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Conserved domains on  [gi|2056190682|gb|QWV86534|]
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GTP cyclohydrolase I FolE [Streptococcus parasuis]

Protein Classification

GTP cyclohydrolase I( domain architecture ID 10001019)

GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin triphosphate

EC:  3.5.4.16
Gene Symbol:  folE
PubMed:  12559918|10737935
SCOP:  4001710

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FolE COG0302
GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the ...
3-186 2.44e-114

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: 322.43  E-value: 2.44e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682   3 KQEQIEQTIYQLLELLGEDPNREGLLDTPKRVAKMYLEMFNGLKEDPKDQFTAVFSEGHEEVVLVKDIPFHSMCEHHLVP 82
Cdd:COG0302     4 DREEIEAAVREILEALGEDPDREGLLDTPKRVAKAYEELFSGYDQDPAEVLNTTFEEGYDEMVLVKDIEFYSMCEHHLLP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682  83 FYGIAHVAYIPsKGRVTGLSKLARAVEVASRRPQLQERLTHQVAHALQDALEPEGVFVMVEAEHMCMSMRGIRKPGSKTV 162
Cdd:COG0302    84 FFGKAHVAYIP-NGKVVGLSKLARLVDVFARRPQVQERLTAQIADALQEVLGPRGVAVVIEAEHMCMTMRGVRKPGSSTV 162
                         170       180
                  ....*....|....*....|....
gi 2056190682 163 TTVALGKYKEDAVLRRELLSMIHN 186
Cdd:COG0302   163 TSAMRGVFREDPATRAEFLSLIRG 186
 
Name Accession Description Interval E-value
FolE COG0302
GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the ...
3-186 2.44e-114

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: 322.43  E-value: 2.44e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682   3 KQEQIEQTIYQLLELLGEDPNREGLLDTPKRVAKMYLEMFNGLKEDPKDQFTAVFSEGHEEVVLVKDIPFHSMCEHHLVP 82
Cdd:COG0302     4 DREEIEAAVREILEALGEDPDREGLLDTPKRVAKAYEELFSGYDQDPAEVLNTTFEEGYDEMVLVKDIEFYSMCEHHLLP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682  83 FYGIAHVAYIPsKGRVTGLSKLARAVEVASRRPQLQERLTHQVAHALQDALEPEGVFVMVEAEHMCMSMRGIRKPGSKTV 162
Cdd:COG0302    84 FFGKAHVAYIP-NGKVVGLSKLARLVDVFARRPQVQERLTAQIADALQEVLGPRGVAVVIEAEHMCMTMRGVRKPGSSTV 162
                         170       180
                  ....*....|....*....|....
gi 2056190682 163 TTVALGKYKEDAVLRRELLSMIHN 186
Cdd:COG0302   163 TSAMRGVFREDPATRAEFLSLIRG 186
folE PRK09347
GTP cyclohydrolase I; Provisional
3-186 5.58e-112

GTP cyclohydrolase I; Provisional


Pssm-ID: 236472 [Multi-domain]  Cd Length: 188  Bit Score: 316.72  E-value: 5.58e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682   3 KQEQIEQTIYQLLELLGEDPNREGLLDTPKRVAKMYLEMFNGLKEDPKDQFTAVFSE--GHEEVVLVKDIPFHSMCEHHL 80
Cdd:PRK09347    4 DKEKIEEAVREILEALGEDPDREGLLDTPKRVAKMYEELFSGYANDPKEVLNKTFEEemGYDEMVLVKDITFYSMCEHHL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682  81 VPFYGIAHVAYIPsKGRVTGLSKLARAVEVASRRPQLQERLTHQVAHALQDALEPEGVFVMVEAEHMCMSMRGIRKPGSK 160
Cdd:PRK09347   84 LPFIGKAHVAYIP-KGKVIGLSKIARIVDFFARRPQVQERLTAQIADALQEILGPRGVAVVIEAEHMCMTMRGVRKPGSK 162
                         170       180
                  ....*....|....*....|....*.
gi 2056190682 161 TVTTVALGKYKEDAVLRRELLSMIHN 186
Cdd:PRK09347  163 TVTSALRGLFKTDPATRAEFLSLIRH 188
GTP_cyclohydroI pfam01227
GTP cyclohydrolase I; This family includes GTP cyclohydrolase enzymes and a family of related ...
7-183 2.60e-104

