|
Name |
Accession |
Description |
Interval |
E-value |
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
157-291 |
1.45e-58 |
|
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: 188.10 E-value: 1.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 157 GEDSDYFVSPTAGAVMELLE----DLDGKTVLLVGIDGALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSP 232
Cdd:cd05212 1 GPCTPLFVSPVAKAVKELLNkegvRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 233 KPDSVPKSWLKPGTTIINCSPDLLSEKHSYDQKNSNT-TENAVCSLAVAMRMQNMVKNTE 291
Cdd:cd05212 81 KPEKVPTEWIKPGATVINCSPTKLSGDDVKESASLYVpMTGGVGKLTVAMRMQNMVRSVR 140
|
|
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
316-420 |
9.34e-57 |
|
Formate--tetrahydrofolate ligase;
Pssm-ID: 460143 Cd Length: 555 Bit Score: 195.62 E-value: 9.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 316 PSDIEISRAQSPKAVDVLAKEIGLLTDEIEIYGQTKAKVRLSLLERLKDQPDGKYVLVAGITPTPLGEGKSTVTIGLVQA 395
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100
....*....|....*....|....*
gi 2024392726 396 LtAHLNINSFACLRQPSQGPTFGVK 420
Cdd:pfam01268 81 L-NRLGKKAIAALREPSLGPVFGIK 104
|
|
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
308-420 |
6.41e-50 |
|
Formate--tetrahydrofolate ligase
Pssm-ID: 178359 Cd Length: 637 Bit Score: 178.81 E-value: 6.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 308 KLQPLSPVPSDIEISRAQSPKAVDVLAKEIGLLTDEIEIYGQTKAKVRLSLLERLKDQPDGKYVLVAGITPTPLGEGKST 387
Cdd:PLN02759 9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88
|
90 100 110
....*....|....*....|....*....|...
gi 2024392726 388 VTIGLVQALTAHLNINSFACLRQPSQGPTFGVK 420
Cdd:PLN02759 89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIK 121
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
315-420 |
5.53e-46 |
|
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
Pssm-ID: 442046 Cd Length: 556 Bit Score: 166.75 E-value: 5.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 315 VPSDIEISRAQSPKAVDVLAKEIGLLTDEIEIYGQTKAKVRLSLLERLKDQPDGKYVLVAGITPTPLGEGKSTVTIGLVQ 394
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100
....*....|....*....|....*.
gi 2024392726 395 ALtAHLNINSFACLRQPSQGPTFGVK 420
Cdd:COG2759 81 AL-NRLGKKAIVALREPSLGPVFGIK 105
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
330-420 |
4.25e-45 |
|
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: 163.86 E-value: 4.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 330 VDVLAKEIGLLTDEIEIYGQTKAKVRLSLLERLKDQPDGKYVLVAGITPTPLGEGKSTVTIGLVQALTAHLNiNSFACLR 409
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79
|
90
....*....|.
gi 2024392726 410 QPSQGPTFGVK 420
Cdd:cd00477 80 QPSLGPTFGIK 90
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
39-249 |
1.96e-40 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 145.54 E-value: 1.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 39 ARKITENARKSLASLKREHprLEPTLAIIQAHNAP--LVQEMNK-NFAEEVGLRVINVCLPEDSSKDEIVNEILRLNEDP 115
Cdd:COG0190 12 AAEIREELKERVAALKAKG--ITPGLAVVLVGDDPasQVYVRNKhKACEEVGIESELIRLPADTTQEELLALIDELNADP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 116 NVQG--LALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSdyFVSPTAGAVMELLE----DLDGKTVLLVG-- 187
Cdd:COG0190 90 SVHGilVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPG--FVPCTPAGIMELLErygiDLAGKHAVVVGrs 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024392726 188 -IdgaLGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTII 249
Cdd:COG0190 168 nI---VGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVI 227
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
37-292 |
1.86e-35 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 132.06 E-value: 1.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 37 QAARKITENARKSLASLKREhpRLEPTLAIIQAHNAPLVQ---EMNKNFAEEVGLRVINVCLPEDSSKDEIVNEILRLNE 113
Cdd:PRK14190 10 EVAKEKREQLKEEVVKLKEQ--GIVPGLAVILVGDDPASHsyvRGKKKAAEKVGIYSELYEFPADITEEELLALIDRLNA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 114 DPNVQGL--ALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEdsDYFVSPTAGAVMELLE----DLDGKTVLLVG 187
Cdd:PRK14190 88 DPRINGIlvQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQ--DTFLPCTPHGILELLKeyniDISGKHVVVVG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 188 IDGALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIINCSPDLLSEKH-----SY 262
Cdd:PRK14190 166 RSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRLENGKlcgdvDF 245
|
250 260 270
....*....|....*....|....*....|....*
gi 2024392726 263 D---QKNSNTT--ENAVCSLAVAMRMQNMVKNTER 292
Cdd:PRK14190 246 DnvkEKASYITpvPGGVGPMTITMLMHNTVELAKR 280
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
147-293 |
6.88e-30 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 113.33 E-value: 6.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 147 SDINLGRLVRGEDsdYFVSPTAGAVMELLE----DLDGKTVLLVGIDGALGSSLQCLLQRRGAITASCLWKSPGLQSKLH 222
Cdd:pfam02882 1 HPYNLGRLVLGKP--CFVPCTPRGIMELLKrygiDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 223 HADVVVAGSPKPDSVPKSWLKPGTTIINCSPDLLSEKH--------SYDQKNSNTT--ENAVCSLAVAMRMQNMVKNTER 292
Cdd:pfam02882 79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKlvgdvdfeNVKEKASAITpvPGGVGPMTVAMLLQNTVEAAKR 158
|
.
