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Conserved domains on  [gi|1034649741|ref|XP_016866191|]
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monofunctional C1-tetrahydrofolate synthase, mitochondrial isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02759 PLN02759
Formate--tetrahydrofolate ligase
353-979 0e+00

Formate--tetrahydrofolate ligase


:

Pssm-ID: 178359  Cd Length: 637  Bit Score: 1028.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 353 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKST 432
Cdd:PLN02759    9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 433 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 512
Cdd:PLN02759   89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 513 TQTDKALYNRLVPL-VNGVREFSEIQLARLKKLGINKTDPSTLTEEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIG 591
Cdd:PLN02759  169 TQSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVG 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 592 QGNTEKGHYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTL 671
Cdd:PLN02759  249 QGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTL 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 672 EGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMH 751
Cdd:PLN02759  329 EGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMH 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 752 GGGPSVTAGVPLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYH 831
Cdd:PLN02759  409 GGGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTH 488
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 832 WSVGGKGSVDLARAVREAASKRSR-FQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAK 910
Cdd:PLN02759  489 HAHGGKGAVDLGEAVQKACEGNSQpFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAK 568
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034649741 911 THLSLSHQPDKKGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVKGLF 979
Cdd:PLN02759  569 TQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTETGKVLGLS 637
NAD_bind_m-THF_DH_Cyclohyd_like cd05212
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ...
193-336 4.24e-65

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: 215.45  E-value: 4.24e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 193 GDAHECFVSPVAKAVIELLEKSvGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGS 272
Cdd:cd05212     1 GPCTPLFVSPVAKAVKELLNKE-GVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGS 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034649741 273 PKPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSPRIHFGGLIeedDVILLAAALRIQNMVSSGR 336
Cdd:cd05212    80 PKPEKVPTEWIKPGATVINCSPTKLSGDDVKESASLYVPMTG---GVGKLTVAMRMQNMVRSVR 140
PLN02897 super family cl31946
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
52-291 5.32e-24

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


The actual alignment was detected with superfamily member PLN02897:

Pssm-ID: 178485 [Multi-domain]  Cd Length: 345  Bit Score: 104.66  E-value: 5.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  52 PQDGQARSSCSPGGRTPAARDSIVREVIQNSKEVLSLLQEKNPAFK------PVLAIIQAGDDNLMQEINQN---LAEEA 122
Cdd:PLN02897   35 PENWIPYSDPPPPVSFETEQKTVVIDGNVIAEEIRTKIASEVRKMKkavgkvPGLAVVLVGQQRDSQTYVRNkikACEET 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 123 GLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFV 200
Cdd:PLN02897  115 GIKSLLAELPEDCTEGQILSALRKFNEDTSIHGILVQLPlpQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREPLFV 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 201 SPVAKAVIELLEKSvGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPL 280
Cdd:PLN02897  195 SCTPKGCVELLIRS-GVEIAGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRG 273
                         250
                  ....*....|.
gi 1034649741 281 TWIQPGTTVLN 291
Cdd:PLN02897  274 SWLKPGAVVID 284
 
Name Accession Description Interval E-value
PLN02759 PLN02759
Formate--tetrahydrofolate ligase
353-979 0e+00

Formate--tetrahydrofolate ligase


Pssm-ID: 178359  Cd Length: 637  Bit Score: 1028.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 353 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKST 432
Cdd:PLN02759    9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 433 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 512
Cdd:PLN02759   89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 513 TQTDKALYNRLVPL-VNGVREFSEIQLARLKKLGINKTDPSTLTEEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIG 591
Cdd:PLN02759  169 TQSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVG 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 592 QGNTEKGHYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTL 671
Cdd:PLN02759  249 QGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTL 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 672 EGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMH 751
Cdd:PLN02759  329 EGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMH 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 752 GGGPSVTAGVPLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYH 831
Cdd:PLN02759  409 GGGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTH 488
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 832 WSVGGKGSVDLARAVREAASKRSR-FQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAK 910
Cdd:PLN02759  489 HAHGGKGAVDLGEAVQKACEGNSQpFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAK 568
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034649741 911 THLSLSHQPDKKGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVKGLF 979
Cdd:PLN02759  569 TQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTETGKVLGLS 637
FTHFS pfam01268
Formate--tetrahydrofolate ligase;
361-979 0e+00

Formate--tetrahydrofolate ligase;


Pssm-ID: 460143  Cd Length: 555  Bit Score: 985.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 361 PSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQA 440
Cdd:pfam01268   1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 441 LtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkaly 520
Cdd:pfam01268  81 L-NRLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 521 nrlvplvngvrefseiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHY 600
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 601 RQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHA 680
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 681 GPFANIAHGNSSVLADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGgpsvtag 760
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGG------- 338
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 761 vPLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKrAGAFDAVPCYHWSVGGKGSV 840
Cdd:pfam01268 339 -VGKDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRELCE-AGGVDAALSEHWAKGGEGAI 416
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 841 DLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQP 919
Cdd:pfam01268 417 ELAEAVVEACeEEPSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 920 DKKGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTEtEQVKGLF 979
Cdd:pfam01268 497 KLKGAPTGFTLPVRDVRLSAGAGFIVALTGDIMTMPGLPKRPAAENIDVDED-GKITGLF 555
FTHFS cd00477
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ...
375-978 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: 935.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 375 VDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALTAHLNvNSFACLR 454
Cdd:cd00477     1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 455 QPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkalynrlvplvngvrefs 534
Cdd:cd00477    80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 535 eiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYRQAQFDIAVASEIM 614
Cdd:cd00477   139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 615 AVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSVL 694
Cdd:cd00477   189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 695 ADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGvplkkeytEENIQL 774
Cdd:cd00477   269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 775 VADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVpCYHWSVGGKGSVDLARAVREAASK-R 853
Cdd:cd00477   338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKpK 416
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 854 SRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQPDKKGVPRDFILPIS 933
Cdd:cd00477   417 SNFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 1034649741 934 DVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDtETEQVKGL 978
Cdd:cd00477   497 DVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDID-DTGKIEGL 540
MIS1 COG2759
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
360-979 0e+00

Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];


