKDVDGVTDVNLGKLVRGDAHECFVSPVARAVIELLEKSGVNLDGKKVLV 222
Cdd:PLN02616  157 NNDPSVHGILVQLPLPSHmdEQNILNAVSIEKDVDGFHPLNIGRLAMRGREPLFVPCTPKGCIELLHRYNVEIKGKRAVV 236
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2327289797 223 LGAHGPLEAALQCLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PLN02616  237 IGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVID 301
PLN02516 PLN02516
methylenetetrahydrofolate dehydrogenase (NADP+)
95-287 8.85e-26

methylenetetrahydrofolate dehydrogenase (NADP+)


Pssm-ID: 178131 [Multi-domain]  Cd Length: 299  Bit Score: 108.83  E-value: 8.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  95 PVLAVIQAG---DDNLLQEVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQVP--ENSLSSKVLNA 169
Cdd:PLN02516   40 PGLAVVIVGsrkDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISKVHELNANPDVHGILVQLPlpKHINEEKILNE 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 170 LKPEKDVDGVTDVNLGKLVRGDAHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMSSQW 249
Cdd:PLN02516  120 ISLEKDVDGFHPLNIGKLAMKGREPLFLPCTPKGCLELLSRSGIPIKGKKAVVVGRSNIVGLPVSLLLLKADATVTVVHS 199
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2327289797 250 KTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PLN02516  200 RTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVID 237
PLN02897 PLN02897
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
95-287 1.88e-25

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 178485 [Multi-domain]  Cd Length: 345  Bit Score: 108.89  E-value: 1.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  95 PVLAVIQAGDDNLLQEVNQN---LAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQVP--ENSLSSKVLNA 169
Cdd:PLN02897   87 PGLAVVLVGQQRDSQTYVRNkikACEETGIKSLLAELPEDCTEGQILSALRKFNEDTSIHGILVQLPlpQHLDESKILNM 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 170 LKPEKDVDGVTDVNLGKLVRGDAHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMSSQW 249
Cdd:PLN02897  167 VRLEKDVDGFHPLNVGNLAMRGREPLFVSCTPKGCVELLIRSGVEIAGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHA 246
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2327289797 250 KTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PLN02897  247 FTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVID 284
PRK14172 PRK14172
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
94-287 3.37e-25

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 172660 [Multi-domain]  Cd Length: 278  Bit Score: 106.40  E-value: 3.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  94 KPVLAVIQAGDD--NLLQEVNQN-LAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ--VPENSLSSKVLN 168
Cdd:PRK14172   32 IPKIASILVGNDggSIYYMNNQEkVANSLGIDFKKIKLDESISEEDLINEIEELNKDNNVHGIMLQlpLPKHLDEKKITN 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 169 ALKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMSSQ 248
Cdd:PRK14172  112 KIDANKDIDCLTFISVGKFYKGE--KCFLPCTPNSVITLIKSLNIDIEGKEVVVIGRSNIVGKPVAQLLLNENATVTICH 189
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2327289797 249 WKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14172  190 SKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVID 228
PRK14187 PRK14187
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
95-287 5.68e-24

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172675 [Multi-domain]  Cd Length: 294  Bit Score: 103.37  E-value: 5.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  95 PVLAVIQAGDD---NLLQEVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ--VPENSLSSKVLNA 169
Cdd:PRK14187   33 PCLIVILVGDDpasQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKINELNNDDSVHGILVQlpVPNHIDKNLIINT 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 170 LKPEKDVDGVTDVNLGKLVRGDAHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMSSQW 249
Cdd:PRK14187  113 IDPEKDVDGFHNENVGRLFTGQKKNCLIPCTPKGCLYLIKTITRNLSGSDAVVIGRSNIVGKPMACLLLGENCTVTTVHS 192
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2327289797 250 KTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14187  193 ATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVID 230
PRK14167 PRK14167
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
94-287 6.95e-22