gi 2024392726 293 W 293
Cdd:pfam02882 159 Q 159
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
36-250 |
2.68e-28 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 112.94 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 36 GQA-ARKITENARKSLASLKREHpRLEPTLAIIQAHNAPLVQ---EMNKNFAEEVGLRVINVCLPEDSSKDEIVNEILRL 111
Cdd:PRK14191 6 GKAlSYKIEKDLKNKIQILTAQT-GKRPKLAVILVGKDPASQtyvNMKIKACERVGMDSDLHTLQENTTEAELLSLIKDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 112 NEDPNVQGL--ALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSdyFVSPTAGAVMELLE----DLDGKTVLL 185
Cdd:PRK14191 85 NTDQNIDGIlvQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDG--FVPATPMGVMRLLKhyhiEIKGKDVVI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024392726 186 VGIDGALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIIN 250
Cdd:PRK14191 163 IGASNIVGKPLAMLMLNAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVD 227
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
39-144 |
3.41e-20 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 85.53 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 39 ARKITENARKSLASLKRehPRLEPTLAIIQAHNAPLVQ---EMNKNFAEEVGLRVINVCLPEDSSKDEIVNEILRLNEDP 115
Cdd:pfam00763 7 AKKIREELKEEVAALKA--GGRKPGLAVILVGDDPASQvyvRNKKKACEEVGIESELIRLPEDTTEEELLALIDKLNADP 84
|
90 100 110
....*....|....*....|....*....|.
gi 2024392726 116 NVQG--LALDLPESLCSSKILNAVKPEKDVD 144
Cdd:pfam00763 85 SVHGilVQLPLPKHIDEEKVLEAIDPEKDVD 115
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
157-291 |
1.45e-58 |
|
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: 188.10 E-value: 1.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 157 GEDSDYFVSPTAGAVMELLE----DLDGKTVLLVGIDGALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSP 232
Cdd:cd05212 1 GPCTPLFVSPVAKAVKELLNkegvRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 233 KPDSVPKSWLKPGTTIINCSPDLLSEKHSYDQKNSNT-TENAVCSLAVAMRMQNMVKNTE 291
Cdd:cd05212 81 KPEKVPTEWIKPGATVINCSPTKLSGDDVKESASLYVpMTGGVGKLTVAMRMQNMVRSVR 140
|
|
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
316-420 |
9.34e-57 |
|
Formate--tetrahydrofolate ligase;
Pssm-ID: 460143 Cd Length: 555 Bit Score: 195.62 E-value: 9.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 316 PSDIEISRAQSPKAVDVLAKEIGLLTDEIEIYGQTKAKVRLSLLERLKDQPDGKYVLVAGITPTPLGEGKSTVTIGLVQA 395
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100
....*....|....*....|....*
gi 2024392726 396 LtAHLNINSFACLRQPSQGPTFGVK 420
Cdd:pfam01268 81 L-NRLGKKAIAALREPSLGPVFGIK 104
|
|
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
308-420 |
6.41e-50 |
|
Formate--tetrahydrofolate ligase
Pssm-ID: 178359 Cd Length: 637 Bit Score: 178.81 E-value: 6.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 308 KLQPLSPVPSDIEISRAQSPKAVDVLAKEIGLLTDEIEIYGQTKAKVRLSLLERLKDQPDGKYVLVAGITPTPLGEGKST 387
Cdd:PLN02759 9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88
|
90 100 110
....*....|....*....|....*....|...
gi 2024392726 388 VTIGLVQALTAHLNINSFACLRQPSQGPTFGVK 420
Cdd:PLN02759 89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIK 121
|
|
| PTZ00386 |
PTZ00386 |
formyl tetrahydrofolate synthetase; Provisional |
308-420 |
2.65e-47 |
|
formyl tetrahydrofolate synthetase; Provisional
Pssm-ID: 240394 Cd Length: 625 Bit Score: 171.55 E-value: 2.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 308 KLQPLSPVPSDIEISRAQSPKAVDVLAKEIGLLTDEIEIYGQTKAKVRLSLLERLKDQPDGKYVLVAGITPTPLGEGKST 387
Cdd:PTZ00386 8 KLSCQWPVPSDIDIAQSVKPQPITSVAESAGILLSELDPYGSTRAKVKLSVLKRLENSPNGKYVVVAGMNPTPLGEGKST 87
|
90 100 110
....*....|....*....|....*....|...
gi 2024392726 388 VTIGLVQALTAHLNINSFACLRQPSQGPTFGVK 420
Cdd:PTZ00386 88 TTIGLAQSLGAHLHRKTFACIRQPSQGPTFGIK 120
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
315-420 |
5.53e-46 |
|
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
Pssm-ID: 442046 Cd Length: 556 Bit Score: 166.75 E-value: 5.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 315 VPSDIEISRAQSPKAVDVLAKEIGLLTDEIEIYGQTKAKVRLSLLERLKDQPDGKYVLVAGITPTPLGEGKSTVTIGLVQ 394
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100
....*....|....*....|....*.
gi 2024392726 395 ALtAHLNINSFACLRQPSQGPTFGVK 420
Cdd:COG2759 81 AL-NRLGKKAIVALREPSLGPVFGIK 105
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
330-420 |
4.25e-45 |
|
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: 163.86 E-value: 4.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 330 VDVLAKEIGLLTDEIEIYGQTKAKVRLSLLERLKDQPDGKYVLVAGITPTPLGEGKSTVTIGLVQALTAHLNiNSFACLR 409
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79
|
90
....*....|.
gi 2024392726 410 QPSQGPTFGVK 420
Cdd:cd00477 80 QPSLGPTFGIK 90
|
|
| PRK13506 |
PRK13506 |
formate--tetrahydrofolate ligase; Provisional |
317-420 |
9.79e-41 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237404 Cd Length: 578 Bit Score: 152.46 E-value: 9.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 317 SDIEISRAQSPKAVDVLAKEIGLLTDEIEIYGQTKAKVRLSLLERLKDQPDGKYVLVAGITPTPLGEGKSTVTIGLVQAL 396
Cdd:PRK13506 3 SDIEISRQAPLKPIAEIAAKLGLLPDELSPFGHTKAKVSLSVLKRLADKPKGKLVLVTAITPTPLGEGKTVTTIGLTQGL 82
|
90 100
....*....|....*....|....