Pssm-ID: 442046  Cd Length: 556  Bit Score: 877.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 360 VPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQ 439
Cdd:COG2759     1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 440 ALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENtqtdkal 519
Cdd:COG2759    81 AL-NRLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQGN------- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 520 ynrlvplvngvrefseiqlarlkklginktdpstlteeevskfaRLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGH 599
Cdd:COG2759   153 --------------------------------------------ELNIDPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 600 YRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVH 679
Cdd:COG2759   189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 680 AGPFANIAHGNSSVLADKIALKLvGEegFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPsvta 759
Cdd:COG2759   269 GGPFANIAHGCNSVIATKLALKL-AD--YVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA---- 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 760 gvplKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAfDAVPCYHWSVGGKGS 839
Cdd:COG2759   342 ----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEGA 416
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 840 VDLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQ 918
Cdd:COG2759   417 EELAEAVVEACeEGPSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSDD 496
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034649741 919 PDKKGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDtETEQVKGLF 979
Cdd:COG2759   497 PKLLGAPTGFTLTVREVRLSAGAGFIVALTGDIMTMPGLPKVPAAERIDID-EDGKITGLF 556
NAD_bind_m-THF_DH_Cyclohyd_like cd05212
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ...
193-336 4.24e-65

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: 215.45  E-value: 4.24e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 193 GDAHECFVSPVAKAVIELLEKSvGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGS 272
Cdd:cd05212     1 GPCTPLFVSPVAKAVKELLNKE-GVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGS 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034649741 273 PKPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSPRIHFGGLIeedDVILLAAALRIQNMVSSGR 336
Cdd:cd05212    80 PKPEKVPTEWIKPGATVINCSPTKLSGDDVKESASLYVPMTG---GVGKLTVAMRMQNMVRSVR 140
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
183-339 9.37e-34

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


Pssm-ID: 427036  Cd Length: 160  Bit Score: 127.20  E-value: 9.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 183 TDINLGKLVRGdaHECFVSPVAKAVIELLEKSvGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKL 262
Cdd:pfam02882   1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRY-GIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEIT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 263 HEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSprIHF--------------GGlieeddVILLAAALRI 328
Cdd:pfam02882  78 READIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGD--VDFenvkekasaitpvpGG------VGPMTVAMLL 149
                         170
                  ....*....|.
gi 1034649741 329 QNMVSSGRRWL 339
Cdd:pfam02882 150 QNTVEAAKRQL 160
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
97-290 9.32e-32

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


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 125.51  E-value: 9.32e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  97 KPVLAIIQAGDD--------NLmqeinQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ------ISE 162
Cdd:COG0190    32 TPGLAVVLVGDDpasqvyvrNK-----HKACEEVGIESELIRLPADTTQEELLALIDELNADPSVHGILVQlplpkhIDE 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 163 NlfsnKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEkSVGVNLDGKKILVVGAhgSLE-----AAL 237
Cdd:COG0190   107 E----AVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLE-RYGIDLAGKHAVVVGR--SNIvgkplALL 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034649741 238 qcLFQRKGSMTM--SiqwKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVL 290
Cdd:COG0190   178 --LLRRNATVTVchS---RTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVI 227
PRK14187 PRK14187
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
98-291 3.87e-24

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172675 [Multi-domain]  Cd Length: 294  Bit Score: 103.75  E-value: 3.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  98 PVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNA 172
Cdd:PRK14187   33 PCLIVILVGDDPASQlyvRNKQRKAEMLGLRSETILLPSTISESSLIEKINELNNDDSVHGILVQlpVPNHIDKNLIINT 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 173 LKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLeKSVGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQ 252
Cdd:PRK14187  113 IDPEKDVDGFHNENVGRLFTGQKKNCLIPCTPKGCLYLI-KTITRNLSGSDAVVIGRSNIVGKPMACLLLGENCTVTTVH 191
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034649741 253 WKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 291
Cdd:PRK14187  192 SATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVID 230
PLN02897 PLN02897
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
52-291 5.32e-24

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 178485 [Multi-domain]  Cd Length: 345  Bit Score: 104.66  E-value: 5.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  52 PQDGQARSSCSPGGRTPAARDSIVREVIQNSKEVLSLLQEKNPAFK------PVLAIIQAGDDNLMQEINQN---LAEEA 122
Cdd:PLN02897   35 PENWIPYSDPPPPVSFETEQKTVVIDGNVIAEEIRTKIASEVRKMKkavgkvPGLAVVLVGQQRDSQTYVRNkikACEET 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 123 GLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFV 200
Cdd:PLN02897  115 GIKSLLAELPEDCTEGQILSALRKFNEDTSIHGILVQLPlpQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREPLFV 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 201 SPVAKAVIELLEKSvGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPL 280
Cdd:PLN02897  195 SCTPKGCVELLIRS-GVEIAGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRG 273
                         250
                  ....*....|.
gi 1034649741 281 TWIQPGTTVLN 291
Cdd:PLN02897  274 SWLKPGAVVID 284
THF_DHG_CYH pfam00763
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
90-180 1.53e-17

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;


Pssm-ID: 459930 [Multi-domain]  Cd Length: 115  Bit Score: 79.37  E-value: 1.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  90 QEKNPAFKPVLAIIQAGDD---NLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENL 164
Cdd:pfam00763  20 ALKAGGRKPGLAVILVGDDpasQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKLNADPSVHGILVQlpLPKHI 99
                          90
                  ....*....|....*.
gi 1034649741 165 FSNKVLNALKPEKDVD 180
Cdd:pfam00763 100 DEEKVLEAIDPEKDVD 115
 
Name Accession Description Interval E-value
PLN02759 PLN02759
Formate--tetrahydrofolate ligase
353-979 0e+00

Formate--tetrahydrofolate ligase


Pssm-ID: 178359  Cd Length: 637  Bit Score: 1028.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 353 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKST 432
Cdd:PLN02759    9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 433 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 512
Cdd:PLN02759   89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 513 TQTDKALYNRLVPL-VNGVREFSEIQLARLKKLGINKTDPSTLTEEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIG 591
Cdd:PLN02759  169 TQSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVG 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 592 QGNTEKGHYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTL 671
Cdd:PLN02759  249 QGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTL 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 672 EGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMH 751
Cdd:PLN02759  329 EGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMH 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 752 GGGPSVTAGVPLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYH 831
Cdd:PLN02759  409 GGGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTH 488
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 832 WSVGGKGSVDLARAVREAASKRSR-FQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAK 910
Cdd:PLN02759  489 HAHGGKGAVDLGEAVQKACEGNSQpFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAK 568
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034649741 911 THLSLSHQPDKKGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVKGLF 979
Cdd:PLN02759  569 TQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTETGKVLGLS 637
FTHFS pfam01268
Formate--tetrahydrofolate ligase;
361-979 0e+00

Formate--tetrahydrofolate ligase;