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 184549 [Multi-domain]  Cd Length: 297  Bit Score: 97.15  E-value: 6.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  94 KPVLAVIQAGDDNLLQ---EVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ--VPENSLSSKVLN 168
Cdd:PRK14167   31 TPGLATVLMSDDPASEtyvSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTIDELNADEDVHGILVQmpVPDHVDDREVLR 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 169 ALKPEKDVDGVTDVNLGKLVRGDAHecFVSPVARAVIELLEKSGVNLDGKKVLVLGAH---GPLEAALqcLFQRKD---S 242
Cdd:PRK14167  111 RIDPAKDVDGFHPENVGRLVAGDAR--FKPCTPHGIQKLLAAAGVDTEGADVVVVGRSdivGKPMANL--LIQKADggnA 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2327289797 243 MTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14167  187 TVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVID 231
PRK14175 PRK14175
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
71-287 8.15e-22

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184552 [Multi-domain]  Cd Length: 286  Bit Score: 96.91  E-value: 8.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  71 IVREVIQNSKEVLSLLQEKnpAFKPVLAVIQAGDDNLLQE-VN--QNLAEEAGLNITHICLPPDSSEDEIIDEILKMNED 147
Cdd:PRK14175   11 IAKDYRQGLQDQVEALKEK--GFTPKLSVILVGNDGASQSyVRskKKAAEKIGMISEIVHLEETATEEEVLNELNRLNND 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 148 ARVHGLSLQVPENSLSS--KVLNALKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLG- 224
Cdd:PRK14175   89 DSVSGILVQVPLPKQVSeqKILEAINPEKDVDGFHPINIGKLYIDE--QTFVPCTPLGIMEILKHADIDLEGKNAVVIGr 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2327289797 225 AHGPLEAALQCLFQRKDSMTMSSQwKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14175  167 SHIVGQPVSKLLLQKNASVTILHS-RSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIID 228
PRK14186 PRK14186
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
95-287 2.07e-21

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237636 [Multi-domain]  Cd Length: 297  Bit Score: 95.90  E-value: 2.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  95 PVLAVIQAGDDNLlQEVNQNLAEEA----GLN--ITHicLPPDSSEDEIIDEILKMNEDARVHGLSLQ--VPENSLSSKV 166
Cdd:PRK14186   33 PGLAVLRVGDDPA-SAVYVRNKEKAcarvGIAsfGKH--LPADTSQAEVEALIAQLNQDERVDGILLQlpLPKHLDEVPL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 167 LNALKPEKDVDGVTDVNLGKLVRGDAHECFVSPVarAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMS 246
Cdd:PRK14186  110 LHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPA--GVMRLLRSQQIDIAGKKAVVVGRSILVGKPLALMLLAANATVTI 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2327289797 247 SQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14186  188 AHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVD 228
PRK10792 PRK10792
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
94-286 3.21e-21

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 236760 [Multi-domain]  Cd Length: 285  Bit Score: 94.98  E-value: 3.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  94 KPVLAVIQAGDDNLLQ-EVN--QNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ--VPENSLSSKVLN 168
Cdd:PRK10792   33 APGLAVVLVGSDPASQvYVAskRKACEEVGFVSRSYDLPETTSEAELLALIDELNADPTIDGILVQlpLPAHIDNVKVLE 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 169 ALKPEKDVDGVTDVNLGKLvrgdaheCFVSPVARA-----VIELLEKSGVNLDGKKVLVLGAHG----PLeaALQCLFQR 239
Cdd:PRK10792  113 RIHPDKDVDGFHPYNVGRL-------AQRIPLLRPctprgIMTLLERYGIDTYGLNAVVVGASNivgrPM--SLELLLAG 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2327289797 240 kdSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVL 286
Cdd:PRK10792  184 --CTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVI 228
PRK14170 PRK14170
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
79-287 2.50e-20

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172658 [Multi-domain]  Cd Length: 284  Bit Score: 92.45  E-value: 2.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  79 SKEVLSLLQEKNpafKPVLAVIQAGDDNLLQEV---NQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSL 155
Cdd:PRK14170   19 TREVAELVKEGK---KPGLAVVLVGDNQASRTYvrnKQKRTEEAGMKSVLIELPENVTEEKLLSVVEELNEDKTIHGILV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 156 QVP--ENSLSSKVLNALKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAAL 233
Cdd:PRK14170   96 QLPlpEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGK--DSFVPCTPAGIIELIKSTGTQIEGKRAVVIGRSNIVGKPV 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2327289797 234 QCLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14170  174 AQLLLNENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVID 227
PRK14192 PRK14192
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
95-290 4.27e-20

