|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02531 |
PLN02531 |
GTP cyclohydrolase I |
1-460 |
0e+00 |
|
GTP cyclohydrolase I
Pssm-ID: 215290 [Multi-domain] Cd Length: 469 Bit Score: 778.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 1 MDTKDEGCLNLELDIGMKNGCIELAFEHQPETLAIQDAVKLLLQGLHEDVNREGIKKTPFRVAKALREGTRGYKQKVKDY 80
Cdd:PLN02531 1 MGALDEGHFNLELDNGVKLDCLELGFEDQPETLAIESAVKVLLQGLGEDVNREGLKKTPLRVAKALREATRGYKQSAKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 81 VQSALFPEAGLDEGVGQAGGVGGLVVVRDLDHYSYCESCLLPFHVKCHIGYVPSGQRVLGLSKFSRVTDVFAKRLQDPQR 160
Cdd:PLN02531 81 VGGALFPEAGLDDGVGHGGGCGGLVVVRDLDLFSYCESCLLPFQVKCHIGYVPSGQRVVGLSKLSRVAEVFAKRLQDPQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 161 LADDICSALQHWVKPAGVAVVLECSHIHFPSLDLDSLNLSSHRGFVKLLVSSGSGVFEDESSNLWGEFQSFLMFKGVKTQ 240
Cdd:PLN02531 161 LADEICSALHHGIKPAGVAVVLECSHIHFPNESLGSLDLSSHQGWVKASVCSGSGVFEDESGNLWEEFVSLLQFRGINVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 241 ALCRNGSSVKEWCPSVKSSSKLSPeVDPEMVSAVVSILKSLGEDPLRKELIATPTRFLKWMLNFQRT-----NLEMKLNS 315
Cdd:PLN02531 241 KRCRKDSSSPCWCPSQDSSSASPE-PNPAMVSAVESILRSLGEDPLRKELVLTPSRFVRWLLNSTQGsrmgrNLEMKLNG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 316 FNPAKVNG---EVKEKRLHCELNMPFWSMCEHHLLPFYGVVHIGYFCAEG--SNPNPVGSSLMKAIVHFYGFKLQVQERM 390
Cdd:PLN02531 320 FACEKMDPlhaNLNEKTMHTELNLPFWSQCEHHLLPFYGVVHVGYFCAEGgrGNRNPISRSLLQSIVHFYGFRLQVQERL 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 391 TRQIAETLSPLVGGDVIVVAEAGHTCMISRGIEKFGSSTATIAVLGRFSSDNSARAMFLDKIHTTNALKT 460
Cdd:PLN02531 400 TRQIAETVSSLLGGDVMVVVEASHTCMISRGVEKFGSSTATIAVLGRFSSDAKARAMFLQSIATTNSSGT 469
|
|
| FolE |
COG0302 |
GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the ... |
264-452 |
4.45e-48 |
|
GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the Pathway/BioSystem: Folate biosynthesis
Pssm-ID: 440071 [Multi-domain] Cd Length: 186 Bit Score: 163.34 E-value: 4.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 264 PEVDPE-MVSAVVSILKSLGEDPLRKELIATPTRFLKwMLNF----QRTNLEMKLNSFNPAKVNGEVKEKrlhcelNMPF 338
Cdd:COG0302 1 DEPDREeIEAAVREILEALGEDPDREGLLDTPKRVAK-AYEElfsgYDQDPAEVLNTTFEEGYDEMVLVK------DIEF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 339 WSMCEHHLLPFYGVVHIGYFcaegsnPNP--VGSSLMKAIVHFYGFKLQVQERMTRQIAETLSPLVG-GDVIVVAEAGHT 415
Cdd:COG0302 74 YSMCEHHLLPFFGKAHVAYI------PNGkvVGLSKLARLVDVFARRPQVQERLTAQIADALQEVLGpRGVAVVIEAEHM 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 42572301 416 CMISRGIEKFGSSTATIAVLGRFSSDNSARAMFLDKI 452
Cdd:COG0302 148 CMTMRGVRKPGSSTVTSAMRGVFREDPATRAEFLSLI 184
|
|
| GTP_cyclohydroI |
pfam01227 |
GTP cyclohydrolase I; This family includes GTP cyclohydrolase enzymes and a family of related ... |
270-450 |
2.04e-45 |
|
GTP cyclohydrolase I; This family includes GTP cyclohydrolase enzymes and a family of related bacterial proteins.