Pssm-ID: 460143  Cd Length: 555  Bit Score: 985.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 361 PSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQA 440
Cdd:pfam01268   1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 441 LtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkaly 520
Cdd:pfam01268  81 L-NRLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 521 nrlvplvngvrefseiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHY 600
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 601 RQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHA 680
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 681 GPFANIAHGNSSVLADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGgpsvtag 760
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGG------- 338
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 761 vPLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKrAGAFDAVPCYHWSVGGKGSV 840
Cdd:pfam01268 339 -VGKDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRELCE-AGGVDAALSEHWAKGGEGAI 416
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 841 DLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQP 919
Cdd:pfam01268 417 ELAEAVVEACeEEPSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 920 DKKGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTEtEQVKGLF 979
Cdd:pfam01268 497 KLKGAPTGFTLPVRDVRLSAGAGFIVALTGDIMTMPGLPKRPAAENIDVDED-GKITGLF 555
FTHFS cd00477
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ...
375-978 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: 935.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 375 VDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALTAHLNvNSFACLR 454
Cdd:cd00477     1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 455 QPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkalynrlvplvngvrefs 534
Cdd:cd00477    80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 535 eiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYRQAQFDIAVASEIM 614
Cdd:cd00477   139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 615 AVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSVL 694
Cdd:cd00477   189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 695 ADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGvplkkeytEENIQL 774
Cdd:cd00477   269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 775 VADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVpCYHWSVGGKGSVDLARAVREAASK-R 853
Cdd:cd00477   338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKpK 416
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 854 SRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQPDKKGVPRDFILPIS 933
Cdd:cd00477   417 SNFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 1034649741 934 DVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDtETEQVKGL 978
Cdd:cd00477   497 DVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDID-DTGKIEGL 540
PTZ00386 PTZ00386
formyl tetrahydrofolate synthetase; Provisional
353-978 0e+00

formyl tetrahydrofolate synthetase; Provisional


Pssm-ID: 240394  Cd Length: 625  Bit Score: 924.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 353 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKST 432
Cdd:PTZ00386    8 KLSCQWPVPSDIDIAQSVKPQPITSVAESAGILLSELDPYGSTRAKVKLSVLKRLENSPNGKYVVVAGMNPTPLGEGKST 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 433 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 512
Cdd:PTZ00386   88 TTIGLAQSLGAHLHRKTFACIRQPSQGPTFGIKGGAAGGGYSQVIPMEDFNLHGTGDIHAITAANNLLAAALDTRIFHER 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 513 TQTDKALYNRLVplvNGVREFSEIQLARLKKLGINKTDPSTLTEEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIGQ 592
Cdd:PTZ00386  168 TQSDAALYRRLT---DELKKFTPIMLKRLEKLGISKTDPKQLTEEERVRFARLDIDPDTISWRRVTDVNDRMLREITIGQ 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 593 GNTEKGHYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLE 672
Cdd:PTZ00386  245 GKEEKGITRKTGFDISVASEVMAILALATDLADMRQRLGAIVVAKSKSGEPVTAEDLGCAGAMTVLMKDTIEPTLMQTLE 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 673 GTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHG 752
Cdd:PTZ00386  325 GTPVLVHAGPFGNIAHGNSSIVADQIALKLAGQDGFVLTEAGFGADIGCEKFFNIKCRTSGLKPDAAVLVATVRALKFHG 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 753 GGPSVTAGvplkkeytEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELA-KRAGAFDAVPCYH 831
Cdd:PTZ00386  405 GVEPVVAG--------KENLEAVRKGLSNLQRHIQNIRKFGVPVVVALNKFSTDTDAELELVKELAlQEGGAADVVVTDH 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 832 WSVGGKGSVDLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAK 910
Cdd:PTZ00386  477 WAKGGAGAVDLAQALIRVTeNVPSNFKLLYPLDASLKEKIETICKEIYGAAGVEYLNDADEKLEDFERMGYGKFPVCMAK 556
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034649741 911 THLSLSHQPDKKGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVKGL 978
Cdd:PTZ00386  557 TQYSFSHDPELRGAPTGFTVPIRDVRVNCGAGFVFPLLGDISTMPGLPTRPAFYNIDIDCETGKIVGL 624
MIS1 COG2759
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
360-979 0e+00

Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];


Pssm-ID: 442046  Cd Length: 556  Bit Score: 877.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 360 VPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQ 439
Cdd:COG2759     1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 440 ALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENtqtdkal 519
Cdd:COG2759    81 AL-NRLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQGN------- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 520 ynrlvplvngvrefseiqlarlkklginktdpstlteeevskfaRLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGH 599
Cdd:COG2759   153 --------------------------------------------ELNIDPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 600 YRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVH 679
Cdd:COG2759   189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 680 AGPFANIAHGNSSVLADKIALKLvGEegFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPsvta 759
Cdd:COG2759   269 GGPFANIAHGCNSVIATKLALKL-AD--YVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA---- 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 760 gvplKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAfDAVPCYHWSVGGKGS 839
Cdd:COG2759   342 ----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEGA 416
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 840 VDLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQ 918
Cdd:COG2759   417 EELAEAVVEACeEGPSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSDD 496
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034649741 919 PDKKGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDtETEQVKGLF 979
Cdd:COG2759   497 PKLLGAPTGFTLTVREVRLSAGAGFIVALTGDIMTMPGLPKVPAAERIDID-EDGKITGLF 556
PRK13505 PRK13505
formate--tetrahydrofolate ligase; Provisional
359-979 0e+00

formate--tetrahydrofolate ligase; Provisional


Pssm-ID: 237403  Cd Length: 557  Bit Score: 748.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 359 PVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLV 438
Cdd:PRK13505    1 TMKSDIEIAQEATLKPITEIAAKLGIPEDDLEPYGKYKAKISLDKIKALKDKKDGKLILVTAINPTPAGEGKSTVTVGLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 439 QALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdka 518
Cdd:PRK13505   81 DAL-NKIGKKTVIALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITSANNLLAALIDNHIHQGNE----- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 519 lynrlvplvngvrefseiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKG 598
Cdd:PRK13505  155 ----------------------------------------------LGIDPRRITWKRVLDMNDRALRNIVVGLGGPANG 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 599 HYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFV 678
Cdd:PRK13505  189 VPREDGFDITVASEIMAILCLATDLKDLKERLGRIVVGYTYDGKPVTVKDLKVEGAMALLLKDAIKPNLVQTLEGTPAFV 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 679 HAGPFANIAHGNSSVLADKIALKLvGEegFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPsvt 758
Cdd:PRK13505  269 HGGPFANIAHGCNSVLATKTALKL-AD--YVVTEAGFGADLGAEKFLDIKCRKAGLKPDAVVIVATVRALKMHGGVA--- 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 759 agvplKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAfDAVPCYHWSVGGKG 838
Cdd:PRK13505  343 -----KDDLKEENVEALKKGFANLERHIENIRKFGVPVVVAINKFVTDTDAEIAALKELCEELGV-EVALSEVWAKGGEG 416
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 839 SVDLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSH 917
Cdd:PRK13505  417 GVELAEKVVELIeEGESNFKPLYDDEDSLEEKIEKIATKIYGAKGVEFSPKAKKQLKQIEKNGWDKLPVCMAKTQYSFSD 496
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034649741 918 QPDKKGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDtETEQVKGLF 979
Cdd:PRK13505  497 DPKLLGAPTGFTITVRELRPSAGAGFIVALTGDIMTMPGLPKVPAALNIDVD-EDGNIVGLF 557
PRK13506 PRK13506
formate--tetrahydrofolate ligase; Provisional
362-978 0e+00