gi 2024392726 397 tAHLNINSFACLRQPSQGPTFGVK 420
Cdd:PRK13506 83 -NALGQKVCACIRQPSMGPVFGVK 105
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
39-249 |
1.96e-40 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 145.54 E-value: 1.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 39 ARKITENARKSLASLKREHprLEPTLAIIQAHNAP--LVQEMNK-NFAEEVGLRVINVCLPEDSSKDEIVNEILRLNEDP 115
Cdd:COG0190 12 AAEIREELKERVAALKAKG--ITPGLAVVLVGDDPasQVYVRNKhKACEEVGIESELIRLPADTTQEELLALIDELNADP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 116 NVQG--LALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSdyFVSPTAGAVMELLE----DLDGKTVLLVG-- 187
Cdd:COG0190 90 SVHGilVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPG--FVPCTPAGIMELLErygiDLAGKHAVVVGrs 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024392726 188 -IdgaLGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTII 249
Cdd:COG0190 168 nI---VGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVI 227
|
|
| PRK13505 |
PRK13505 |
formate--tetrahydrofolate ligase; Provisional |
314-420 |
3.17e-39 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237403 Cd Length: 557 Bit Score: 148.02 E-value: 3.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 314 PVPSDIEISRAQSPKAVDVLAKEIGLLTDEIEIYGQTKAKVRLSLLERLKDQPDGKYVLVAGITPTPLGEGKSTVTIGLV 393
Cdd:PRK13505 1 TMKSDIEIAQEATLKPITEIAAKLGIPEDDLEPYGKYKAKISLDKIKALKDKKDGKLILVTAINPTPAGEGKSTVTVGLG 80
|
90 100
....*....|....*....|....*..
gi 2024392726 394 QALtAHLNINSFACLRQPSQGPTFGVK 420
Cdd:PRK13505 81 DAL-NKIGKKTVIALREPSLGPVFGIK 106
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
37-292 |
1.86e-35 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 132.06 E-value: 1.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 37 QAARKITENARKSLASLKREhpRLEPTLAIIQAHNAPLVQ---EMNKNFAEEVGLRVINVCLPEDSSKDEIVNEILRLNE 113
Cdd:PRK14190 10 EVAKEKREQLKEEVVKLKEQ--GIVPGLAVILVGDDPASHsyvRGKKKAAEKVGIYSELYEFPADITEEELLALIDRLNA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 114 DPNVQGL--ALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEdsDYFVSPTAGAVMELLE----DLDGKTVLLVG 187
Cdd:PRK14190 88 DPRINGIlvQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQ--DTFLPCTPHGILELLKeyniDISGKHVVVVG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 188 IDGALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIINCSPDLLSEKH-----SY 262
Cdd:PRK14190 166 RSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRLENGKlcgdvDF 245
|
250 260 270
....*....|....*....|....*....|....*
gi 2024392726 263 D---QKNSNTT--ENAVCSLAVAMRMQNMVKNTER 292
Cdd:PRK14190 246 DnvkEKASYITpvPGGVGPMTITMLMHNTVELAKR 280
|
|
| PRK13507 |
PRK13507 |
formate--tetrahydrofolate ligase; Provisional |
318-420 |
3.82e-30 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 184098 Cd Length: 587 Bit Score: 122.51 E-value: 3.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 318 DIEISRA--QSPKAVDVLAKEIGLLTDEIEIYGQTKAKVR-LSLLERLKDQPDGKYVLVAGITPTPLGEGKSTVTIGLVQ 394
Cdd:PRK13507 10 DWEIAEEaeKFMKPVEELAEELGLTKEELLPYGHYIAKVDfRKVLDRLKDRPDGKYIDVTAITPTPLGEGKSTTTMGLVQ 89
|
90 100
....*....|....*....|....*.
gi 2024392726 395 ALtAHLNINSFACLRQPSQGPTFGVK 420
Cdd:PRK13507 90 GL-GKRGKKVSGAIRQPSGGPTMNIK 114
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
147-293 |
6.88e-30 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 113.33 E-value: 6.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 147 SDINLGRLVRGEDsdYFVSPTAGAVMELLE----DLDGKTVLLVGIDGALGSSLQCLLQRRGAITASCLWKSPGLQSKLH 222
Cdd:pfam02882 1 HPYNLGRLVLGKP--CFVPCTPRGIMELLKrygiDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 223 HADVVVAGSPKPDSVPKSWLKPGTTIINCSPDLLSEKH--------SYDQKNSNTT--ENAVCSLAVAMRMQNMVKNTER 292
Cdd:pfam02882 79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKlvgdvdfeNVKEKASAITpvPGGVGPMTVAMLLQNTVEAAKR 158
|
.
gi 2024392726 293 W 293
Cdd:pfam02882 159 Q 159
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
36-250 |
2.68e-28 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 112.94 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 36 GQA-ARKITENARKSLASLKREHpRLEPTLAIIQAHNAPLVQ---EMNKNFAEEVGLRVINVCLPEDSSKDEIVNEILRL 111
Cdd:PRK14191 6 GKAlSYKIEKDLKNKIQILTAQT-GKRPKLAVILVGKDPASQtyvNMKIKACERVGMDSDLHTLQENTTEAELLSLIKDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 112 NEDPNVQGL--ALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSdyFVSPTAGAVMELLE----DLDGKTVLL 185
Cdd:PRK14191 85 NTDQNIDGIlvQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDG--FVPATPMGVMRLLKhyhiEIKGKDVVI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024392726 186 VGIDGALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIIN 250
Cdd:PRK14191 163 IGASNIVGKPLAMLMLNAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVD 227
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
39-250 |
4.23e-28 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 112.23 E-value: 4.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 39 ARKITENARKSLASLKREHpRLEPTLAIIQAHNAPLVQ---EMNKNFAEEVGLRVINVCLPEDSSKDEIVNEILRLNEDP 115
Cdd:PRK14183 10 SDKIKENVKKEVDELKLVK-NIVPGLAVILVGDDPASHtyvKMKAKACDRVGIYSITHEMPSTISQKEILETIAMMNNNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 116 NVQGL--ALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSdyFVSPTAGAVMELLE----DLDGKTVLLVGID 189
Cdd:PRK14183 89 NIDGIlvQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDG--FVPCTPLGVMELLEeyeiDVKGKDVCVVGAS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024392726 190 GALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIIN 250
Cdd:PRK14183 167 NIVGKPMAALLLNANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVID 227
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
39-250 |
6.87e-28 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 111.84 E-value: 6.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 39 ARKITENARKSLASLKREHpRLEPTLAIIQAHNAPLVQEMNKNF---AEEVGLRVINVCLPEDSSKDEIVNEILRLNEDP 115
Cdd:PRK14187 11 ANDITEILATCIDDLKRQH-NLFPCLIVILVGDDPASQLYVRNKqrkAEMLGLRSETILLPSTISESSLIEKINELNNDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 116 NVQGL--ALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSDYFVSPTAGAVMELL----EDLDGKTVLLVGID 189
Cdd:PRK14187 90 SVHGIlvQLPVPNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQKKNCLIPCTPKGCLYLIktitRNLSGSDAVVIGRS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024392726 190 GALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIIN 250
Cdd:PRK14187 170 NIVGKPMACLLLGENCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVID 230
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
17-250 |
3.26e-27 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 111.63 E-value: 3.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 17 SLPFAAAPYRALSGWQAASGQA-ARKITENARKSLASLKrEHPRLEPTLAII----QAHNAPLVQEmNKNFAEEVGLRVI 91
Cdd:PLN02616 59 PSPVINADTGSEGGAKVIDGKAvAKKIRDEITIEVSRMK-ESIGVVPGLAVIlvgdRKDSATYVRN-KKKACDSVGINSF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 92 NVCLPEDSSKDEIVNEILRLNEDPNVQGL--ALDLPESLCSSKILNAVKPEKDVDGLSDINLGRL-VRGEDSdYFVSPTA 168
Cdd:PLN02616 137 EVRLPEDSTEQEVLKFISGFNNDPSVHGIlvQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLaMRGREP-LFVPCTP 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 169 GAVMELLE----DLDGKTVLLVGIDGALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKP 244
Cdd:PLN02616 216 KGCIELLHrynvEIKGKRAVVIGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKP 295
|
....*.