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: 296.75  E-value: 2.60e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682   7 IEQTIYQLLELLGEDPNREGLLDTPKRVAKMYLEMFNGLKEDPKDQFTAVFSEGHEEVVLVKDIPFHSMCEHHLVPFYGI 86
Cdd:pfam01227   1 IEEAVREILEAIGEDPDREGLLETPKRVAKMYEELFSGYHEDPEKVLKATFEEGYDEMVLVKDIEFYSMCEHHLLPFFGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682  87 AHVAYIPsKGRVTGLSKLARAVEVASRRPQLQERLTHQVAHALQDALEPEGVFVMVEAEHMCMSMRGIRKPGSKTVTTVA 166
Cdd:pfam01227  81 AHVAYIP-NGKVIGLSKIARIVDIFARRLQVQERLTAQIADALQEILKPRGVAVVIEAEHLCMTMRGVRKPGSKTVTSAF 159
                         170
                  ....*....|....*..
gi 2056190682 167 LGKYKEDAVLRRELLSM 183
Cdd:pfam01227 160 RGVFKTDPALRAEFLAL 176
GTP_cyclohydro1 cd00642
GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin ...
3-184 2.14e-93

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: 269.64  E-value: 2.14e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682   3 KQEQIEQTIYQLLELLGEDPNREGLLDTPKRVAKMYLEMFNGLKEDPKD-QFTAVFSEGHEEVVLVKDIPFHSMCEHHLV 81
Cdd:cd00642     2 RLEKIAAAVREILELLGEDPNREGLLETPERVAKAYQEITSGYDQALNDpKNTAIFDEDHDEMVIVKDITLFSMCEHHLV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682  82 PFYGIAHVAYIPsKGRVTGLSKLARAVEVASRRPQLQERLTHQVAHALQDALEPEGVFVMVEAEHMCMSMRGIRKPGSKT 161
Cdd:cd00642    82 PFYGKVHIAYIP-KDKVIGLSKLARIVEFFSRRLQVQERLTKQIAVAIQEILGPQGVAVVIEATHMCMVMRGVRKPGSKT 160
                         170       180
                  ....*....|....*....|...
gi 2056190682 162 VTTVALGKYKEDAVLRRELLSMI 184
Cdd:cd00642   161 VTSAMLGVFKEDPKTREEFLRLI 183
folE TIGR00063
GTP cyclohydrolase I; alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) ...
7-184 6.28e-89

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: 258.15  E-value: 6.28e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682   7 IEQTIYQLLELLGEDPNREGLLDTPKRVAKMYLEMFNGLKEDPKDQFT-AVFSEGHEEVVLVKDIPFHSMCEHHLVPFYG 85
Cdd:TIGR00063   1 IAGAMREILELIGEDLNREGLLETPKRVAKMYVEIFSGYDYANFPKITlAIFQEKHDEMVLVRDITFTSTCEHHLVPFDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682  86 IAHVAYIPsKGRVTGLSKLARAVEVASRRPQLQERLTHQVAHALQDALEPEGVFVMVEAEHMCMSMRGIRKPGSKTVTTV 165
Cdd:TIGR00063  81 KAHVAYIP-KDKVIGLSKIARIVEFFARRPQVQERLTQQIAEALQEILEPNGVAVVVEATHMCMKMRGIRKPGSATVTSA 159
                         170
                  ....*....|....*....
gi 2056190682 166 ALGKYKEDAVLRRELLSMI 184
Cdd:TIGR00063 160 LGGLFKSDQKTRAEFLRLV 178
 
Name Accession Description Interval E-value
FolE COG0302
GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the ...
3-186 2.44e-114