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184561 [Multi-domain]  Cd Length: 283  Bit Score: 91.45  E-value: 4.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  95 PVLAVIQAGDD---NLLQEVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ--VPENSLSSKVLNA 169
Cdd:PRK14192   34 PILATILVGDDpasATYVRMKGNACRRVGMDSLKVELPQETTTEQLLAKIEELNANPDVHGILLQhpVPAQIDERACFDA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 170 LKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAAL-QCLFQRKDSMTMSSQ 248
Cdd:PRK14192  114 ISLAKDVDGVTCLGFGRMAMGE--AAYGSATPAGIMRLLKAYNIELAGKHAVVVGRSAILGKPMaMMLLNANATVTICHS 191
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2327289797 249 wKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLNC-FH 290
Cdd:PRK14192  192 -RTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAgFH 233
PRK14174 PRK14174
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
95-287 5.34e-20

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 172662 [Multi-domain]  Cd Length: 295  Bit Score: 91.42  E-value: 5.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  95 PVLAVIQAGDDNLLQEVNQNLAE---EAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ--VPENSLSSKVLNA 169
Cdd:PRK14174   32 PGLTVIIVGEDPASQVYVRNKAKsckEIGMNSTVIELPADTTEEHLLKKIEDLNNDPDVHGILVQqpLPKQIDEFAVTLA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 170 LKPEKDVDGVTDVNLGKLVRGDAHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHG----PL-EAALQCLFQRKDSMT 244
Cdd:PRK14174  112 IDPAKDVDGFHPENLGRLVMGHLDKCFVSCTPYGILELLGRYNIETKGKHCVVVGRSNivgkPMaNLMLQKLKESNCTVT 191
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2327289797 245 MSSQwKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14174  192 ICHS-ATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVID 233
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
172-288 4.47e-19

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: 85.30  E-value: 4.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 172 PEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHG----PLeAALqcLFQRKDSMTMSS 247
Cdd:cd01080     1 PEKDVDGLHPVNLGRLALGR--PGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNivgkPL-AAL--LLNRNATVTVCH 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2327289797 248 QwKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLNC 288
Cdd:cd01080    76 S-KTKNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDV 115
PRK14183 PRK14183
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
80-287 5.10e-19

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 184555 [Multi-domain]  Cd Length: 281  Bit Score: 88.35  E-value: 5.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  80 KEVLSLLQEKNpaFKPVLAVIQAGDDNLLQ---EVNQNLAEEAGL-NITHIcLPPDSSEDEIIDEILKMNEDARVHGLSL 155
Cdd:PRK14183   19 KEVDELKLVKN--IVPGLAVILVGDDPASHtyvKMKAKACDRVGIySITHE-MPSTISQKEILETIAMMNNNPNIDGILV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 156 Q--VPENSLSSKVLNALKPEKDVDGVTDVNLGKLVRGdaHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAAL 233
Cdd:PRK14183   96 QlpLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTG--LDGFVPCTPLGVMELLEEYEIDVKGKDVCVVGASNIVGKPM 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2327289797 234 QCLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14183  174 AALLLNANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVID 227
PRK14191 PRK14191
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
95-287 2.01e-18

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172679 [Multi-domain]  Cd Length: 285  Bit Score: 86.74  E-value: 2.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  95 PVLAVIQAGDDNLLQE-VN--QNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQVP--ENSLSSKVLNA 169
Cdd:PRK14191   32 PKLAVILVGKDPASQTyVNmkIKACERVGMDSDLHTLQENTTEAELLSLIKDLNTDQNIDGILVQLPlpRHIDTKMVLEA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 170 LKPEKDVDGVTDVNLGKLVRGdaHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTMSSQW 249
Cdd:PRK14191  112 IDPNKDVDGFHPLNIGKLCSQ--LDGFVPATPMGVMRLLKHYHIEIKGKDVVIIGASNIVGKPLAMLMLNAGASVSVCHI 189
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2327289797 250 KTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14191  190 LTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVD 227
PRK14179 PRK14179
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
80-287 2.03e-18