gi 2024392726 245 GTTIIN 250
Cdd:PLN02616 296 GAVVID 301
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
32-258 |
1.61e-26 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 108.06 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 32 QAASGQA-ARKITENARKSLASLKREHPRLePTLAIIQAHNAPLVQ---EMNKNFAEEVGLRVINVCLPEDSSKDEIVNE 107
Cdd:PLN02516 10 QIIDGKAiAKAIRSEIAEEVAQLSEKHGKV-PGLAVVIVGSRKDSQtyvNMKRKACAEVGIKSFDVDLPENISEAELISK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 108 ILRLNEDPNVQGL--ALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSDYFVSPTAGAVMELLE----DLDGK 181
Cdd:PLN02516 89 VHELNANPDVHGIlvQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMKGREPLFLPCTPKGCLELLSrsgiPIKGK 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024392726 182 TVLLVGIDGALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIINCSPDLLSE 258
Cdd:PLN02516 169 KAVVVGRSNIVGLPVSLLLLKADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVSD 245
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
39-249 |
1.82e-26 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 107.74 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 39 ARKITENARKSLASLKREHpRLEPTLAIIQAHNAPLVQEMNKN---FAEEVGLRVINVCLPEDSSKDEIVNEILRLNEDP 115
Cdd:PRK14188 11 AADVRATVAAEVARLKAAH-GVTPGLAVVLVGEDPASQVYVRSkgkQTKEAGMASFEHKLPADTSQAELLALIARLNADP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 116 NVQGL--ALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSdyFVSPT-AGAVMEL---LEDLDGKTVLLVGID 189
Cdd:PRK14188 90 AIHGIlvQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETA--LVPCTpLGCMMLLrrvHGDLSGLNAVVIGRS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 190 GALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTII 249
Cdd:PRK14188 168 NLVGKPMAQLLLAANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVI 227
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
80-250 |
9.80e-26 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 105.63 E-value: 9.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 80 KNFAEEVGLRVINVCLPEDSSKDEIVNEILRLNEDPNVQG--LALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRG 157
Cdd:PRK14172 54 EKVANSLGIDFKKIKLDESISEEDLINEIEELNKDNNVHGimLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 158 EDSdyFVSPTAGAVMELL----EDLDGKTVLLVGIDGALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPK 233
Cdd:PRK14172 134 EKC--FLPCTPNSVITLIkslnIDIEGKEVVVIGRSNIVGKPVAQLLLNENATVTICHSKTKNLKEVCKKADILVVAIGR 211
|
170
....*....|....*..
gi 2024392726 234 PDSVPKSWLKPGTTIIN 250
Cdd:PRK14172 212 PKFIDEEYVKEGAIVID 228
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
37-254 |
5.54e-25 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 103.46 E-value: 5.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 37 QAARKITENARKSLASLKREHprLEPTLAIIQAHNAPLVQEM---NKNFAEEVGLRVINVCLPEDSSKDEIVNEILRLNE 113
Cdd:PRK14175 10 QIAKDYRQGLQDQVEALKEKG--FTPKLSVILVGNDGASQSYvrsKKKAAEKIGMISEIVHLEETATEEEVLNELNRLNN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 114 DPNVQGLALD--LPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSdyFVSPTAGAVMELLE----DLDGKTVLLVG 187
Cdd:PRK14175 88 DDSVSGILVQvpLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQT--FVPCTPLGIMEILKhadiDLEGKNAVVIG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024392726 188 IDGALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIINC--SPD 254
Cdd:PRK14175 166 RSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVgnTPD 234
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
39-250 |
5.77e-25 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 103.60 E-value: 5.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 39 ARKITENARKSLASLKREHPRlEPTLAIIQAHNAPL--VQEMNKNFA-EEVGLRVINVCLPEDSSKDEIVNEILRLNEDP 115
Cdd:PRK14186 11 AAEIEQRLQAQIESNLPKAGR-PPGLAVLRVGDDPAsaVYVRNKEKAcARVGIASFGKHLPADTSQAEVEALIAQLNQDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 116 NVQG--LALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSdyFVSPTAGAVMELLE----DLDGKTVLLVGID 189
Cdd:PRK14186 90 RVDGilLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPG--LRSCTPAGVMRLLRsqqiDIAGKKAVVVGRS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024392726 190 GALGSSLQCLLQRRGA---ITASclwKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIIN 250
Cdd:PRK14186 168 ILVGKPLALMLLAANAtvtIAHS---RTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVD 228
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
36-250 |
7.77e-25 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 103.00 E-value: 7.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 36 GQA-ARKITENARKSLASLKREHPRlEPTLAIIQAHNAPLVQ---EMNKNFAEEVGLRVINVCLPEDSSKDEIVNEILRL 111
Cdd:PRK14192 8 GKAlAKQIEEELSVRVEALKAKTGR-TPILATILVGDDPASAtyvRMKGNACRRVGMDSLKVELPQETTTEQLLAKIEEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 112 NEDPNVQGLALDLP------ESLCsskiLNAVKPEKDVDGLSDINLGRLVRGEDSdyFVSPTAGAVMELLE----DLDGK 181
Cdd:PRK14192 87 NANPDVHGILLQHPvpaqidERAC----FDAISLAKDVDGVTCLGFGRMAMGEAA--YGSATPAGIMRLLKayniELAGK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024392726 182 TVLLVGIDGALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIIN 250
Cdd:PRK14192 161 HAVVVGRSAILGKPMAMMLLNANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVD 229
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
40-249 |
1.14e-24 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 102.69 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 40 RKITENARKSLAslKREHPRLE-----PTLAII--QAHNAPLVQEMNKNFA-EEVGLRVINVCLPEDSSKDEIVNEILRL 111
Cdd:PRK10792 9 KTIAQQVRSEVA--QKVQARVAaglraPGLAVVlvGSDPASQVYVASKRKAcEEVGFVSRSYDLPETTSEAELLALIDEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 112 NEDPNVQG--LALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDsdyFVSP-TAGAVMELLE----DLDGKTVL 184
Cdd:PRK10792 87 NADPTIDGilVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIP---LLRPcTPRGIMTLLErygiDTYGLNAV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024392726 185 LVGIDGALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTII 249
Cdd:PRK10792 164 VVGASNIVGRPMSLELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVI 228
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
11-250 |