Pssm-ID: 426139 [Multi-domain] Cd Length: 176 Bit Score: 156.15 E-value: 2.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 270 MVSAVVSILKSLGEDPLRKELIATPTRFLKwMLNF----QRTNLEMKLNSFNPAKVNGEVKEKrlhcelNMPFWSMCEHH 345
Cdd:pfam01227 1 IEEAVREILEAIGEDPDREGLLETPKRVAK-MYEElfsgYHEDPEKVLKATFEEGYDEMVLVK------DIEFYSMCEHH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 346 LLPFYGVVHIGYFcaegsnPNP--VGSSLMKAIVHFYGFKLQVQERMTRQIAETLSPLVG-GDVIVVAEAGHTCMISRGI 422
Cdd:pfam01227 74 LLPFFGKAHVAYI------PNGkvIGLSKIARIVDIFARRLQVQERLTAQIADALQEILKpRGVAVVIEAEHLCMTMRGV 147
|
170 180
....*....|....*....|....*...
gi 42572301 423 EKFGSSTATIAVLGRFSSDNSARAMFLD 450
Cdd:pfam01227 148 RKPGSKTVTSAFRGVFKTDPALRAEFLA 175
|
|
| folE |
TIGR00063 |
GTP cyclohydrolase I; alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) ... |
270-452 |
4.56e-42 |
|
GTP cyclohydrolase I; alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) catalyzes the biosynthesis of formic acid and dihydroneopterin triphosphate from GTP. This reaction is the first step in the biosynthesis of tetrahydrofolate in prokaryotes, of tetrahydrobiopterin in vertebrates, and of pteridine-containing pigments in insects. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
Pssm-ID: 129173 [Multi-domain] Cd Length: 180 Bit Score: 147.60 E-value: 4.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 270 MVSAVVSILKSLGEDPLRKELIATPTRFLKWMLNFQRtnlemKLNSFNPAKVNGEVKEKRlHCEL----NMPFWSMCEHH 345
Cdd:TIGR00063 1 IAGAMREILELIGEDLNREGLLETPKRVAKMYVEIFS-----GYDYANFPKITLAIFQEK-HDEMvlvrDITFTSTCEHH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 346 LLPFYGVVHIGYFcaegsnPNP--VGSSLMKAIVHFYGFKLQVQERMTRQIAETLSPLVG-GDVIVVAEAGHTCMISRGI 422
Cdd:TIGR00063 75 LVPFDGKAHVAYI------PKDkvIGLSKIARIVEFFARRPQVQERLTQQIAEALQEILEpNGVAVVVEATHMCMKMRGI 148
|
170 180 190
....*....|....*....|....*....|
gi 42572301 423 EKFGSSTATIAVLGRFSSDNSARAMFLDKI 452
Cdd:TIGR00063 149 RKPGSATVTSALGGLFKSDQKTRAEFLRLV 178
|
|
| GTP_cyclohydro1 |
cd00642 |
GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin ... |
268-452 |
1.47e-41 |
|
GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin triphosphate. The enzyme product is the precursor of tetrahydrofolate in eubacteria, fungi, and plants and of the folate analogs in methanogenic bacteria. In vertebrates and insects it is the biosynthtic precursor of tetrahydrobiopterin (BH4) which is involved in the formation of catacholamines, nitric oxide, and the stimulation of T lymphocytes. The biosynthetic reaction of BH4 is controlled by a regulatory protein GFRP which mediates feedback inhibition of GTP-CH-I by BH4. This inhibition is reversed by phenylalanine. The decameric GTP-CH-I forms a complex with two pentameric GFRP in the presence of phenylalanine or a combination of GTP and BH4, respectively.
Pssm-ID: 238349 [Multi-domain] Cd Length: 185 Bit Score: 146.37 E-value: 1.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 268 PEMVSAVVSILKSLGEDPLRKELIATPTRFLKWMLNFQRtnlemKLNSFNPAKVNGEVKEKRlHCEL----NMPFWSMCE 343
Cdd:cd00642 4 EKIAAAVREILELLGEDPNREGLLETPERVAKAYQEITS-----GYDQALNDPKNTAIFDED-HDEMvivkDITLFSMCE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 344 HHLLPFYGVVHIGYFcaegsnPNP--VGSSLMKAIVHFYGFKLQVQERMTRQIAETLSPLVG-GDVIVVAEAGHTCMISR 420
Cdd:cd00642 78 HHLVPFYGKVHIAYI------PKDkvIGLSKLARIVEFFSRRLQVQERLTKQIAVAIQEILGpQGVAVVIEATHMCMVMR 151
|
170 180 190
....*....|....*....|....*....|..
