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Conserved domains on  [gi|2324468619|gb|UYZ08807|]
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GTP cyclohydrolase I FolE [Agrobacterium salinitolerans]

Protein Classification

GTP cyclohydrolase I( domain architecture ID 10013185)

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 PRK09347
GTP cyclohydrolase I; Provisional
21-207 1.06e-104

GTP cyclohydrolase I; Provisional


:

Pssm-ID: 236472 [Multi-domain]  Cd Length: 188  Bit Score: 299.38  E-value: 1.06e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619  21 RPSQAEAEEAVRVLLRWAGENPAREGLLDTPKRVAKAYRELFAGYELNVQDVLGTTFEEVGGYDDVVLVRDIPFFSHCEH 100
Cdd:PRK09347    2 EPDKEKIEEAVREILEALGEDPDREGLLDTPKRVAKMYEELFSGYANDPKEVLNKTFEEEMGYDEMVLVKDITFYSMCEH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619 101 HMVPIVGKAHVAYLPAGRVLGLSKIARVVEIFGRRLQTQENMTAQIARSIEETLKPRGVAVMIDAEHMCMSMRGVNKQGS 180
Cdd:PRK09347   82 HLLPFIGKAHVAYIPKGKVIGLSKIARIVDFFARRPQVQERLTAQIADALQEILGPRGVAVVIEAEHMCMTMRGVRKPGS 161
                         170       180
                  ....*....|....*....|....*..
gi 2324468619 181 TTLTTSFTGTFKNDPAEQVRFMTMVRN 207
Cdd:PRK09347  162 KTVTSALRGLFKTDPATRAEFLSLIRH 188
 
Name Accession Description Interval E-value
folE PRK09347
GTP cyclohydrolase I; Provisional
21-207 1.06e-104

GTP cyclohydrolase I; Provisional


Pssm-ID: 236472 [Multi-domain]  Cd Length: 188  Bit Score: 299.38  E-value: 1.06e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619  21 RPSQAEAEEAVRVLLRWAGENPAREGLLDTPKRVAKAYRELFAGYELNVQDVLGTTFEEVGGYDDVVLVRDIPFFSHCEH 100
Cdd:PRK09347    2 EPDKEKIEEAVREILEALGEDPDREGLLDTPKRVAKMYEELFSGYANDPKEVLNKTFEEEMGYDEMVLVKDITFYSMCEH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619 101 HMVPIVGKAHVAYLPAGRVLGLSKIARVVEIFGRRLQTQENMTAQIARSIEETLKPRGVAVMIDAEHMCMSMRGVNKQGS 180
Cdd:PRK09347   82 HLLPFIGKAHVAYIPKGKVIGLSKIARIVDFFARRPQVQERLTAQIADALQEILGPRGVAVVIEAEHMCMTMRGVRKPGS 161
                         170       180
                  ....*....|....*....|....*..
gi 2324468619 181 TTLTTSFTGTFKNDPAEQVRFMTMVRN 207
Cdd:PRK09347  162 KTVTSALRGLFKTDPATRAEFLSLIRH 188
FolE COG0302
GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the ...
20-207 2.23e-103

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: 295.85  E-value: 2.23e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619  20 ARPSQAEAEEAVRVLLRWAGENPAREGLLDTPKRVAKAYRELFAGYELNVQDVLGTTFEEvgGYDDVVLVRDIPFFSHCE 99
Cdd:COG0302     1 DEPDREEIEAAVREILEALGEDPDREGLLDTPKRVAKAYEELFSGYDQDPAEVLNTTFEE--GYDEMVLVKDIEFYSMCE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619 100 HHMVPIVGKAHVAYLPAGRVLGLSKIARVVEIFGRRLQTQENMTAQIARSIEETLKPRGVAVMIDAEHMCMSMRGVNKQG 179
Cdd:COG0302    79 HHLLPFFGKAHVAYIPNGKVVGLSKLARLVDVFARRPQVQERLTAQIADALQEVLGPRGVAVVIEAEHMCMTMRGVRKPG 158
                         170       180
                  ....*....|....*....|....*...
gi 2324468619 180 STTLTTSFTGTFKNDPAEQVRFMTMVRN 207
Cdd:COG0302   159 SSTVTSAMRGVFREDPATRAEFLSLIRG 186
GTP_cyclohydroI pfam01227
GTP cyclohydrolase I; This family includes GTP cyclohydrolase enzymes and a family of related ...
27-204 1.72e-94