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 237634 [Multi-domain]  Cd Length: 284  Bit Score: 86.73  E-value: 2.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  80 KEVLSLLQEKnpAFKPVLAVIQAGDDNLLQEVNQN---LAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ 156
Cdd:PRK14179   20 EKVAKLKEEK--GIVPGLVVILVGDNPASQVYVRNkerSALAAGFKSEVVRLPETISQEELLDLIERYNQDPTWHGILVQ 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 157 --VPENSLSSKVLNALKPEKDVDGVTDVNLGKLVRGdaHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQ 234
Cdd:PRK14179   98 lpLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSG--RPVMIPCTPAGIMEMFREYNVELEGKHAVVIGRSNIVGKPMA 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2327289797 235 CLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14179  176 QLLLDKNATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVID 228
PRK14177 PRK14177
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
72-287 2.18e-18

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172665 [Multi-domain]  Cd Length: 284  Bit Score: 86.57  E-value: 2.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  72 VREVIQNskEVLSLLQEKNPAFK--PVLAVIQAGDdNLLQEVNQNL----AEEAGLNITHICLPPDSSEDEIIDEILKMN 145
Cdd:PRK14177   11 LSEKIRN--EIRETIEERKTKNKriPKLATILVGN-NPASETYVSMkvkaCHKVGMGSEMIRLKEQTTTEELLGVIDKLN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 146 EDARVHGLSLQ--VPENSLSSKVLNALKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVL 223
Cdd:PRK14177   88 LDPNVDGILLQhpVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGV--ETYLPCTPYGMVLLLKEYGIDVTGKNAVVV 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2327289797 224 GAHGPLEAALQCLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14177  166 GRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLD 229
PRK14193 PRK14193
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
74-287 3.07e-18

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 237637 [Multi-domain]  Cd Length: 284  Bit Score: 86.22  E-value: 3.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  74 EVIQNSKEVLSLLQEKnpAFKPVLAVIQAGDDNLLQE-VNQNLAEEAGLNITHIC--LPPDSSEDEIIDEILKMNEDARV 150
Cdd:PRK14193   14 EIKADLAERVAALKEK--GITPGLGTVLVGDDPGSQAyVRGKHRDCAEVGITSIRrdLPADATQEELNAVIDELNADPAC 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 151 HGLSLQVP------ENslssKVLNALKPEKDVDGVTDVNLGKLVRGDAHECFVSPvaRAVIELLEKSGVNLDGKKVLVLG 224
Cdd:PRK14193   92 TGYIVQLPlpkhldEN----AVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTP--RGIVHLLRRYDVELAGAHVVVIG 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2327289797 225 AHGPLEAALQCLFQRK--DSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14193  166 RGVTVGRPIGLLLTRRseNATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLD 230
PRK14168 PRK14168
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
128-287 5.89e-18

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237633 [Multi-domain]  Cd Length: 297  Bit Score: 85.70  E-value: 5.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 128 LPPDSSEDEIIDEILKMNEDARVHGLSLQ--VPENSLSSKVLNALKPEKDVDGVTDVNLGKLVRGDAHECFVSPVARAVI 205
Cdd:PRK14168   70 QSVDITEEELLALIDKYNNDDSIHGILVQlpLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIGGDEVKFLPCTPAGIQ 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 206 ELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRK----DSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRP 281
Cdd:PRK14168  150 EMLVRSGVETSGAEVVVVGRSNIVGKPIANMMTQKgpgaNATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKP 229

                  ....*.
gi 2327289797 282 GTTVLN 287
Cdd:PRK14168  230 GATVID 235
THF_DHG_CYH pfam00763
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
87-177 6.99e-18

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;


Pssm-ID: 459930 [Multi-domain]  Cd Length: 115  Bit Score: 80.14  E-value: 6.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  87 QEKNPAFKPVLAVIQAGDD--------NLlqevnQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ-- 156
Cdd:pfam00763  20 ALKAGGRKPGLAVILVGDDpasqvyvrNK-----KKACEEVGIESELIRLPEDTTEEELLALIDKLNADPSVHGILVQlp 94
                          90       100
                  ....*....|....*....|.
gi 2327289797 157 VPENSLSSKVLNALKPEKDVD 177
Cdd:pfam00763  95 LPKHIDEEKVLEAIDPEKDVD 115
PRK14189 PRK14189
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
94-287 1.10e-17