gi 42572301 421 GIEKFGSSTATIAVLGRFSSDNSARAMFLDKI 452
Cdd:cd00642 152 GVRKPGSKTVTSAMLGVFKEDPKTREEFLRLI 183
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02531 |
PLN02531 |
GTP cyclohydrolase I |
1-460 |
0e+00 |
|
GTP cyclohydrolase I
Pssm-ID: 215290 [Multi-domain] Cd Length: 469 Bit Score: 778.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 1 MDTKDEGCLNLELDIGMKNGCIELAFEHQPETLAIQDAVKLLLQGLHEDVNREGIKKTPFRVAKALREGTRGYKQKVKDY 80
Cdd:PLN02531 1 MGALDEGHFNLELDNGVKLDCLELGFEDQPETLAIESAVKVLLQGLGEDVNREGLKKTPLRVAKALREATRGYKQSAKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 81 VQSALFPEAGLDEGVGQAGGVGGLVVVRDLDHYSYCESCLLPFHVKCHIGYVPSGQRVLGLSKFSRVTDVFAKRLQDPQR 160
Cdd:PLN02531 81 VGGALFPEAGLDDGVGHGGGCGGLVVVRDLDLFSYCESCLLPFQVKCHIGYVPSGQRVVGLSKLSRVAEVFAKRLQDPQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 161 LADDICSALQHWVKPAGVAVVLECSHIHFPSLDLDSLNLSSHRGFVKLLVSSGSGVFEDESSNLWGEFQSFLMFKGVKTQ 240
Cdd:PLN02531 161 LADEICSALHHGIKPAGVAVVLECSHIHFPNESLGSLDLSSHQGWVKASVCSGSGVFEDESGNLWEEFVSLLQFRGINVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 241 ALCRNGSSVKEWCPSVKSSSKLSPeVDPEMVSAVVSILKSLGEDPLRKELIATPTRFLKWMLNFQRT-----NLEMKLNS 315
Cdd:PLN02531 241 KRCRKDSSSPCWCPSQDSSSASPE-PNPAMVSAVESILRSLGEDPLRKELVLTPSRFVRWLLNSTQGsrmgrNLEMKLNG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 316 FNPAKVNG---EVKEKRLHCELNMPFWSMCEHHLLPFYGVVHIGYFCAEG--SNPNPVGSSLMKAIVHFYGFKLQVQERM 390
Cdd:PLN02531 320 FACEKMDPlhaNLNEKTMHTELNLPFWSQCEHHLLPFYGVVHVGYFCAEGgrGNRNPISRSLLQSIVHFYGFRLQVQERL 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 391 TRQIAETLSPLVGGDVIVVAEAGHTCMISRGIEKFGSSTATIAVLGRFSSDNSARAMFLDKIHTTNALKT 460
Cdd:PLN02531 400 TRQIAETVSSLLGGDVMVVVEASHTCMISRGVEKFGSSTATIAVLGRFSSDAKARAMFLQSIATTNSSGT 469
|
|
| FolE |
COG0302 |
GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the ... |
264-452 |
4.45e-48 |
|
GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the Pathway/BioSystem: Folate biosynthesis
Pssm-ID: 440071 [Multi-domain] Cd Length: 186 Bit Score: 163.34 E-value: 4.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 264 PEVDPE-MVSAVVSILKSLGEDPLRKELIATPTRFLKwMLNF----QRTNLEMKLNSFNPAKVNGEVKEKrlhcelNMPF 338
Cdd:COG0302 1 DEPDREeIEAAVREILEALGEDPDREGLLDTPKRVAK-AYEElfsgYDQDPAEVLNTTFEEGYDEMVLVK------DIEF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 339 WSMCEHHLLPFYGVVHIGYFcaegsnPNP--VGSSLMKAIVHFYGFKLQVQERMTRQIAETLSPLVG-GDVIVVAEAGHT 415
Cdd:COG0302 74 YSMCEHHLLPFFGKAHVAYI------PNGkvVGLSKLARLVDVFARRPQVQERLTAQIADALQEVLGpRGVAVVIEAEHM 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 42572301 416 CMISRGIEKFGSSTATIAVLGRFSSDNSARAMFLDKI 452
Cdd:COG0302 148 CMTMRGVRKPGSSTVTSAMRGVFREDPATRAEFLSLI 184
|
|
| GTP_cyclohydroI |
pfam01227 |
GTP cyclohydrolase I; This family includes GTP cyclohydrolase enzymes and a family of related ... |
270-450 |
2.04e-45 |
|
GTP cyclohydrolase I; This family includes GTP cyclohydrolase enzymes and a family of related bacterial proteins.