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: 322.43  E-value: 2.44e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682   3 KQEQIEQTIYQLLELLGEDPNREGLLDTPKRVAKMYLEMFNGLKEDPKDQFTAVFSEGHEEVVLVKDIPFHSMCEHHLVP 82
Cdd:COG0302     4 DREEIEAAVREILEALGEDPDREGLLDTPKRVAKAYEELFSGYDQDPAEVLNTTFEEGYDEMVLVKDIEFYSMCEHHLLP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682  83 FYGIAHVAYIPsKGRVTGLSKLARAVEVASRRPQLQERLTHQVAHALQDALEPEGVFVMVEAEHMCMSMRGIRKPGSKTV 162
Cdd:COG0302    84 FFGKAHVAYIP-NGKVVGLSKLARLVDVFARRPQVQERLTAQIADALQEVLGPRGVAVVIEAEHMCMTMRGVRKPGSSTV 162
                         170       180
                  ....*....|....*....|....
gi 2056190682 163 TTVALGKYKEDAVLRRELLSMIHN 186
Cdd:COG0302   163 TSAMRGVFREDPATRAEFLSLIRG 186
folE PRK09347
GTP cyclohydrolase I; Provisional
3-186 5.58e-112

GTP cyclohydrolase I; Provisional


Pssm-ID: 236472 [Multi-domain]  Cd Length: 188  Bit Score: 316.72  E-value: 5.58e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682   3 KQEQIEQTIYQLLELLGEDPNREGLLDTPKRVAKMYLEMFNGLKEDPKDQFTAVFSE--GHEEVVLVKDIPFHSMCEHHL 80
Cdd:PRK09347    4 DKEKIEEAVREILEALGEDPDREGLLDTPKRVAKMYEELFSGYANDPKEVLNKTFEEemGYDEMVLVKDITFYSMCEHHL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682  81 VPFYGIAHVAYIPsKGRVTGLSKLARAVEVASRRPQLQERLTHQVAHALQDALEPEGVFVMVEAEHMCMSMRGIRKPGSK 160
Cdd:PRK09347   84 LPFIGKAHVAYIP-KGKVIGLSKIARIVDFFARRPQVQERLTAQIADALQEILGPRGVAVVIEAEHMCMTMRGVRKPGSK 162
                         170       180
                  ....*....|....*....|....*.
gi 2056190682 161 TVTTVALGKYKEDAVLRRELLSMIHN 186
Cdd:PRK09347  163 TVTSALRGLFKTDPATRAEFLSLIRH 188
GTP_cyclohydroI pfam01227
GTP cyclohydrolase I; This family includes GTP cyclohydrolase enzymes and a family of related ...
7-183 2.60e-104

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: 296.75  E-value: 2.60e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682   7 IEQTIYQLLELLGEDPNREGLLDTPKRVAKMYLEMFNGLKEDPKDQFTAVFSEGHEEVVLVKDIPFHSMCEHHLVPFYGI 86
Cdd:pfam01227   1 IEEAVREILEAIGEDPDREGLLETPKRVAKMYEELFSGYHEDPEKVLKATFEEGYDEMVLVKDIEFYSMCEHHLLPFFGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682  87 AHVAYIPsKGRVTGLSKLARAVEVASRRPQLQERLTHQVAHALQDALEPEGVFVMVEAEHMCMSMRGIRKPGSKTVTTVA 166
Cdd:pfam01227  81 AHVAYIP-NGKVIGLSKIARIVDIFARRLQVQERLTAQIADALQEILKPRGVAVVIEAEHLCMTMRGVRKPGSKTVTSAF 159
                         170
                  ....*....|....*..
gi 2056190682 167 LGKYKEDAVLRRELLSM 183
Cdd:pfam01227 160 RGVFKTDPALRAEFLAL 176
GTP_cyclohydro1 cd00642
GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin ...
3-184 2.14e-93

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: 269.64  E-value: 2.14e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682   3 KQEQIEQTIYQLLELLGEDPNREGLLDTPKRVAKMYLEMFNGLKEDPKD-QFTAVFSEGHEEVVLVKDIPFHSMCEHHLV 81
Cdd:cd00642     2 RLEKIAAAVREILELLGEDPNREGLLETPERVAKAYQEITSGYDQALNDpKNTAIFDEDHDEMVIVKDITLFSMCEHHLV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682  82 PFYGIAHVAYIPsKGRVTGLSKLARAVEVASRRPQLQERLTHQVAHALQDALEPEGVFVMVEAEHMCMSMRGIRKPGSKT 161
Cdd:cd00642    82 PFYGKVHIAYIP-KDKVIGLSKLARIVEFFSRRLQVQERLTKQIAVAIQEILGPQGVAVVIEATHMCMVMRGVRKPGSKT 160
                         170       180
                  ....*....|....*....|...
gi 2056190682 162 VTTVALGKYKEDAVLRRELLSMI 184
Cdd:cd00642   161 VTSAMLGVFKEDPKTREEFLRLI 183
folE TIGR00063
GTP cyclohydrolase I; alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) ...
7-184 6.28e-89