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 184559 [Multi-domain]  Cd Length: 285  Bit Score: 84.35  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  94 KPVLAVIQAGDDNLLQEVNQNLA---EEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ--VPENSLSSKVLN 168
Cdd:PRK14189   32 QPGLAVILVGDNPASQVYVRNKVkacEDNGFHSLKDRYPADLSEAELLARIDELNRDPKIHGILVQlpLPKHIDSHKVIE 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 169 ALKPEKDVDGVTDVNLGKLVRGdaHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAH---GPLEAALqcLFQRKDSMTM 245
Cdd:PRK14189  112 AIAPEKDVDGFHVANAGALMTG--QPLFRPCTPYGVMKMLESIGIPLRGAHAVVIGRSnivGKPMAML--LLQAGATVTI 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2327289797 246 SSQwKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14189  188 CHS-KTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVID 228
PRK14180 PRK14180
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
92-287 1.77e-17

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 172668 [Multi-domain]  Cd Length: 282  Bit Score: 83.93  E-value: 1.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  92 AFKPVLAVIQAGDDNLLQ---EVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQVP--ENSLSSKV 166
Cdd:PRK14180   29 AITPKLVAIIVGNDPASKtyvASKEKACAQVGIDSQVITLPEHTTESELLELIDQLNNDSSVHAILVQLPlpAHINKNNV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 167 LNALKPEKDVDGVTDVNLGKLVRGDaHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPL-EAALQCLFQRKDSMTM 245
Cdd:PRK14180  109 IYSIKPEKDVDGFHPTNVGRLQLRD-KKCLESCTPKGIMTMLREYGIKTEGAYAVVVGASNVVgKPVSQLLLNAKATVTT 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2327289797 246 SSQWkTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14180  188 CHRF-TTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVID 228
PRK14184 PRK14184
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
80-287 2.47e-17

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 237635 [Multi-domain]  Cd Length: 286  Bit Score: 83.67  E-value: 2.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  80 KEVLSLLQEKNPAfkPVLAVIQAGDDNLLQEVNQN---LAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQ 156
Cdd:PRK14184   19 TEVAALTARHGRA--PGLAVILVGEDPASQVYVRNkerACEDAGIVSEAFRLPADTTQEELEDLIAELNARPDIDGILLQ 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 157 VP--ENSLSSKVLNALKPEKDVDGVTDVNLGKLVRGdaHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHG----PLE 230
Cdd:PRK14184   97 LPlpKGLDSQRCLELIDPAKDVDGFHPENMGRLALG--LPGFRPCTPAGVMTLLERYGLSPAGKKAVVVGRSNivgkPLA 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2327289797 231 AALQCLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14184  175 LMLGAPGKFANATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVD 231
PRK14176 PRK14176
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
88-287 2.86e-17

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 184553 [Multi-domain]  Cd Length: 287  Bit Score: 83.32  E-value: 2.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  88 EKNPAFKPVLAVIQAGDD---NLLQEVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQVP--ENSL 162
Cdd:PRK14176   32 KSNRGITPGLATILVGDDpasKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELIDSLNKRKDVHGILLQLPlpKHLD 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 163 SSKVLNALKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDS 242
Cdd:PRK14176  112 PQEAMEAIDPAKDADGFHPYNMGKLMIGD--EGLVPCTPHGVIRALEEYGVDIEGKNAVIVGHSNVVGKPMAAMLLNRNA 189
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2327289797 243 MTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14176  190 TVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFD 234
PRK14194 PRK14194
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
89-287 4.05e-17

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172682 [Multi-domain]  Cd Length: 301  Bit Score: 83.36  E-value: 4.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  89 KNPAFKPVLAVIQAGDDNLLQEVNQN---LAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQVPENSL--S 163
Cdd:PRK14194   28 KAAGIEPALAVILVGNDPASQVYVRNkilRAEEAGIRSLEHRLPADTSQARLLALIAELNADPSVNGILLQLPLPAHidE 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 164 SKVLNALKPEKDVDGVTDVNLGKLVRGDAHECFVSPvaRAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSM 243
Cdd:PRK14194  108 ARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTP--SGCLRLLEDTCGDLTGKHAVVIGRSNIVGKPMAALLLQAHCS 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2327289797 244 TMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14194  186 VTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVID 229
PRK14188 PRK14188
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
94-286 2.76e-16