formate--tetrahydrofolate ligase; Provisional


Pssm-ID: 237404  Cd Length: 578  Bit Score: 716.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 362 SDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQAL 441
Cdd:PRK13506    3 SDIEISRQAPLKPIAEIAAKLGLLPDELSPFGHTKAKVSLSVLKRLADKPKGKLVLVTAITPTPLGEGKTVTTIGLTQGL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 442 tAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENtqtdkalyn 521
Cdd:PRK13506   83 -NALGQKVCACIRQPSMGPVFGVKGGAAGGGYAQVVPMEELNLHLTGDIHAVSAAHNLAAAAIDARLFHEQ--------- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 522 RLvplvnGVREFseiqlarlkklginktdpstlteEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYR 601
Cdd:PRK13506  153 RL-----GYDAF-----------------------EAQSGLPALDIDPEQILWKRVVDHNDRALRMITVGLGENGNGPER 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 602 QAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAG 681
Cdd:PRK13506  205 EDGFDITAASELMAILALSRDLKDMRQRIGRLVLAYNLQGQPITAEDLGVAGAMTVIMKDAIEPTLMQTLEGVPCLIHAG 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 682 PFANIAHGNSSVLADKIALKLVGeegFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGV 761
Cdd:PRK13506  285 PFANIAHGNSSIIADRIALKLAD---YVVTEGGFGSDMGFEKFCNIKARQSGKAPDCAVLVATLRALKANSGLYDLRPGQ 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 762 PLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYHWSVGGKGSVD 841
Cdd:PRK13506  362 ALPDSINAPDQARLEAGFANLKWHINNVAQYGLPVVVAINRFPTDTDEELEWLKEAVLLTGAFGCEISEAFAQGGEGATA 441
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 842 LARAVREAASKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQPDK 921
Cdd:PRK13506  442 LAQAVVRACEQPSQFKLLYPDEMSLEAKLMTLAEVGYGAAGVSLSDKAKQQLAQLTALGYDHLPVCMAKTPLSISHDPAL 521
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034649741 922 KGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVkGL 978
Cdd:PRK13506  522 KGAPTDFEVPIRELRLCAGAGFITALVGNVMTMPGLGLKPGYLNIDIDADGEIV-GL 577
PRK13507 PRK13507
formate--tetrahydrofolate ligase; Provisional
373-979 0e+00

formate--tetrahydrofolate ligase; Provisional


Pssm-ID: 184098  Cd Length: 587  Bit Score: 662.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 373 KAVDVLAKEIGLLADEIEIYGKSKAKVR-LSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALtAHLNVNSFA 451
Cdd:PRK13507   22 KPVEELAEELGLTKEELLPYGHYIAKVDfRKVLDRLKDRPDGKYIDVTAITPTPLGEGKSTTTMGLVQGL-GKRGKKVSG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 452 CLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTQTDKalynrlvplvngvr 531
Cdd:PRK13507  101 AIRQPSGGPTMNIKGSAAGGGLSQCIPLTPFSLGLTGDINAIMNAHNLAMVALTARMQHERNYTDE-------------- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 532 efseiQLARlkklginktdpstlteeevSKFARLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYRQAQFDIAVAS 611
Cdd:PRK13507  167 -----QLAR-------------------RGLKRLDIDPTRVEMGWIIDFCAQALRNIIIGIGGKTDGYMMQSGFGIAVSS 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 612 EIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNS 691
Cdd:PRK13507  223 EVMAILSVATDLKDLRERIGKIVVAYDKNGKPVTTADLEVDGAMTAWMVRAINPNLLQTIEGQPVFVHAGPFANIAIGQS 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 692 SVLADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGVPLKKEYTEEN 771
Cdd:PRK13507  303 SIIADRVGLKL---ADYHVTESGFGADIGFEKFWNLKCRLSGLKPDCAVIVATIRALKMHGGGPKVVPGKPLPEEYTKEN 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 772 IQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPcYHWSVGGKGSVDLARAVREAAS 851
Cdd:PRK13507  380 VGLVEKGCANLLHHIGTVKKSGINPVVCINAFYTDTHAEIAIVRRLAEQAGARVAVS-RHWEKGGEGALELADAVIDACN 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 852 KRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQG-FGNLPICMAKTHLSLSHQPDKKGVPRDFIL 930
Cdd:PRK13507  459 EPNDFKFLYPLEMPLRERIETIAREVYGADGVSYTPEAEAKLKRLESDPeTADFGTCMVKTHLSLSHDPALKGVPKGWTL 538
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*....
gi 1034649741 931 PISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVKGLF 979
Cdd:PRK13507  539 PIRDILTYGGAGFVVPVAGDISLMPGTGSDPAFRRIDVDTQTGKVKGLF 587
NAD_bind_m-THF_DH_Cyclohyd_like cd05212
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ...
193-336 4.24e-65

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: 215.45  E-value: 4.24e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 193 GDAHECFVSPVAKAVIELLEKSvGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGS 272
Cdd:cd05212     1 GPCTPLFVSPVAKAVKELLNKE-GVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGS 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034649741 273 PKPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSPRIHFGGLIeedDVILLAAALRIQNMVSSGR 336
Cdd:cd05212    80 PKPEKVPTEWIKPGATVINCSPTKLSGDDVKESASLYVPMTG---GVGKLTVAMRMQNMVRSVR 140
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
183-339 9.37e-34

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


Pssm-ID: 427036  Cd Length: 160  Bit Score: 127.20  E-value: 9.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 183 TDINLGKLVRGdaHECFVSPVAKAVIELLEKSvGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKL 262
Cdd:pfam02882   1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRY-GIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEIT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 263 HEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSprIHF--------------GGlieeddVILLAAALRI 328
Cdd:pfam02882  78 READIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGD--VDFenvkekasaitpvpGG------VGPMTVAMLL 149
                         170
                  ....*....|.
gi 1034649741 329 QNMVSSGRRWL 339
Cdd:pfam02882 150 QNTVEAAKRQL 160
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
97-290 9.32e-32