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: 258.15  E-value: 6.28e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682   7 IEQTIYQLLELLGEDPNREGLLDTPKRVAKMYLEMFNGLKEDPKDQFT-AVFSEGHEEVVLVKDIPFHSMCEHHLVPFYG 85
Cdd:TIGR00063   1 IAGAMREILELIGEDLNREGLLETPKRVAKMYVEIFSGYDYANFPKITlAIFQEKHDEMVLVRDITFTSTCEHHLVPFDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682  86 IAHVAYIPsKGRVTGLSKLARAVEVASRRPQLQERLTHQVAHALQDALEPEGVFVMVEAEHMCMSMRGIRKPGSKTVTTV 165
Cdd:TIGR00063  81 KAHVAYIP-KDKVIGLSKIARIVEFFARRPQVQERLTQQIAEALQEILEPNGVAVVVEATHMCMKMRGIRKPGSATVTSA 159
                         170
                  ....*....|....*....
gi 2056190682 166 ALGKYKEDAVLRRELLSMI 184
Cdd:TIGR00063 160 LGGLFKSDQKTRAEFLRLV 178
PRK12606 PRK12606
GTP cyclohydrolase I; Reviewed
4-187 3.71e-80

GTP cyclohydrolase I; Reviewed


Pssm-ID: 237149  Cd Length: 201  Bit Score: 236.96  E-value: 3.71e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682   4 QEQIEQTIYQLLELLGEDPNREGLLDTPKRVAKMYLEMFNGLKEDPKDQFTAVFSEGHEEVVLVKDIPFHSMCEHHLVPF 83
Cdd:PRK12606   19 PPALEAAVRELLEALGEDPDREGLLDTPQRVAKAMQYLCDGYEQDPAEALGALFDSDNDEMVIVRDIELYSLCEHHLLPF 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682  84 YGIAHVAYIPSkGRVTGLSKLARAVEVASRRPQLQERLTHQVAHALQDALEPEGVFVMVEAEHMCMSMRGIRKPGSKTVT 163
Cdd:PRK12606   99 IGVAHVAYLPG-GKVLGLSKIARIVDMFARRLQIQENLTRQIATAVVTVTQARGAAVVIEAEHLCMMMRGVRKQNSRMIT 177
                         170       180
                  ....*....|....*....|....
gi 2056190682 164 TVALGKYKEDAVLRRELLSMIHNK 187
Cdd:PRK12606  178 SVMLGAFRDSAQTRNEFLRLIGRS 201
PLN03044 PLN03044
GTP cyclohydrolase I; Provisional
7-184 5.17e-75

GTP cyclohydrolase I; Provisional


Pssm-ID: 215549 [Multi-domain]  Cd Length: 188  Bit Score: 223.21  E-value: 5.17e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682   7 IEQTIYQLLELLGEDPNREGLLDTPKRVAKMYLEMFNGLKEDPKDQF-TAVFSE-----GHEEVVLVKDIPFHSMCEHHL 80
Cdd:PLN03044    1 MEQAVRTILECLGEDVEREGLLDTPKRVAKALLFMTQGYDQDPEVVLgTALFHEpevhdGHEEMVVVRDIDIHSTCEETM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682  81 VPFYGIAHVAYIPSKGRVTGLSKLARAVEVASRRPQLQERLTHQVAHALQDALEPEGVFVMVEAEHMCMSMRGIRKPGSK 160
Cdd:PLN03044   81 VPFTGRIHVGYIPNAGVILGLSKLARIAEVYARRLQTQERLTRQIADAIVESVEPLGVMVVVEAAHFCMVMRGVEKHGAS 160
                         170       180
                  ....*....|....*....|....
gi 2056190682 161 TVTTVALGKYKEDAVLRRELLSMI 184
Cdd:PLN03044  161 TTTSAVRGCFASNPKLRAEFFRII 184
PTZ00484 PTZ00484
GTP cyclohydrolase I; Provisional
2-184 5.13e-70