1.21e-24 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 103.89 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 11 PMRLCLSLPFAAAPY------RALSGWQAASGQAARKITENARKSLASlkrEHPRLE------PTLAIIQAHNAPLVQEM 78
Cdd:PLN02897 27 PPLVSLDLPENWIPYsdppppVSFETEQKTVVIDGNVIAEEIRTKIAS---EVRKMKkavgkvPGLAVVLVGQQRDSQTY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 79 NKN---FAEEVGLRVINVCLPEDSSKDEIVNEILRLNEDPNVQGL--ALDLPESLCSSKILNAVKPEKDVDGLSDINLGR 153
Cdd:PLN02897 104 VRNkikACEETGIKSLLAELPEDCTEGQILSALRKFNEDTSIHGIlvQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 154 L-VRGEDSdYFVSPTAGAVMELL----EDLDGKTVLLVGIDGALGSSLQCLLQRRGAI--TASCLWKSPglQSKLHHADV 226
Cdd:PLN02897 184 LaMRGREP-LFVSCTPKGCVELLirsgVEIAGKNAVVIGRSNIVGLPMSLLLQRHDATvsTVHAFTKDP--EQITRKADI 260
|
250 260
....*....|....*....|....
gi 2024392726 227 VVAGSPKPDSVPKSWLKPGTTIIN 250
Cdd:PLN02897 261 VIAAAGIPNLVRGSWLKPGAVVID 284
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
39-250 |
7.07e-24 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 100.43 E-value: 7.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 39 ARKITENARKSLASLKREHPRLePTLAIIQAHNAPLVQ---EMNKNFAEEVGLRVINVCLPEDSSKDEIVNEILRLNEDP 115
Cdd:PRK14177 12 SEKIRNEIRETIEERKTKNKRI-PKLATILVGNNPASEtyvSMKVKACHKVGMGSEMIRLKEQTTTEELLGVIDKLNLDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 116 NVQGLALD--LPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSDYFVSPTaGAVMELLE---DLDGKTVLLVGIDG 190
Cdd:PRK14177 91 NVDGILLQhpVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPY-GMVLLLKEygiDVTGKNAVVVGRSP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 191 ALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIIN 250
Cdd:PRK14177 170 ILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLD 229
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
36-250 |
7.67e-24 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 100.47 E-value: 7.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 36 GQAAR-KITENARKSLASLKREHprLEPTLAIIQAHNAPLVQ---EMNKNFAEEVGLRVINVCLPEDSSKDEIVNEILRL 111
Cdd:PRK14193 8 GKATAdEIKADLAERVAALKEKG--ITPGLGTVLVGDDPGSQayvRGKHRDCAEVGITSIRRDLPADATQEELNAVIDEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 112 NEDPNVQG--LALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDsdyfvSP---TAGAVMELLE----DLDGKT 182
Cdd:PRK14193 86 NADPACTGyiVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEP-----APlpcTPRGIVHLLRrydvELAGAH 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 183 VLLVGIDGALGSSLQCLLQRRG--AITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIIN 250
Cdd:PRK14193 161 VVVIGRGVTVGRPIGLLLTRRSenATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLD 230
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
46-250 |
4.93e-23 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 97.99 E-value: 4.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 46 ARKSLASLKRE--HPRLEPTLAIIQAHNAPLVQ---EMNKNFAEEVGLRVINVCLPEDSSKDEIVNEILRLNEDPNVQGL 120
Cdd:PRK14178 9 SEKRLELLKEEiiESGLYPRLATVIVGDDPASQmyvRMKHRACERVGIGSVGIELPGDATTRTVLERIRRLNEDPDINGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 121 --ALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGedSDYFVSPTAGAVMELLE----DLDGKTVLLVGIDGALGS 194
Cdd:PRK14178 89 lvQLPLPKGVDTERVIAAILPEKDVDGFHPLNLGRLVSG--LPGFAPCTPNGIMTLLHeykiSIAGKRAVVVGRSIDVGR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024392726 195 SLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIIN 250
Cdd:PRK14178 167 PMAALLLNADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVID 222
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
38-250 |
6.04e-23 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 98.38 E-value: 6.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 38 AARKITENARKSLASLKREHprLEPTLAIIQAHNAPLVQEMNKN---FAEEVGLRVINVCLPEDSSKDEIVNEILRLNED 114
Cdd:PRK14194 12 AAARVLAQVREDVRTLKAAG--IEPALAVILVGNDPASQVYVRNkilRAEEAGIRSLEHRLPADTSQARLLALIAELNAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 115 PNVQG--LALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDsdyFVSP-TAGAVMELLE----DLDGKTVLLVG 187
Cdd:PRK14194 90 PSVNGilLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRD---VLTPcTPSGCLRLLEdtcgDLTGKHAVVIG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024392726 188 IDGALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIIN 250
Cdd:PRK14194 167 RSNIVGKPMAALLLQAHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVID 229
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
39-250 |
1.83e-22 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 96.55 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 39 ARKITENARKSLASLKREHprLEPTLAIIQAHNAPLVQEMNKN---FAEEVGLRVINVCLPEDSSKDEIVNEILRLNEDP 115
Cdd:PRK14169 10 SKKILADLKQTVAKLAQQD--VTPTLAVVLVGSDPASEVYVRNkqrRAEDIGVRSLMFRLPEATTQADLLAKVAELNHDP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 116 NVQGL--ALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSdyFVSPTAGAVMELLE----DLDGKTVLLVGID 189
Cdd:PRK14169 88 DVDAIlvQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPT--VVASTPYGIMALLDaydiDVAGKRVVIVGRS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024392726 190 GALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIIN 250
Cdd:PRK14169 166 NIVGRPLAGLMVNHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVID 226
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
34-292 |
2.50e-22 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 96.05 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 34 ASGQAARKITENARKSLASLKrehprLEPTLAIIQAHNAP----LVQEMNKNfAEEVGLRVINVCLPEDSSKDEIVNEIL 109
Cdd:PRK14173 7 SGPPAAEAVYAELRARLAKLP-----FVPHLRVVRLGEDPasvsYVRLKDRQ-AKALGLRSQVEVLPESTSQEELLELIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 110 RLNEDPNVQGL--ALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSdyFVSPTAGAVMELLE----DLDGKTV 183
Cdd:PRK14173 81 RLNADPEVDGIlvQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEA--LEPCTPAGVVRLLKhygiPLAGKEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 184 LLVGIDGALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIINCSPD-LLSEKHSY 262
Cdd:PRK14173 159 VVVGRSNIVGKPLAALLLREDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINrVGGNGGRD 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2024392726 263 DQKNSNTTENA------------VCSLAVAMRMQNMVKNTER 292
Cdd:PRK14173 239 ILTGDVHPEVAevagaltpvpggVGPMTVAMLMANTVIAALR 280