Pssm-ID: 426139 [Multi-domain] Cd Length: 176 Bit Score: 156.15 E-value: 2.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 270 MVSAVVSILKSLGEDPLRKELIATPTRFLKwMLNF----QRTNLEMKLNSFNPAKVNGEVKEKrlhcelNMPFWSMCEHH 345
Cdd:pfam01227 1 IEEAVREILEAIGEDPDREGLLETPKRVAK-MYEElfsgYHEDPEKVLKATFEEGYDEMVLVK------DIEFYSMCEHH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 346 LLPFYGVVHIGYFcaegsnPNP--VGSSLMKAIVHFYGFKLQVQERMTRQIAETLSPLVG-GDVIVVAEAGHTCMISRGI 422
Cdd:pfam01227 74 LLPFFGKAHVAYI------PNGkvIGLSKIARIVDIFARRLQVQERLTAQIADALQEILKpRGVAVVIEAEHLCMTMRGV 147
|
170 180
....*....|....*....|....*...
gi 42572301 423 EKFGSSTATIAVLGRFSSDNSARAMFLD 450
Cdd:pfam01227 148 RKPGSKTVTSAFRGVFKTDPALRAEFLA 175
|
|
| PLN03044 |
PLN03044 |
GTP cyclohydrolase I; Provisional |
38-187 |
5.28e-45 |
|
GTP cyclohydrolase I; Provisional
Pssm-ID: 215549 [Multi-domain] Cd Length: 188 Bit Score: 155.42 E-value: 5.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 38 AVKLLLQGLHEDVNREGIKKTPFRVAKALREGTRGYKQKVKDYVQSALFPEAGLDEGVGQAGGVgglvvvRDLDHYSYCE 117
Cdd:PLN03044 4 AVRTILECLGEDVEREGLLDTPKRVAKALLFMTQGYDQDPEVVLGTALFHEPEVHDGHEEMVVV------RDIDIHSTCE 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 118 SCLLPFHVKCHIGYVPSGQRVLGLSKFSRVTDVFAKRLQDPQRLADDICSALQHWVKPAGVAVVLECSHI 187
Cdd:PLN03044 78 ETMVPFTGRIHVGYIPNAGVILGLSKLARIAEVYARRLQTQERLTRQIADAIVESVEPLGVMVVVEAAHF 147
|
|
| folE |
PRK09347 |
GTP cyclohydrolase I; Provisional |
268-453 |
1.91e-44 |
|
GTP cyclohydrolase I; Provisional
Pssm-ID: 236472 [Multi-domain] Cd Length: 188 Bit Score: 153.78 E-value: 1.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 268 PEMVSAVVSILKSLGEDPLRKELIATPTRFLKwMLNFQ----RTNLEMKLNS--FNPAKVNGEVKEKrlhcelNMPFWSM 341
Cdd:PRK09347 6 EKIEEAVREILEALGEDPDREGLLDTPKRVAK-MYEELfsgyANDPKEVLNKtfEEEMGYDEMVLVK------DITFYSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 342 CEHHLLPFYGVVHIGYFcaegsnPNP--VGSSLMKAIVHFYGFKLQVQERMTRQIAET----LSPLvggDVIVVAEAGHT 415
Cdd:PRK09347 79 CEHHLLPFIGKAHVAYI------PKGkvIGLSKIARIVDFFARRPQVQERLTAQIADAlqeiLGPR---GVAVVIEAEHM 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 42572301 416 CMISRGIEKFGSSTATIAVLGRFSSDNSARAMFLDKIH 453
Cdd:PRK09347 150 CMTMRGVRKPGSKTVTSALRGLFKTDPATRAEFLSLIR 187
|
|
| FolE |
COG0302 |
GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the ... |
34-186 |
7.82e-44 |
|
GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the Pathway/BioSystem: Folate biosynthesis
Pssm-ID: 440071 [Multi-domain] Cd Length: 186 Bit Score: 152.17 E-value: 7.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 34 AIQDAVKLLLQGLHEDVNREGIKKTPFRVAKALREGTRGYKQKVKDYVqSALFpEAGLDEgvgqaggvggLVVVRDLDHY 113
Cdd:COG0302 7 EIEAAVREILEALGEDPDREGLLDTPKRVAKAYEELFSGYDQDPAEVL-NTTF-EEGYDE----------MVLVKDIEFY 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42572301 114 SYCESCLLPFHVKCHIGYVPSGqRVLGLSKFSRVTDVFAKRLQDPQRLADDICSALQHWVKPAGVAVVLECSH 186
Cdd:COG0302 75 SMCEHHLLPFFGKAHVAYIPNG-KVVGLSKLARLVDVFARRPQVQERLTAQIADALQEVLGPRGVAVVIEAEH 146
|
|
| PTZ00484 |
PTZ00484 |
GTP cyclohydrolase I; Provisional |
34-187 |
2.22e-43 |
|
GTP cyclohydrolase I; Provisional
Pssm-ID: 240434 Cd Length: 259 Bit Score: 153.48 E-value: 2.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 34 AIQDAVKLLLQGLH-EDVNREGIKKTPFRVAKALREGTRGYKQKVKDYVQSALFpeagldegVGQAGGVGGLVVVRDLDH 112