GTP cyclohydrolase I; Provisional


Pssm-ID: 240434  Cd Length: 259  Bit Score: 213.18  E-value: 5.13e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682   2 SKQEQIEQTIYQLLE-LLGEDPNREGLLDTPKRVAKMYLEMFNGLKEDPKDQFT----AVFSEGHEEVVLVKDIPFHSMC 76
Cdd:PTZ00484   71 EKKGAIESARRKILKsLEGEDPDRDGLKKTPKRVAKALEFLTKGYHMSVEEVIKkalfKVEPKNNDEMVKVRDIDIFSLC 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682  77 EHHLVPFYGIAHVAYIPsKGRVTGLSKLARAVEVASRRPQLQERLTHQVAHALQDALEPEGVFVMVEAEHMCMSMRGIRK 156
Cdd:PTZ00484  151 EHHLLPFEGECTIGYIP-NKKVLGLSKFARIIEIFSRRLQVQERLTQQIANALQKYLKPMGVAVVIVASHMCMNMRGVQK 229
                         170       180
                  ....*....|....*....|....*...
gi 2056190682 157 PGSKTVTTVALGKYKEDAVLRRELLSMI 184
Cdd:PTZ00484  230 HDASTTTSAYLGVFRSDPKLRAEFFSLI 257
PLN02531 PLN02531
GTP cyclohydrolase I
14-186 2.92e-43

GTP cyclohydrolase I


Pssm-ID: 215290 [Multi-domain]  Cd Length: 469  Bit Score: 149.92  E-value: 2.92e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682  14 LLELLGEDPNREGLLDTPKRVAKMYL-------------EMFNGLKEDPKDQFTAVFSEghEEVVLVKDIPFHSMCEHHL 80
Cdd:PLN02531  276 ILRSLGEDPLRKELVLTPSRFVRWLLnstqgsrmgrnleMKLNGFACEKMDPLHANLNE--KTMHTELNLPFWSQCEHHL 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682  81 VPFYGIAHVAYIPSKGRVTGLSKLARA-----VEVASRRPQLQERLTHQVAHALQdALEPEGVFVMVEAEHMCMSMRGIR 155
Cdd:PLN02531  354 LPFYGVVHVGYFCAEGGRGNRNPISRSllqsiVHFYGFRLQVQERLTRQIAETVS-SLLGGDVMVVVEASHTCMISRGVE 432
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2056190682 156 KPGSKTVTTVALGKYKEDAVLRRELLSMIHN 186
Cdd:PLN02531  433 KFGSSTATIAVLGRFSSDAKARAMFLQSIAT 463
PLN02531 PLN02531
GTP cyclohydrolase I
7-147 3.22e-38

GTP cyclohydrolase I


Pssm-ID: 215290 [Multi-domain]  Cd Length: 469  Bit Score: 136.44  E-value: 3.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682   7 IEQTIYQLLELLGEDPNREGLLDTPKRVAKMYLEMFNGLKEDPKDQF-TAVFSE-----------GHEEVVLVKDIPFHS 74
Cdd:PLN02531   35 IESAVKVLLQGLGEDVNREGLKKTPLRVAKALREATRGYKQSAKDIVgGALFPEaglddgvghggGCGGLVVVRDLDLFS 114
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056190682  75 MCEHHLVPFYGIAHVAYIPSKGRVTGLSKLARAVEVASRRPQLQERLTHQVAHALQDALEPEGVFVMVEAEHM 147
Cdd:PLN02531  115 YCESCLLPFQVKCHIGYVPSGQRVVGLSKLSRVAEVFAKRLQDPQRLADEICSALHHGIKPAGVAVVLECSHI 187
TFold cd00651
Tunnelling fold (T-fold). The five known T-folds are found in five different enzymes with ...
65-165 1.26e-10

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: 56.30  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056190682  65 VLVKDIPFHSMC----EHHLVPFYGIAHVAYIPsKGRV----------TGLSKLARAVEVASRRPQLQERLTHQVAHALQ 130
Cdd:cd00651     4 VRVKDLLKVTRLgfvtLERTVGQIFEVDVTLSW-DGKKaaasddvatdTVYNTIYRLAKEYVEGSQLIERLAEEIAYLIA 82
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2056190682 131 DAL--EPEGVFVMVEAEHMCMSMRGIRKPGSKTVTTV 165
Cdd:cd00651    83 EHFlsSVAEVKVEEKKPHAVIPDRGVFKPTDSPGVTI 119
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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