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
32-250 |
4.94e-22 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 95.14 E-value: 4.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 32 QAASGQA-ARKITENARKSLASLKREHPRlePTLAIIQAHNAPLVQEMNKNFA---EEVGLRVINVCLPEDSSKDEIVNE 107
Cdd:PRK14189 4 QLIDGNAlSKQLRAEAAQRAAALTARGHQ--PGLAVILVGDNPASQVYVRNKVkacEDNGFHSLKDRYPADLSEAELLAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 108 ILRLNEDPNVQGL--ALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSdyFVSPTAGAVMELLE----DLDGK 181
Cdd:PRK14189 82 IDELNRDPKIHGIlvQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPL--FRPCTPYGVMKMLEsigiPLRGA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024392726 182 TVLLVGIDGALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIIN 250
Cdd:PRK14189 160 HAVVIGRSNIVGKPMAMLLLQAGATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVID 228
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
41-295 |
8.43e-22 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 94.71 E-value: 8.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 41 KITENARKSLASLKREHprLEPTLAIIQAHNAPLVQEMNKNFA---EEVGLRVINVCLPEDSSKDEIVNEILRLNEDPNV 117
Cdd:PRK14166 12 KIKEELKEKNQFLKSKG--IESCLAVILVGDNPASQTYVKSKAkacEECGIKSLVYHLNENTTQNELLALINTLNHDDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 118 QGL--ALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSDyFVSPTAGAVMELLE----DLDGKTVLLVGIDGA 191
Cdd:PRK14166 90 HGIlvQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGLESG-FLPCTPLGVMKLLKayeiDLEGKDAVIIGASNI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 192 LGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIINCSPDLL--------------S 257
Cdd:PRK14166 169 VGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLesgkivgdvdfeevS 248
|
250 260 270
....*....|....*....|....*....|....*...
gi 2024392726 258 EKHSYdqknSNTTENAVCSLAVAMRMQNMVKNTERWIQ 295
Cdd:PRK14166 249 KKSSY----ITPVPGGVGPMTIAMLLENTVKSAKNRLN 282
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
139-251 |
9.83e-22 |
|
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: 91.46 E-value: 9.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 139 PEKDVDGLSDINLGRLVRGEDsdYFVSPTAGAVMELLE----DLDGKTVLLVGIDGALGSSLQCLLQRRGAITASCLWKS 214
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGRP--GFIPCTPAGILELLKrygiDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKT 78
|
90 100 110
....*....|....*....|....*....|....*..
gi 2024392726 215 PGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIINC 251
Cdd:cd01080 79 KNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDV 115
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
39-250 |
2.17e-21 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 93.30 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 39 ARKITENARKSLASLKREHPRlEPTLAIIQAHNAPLVQEM--NKNFA-EEVGLRVINVCLPEDSSKDEIVNEILRLNEDP 115
Cdd:PRK14184 10 AATIREELKTEVAALTARHGR-APGLAVILVGEDPASQVYvrNKERAcEDAGIVSEAFRLPADTTQEELEDLIAELNARP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 116 NVQG--LALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSdyFVSPTAGAVMELLE--DLD--GKTVLLVGID 189
Cdd:PRK14184 89 DIDGilLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPG--FRPCTPAGVMTLLEryGLSpaGKKAVVVGRS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024392726 190 GALGSSLQCLLQRRG----AITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIIN 250
Cdd:PRK14184 167 NIVGKPLALMLGAPGkfanATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVD 231
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
39-250 |
2.77e-21 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 93.30 E-value: 2.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 39 ARKITENARKSLASLKREHPRlePTLAIIQAHNAPLVQ---EMNKNFAEEVGLRVINVCLPEDSSKDEIVNEILRLNEDP 115
Cdd:PRK14167 11 AAQIRDDLTDAIETLEDAGVT--PGLATVLMSDDPASEtyvSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTIDELNADE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 116 NVQGL--ALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSdyFVSPTAGAVMELLE----DLDGKTVLLVGID 189
Cdd:PRK14167 89 DVHGIlvQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDAR--FKPCTPHGIQKLLAaagvDTEGADVVVVGRS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024392726 190 GALGSSLQCLLQRRG----AITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIIN 250
Cdd:PRK14167 167 DIVGKPMANLLIQKAdggnATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVID 231
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
46-250 |
3.68e-21 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 92.71 E-value: 3.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 46 ARKSLASLKREHPRLE------PTLAIIQAHNAP----LVQEMNKNfAEEVGLRVINVCLPEDSSKDEIVNEILRLNEDP 115
Cdd:PRK14171 11 ANEILADLKLEIQELKsqtnasPKLAIVLVGDNPasiiYVKNKIKN-AHKIGIDTLLVNLSTTIHTNDLISKINELNLDN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 116 NVQGL--ALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSDyFVSPTAGAVMELLE----DLDGKTVLLVGID 189
Cdd:PRK14171 90 EISGIivQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSGISQG-FIPCTALGCLAVIKkyepNLTGKNVVIIGRS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024392726 190 GALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIIN 250
Cdd:PRK14171 169 NIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVID 229
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
35-261 |
7.03e-21 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 92.25 E-value: 7.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 35 SGQAARK-ITENARKSLASLKREHPRLePTLAIIQAHNAPLVQE---MNKNFAEEVGLRVINVCLPEDSSKDEIVNEILR 110
Cdd:PRK14168 7 KGTEIREeILEEIRGEVAELKEKYGKV-PGLVTILVGESPASLSyvtLKIKTAHRLGFHEIQDNQSVDITEEELLALIDK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 111 LNEDPNVQGL--ALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSDYFVSPTAGAVMELL----EDLDGKTVL 184
Cdd:PRK14168 86 YNNDDSIHGIlvQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIGGDEVKFLPCTPAGIQEMLvrsgVETSGAEVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 185 LVGIDGALGSSLQCLLQRRG----AITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIINCSPDLLSEKH 260
Cdd:PRK14168 166 VVGRSNIVGKPIANMMTQKGpganATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVNRVGTNE 245
|
.