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: 272.86  E-value: 1.72e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619  27 AEEAVRVLLRWAGENPAREGLLDTPKRVAKAYRELFAGYELNVQDVLGTTFEEvgGYDDVVLVRDIPFFSHCEHHMVPIV 106
Cdd:pfam01227   1 IEEAVREILEAIGEDPDREGLLETPKRVAKMYEELFSGYHEDPEKVLKATFEE--GYDEMVLVKDIEFYSMCEHHLLPFF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619 107 GKAHVAYLPAGRVLGLSKIARVVEIFGRRLQTQENMTAQIARSIEETLKPRGVAVMIDAEHMCMSMRGVNKQGSTTLTTS 186
Cdd:pfam01227  79 GKAHVAYIPNGKVIGLSKIARIVDIFARRLQVQERLTAQIADALQEILKPRGVAVVIEAEHLCMTMRGVRKPGSKTVTSA 158
                         170
                  ....*....|....*...
gi 2324468619 187 FTGTFKNDPAEQVRFMTM 204
Cdd:pfam01227 159 FRGVFKTDPALRAEFLAL 176
GTP_cyclohydro1 cd00642
GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin ...
23-206 1.81e-70

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: 212.63  E-value: 1.81e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619  23 SQAEAEEAVRVLLRWAGENPAREGLLDTPKRVAKAYRELFAGYELNVQDVL-GTTFEEvgGYDDVVLVRDIPFFSHCEHH 101
Cdd:cd00642     2 RLEKIAAAVREILELLGEDPNREGLLETPERVAKAYQEITSGYDQALNDPKnTAIFDE--DHDEMVIVKDITLFSMCEHH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619 102 MVPIVGKAHVAYLPAGRVLGLSKIARVVEIFGRRLQTQENMTAQIARSIEETLKPRGVAVMIDAEHMCMSMRGVNKQGST 181
Cdd:cd00642    80 LVPFYGKVHIAYIPKDKVIGLSKLARIVEFFSRRLQVQERLTKQIAVAIQEILGPQGVAVVIEATHMCMVMRGVRKPGSK 159
                         170       180
                  ....*....|....*....|....*
gi 2324468619 182 TLTTSFTGTFKNDPAEQVRFMTMVR 206
Cdd:cd00642   160 TVTSAMLGVFKEDPKTREEFLRLIR 184
folE TIGR00063
GTP cyclohydrolase I; alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) ...
28-206 4.33e-70

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: 211.54  E-value: 4.33e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619  28 EEAVRVLLRWAGENPAREGLLDTPKRVAKAYRELFAGYELNVQDVL-GTTFEEvgGYDDVVLVRDIPFFSHCEHHMVPIV 106
Cdd:TIGR00063   2 AGAMREILELIGEDLNREGLLETPKRVAKMYVEIFSGYDYANFPKItLAIFQE--KHDEMVLVRDITFTSTCEHHLVPFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619 107 GKAHVAYLPAGRVLGLSKIARVVEIFGRRLQTQENMTAQIARSIEETLKPRGVAVMIDAEHMCMSMRGVNKQGSTTLTTS 186
Cdd:TIGR00063  80 GKAHVAYIPKDKVIGLSKIARIVEFFARRPQVQERLTQQIAEALQEILEPNGVAVVVEATHMCMKMRGIRKPGSATVTSA 159
                         170       180
                  ....*....|....*....|
gi 2324468619 187 FTGTFKNDPAEQVRFMTMVR 206
Cdd:TIGR00063 160 LGGLFKSDQKTRAEFLRLVR 179
 