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


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 125.51  E-value: 9.32e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  97 KPVLAIIQAGDD--------NLmqeinQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ------ISE 162
Cdd:COG0190    32 TPGLAVVLVGDDpasqvyvrNK-----HKACEEVGIESELIRLPADTTQEELLALIDELNADPSVHGILVQlplpkhIDE 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 163 NlfsnKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEkSVGVNLDGKKILVVGAhgSLE-----AAL 237
Cdd:COG0190   107 E----AVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLE-RYGIDLAGKHAVVVGR--SNIvgkplALL 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034649741 238 qcLFQRKGSMTM--SiqwKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVL 290
Cdd:COG0190   178 --LLRRNATVTVchS---RTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVI 227
PRK14187 PRK14187
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
98-291 3.87e-24

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172675 [Multi-domain]  Cd Length: 294  Bit Score: 103.75  E-value: 3.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  98 PVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNA 172
Cdd:PRK14187   33 PCLIVILVGDDPASQlyvRNKQRKAEMLGLRSETILLPSTISESSLIEKINELNNDDSVHGILVQlpVPNHIDKNLIINT 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 173 LKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLeKSVGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQ 252
Cdd:PRK14187  113 IDPEKDVDGFHNENVGRLFTGQKKNCLIPCTPKGCLYLI-KTITRNLSGSDAVVIGRSNIVGKPMACLLLGENCTVTTVH 191
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034649741 253 WKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 291
Cdd:PRK14187  192 SATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVID 230
PLN02897 PLN02897
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
52-291 5.32e-24

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 178485 [Multi-domain]  Cd Length: 345  Bit Score: 104.66  E-value: 5.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  52 PQDGQARSSCSPGGRTPAARDSIVREVIQNSKEVLSLLQEKNPAFK------PVLAIIQAGDDNLMQEINQN---LAEEA 122
Cdd:PLN02897   35 PENWIPYSDPPPPVSFETEQKTVVIDGNVIAEEIRTKIASEVRKMKkavgkvPGLAVVLVGQQRDSQTYVRNkikACEET 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 123 GLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFV 200
Cdd:PLN02897  115 GIKSLLAELPEDCTEGQILSALRKFNEDTSIHGILVQLPlpQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREPLFV 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 201 SPVAKAVIELLEKSvGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPL 280
Cdd:PLN02897  195 SCTPKGCVELLIRS-GVEIAGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRG 273
                         250
                  ....*....|.
gi 1034649741 281 TWIQPGTTVLN 291
Cdd:PLN02897  274 SWLKPGAVVID 284
PRK14190 PRK14190
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
65-291 8.71e-24

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


Pssm-ID: 184560 [Multi-domain]  Cd Length: 284  Bit Score: 102.40  E-value: 8.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  65 GRTPAARdsiVREviQNSKEVLSLlqeKNPAFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEII 141
Cdd:PRK14190    8 GKEVAKE---KRE--QLKEEVVKL---KEQGIVPGLAVILVGDDPASHsyvRGKKKAAEKVGIYSELYEFPADITEEELL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 142 DEILKINEDTRVHGLALQ------ISENlfsnKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLeKSV 215
Cdd:PRK14190   80 ALIDRLNADPRINGILVQlplpkhIDEK----AVIERISPEKDVDGFHPINVGRMMLGQ--DTFLPCTPHGILELL-KEY 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034649741 216 GVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 291
Cdd:PRK14190  153 NIDISGKHVVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVID 228
PLN02616 PLN02616
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
71-291 1.44e-23

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 215332 [Multi-domain]  Cd Length: 364  Bit Score: 103.55  E-value: 1.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  71 RDSIVREVIQnSKEVLSLLqeknpafkPVLAIIQAGD--DNLMQEINQNLA-EEAGLNITHICLPPDSSEAEIIDEILKI 147
Cdd:PLN02616   86 RDEITIEVSR-MKESIGVV--------PGLAVILVGDrkDSATYVRNKKKAcDSVGINSFEVRLPEDSTEQEVLKFISGF 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 148 NEDTRVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKsVGVNLDGKKIL 225
Cdd:PLN02616  157 NNDPSVHGILVQLPlpSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMRGREPLFVPCTPKGCIELLHR-YNVEIKGKRAV 235
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034649741 226 VVGAHG--SLEAALqcLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 291
Cdd:PLN02616  236 VIGRSNivGMPAAL--LLQREDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVID 301
PRK14172 PRK14172
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
97-301 1.46e-23

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


Pssm-ID: 172660 [Multi-domain]  Cd Length: 278  Bit Score: 101.78  E-value: 1.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  97 KPVLAIIQAGDD--NLMQEINQN-LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLN 171
Cdd:PRK14172   32 IPKIASILVGNDggSIYYMNNQEkVANSLGIDFKKIKLDESISEEDLINEIEELNKDNNVHGIMLQlpLPKHLDEKKITN 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 172 ALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLeKSVGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSI 251
Cdd:PRK14172  112 KIDANKDIDCLTFISVGKFYKGE--KCFLPCTPNSVITLI-KSLNIDIEGKEVVVIGRSNIVGKPVAQLLLNENATVTIC 188
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034649741 252 QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKV 301
Cdd:PRK14172  189 HSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSVNGKI 238
PLN02516 PLN02516
methylenetetrahydrofolate dehydrogenase (NADP+)
98-291 5.95e-23

methylenetetrahydrofolate dehydrogenase (NADP+)


Pssm-ID: 178131 [Multi-domain]  Cd Length: 299  Bit Score: 100.35  E-value: 5.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  98 PVLAIIQAG---DDNLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNA 172
Cdd:PLN02516   40 PGLAVVIVGsrkDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISKVHELNANPDVHGILVQLPlpKHINEEKILNE 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 173 LKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSvGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQ 252
Cdd:PLN02516  120 ISLEKDVDGFHPLNIGKLAMKGREPLFLPCTPKGCLELLSRS-GIPIKGKKAVVVGRSNIVGLPVSLLLLKADATVTVVH 198
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034649741 253 WKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 291
Cdd:PLN02516  199 SRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVID 237
PRK14175 PRK14175
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
74-275 1.31e-20

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184552 [Multi-domain]  Cd Length: 286  Bit Score: 93.06  E-value: 1.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  74 IVREVIQNSKEVLSLLQEKnpAFKPVLAIIQAGDDNLMQEI---NQNLAEEAGLNITHICLPPDSSEAEIIDEILKINED 150
Cdd:PRK14175   11 IAKDYRQGLQDQVEALKEK--GFTPKLSVILVGNDGASQSYvrsKKKAAEKIGMISEIVHLEETATEEEVLNELNRLNND 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 151 TRVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLeKSVGVNLDGKKILVVG 228
Cdd:PRK14175   89 DSVSGILVQVPlpKQVSEQKILEAINPEKDVDGFHPINIGKLYIDE--QTFVPCTPLGIMEIL-KHADIDLEGKNAVVIG 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034649741 229 -AHGSLEAALQCLFQRKGSMTMsIQWKTRQLQSKLHEADIVVLGSPKP 275
Cdd:PRK14175  166 rSHIVGQPVSKLLLQKNASVTI-LHSRSKDMASYLKDADVIVSAVGKP 212
PRK14167 PRK14167
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
97-291 1.86e-20