Cdd:PTZ00484 75 AIESARRKILKSLEgEDPDRDGLKKTPKRVAKALEFLTKGYHMSVEEVIKKALF--------KVEPKNNDEMVKVRDIDI 146
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42572301 113 YSYCESCLLPFHVKCHIGYVPSgQRVLGLSKFSRVTDVFAKRLQDPQRLADDICSALQHWVKPAGVAVVLECSHI 187
Cdd:PTZ00484 147 FSLCEHHLLPFEGECTIGYIPN-KKVLGLSKFARIIEIFSRRLQVQERLTQQIANALQKYLKPMGVAVVIVASHM 220
|
|
| folE |
PRK09347 |
GTP cyclohydrolase I; Provisional |
34-186 |
9.31e-43 |
|
GTP cyclohydrolase I; Provisional
Pssm-ID: 236472 [Multi-domain] Cd Length: 188 Bit Score: 149.54 E-value: 9.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 34 AIQDAVKLLLQGLHEDVNREGIKKTPFRVAKALREGTRGYKQKVKDYVQSALFPEAGLDEgvgqaggvggLVVVRDLDHY 113
Cdd:PRK09347 7 KIEEAVREILEALGEDPDREGLLDTPKRVAKMYEELFSGYANDPKEVLNKTFEEEMGYDE----------MVLVKDITFY 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42572301 114 SYCESCLLPFHVKCHIGYVPSGqRVLGLSKFSRVTDVFAKRLQDPQRLADDICSALQHWVKPAGVAVVLECSH 186
Cdd:PRK09347 77 SMCEHHLLPFIGKAHVAYIPKG-KVIGLSKIARIVDFFARRPQVQERLTAQIADALQEILGPRGVAVVIEAEH 148
|
|
| folE |
TIGR00063 |
GTP cyclohydrolase I; alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) ... |
270-452 |
4.56e-42 |
|
GTP cyclohydrolase I; alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) catalyzes the biosynthesis of formic acid and dihydroneopterin triphosphate from GTP. This reaction is the first step in the biosynthesis of tetrahydrofolate in prokaryotes, of tetrahydrobiopterin in vertebrates, and of pteridine-containing pigments in insects. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
Pssm-ID: 129173 [Multi-domain] Cd Length: 180 Bit Score: 147.60 E-value: 4.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 270 MVSAVVSILKSLGEDPLRKELIATPTRFLKWMLNFQRtnlemKLNSFNPAKVNGEVKEKRlHCEL----NMPFWSMCEHH 345
Cdd:TIGR00063 1 IAGAMREILELIGEDLNREGLLETPKRVAKMYVEIFS-----GYDYANFPKITLAIFQEK-HDEMvlvrDITFTSTCEHH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 346 LLPFYGVVHIGYFcaegsnPNP--VGSSLMKAIVHFYGFKLQVQERMTRQIAETLSPLVG-GDVIVVAEAGHTCMISRGI 422
Cdd:TIGR00063 75 LVPFDGKAHVAYI------PKDkvIGLSKIARIVEFFARRPQVQERLTQQIAEALQEILEpNGVAVVVEATHMCMKMRGI 148
|
170 180 190
....*....|....*....|....*....|
gi 42572301 423 EKFGSSTATIAVLGRFSSDNSARAMFLDKI 452
Cdd:TIGR00063 149 RKPGSATVTSALGGLFKSDQKTRAEFLRLV 178
|
|
| GTP_cyclohydro1 |
cd00642 |
GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin ... |
268-452 |
1.47e-41 |
|
GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin triphosphate. The enzyme product is the precursor of tetrahydrofolate in eubacteria, fungi, and plants and of the folate analogs in methanogenic bacteria. In vertebrates and insects it is the biosynthtic precursor of tetrahydrobiopterin (BH4) which is involved in the formation of catacholamines, nitric oxide, and the stimulation of T lymphocytes. The biosynthetic reaction of BH4 is controlled by a regulatory protein GFRP which mediates feedback inhibition of GTP-CH-I by BH4. This inhibition is reversed by phenylalanine. The decameric GTP-CH-I forms a complex with two pentameric GFRP in the presence of phenylalanine or a combination of GTP and BH4, respectively.