Name Accession Description Interval E-value
folE PRK09347
GTP cyclohydrolase I; Provisional
21-207 1.06e-104

GTP cyclohydrolase I; Provisional


Pssm-ID: 236472 [Multi-domain]  Cd Length: 188  Bit Score: 299.38  E-value: 1.06e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619  21 RPSQAEAEEAVRVLLRWAGENPAREGLLDTPKRVAKAYRELFAGYELNVQDVLGTTFEEVGGYDDVVLVRDIPFFSHCEH 100
Cdd:PRK09347    2 EPDKEKIEEAVREILEALGEDPDREGLLDTPKRVAKMYEELFSGYANDPKEVLNKTFEEEMGYDEMVLVKDITFYSMCEH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619 101 HMVPIVGKAHVAYLPAGRVLGLSKIARVVEIFGRRLQTQENMTAQIARSIEETLKPRGVAVMIDAEHMCMSMRGVNKQGS 180
Cdd:PRK09347   82 HLLPFIGKAHVAYIPKGKVIGLSKIARIVDFFARRPQVQERLTAQIADALQEILGPRGVAVVIEAEHMCMTMRGVRKPGS 161
                         170       180
                  ....*....|....*....|....*..
gi 2324468619 181 TTLTTSFTGTFKNDPAEQVRFMTMVRN 207
Cdd:PRK09347  162 KTVTSALRGLFKTDPATRAEFLSLIRH 188
FolE COG0302
GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the ...
20-207 2.23e-103

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: 295.85  E-value: 2.23e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619  20 ARPSQAEAEEAVRVLLRWAGENPAREGLLDTPKRVAKAYRELFAGYELNVQDVLGTTFEEvgGYDDVVLVRDIPFFSHCE 99
Cdd:COG0302     1 DEPDREEIEAAVREILEALGEDPDREGLLDTPKRVAKAYEELFSGYDQDPAEVLNTTFEE--GYDEMVLVKDIEFYSMCE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619 100 HHMVPIVGKAHVAYLPAGRVLGLSKIARVVEIFGRRLQTQENMTAQIARSIEETLKPRGVAVMIDAEHMCMSMRGVNKQG 179
Cdd:COG0302    79 HHLLPFFGKAHVAYIPNGKVVGLSKLARLVDVFARRPQVQERLTAQIADALQEVLGPRGVAVVIEAEHMCMTMRGVRKPG 158
                         170       180
                  ....*....|....*....|....*...
gi 2324468619 180 STTLTTSFTGTFKNDPAEQVRFMTMVRN 207
Cdd:COG0302   159 SSTVTSAMRGVFREDPATRAEFLSLIRG 186
GTP_cyclohydroI pfam01227
GTP cyclohydrolase I; This family includes GTP cyclohydrolase enzymes and a family of related ...
27-204 1.72e-94

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: 272.86  E-value: 1.72e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619  27 AEEAVRVLLRWAGENPAREGLLDTPKRVAKAYRELFAGYELNVQDVLGTTFEEvgGYDDVVLVRDIPFFSHCEHHMVPIV 106
Cdd:pfam01227   1 IEEAVREILEAIGEDPDREGLLETPKRVAKMYEELFSGYHEDPEKVLKATFEE--GYDEMVLVKDIEFYSMCEHHLLPFF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619 107 GKAHVAYLPAGRVLGLSKIARVVEIFGRRLQTQENMTAQIARSIEETLKPRGVAVMIDAEHMCMSMRGVNKQGSTTLTTS 186
Cdd:pfam01227  79 GKAHVAYIPNGKVIGLSKIARIVDIFARRLQVQERLTAQIADALQEILKPRGVAVVIEAEHLCMTMRGVRKPGSKTVTSA 158
                         170
                  ....*....|....*...
gi 2324468619 187 FTGTFKNDPAEQVRFMTM 204
Cdd:pfam01227 159 FRGVFKTDPALRAEFLAL 176
PRK12606 PRK12606
GTP cyclohydrolase I; Reviewed
24-178 5.05e-75