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


Pssm-ID: 184549 [Multi-domain]  Cd Length: 297  Bit Score: 92.92  E-value: 1.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  97 KPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLN 171
Cdd:PRK14167   31 TPGLATVLMSDDPASEtyvSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTIDELNADEDVHGILVQmpVPDHVDDREVLR 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 172 ALKPEKDVDGVTDINLGKLVRGDAHecfVSPVAKAVIELLEKSVGVNLDGKKILVVGAHGSLEAALQCLFQRK---GSMT 248
Cdd:PRK14167  111 RIDPAKDVDGFHPENVGRLVAGDAR---FKPCTPHGIQKLLAAAGVDTEGADVVVVGRSDIVGKPMANLLIQKadgGNAT 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1034649741 249 MSI-QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 291
Cdd:PRK14167  188 VTVcHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVID 231
PRK14170 PRK14170
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
82-320 4.95e-20

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172658 [Multi-domain]  Cd Length: 284  Bit Score: 91.68  E-value: 4.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  82 SKEVLSLLQEKNpafKPVLAIIQAGDDNLMQEI---NQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLAL 158
Cdd:PRK14170   19 TREVAELVKEGK---KPGLAVVLVGDNQASRTYvrnKQKRTEEAGMKSVLIELPENVTEEKLLSVVEELNEDKTIHGILV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 159 Q--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLeKSVGVNLDGKKILVVGAHGSL-EA 235
Cdd:PRK14170   96 QlpLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGK--DSFVPCTPAGIIELI-KSTGTQIEGKRAVVIGRSNIVgKP 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 236 ALQCLFQRKGSMTMSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSprIHFGGLIE 315
Cdd:PRK14170  173 VAQLLLNENATVTIA-HSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDRDENNKLCGD--VDFDDVVE 249

                  ....*
gi 1034649741 316 EDDVI 320
Cdd:PRK14170  250 EAGFI 254
PRK10792 PRK10792
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
97-290 2.57e-19

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 236760 [Multi-domain]  Cd Length: 285  Bit Score: 89.21  E-value: 2.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  97 KPVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLN 171
Cdd:PRK10792   33 APGLAVVLVGSDPASQVYVASkrkACEEVGFVSRSYDLPETTSEAELLALIDELNADPTIDGILVQlpLPAHIDNVKVLE 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 172 ALKPEKDVDGVTDINLGKLvrgdaheCFVSPV-----AKAVIELLEkSVGVNLDGKKILVVGAHG------SLEAALqcl 240
Cdd:PRK10792  113 RIHPDKDVDGFHPYNVGRL-------AQRIPLlrpctPRGIMTLLE-RYGIDTYGLNAVVVGASNivgrpmSLELLL--- 181
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034649741 241 fqrKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVL 290
Cdd:PRK10792  182 ---AGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVI 228
PRK14192 PRK14192
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
98-315 5.00e-19

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184561 [Multi-domain]  Cd Length: 283  Bit Score: 88.36  E-value: 5.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  98 PVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNA 172
Cdd:PRK14192   34 PILATILVGDDPASAtyvRMKGNACRRVGMDSLKVELPQETTTEQLLAKIEELNANPDVHGILLQhpVPAQIDERACFDA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 173 LKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSvGVNLDGKKILVVGAHGSLEAAL-QCLFQRKGSMTMSi 251
Cdd:PRK14192  114 ISLAKDVDGVTCLGFGRMAMGE--AAYGSATPAGIMRLLKAY-NIELAGKHAVVVGRSAILGKPMaMMLLNANATVTIC- 189
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034649741 252 QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCS-HDFLSGKVGcgspRIHFGGLIE 315
Cdd:PRK14192  190 HSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGfHPRDGGGVG----DIELQGIEE 250
PRK14186 PRK14186
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
131-291 7.13e-19

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237636 [Multi-domain]  Cd Length: 297  Bit Score: 88.20  E-value: 7.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 131 LPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPVakAVI 208
Cdd:PRK14186   69 LPADTSQAEVEALIAQLNQDERVDGILLQlpLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPA--GVM 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 209 ELLEkSVGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTT 288
Cdd:PRK14186  147 RLLR-SQQIDIAGKKAVVVGRSILVGKPLALMLLAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAV 225

                  ...
gi 1034649741 289 VLN 291
Cdd:PRK14186  226 VVD 228
PRK14194 PRK14194
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
65-291 3.54e-18

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172682 [Multi-domain]  Cd Length: 301  Bit Score: 86.44  E-value: 3.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  65 GRTPAARdsivreVIQNSKEVLSLLqeKNPAFKPVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEII 141
Cdd:PRK14194    9 GKAAAAR------VLAQVREDVRTL--KAAGIEPALAVILVGNDPASQVYVRNkilRAEEAGIRSLEHRLPADTSQARLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 142 DEILKINEDTRVHGLALQ--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAhecFVSPVAKA-VIELLEKSVGvN 218
Cdd:PRK14194   81 ALIAELNADPSVNGILLQlpLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRD---VLTPCTPSgCLRLLEDTCG-D 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034649741 219 LDGKKILVVGAH---GSLEAALqcLFQRKGSMTMsIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 291
Cdd:PRK14194  157 LTGKHAVVIGRSnivGKPMAAL--LLQAHCSVTV-VHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVID 229
PRK14189 PRK14189
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
97-291 4.86e-18

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 184559 [Multi-domain]  Cd Length: 285  Bit Score: 85.51  E-value: 4.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  97 KPVLAIIQAGDDNLMQEINQNLA---EEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLN 171
Cdd:PRK14189   32 QPGLAVILVGDNPASQVYVRNKVkacEDNGFHSLKDRYPADLSEAELLARIDELNRDPKIHGILVQlpLPKHIDSHKVIE 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 172 ALKPEKDVDGVTDINLGKLVRGdaHECFVSPVAKAVIELLEkSVGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSI 251
Cdd:PRK14189  112 AIAPEKDVDGFHVANAGALMTG--QPLFRPCTPYGVMKMLE-SIGIPLRGAHAVVIGRSNIVGKPMAMLLLQAGATVTIC 188
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1034649741 252 QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 291
Cdd:PRK14189  189 HSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVID 228
PRK14180 PRK14180
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
95-301 5.56e-18