Pssm-ID: 238349 [Multi-domain] Cd Length: 185 Bit Score: 146.37 E-value: 1.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 268 PEMVSAVVSILKSLGEDPLRKELIATPTRFLKWMLNFQRtnlemKLNSFNPAKVNGEVKEKRlHCEL----NMPFWSMCE 343
Cdd:cd00642 4 EKIAAAVREILELLGEDPNREGLLETPERVAKAYQEITS-----GYDQALNDPKNTAIFDED-HDEMvivkDITLFSMCE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 344 HHLLPFYGVVHIGYFcaegsnPNP--VGSSLMKAIVHFYGFKLQVQERMTRQIAETLSPLVG-GDVIVVAEAGHTCMISR 420
Cdd:cd00642 78 HHLVPFYGKVHIAYI------PKDkvIGLSKLARIVEFFSRRLQVQERLTKQIAVAIQEILGpQGVAVVIEATHMCMVMR 151
|
170 180 190
....*....|....*....|....*....|..
gi 42572301 421 GIEKFGSSTATIAVLGRFSSDNSARAMFLDKI 452
Cdd:cd00642 152 GVRKPGSKTVTSAMLGVFKEDPKTREEFLRLI 183
|
|
| PLN03044 |
PLN03044 |
GTP cyclohydrolase I; Provisional |
270-452 |
1.23e-40 |
|
GTP cyclohydrolase I; Provisional
Pssm-ID: 215549 [Multi-domain] Cd Length: 188 Bit Score: 143.86 E-value: 1.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 270 MVSAVVSILKSLGEDPLRKELIATPTRFLKWMLNF-----QRTNLEMKLNSFNPAKVNGEVKEKRLhcELNMPFWSMCEH 344
Cdd:PLN03044 1 MEQAVRTILECLGEDVEREGLLDTPKRVAKALLFMtqgydQDPEVVLGTALFHEPEVHDGHEEMVV--VRDIDIHSTCEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 345 HLLPFYGVVHIGYFcaegsnPNP---VGSSLMKAIVHFYGFKLQVQERMTRQIAETLSPLVG-GDVIVVAEAGHTCMISR 420
Cdd:PLN03044 79 TMVPFTGRIHVGYI------PNAgviLGLSKLARIAEVYARRLQTQERLTRQIADAIVESVEpLGVMVVVEAAHFCMVMR 152
|
170 180 190
....*....|....*....|....*....|..
gi 42572301 421 GIEKFGSSTATIAVLGRFSSDNSARAMFLDKI 452
Cdd:PLN03044 153 GVEKHGASTTTSAVRGCFASNPKLRAEFFRII 184
|
|
| GTP_cyclohydroI |
pfam01227 |
GTP cyclohydrolase I; This family includes GTP cyclohydrolase enzymes and a family of related ... |
35-186 |
1.08e-39 |
|
GTP cyclohydrolase I; This family includes GTP cyclohydrolase enzymes and a family of related bacterial proteins.