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184558 [Multi-domain]  Cd Length: 296  Bit Score: 80.77  E-value: 2.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  94 KPVLAVIQAGDDNLLQEVNQN---LAEEAGLN-ITHIcLPPDSSEDEIIDEILKMNEDARVHGLSLQ--VPENSLSSKVL 167
Cdd:PRK14188   32 TPGLAVVLVGEDPASQVYVRSkgkQTKEAGMAsFEHK-LPADTSQAELLALIARLNADPAIHGILVQlpLPKHLDSEAVI 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 168 NALKPEKDVDGVTDVNLGKLVRGDahECFVSPVARAVIELLEKSGVNLDGKKVLVLGAH---GPLEAALqcLFQRKDSMT 244
Cdd:PRK14188  111 QAIDPEKDVDGLHVVNAGRLATGE--TALVPCTPLGCMMLLRRVHGDLSGLNAVVIGRSnlvGKPMAQL--LLAANATVT 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2327289797 245 MSSQwKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVL 286
Cdd:PRK14188  187 IAHS-RTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVI 227
PRK14185 PRK14185
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
94-287 8.14e-16

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184556 [Multi-domain]  Cd Length: 293  Bit Score: 79.10  E-value: 8.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  94 KPVLAVIQAGDDNLLQEVNQN---LAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQVP--ENSLSSKVLN 168
Cdd:PRK14185   31 RPHLAAILVGHDGGSETYVANkvkACEECGFKSSLIRYESDVTEEELLAKVRELNQDDDVDGFIVQLPlpKHISEQKVIE 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 169 ALKPEKDVDGVTDVNLGKLVRGdaHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRK----DSMT 244
Cdd:PRK14185  111 AIDYRKDVDGFHPINVGRMSIG--LPCFVSATPNGILELLKRYHIETSGKKCVVLGRSNIVGKPMAQLMMQKaypgDCTV 188
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2327289797 245 MSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14185  189 TVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVID 231
PRK14171 PRK14171
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
70-287 1.38e-15

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172659 [Multi-domain]  Cd Length: 288  Bit Score: 78.46  E-value: 1.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  70 SIVREVIQNSKEVLSLLQEKNPAfKPVLAVIQAGDD--NLLQEVNQ-NLAEEAGLNITHICLPPDSSEDEIIDEILKMNE 146
Cdd:PRK14171    9 ALANEILADLKLEIQELKSQTNA-SPKLAIVLVGDNpaSIIYVKNKiKNAHKIGIDTLLVNLSTTIHTNDLISKINELNL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 147 DARVHGLSLQVP-ENSL-SSKVLNALKPEKDVDGVTDVNLGKLVRGdAHECFVSPVARAVIELLEKSGVNLDGKKVLVLG 224
Cdd:PRK14171   88 DNEISGIIVQLPlPSSIdKNKILSAVSPSKDIDGFHPLNVGYLHSG-ISQGFIPCTALGCLAVIKKYEPNLTGKNVVIIG 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2327289797 225 AHGPLEAALQCLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14171  167 RSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVID 229
PRK14178 PRK14178
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
79-287 1.51e-15

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172666 [Multi-domain]  Cd Length: 279  Bit Score: 77.96  E-value: 1.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  79 SKEVLSLLQEK--NPAFKPVLAVIQAGDD---NLLQEVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGL 153
Cdd:PRK14178    9 SEKRLELLKEEiiESGLYPRLATVIVGDDpasQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIRRLNEDPDINGI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 154 SLQVP--ENSLSSKVLNALKPEKDVDGVTDVNLGKLVRGDAHECFVSPvaRAVIELLEKSGVNLDGKKVLVLGAHGPLEA 231
Cdd:PRK14178   89 LVQLPlpKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTP--NGIMTLLHEYKISIAGKRAVVVGRSIDVGR 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2327289797 232 ALQCLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14178  167 PMAALLLNADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVID 222
PRK14182 PRK14182
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
94-287 6.75e-15