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


Pssm-ID: 172668 [Multi-domain]  Cd Length: 282  Bit Score: 85.47  E-value: 5.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  95 AFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKV 169
Cdd:PRK14180   29 AITPKLVAIIVGNDPASKtyvASKEKACAQVGIDSQVITLPEHTTESELLELIDQLNNDSSVHAILVQLPlpAHINKNNV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 170 LNALKPEKDVDGVTDINLGKLVRGDaHECFVSPVAKAVIELLeKSVGVNLDGKKILVVGAHGSL-EAALQCLFQRKGSMT 248
Cdd:PRK14180  109 IYSIKPEKDVDGFHPTNVGRLQLRD-KKCLESCTPKGIMTML-REYGIKTEGAYAVVVGASNVVgKPVSQLLLNAKATVT 186
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034649741 249 MSIQWkTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKV 301
Cdd:PRK14180  187 TCHRF-TTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHVDGKI 238
PRK14188 PRK14188
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
97-290 1.41e-17

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184558 [Multi-domain]  Cd Length: 296  Bit Score: 84.62  E-value: 1.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  97 KPVLAIIQAGDDNLMQEINQN---LAEEAGLN-ITHIcLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVL 170
Cdd:PRK14188   32 TPGLAVVLVGEDPASQVYVRSkgkQTKEAGMAsFEHK-LPADTSQAELLALIARLNADPAIHGILVQlpLPKHLDSEAVI 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 171 NALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSVGvNLDGKKILVVGAH---GSLEAALqcLFQRKGSM 247
Cdd:PRK14188  111 QAIDPEKDVDGLHVVNAGRLATGE--TALVPCTPLGCMMLLRRVHG-DLSGLNAVVIGRSnlvGKPMAQL--LLAANATV 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1034649741 248 TMSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVL 290
Cdd:PRK14188  186 TIA-HSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVI 227
THF_DHG_CYH pfam00763
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
90-180 1.53e-17

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;


Pssm-ID: 459930 [Multi-domain]  Cd Length: 115  Bit Score: 79.37  E-value: 1.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  90 QEKNPAFKPVLAIIQAGDD---NLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENL 164
Cdd:pfam00763  20 ALKAGGRKPGLAVILVGDDpasQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKLNADPSVHGILVQlpLPKHI 99
                          90
                  ....*....|....*.
gi 1034649741 165 FSNKVLNALKPEKDVD 180
Cdd:pfam00763 100 DEEKVLEAIDPEKDVD 115
PRK14174 PRK14174
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
98-291 1.66e-17

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


Pssm-ID: 172662 [Multi-domain]  Cd Length: 295  Bit Score: 84.10  E-value: 1.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  98 PVLAIIQAGDDNLMQEINQNLAE---EAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNA 172
Cdd:PRK14174   32 PGLTVIIVGEDPASQVYVRNKAKsckEIGMNSTVIELPADTTEEHLLKKIEDLNNDPDVHGILVQqpLPKQIDEFAVTLA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 173 LKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKsVGVNLDGKKILVVGAH---GSLEAALQCLFQRKGSMTM 249
Cdd:PRK14174  112 IDPAKDVDGFHPENLGRLVMGHLDKCFVSCTPYGILELLGR-YNIETKGKHCVVVGRSnivGKPMANLMLQKLKESNCTV 190
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1034649741 250 SI-QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 291
Cdd:PRK14174  191 TIcHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVID 233
PRK14177 PRK14177
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
75-302 2.80e-17

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172665 [Multi-domain]  Cd Length: 284  Bit Score: 83.48  E-value: 2.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  75 VREVIQNskEVLSLLQEKNPAFK--PVLAIIQAGDdNLMQEINQNL----AEEAGLNITHICLPPDSSEAEIIDEILKIN 148
Cdd:PRK14177   11 LSEKIRN--EIRETIEERKTKNKriPKLATILVGN-NPASETYVSMkvkaCHKVGMGSEMIRLKEQTTTEELLGVIDKLN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 149 EDTRVHGLALQ--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDahECFVsPVAKAVIELLEKSVGVNLDGKKILV 226
Cdd:PRK14177   88 LDPNVDGILLQhpVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGV--ETYL-PCTPYGMVLLLKEYGIDVTGKNAVV 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034649741 227 VGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDflSGKVG 302
Cdd:PRK14177  165 VGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYN--PGNVG 238
PRK14191 PRK14191
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
98-291 1.13e-16

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172679 [Multi-domain]  Cd Length: 285  Bit Score: 81.74  E-value: 1.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  98 PVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNA 172
Cdd:PRK14191   32 PKLAVILVGKDPASQtyvNMKIKACERVGMDSDLHTLQENTTEAELLSLIKDLNTDQNIDGILVQLPlpRHIDTKMVLEA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 173 LKPEKDVDGVTDINLGKLVRGdaHECFVSPVAKAVIELLEKsVGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQ 252
Cdd:PRK14191  112 IDPNKDVDGFHPLNIGKLCSQ--LDGFVPATPMGVMRLLKH-YHIEIKGKDVVIIGASNIVGKPLAMLMLNAGASVSVCH 188
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034649741 253 WKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 291
Cdd:PRK14191  189 ILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVD 227
PRK14168 PRK14168
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
131-291 2.14e-16

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237633 [Multi-domain]  Cd Length: 297  Bit Score: 81.08  E-value: 2.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 131 LPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVI 208
Cdd:PRK14168   70 QSVDITEEELLALIDKYNNDDSIHGILVQlpLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIGGDEVKFLPCTPAGIQ 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 209 ELLEKSvGVNLDGKKILVVGAHGSLEAALQCLFQRKG----SMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQ 284
Cdd:PRK14168  150 EMLVRS-GVETSGAEVVVVGRSNIVGKPIANMMTQKGpganATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIK 228

                  ....*..
gi 1034649741 285 PGTTVLN 291
Cdd:PRK14168  229 PGATVID 235
PRK14176 PRK14176
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
91-291 4.00e-16

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


Pssm-ID: 184553 [Multi-domain]  Cd Length: 287  Bit Score: 79.85  E-value: 4.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  91 EKNPAFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLF 165
Cdd:PRK14176   32 KSNRGITPGLATILVGDDPASKmyvRLKHKACERVGIRAEDQFLPADTTQEELLELIDSLNKRKDVHGILLQLPlpKHLD 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 166 SNKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKsVGVNLDGKKILVVGAHGSLEAALQCLFQRKG 245
Cdd:PRK14176  112 PQEAMEAIDPAKDADGFHPYNMGKLMIGD--EGLVPCTPHGVIRALEE-YGVDIEGKNAVIVGHSNVVGKPMAAMLLNRN 188
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034649741 246 SMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 291
Cdd:PRK14176  189 ATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFD 234
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
175-292 8.73e-16