Pssm-ID: 426139 [Multi-domain] Cd Length: 176 Bit Score: 140.74 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 35 IQDAVKLLLQGLHEDVNREGIKKTPFRVAKALREGTRGYKQKVKDyVQSALFpEAGLDEGVGQaggvgglvvvRDLDHYS 114
Cdd:pfam01227 1 IEEAVREILEAIGEDPDREGLLETPKRVAKMYEELFSGYHEDPEK-VLKATF-EEGYDEMVLV----------KDIEFYS 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42572301 115 YCESCLLPFHVKCHIGYVPSGqRVLGLSKFSRVTDVFAKRLQDPQRLADDICSALQHWVKPAGVAVVLECSH 186
Cdd:pfam01227 69 MCEHHLLPFFGKAHVAYIPNG-KVIGLSKIARIVDIFARRLQVQERLTAQIADALQEILKPRGVAVVIEAEH 139
|
|
| PRK12606 |
PRK12606 |
GTP cyclohydrolase I; Reviewed |
22-187 |
1.48e-37 |
|
GTP cyclohydrolase I; Reviewed
Pssm-ID: 237149 Cd Length: 201 Bit Score: 136.03 E-value: 1.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 22 IELAFEHQPETLAIQDAVKLLLQGLHEDVNREGIKKTPFRVAKALREGTRGYKQKVKDYVqSALFpEAGLDEGVGQaggv 101
Cdd:PRK12606 9 AEIRRGRRFDPPALEAAVRELLEALGEDPDREGLLDTPQRVAKAMQYLCDGYEQDPAEAL-GALF-DSDNDEMVIV---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 102 gglvvvRDLDHYSYCESCLLPFHVKCHIGYVPSGqRVLGLSKFSRVTDVFAKRLQDPQRLADDICSALQHWVKPAGVAVV 181
Cdd:PRK12606 83 ------RDIELYSLCEHHLLPFIGVAHVAYLPGG-KVLGLSKIARIVDMFARRLQIQENLTRQIATAVVTVTQARGAAVV 155
|
....*.
gi 42572301 182 LECSHI 187
Cdd:PRK12606 156 IEAEHL 161
|
|
| GTP_cyclohydro1 |
cd00642 |
GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin ... |
35-186 |
6.79e-37 |
|
GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin triphosphate. The enzyme product is the precursor of tetrahydrofolate in eubacteria, fungi, and plants and of the folate analogs in methanogenic bacteria. In vertebrates and insects it is the biosynthtic precursor of tetrahydrobiopterin (BH4) which is involved in the formation of catacholamines, nitric oxide, and the stimulation of T lymphocytes. The biosynthetic reaction of BH4 is controlled by a regulatory protein GFRP which mediates feedback inhibition of GTP-CH-I by BH4. This inhibition is reversed by phenylalanine. The decameric GTP-CH-I forms a complex with two pentameric GFRP in the presence of phenylalanine or a combination of GTP and BH4, respectively.
Pssm-ID: 238349 [Multi-domain] Cd Length: 185 Bit Score: 133.66 E-value: 6.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 35 IQDAVKLLLQGLHEDVNREGIKKTPFRVAKALREGTRGYKQKVKDYVQSALFPEaGLDEGVGQaggvgglvvvRDLDHYS 114
Cdd:cd00642 6 IAAAVREILELLGEDPNREGLLETPERVAKAYQEITSGYDQALNDPKNTAIFDE-DHDEMVIV----------KDITLFS 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42572301 115 YCESCLLPFHVKCHIGYVPSGqRVLGLSKFSRVTDVFAKRLQDPQRLADDICSALQHWVKPAGVAVVLECSH 186
Cdd:cd00642 75 MCEHHLVPFYGKVHIAYIPKD-KVIGLSKLARIVEFFSRRLQVQERLTKQIAVAIQEILGPQGVAVVIEATH 145
|
|
| PTZ00484 |
PTZ00484 |
GTP cyclohydrolase I; Provisional |
254-452 |
5.33e-35 |
|
GTP cyclohydrolase I; Provisional
Pssm-ID: 240434 Cd Length: 259 Bit Score: 131.13 E-value: 5.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 254 PSVKSSSKLSPEVDPEMVSAVVSILKSL-GEDPLRKELIATPTRFLKWMLNFQRtNLEMKLN--------SFNPAKVNGE 324
Cdd:PTZ00484 60 ESSPTCATLMEEKKGAIESARRKILKSLeGEDPDRDGLKKTPKRVAKALEFLTK-GYHMSVEevikkalfKVEPKNNDEM 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 325 VKEKRLHcelnmpFWSMCEHHLLPFYGVVHIGYFcaegsnPNP--VGSSLMKAIVHFYGFKLQVQERMTRQIAETLSPLV 402
Cdd:PTZ00484 139 VKVRDID------IFSLCEHHLLPFEGECTIGYI------PNKkvLGLSKFARIIEIFSRRLQVQERLTQQIANALQKYL 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 42572301 403 GG-DVIVVAEAGHTCMISRGIEKFGSSTATIAVLGRFSSDNSARAMFLDKI 452