gi 2024392726 261 S 261
Cdd:PRK14168 246 S 246
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
39-144 |
3.41e-20 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 85.53 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 39 ARKITENARKSLASLKRehPRLEPTLAIIQAHNAPLVQ---EMNKNFAEEVGLRVINVCLPEDSSKDEIVNEILRLNEDP 115
Cdd:pfam00763 7 AKKIREELKEEVAALKA--GGRKPGLAVILVGDDPASQvyvRNKKKACEEVGIESELIRLPEDTTEEELLALIDKLNADP 84
|
90 100 110
....*....|....*....|....*....|.
gi 2024392726 116 NVQG--LALDLPESLCSSKILNAVKPEKDVD 144
Cdd:pfam00763 85 SVHGilVQLPLPKHIDEEKVLEAIDPEKDVD 115
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
39-292 |
7.38e-20 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 89.09 E-value: 7.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 39 ARKITENARKSLASLKREHpRLEPTLAIIQAHNAPLVQ---EMNKNFAEEVGLRVINVCLPEDSSKDEIVNEILRLNEDP 115
Cdd:PRK14176 17 AKKIEAEVRSGVERLKSNR-GITPGLATILVGDDPASKmyvRLKHKACERVGIRAEDQFLPADTTQEELLELIDSLNKRK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 116 NVQG--LALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSdyFVSPTAGAVMELLEDLD----GKTVLLVGID 189
Cdd:PRK14176 96 DVHGilLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEG--LVPCTPHGVIRALEEYGvdieGKNAVIVGHS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 190 GALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIINCSPDLLSEKHSYDQKNSNT 269
Cdd:PRK14176 174 NVVGKPMAAMLLNRNATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITKEEDKVYGDVDFENV 253
|
250 260 270
....*....|....*....|....*....|..
gi 2024392726 270 TENA---------VCSLAVAMRMQNMVKNTER 292
Cdd:PRK14176 254 IKKAslitpvpggVGPLTIAMLMKHVLMCAEK 285
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
36-250 |
1.05e-19 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 88.66 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 36 GQA-ARKITENARKSLASLKREHPrLEPTLAIIQAHNAPLVQEMNKN---FAEEVGLRVINVCLPEDSSKDEIVNEILRL 111
Cdd:PRK14179 7 GKAlAQKMQAELAEKVAKLKEEKG-IVPGLVVILVGDNPASQVYVRNkerSALAAGFKSEVVRLPETISQEELLDLIERY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 112 NEDPNVQGL--ALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSdyFVSPTAGAVMELLE----DLDGKTVLL 185
Cdd:PRK14179 86 NQDPTWHGIlvQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPV--MIPCTPAGIMEMFReynvELEGKHAVV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024392726 186 VGIDGALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIIN 250
Cdd:PRK14179 164 IGRSNIVGKPMAQLLLDKNATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVID 228
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
46-250 |
1.42e-19 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 88.38 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 46 ARKSLASLKRE--HPRLEPTLAIIQAHNAPLVQ---EMNKNFAEEVGLRVINVCLPEDSSKDEIVNEILRLNEDPNVQGL 120
Cdd:PRK14181 9 AEHILATIKENisASSTAPGLAVVLIGNDPASEvyvGMKVKKATDLGMVSKAHRLPSDATLSDILKLIHRLNNDPNIHGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 121 --ALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEdSDYFVSPTAGAVMELLE----DLDGKTVLLVGIDGALGS 194
Cdd:PRK14181 89 lvQLPLPKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGE-TDGFIPCTPAGIIELLKyyeiPLHGRHVAIVGRSNIVGK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 195 SLQCLLQRRGAITASCLW----KSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIIN 250
Cdd:PRK14181 168 PLAALLMQKHPDTNATVTllhsQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVD 227
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
39-254 |
3.10e-19 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 87.44 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 39 ARKITENARKSLASLKREHPRLEPTLAIIQAHNAPLVQEMNKN-FAEEVGLRVINVCLPEDSSKDEIVNEILRLNEDPNV 117
Cdd:PRK14170 11 AKEIQEKVTREVAELVKEGKKPGLAVVLVGDNQASRTYVRNKQkRTEEAGMKSVLIELPENVTEEKLLSVVEELNEDKTI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 118 QGL--ALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSdyFVSPTAGAVMELLED----LDGKTVLLVGIDGA 191
Cdd:PRK14170 91 HGIlvQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDS--FVPCTPAGIIELIKStgtqIEGKRAVVIGRSNI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024392726 192 LGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIINCSPD 254
Cdd:PRK14170 169 VGKPVAQLLLNENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMD 231
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
84-258 |
2.42e-17 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 81.61 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 84 EEVGLRVINVCLPEDSSKDEIVNEILRLNEDPNVQGL--ALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSD 161
Cdd:PRK14182 56 EEVGITSVEHHLPATTTQAELLALIARLNADPAVHGIlvQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 162 YFVSPTAGaVMELLE----DLDGKTVLLVGIDGALGSSLQCLLQRRGAITASCLWKSPGLQSKLHHADVVVAGSPKPDSV 237
Cdd:PRK14182 136 PRPCTPAG-VMRMLDearvDPKGKRALVVGRSNIVGKPMAMMLLERHATVTIAHSRTADLAGEVGRADILVAAIGKAELV 214
|
170 180
....*....|....*....|.