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: 76.05  E-value: 8.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 175 PEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLeKSVGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWK 254
Cdd:cd01080     1 PEKDVDGLHPVNLGRLALGR--PGFIPCTPAGILELL-KRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSK 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034649741 255 TRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNC 292
Cdd:cd01080    78 TKNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDV 115
PRK14193 PRK14193
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
69-291 1.09e-15

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


Pssm-ID: 237637 [Multi-domain]  Cd Length: 284  Bit Score: 78.52  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  69 AARDSIVREViqnsKEVLSLLQEKnpAFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEIL 145
Cdd:PRK14193   10 ATADEIKADL----AERVAALKEK--GITPGLGTVLVGDDPGSQayvRGKHRDCAEVGITSIRRDLPADATQEELNAVID 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 146 KINEDTRVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPvaKAVIELLEKSvGVNLDGKK 223
Cdd:PRK14193   84 ELNADPACTGYIVQLPlpKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTP--RGIVHLLRRY-DVELAGAH 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 224 ILVVGAHGSLEAALQCLFQRKG-SMTMSI-QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 291
Cdd:PRK14193  161 VVVIGRGVTVGRPIGLLLTRRSeNATVTLcHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLD 230
PRK14178 PRK14178
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
82-304 2.13e-15

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172666 [Multi-domain]  Cd Length: 279  Bit Score: 77.58  E-value: 2.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  82 SKEVLSLLQEK--NPAFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGL 156
Cdd:PRK14178    9 SEKRLELLKEEiiESGLYPRLATVIVGDDPASQmyvRMKHRACERVGIGSVGIELPGDATTRTVLERIRRLNEDPDINGI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 157 ALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPvaKAVIELLeKSVGVNLDGKKILVVGAH---G 231
Cdd:PRK14178   89 LVQLPlpKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTP--NGIMTLL-HEYKISIAGKRAVVVGRSidvG 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034649741 232 SLEAALqcLFQRKGSMTMSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKVgCG 304
Cdd:PRK14178  166 RPMAAL--LLNADATVTIC-HSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQVNGKL-CG 234
PRK14179 PRK14179
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
83-291 2.86e-15

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 237634 [Multi-domain]  Cd Length: 284  Bit Score: 77.48  E-value: 2.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  83 KEVLSLLQEKnpAFKPVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ 159
Cdd:PRK14179   20 EKVAKLKEEK--GIVPGLVVILVGDNPASQVYVRNkerSALAAGFKSEVVRLPETISQEELLDLIERYNQDPTWHGILVQ 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 160 --ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGdaHECFVSPVAKAVIELLeKSVGVNLDGKKILVVGAHGSLEAAL 237
Cdd:PRK14179   98 lpLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSG--RPVMIPCTPAGIMEMF-REYNVELEGKHAVVIGRSNIVGKPM 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034649741 238 -QCLFQRKGSMTMSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 291
Cdd:PRK14179  175 aQLLLDKNATVTLT-HSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVID 228
PRK14182 PRK14182
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
97-291 2.78e-13

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


Pssm-ID: 172670 [Multi-domain]  Cd Length: 282  Bit Score: 71.59  E-value: 2.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  97 KPVLAIIQAGDD---NLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLN 171
Cdd:PRK14182   30 QTGLTVVRVGDDpasAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIARLNADPAVHGILVQLPlpKHVDERAVLD 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 172 ALKPEKDVDGVTDINLGKL---VRGDAHECfvspVAKAVIELLEKSvGVNLDGKKILVVGAH---GSLEAALqcLFQRKG 245
Cdd:PRK14182  110 AISPAKDADGFHPFNVGALsigIAGVPRPC----TPAGVMRMLDEA-RVDPKGKRALVVGRSnivGKPMAMM--LLERHA 182
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034649741 246 SMTMSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 291
Cdd:PRK14182  183 TVTIA-HSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVID 227
PRK14171 PRK14171
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
73-299 1.54e-12

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172659 [Multi-domain]  Cd Length: 288  Bit Score: 69.22  E-value: 1.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  73 SIVREVIQNSKEVLSLLQEKNPAfKPVLAIIQAGDDN-----LMQEINQnlAEEAGLNITHICLPPDSSEAEIIDEILKI 147
Cdd:PRK14171    9 ALANEILADLKLEIQELKSQTNA-SPKLAIVLVGDNPasiiyVKNKIKN--AHKIGIDTLLVNLSTTIHTNDLISKINEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 148 NEDTRVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGdAHECFVSPVAKAVIELLEKsVGVNLDGKKIL 225
Cdd:PRK14171   86 NLDNEISGIIVQLPlpSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSG-ISQGFIPCTALGCLAVIKK-YEPNLTGKNVV 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034649741 226 VVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSG 299
Cdd:PRK14171  164 IIGRSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRISG 237
PRK14166 PRK14166
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
82-301 2.93e-12

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


Pssm-ID: 172654 [Multi-domain]  Cd Length: 282  Bit Score: 68.51  E-value: 2.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  82 SKEVLSLLQEKNPAFK-----PVLAIIQAGDDNLMQEINQNLA---EEAGLNITHICLPPDSSEAEIIDEILKINEDTRV 153
Cdd:PRK14166   10 SAKIKEELKEKNQFLKskgieSCLAVILVGDNPASQTYVKSKAkacEECGIKSLVYHLNENTTQNELLALINTLNHDDSV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 154 HGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGdAHECFVSPVAKAVIELLEkSVGVNLDGKKILVVGAHG 231
Cdd:PRK14166   90 HGILVQLPlpDHICKDLILESIISSKDVDGFHPINVGYLNLG-LESGFLPCTPLGVMKLLK-AYEIDLEGKDAVIIGASN 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034649741 232 SLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFL-SGKV 301
Cdd:PRK14166  168 IVGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLeSGKI 238
PRK14181 PRK14181
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
98-291 5.58e-12

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172669 [Multi-domain]  Cd Length: 287  Bit Score: 67.58  E-value: 5.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741  98 PVLAIIQAGDDNlMQEINQNLAEEAGLNITHIC----LPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLN 171
Cdd:PRK14181   27 PGLAVVLIGNDP-ASEVYVGMKVKKATDLGMVSkahrLPSDATLSDILKLIHRLNNDPNIHGILVQLPlpKHLDAQAILQ 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649741 172 ALKPEKDVDGVTDINLGKLVRGDAhECFVSPVAKAVIELLeKSVGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMS- 250
Cdd:PRK14181  106 AISPDKDVDGLHPVNMGKLLLGET-DGFIPCTPAGIIELL-KYYEIPLHGRHVAIVGRSNIVGKPLAALLMQKHPDTNAt 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1034649741 251 ---IQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 291
Cdd:PRK14181  184 vtlLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVD 227
 
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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