Cdd:PTZ00484 207 KPmGVAVVIVASHMCMNMRGVQKHDASTTTSAYLGVFRSDPKLRAEFFSLI 257
|
|
| PRK12606 |
PRK12606 |
GTP cyclohydrolase I; Reviewed |
268-453 |
3.32e-34 |
|
GTP cyclohydrolase I; Reviewed
Pssm-ID: 237149 Cd Length: 201 Bit Score: 127.17 E-value: 3.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 268 PEMVSAVVSILKSLGEDPLRKELIATPTRFLKWMlnfQRTnlemkLNSF--NPAKVNGEVKEKRlHCEL----NMPFWSM 341
Cdd:PRK12606 20 PALEAAVRELLEALGEDPDREGLLDTPQRVAKAM---QYL-----CDGYeqDPAEALGALFDSD-NDEMvivrDIELYSL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 342 CEHHLLPFYGVVHIGYFcaegsnpnPVGS----SLMKAIVHFYGFKLQVQERMTRQIAETL-SPLVGGDVIVVAEAGHTC 416
Cdd:PRK12606 91 CEHHLLPFIGVAHVAYL--------PGGKvlglSKIARIVDMFARRLQIQENLTRQIATAVvTVTQARGAAVVIEAEHLC 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 42572301 417 MISRGIEKFGSSTATIAVLGRFSSDNSARAMFLDKIH 453
Cdd:PRK12606 163 MMMRGVRKQNSRMITSVMLGAFRDSAQTRNEFLRLIG 199
|
|
| TFold |
cd00651 |
Tunnelling fold (T-fold). The five known T-folds are found in five different enzymes with ... |
338-436 |
6.44e-03 |
|
Tunnelling fold (T-fold). The five known T-folds are found in five different enzymes with different functions: dihydroneopterin-triphosphate epimerase (DHNTPE), dihydroneopterin aldolase (DHNA) , GTP cyclohydrolase I (GTPCH-1), 6-pyrovoyl tetrahydropterin synthetase (PTPS), and uricase (UO,uroate/urate oxidase). They bind to substrates belonging to the purine or pterin families, and share a fold-related binding site with a glutamate or glutamine residue anchoring the substrate and a lot of conserved interactions. They also share a similar oligomerization mode: several T-folds join together to form a beta(2n)alpha(n) barrel, then two barrels join together in a head-to-head fashion to made up the native enzymes. The functional enzyme is a tetramer for UO, a hexamer for PTPS, an octamer for DHNA/DHNTPE and a decamer for GTPCH-1. The substrate is located in a deep and narrow pocket at the interface between monomers. In PTPS, the active site is located at the interface of three monomers, two from one trimer and one from the other trimer. In GTPCH-1, it is also located at the interface of three subunits, two from one pentamer and one from the other pentamer. There are four equivalent active sites in UO, six in PTPS, eight in DHNA/DHNTPE and ten in GTPCH-1. Each globular multimeric enzyme encloses a tunnel which is lined with charged residues for DHNA and UO, and with basic residues in PTPS. The N and C-terminal ends are located on one side of the T-fold while the residues involved in the catalytic activity are located at the opposite side. In PTPS, UO and DHNA/DHNTPE, the N and C-terminal extremities of the enzyme are located on the exterior side of the functional multimeric enzyme. In GTPCH-1, the extra C-terminal helix places the extremity inside the tunnel.
Pssm-ID: 238351 Cd Length: 122 Bit Score: 36.65 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572301 338 FWSMC----EHHLLPFYGVVHIGYF--CAEGSNPNPVGSSLMKAIV----HFYGFKLQVQERMTRQIAETL---SPLVGG 404
Cdd:cd00651 11 KVTRLgfvtLERTVGQIFEVDVTLSwdGKKAAASDDVATDTVYNTIyrlaKEYVEGSQLIERLAEEIAYLIaehFLSSVA 90
|
90 100 110
....*....|....*....|....*....|..
gi 42572301 405 DVIVVAEAGHTCMISRGIEKFGSSTATIAVLG 436
Cdd:cd00651 91 EVKVEEKKPHAVIPDRGVFKPTDSPGVTIERG 122
|
|
| |