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 172670 [Multi-domain]  Cd Length: 282  Bit Score: 76.21  E-value: 6.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  94 KPVLAVIQAGDD---NLLQEVNQNLAEEAGLNITHICLPPDSSEDEIIDEILKMNEDARVHGLSLQVP--ENSLSSKVLN 168
Cdd:PRK14182   30 QTGLTVVRVGDDpasAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIARLNADPAVHGILVQLPlpKHVDERAVLD 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 169 ALKPEKDVDGVTDVNLGKL---VRGDAHECfvSPVAraVIELLEKSGVNLDGKKVLVLGAHGPLEAALQCLFQRKDSMTM 245
Cdd:PRK14182  110 AISPAKDADGFHPFNVGALsigIAGVPRPC--TPAG--VMRMLDEARVDPKGKRALVVGRSNIVGKPMAMMLLERHATVT 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2327289797 246 SSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14182  186 IAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVID 227
PRK14166 PRK14166
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
79-287 6.38e-14

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 172654 [Multi-domain]  Cd Length: 282  Bit Score: 73.14  E-value: 6.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  79 SKEVLSLLQEKNPAFK-----PVLAVIQAGDDNLLQEVNQNLA---EEAGLNITHICLPPDSSEDEIIDEILKMNEDARV 150
Cdd:PRK14166   10 SAKIKEELKEKNQFLKskgieSCLAVILVGDNPASQTYVKSKAkacEECGIKSLVYHLNENTTQNELLALINTLNHDDSV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 151 HGLSLQVPENSLSSK--VLNALKPEKDVDGVTDVNLGKLVRGdAHECFVSPVARAVIELLEKSGVNLDGKKVLVLGAHGP 228
Cdd:PRK14166   90 HGILVQLPLPDHICKdlILESIISSKDVDGFHPINVGYLNLG-LESGFLPCTPLGVMKLLKAYEIDLEGKDAVIIGASNI 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2327289797 229 LEAALQCLFQRKDSMTMSSQWKTPQLESKLQEADIVILGSPKPEKIPVAWIRPGTTVLN 287
Cdd:PRK14166  169 VGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVD 227
PRK14181 PRK14181
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
66-269 6.54e-13

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172669 [Multi-domain]  Cd Length: 287  Bit Score: 70.28  E-value: 6.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797  66 PARDSIVREVIQNSKevlsllqekNPAFKPVLAVIQAGDDNLlQEVNQNLAEEAGLNITHIC----LPPDSSEDEIIDEI 141
Cdd:PRK14181    7 PAAEHILATIKENIS---------ASSTAPGLAVVLIGNDPA-SEVYVGMKVKKATDLGMVSkahrLPSDATLSDILKLI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 142 LKMNEDARVHGLSLQVP--ENSLSSKVLNALKPEKDVDGVTDVNLGKLVRGDAhECFVSPVARAVIELLEKSGVNLDGKK 219
Cdd:PRK14181   77 HRLNNDPNIHGILVQLPlpKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGET-DGFIPCTPAGIIELLKYYEIPLHGRH 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2327289797 220 VLVLGAHGPLEAALQCLFQRKDSMTMSS----QWKTPQLESKLQEADIVI--LGSP 269
Cdd:PRK14181  156 VAIVGRSNIVGKPLAALLMQKHPDTNATvtllHSQSENLTEILKTADIIIaaIGVP 211
NAD_bind_m-THF_DH cd01079
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ...
172-287 4.40e-03

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: 39.33  E-value: 4.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327289797 172 PEKDVDGVTDVNLGKLVrgdAHECFVSPVAR----------AVIELLEKSGV---------NLDGKKVLVLGAHG----P 228
Cdd:cd01079     1 PHKDVEGLSHKYIFNLY---HNIRFLDPENRkksilpctplAIVKILEFLGIynkilpygnRLYGKTITIINRSEvvgrP 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2327289797 229 LEAAL---------------QClFQRKDSMTMSSQW---KTPQLESKLQEADIVILGSPKPE-KIPVAWIRPGTTVLN 287
Cdd:cd01079    78 LAALLandgarvysvdingiQV-FTRGESIRHEKHHvtdEEAMTLDCLSQSDVVITGVPSPNyKVPTELLKDGAICIN 154
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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