gi 2024392726 238 PKSWLKPGTTIINCSPDLLSE 258
Cdd:PRK14182 215 KGAWVKEGAVVIDVGMNRLAD 235
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
62-292 |
2.33e-16 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 79.09 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 62 PTLAIIQAHNAPLVQEMNKNFAE---EVGLRVINVCLPEDSSKDEIVNEILRLNEDPNVQGLALD--LPESLCSSKILNA 136
Cdd:PRK14174 32 PGLTVIIVGEDPASQVYVRNKAKsckEIGMNSTVIELPADTTEEHLLKKIEDLNNDPDVHGILVQqpLPKQIDEFAVTLA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 137 VKPEKDVDGLSDINLGRLVRGEDSDYFVSPTAGAVMELLEDLD----GKTVLLVGIDGALGSSLQCL----LQRRGAITA 208
Cdd:PRK14174 112 IDPAKDVDGFHPENLGRLVMGHLDKCFVSCTPYGILELLGRYNietkGKHCVVVGRSNIVGKPMANLmlqkLKESNCTVT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 209 SCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIINCSPDLL---SEKHSY------DQKNSNTTENA------ 273
Cdd:PRK14174 192 ICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRIedpSTKSGYrlvgdvDYEGVSAKASAitpvpg 271
|
250 260
....*....|....*....|
gi 2024392726 274 -VCSLAVAMRMQNMVKNTER 292
Cdd:PRK14174 272 gVGPMTIAMLLKNTLQSFER 291
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
84-250 |
3.18e-16 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 78.72 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 84 EEVGLRVINVCLPEDSSKDEIVNEILRLNEDPNVQG--LALDLPESLCSSKILNAVKPEKDVDGLSDINLGRLVRGEDSd 161
Cdd:PRK14185 57 EECGFKSSLIRYESDVTEEELLAKVRELNQDDDVDGfiVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPC- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 162 yFVSPTAGAVMELLE----DLDGKTVLLVGIDGALGSSLQCLLQRRG----AITASCLWKSPGLQSKLHHADVVVAGSPK 233
Cdd:PRK14185 136 -FVSATPNGILELLKryhiETSGKKCVVLGRSNIVGKPMAQLMMQKAypgdCTVTVCHSRSKNLKKECLEADIIIAALGQ 214
|
170
....*....|....*..
gi 2024392726 234 PDSVPKSWLKPGTTIIN 250
Cdd:PRK14185 215 PEFVKADMVKEGAVVID 231
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
55-250 |
7.81e-16 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 77.38 E-value: 7.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 55 REHPRLEPTLAIIQAHNAPLVQ---EMNKNFAEEVGLRVINVCLPEDSSKDEIVNEILRLNEDPNVQGL--ALDLPESLC 129
Cdd:PRK14180 25 KHHTAITPKLVAIIVGNDPASKtyvASKEKACAQVGIDSQVITLPEHTTESELLELIDQLNNDSSVHAIlvQLPLPAHIN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 130 SSKILNAVKPEKDVDGLSDINLGRLvRGEDSDYFVSPTAGAVMELLEDL----DGKTVLLVGIDGALGSSLQCLLQRRGA 205
Cdd:PRK14180 105 KNNVIYSIKPEKDVDGFHPTNVGRL-QLRDKKCLESCTPKGIMTMLREYgiktEGAYAVVVGASNVVGKPVSQLLLNAKA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2024392726 206 ITASCLWKSPGLQSKLHHADVVVAGSPKPDSVPKSWLKPGTTIIN 250
Cdd:PRK14180 184 TVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVID 228
|
|
| NAD_bind_m-THF_DH |
cd01079 |
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ... |
139-288 |
8.00e-06 |
|
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of methylene-tetrahydrofolate dehydrogenase (m-THF DH). M-THF is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. M-THF DH is a component of an unusual monofunctional enzyme; in eukaryotes, m-THF DH is typically found as part of a multifunctional protein. NADP-dependent m-THF DHs in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofunctional DH, as well as bifunctional DH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains only the monofunctional DHs from S. cerevisiae and certain bacteria. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133447 [Multi-domain] Cd Length: 197 Bit Score: 46.27 E-value: 8.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 139 PEKDVDGLSDINLG------RLVRGEDSDYFVSP-TAGAVMELLEDLD-------------GKTVLLVGIDGALGSSLQC 198
Cdd:cd01079 1 PHKDVEGLSHKYIFnlyhniRFLDPENRKKSILPcTPLAIVKILEFLGiynkilpygnrlyGKTITIINRSEVVGRPLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 199 LLQRRGAITAS-------CLWKSPGLQSKLHH--------------ADVVVAGSPKPD-SVPKSWLKPGTTIINCSPDLL 256
Cdd:cd01079 81 LLANDGARVYSvdingiqVFTRGESIRHEKHHvtdeeamtldclsqSDVVITGVPSPNyKVPTELLKDGAICINFASIKN 160
|
170 180 190
....*....|....*....|....*....|..
gi 2024392726 257 SEKHSydQKNSNTTENAVCSLAVAMRMQNMVK 288
Cdd:cd01079 161 FEPSV--KEKASIYVPSIGKVTIAMLLRNLLR 190
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
310-422 |
8.99e-03 |
|
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440255 [Multi-domain] Cd Length: 289 Bit Score: 37.86 E-value: 8.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024392726 310 QPLSPVPSDIEISRAQSPKAVDVLAKEIGLLTDEIEIYGQTKAKVRLSLLERLKDQPDGKYVLVAGITPtplGEGKSTVT 389
Cdd:COG0489 34 AAAAAALAAAAPAAAAPAPLPPAPALLLLLLLLLGLLLLLLLALALLLLLLLLLLRLLLEVIAVTSGKG---GEGKSTVA 110
|
90 100 110
....*....|....*....|....*....|....*...
gi 2024392726 390 IGLVQALtAHLN-----INsfACLRQPSQGPTFGVKAE 422
Cdd:COG0489 111 ANLALAL-AQSGkrvllID--ADLRGPSLHRMLGLENR 145
|
|
| |