GTP cyclohydrolase I; Reviewed


Pssm-ID: 237149  Cd Length: 201  Bit Score: 224.63  E-value: 5.05e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619  24 QAEAEEAVRVLLRWAGENPAREGLLDTPKRVAKAYRELFAGYELNVQDVLGTTFEEvgGYDDVVLVRDIPFFSHCEHHMV 103
Cdd:PRK12606   19 PPALEAAVRELLEALGEDPDREGLLDTPQRVAKAMQYLCDGYEQDPAEALGALFDS--DNDEMVIVRDIELYSLCEHHLL 96
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2324468619 104 PIVGKAHVAYLPAGRVLGLSKIARVVEIFGRRLQTQENMTAQIARSIEETLKPRGVAVMIDAEHMCMSMRGVNKQ 178
Cdd:PRK12606   97 PFIGVAHVAYLPGGKVLGLSKIARIVDMFARRLQIQENLTRQIATAVVTVTQARGAAVVIEAEHLCMMMRGVRKQ 171
GTP_cyclohydro1 cd00642
GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin ...
23-206 1.81e-70

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: 212.63  E-value: 1.81e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619  23 SQAEAEEAVRVLLRWAGENPAREGLLDTPKRVAKAYRELFAGYELNVQDVL-GTTFEEvgGYDDVVLVRDIPFFSHCEHH 101
Cdd:cd00642     2 RLEKIAAAVREILELLGEDPNREGLLETPERVAKAYQEITSGYDQALNDPKnTAIFDE--DHDEMVIVKDITLFSMCEHH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619 102 MVPIVGKAHVAYLPAGRVLGLSKIARVVEIFGRRLQTQENMTAQIARSIEETLKPRGVAVMIDAEHMCMSMRGVNKQGST 181
Cdd:cd00642    80 LVPFYGKVHIAYIPKDKVIGLSKLARIVEFFSRRLQVQERLTKQIAVAIQEILGPQGVAVVIEATHMCMVMRGVRKPGSK 159
                         170       180
                  ....*....|....*....|....*
gi 2324468619 182 TLTTSFTGTFKNDPAEQVRFMTMVR 206
Cdd:cd00642   160 TVTSAMLGVFKEDPKTREEFLRLIR 184
folE TIGR00063
GTP cyclohydrolase I; alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) ...
28-206 4.33e-70

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: 211.54  E-value: 4.33e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619  28 EEAVRVLLRWAGENPAREGLLDTPKRVAKAYRELFAGYELNVQDVL-GTTFEEvgGYDDVVLVRDIPFFSHCEHHMVPIV 106
Cdd:TIGR00063   2 AGAMREILELIGEDLNREGLLETPKRVAKMYVEIFSGYDYANFPKItLAIFQE--KHDEMVLVRDITFTSTCEHHLVPFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619 107 GKAHVAYLPAGRVLGLSKIARVVEIFGRRLQTQENMTAQIARSIEETLKPRGVAVMIDAEHMCMSMRGVNKQGSTTLTTS 186
Cdd:TIGR00063  80 GKAHVAYIPKDKVIGLSKIARIVEFFARRPQVQERLTQQIAEALQEILEPNGVAVVVEATHMCMKMRGIRKPGSATVTSA 159
                         170       180
                  ....*....|....*....|
gi 2324468619 187 FTGTFKNDPAEQVRFMTMVR 206
Cdd:TIGR00063 160 LGGLFKSDQKTRAEFLRLVR 179
PTZ00484 PTZ00484
GTP cyclohydrolase I; Provisional
28-206 5.86e-63

GTP cyclohydrolase I; Provisional


Pssm-ID: 240434  Cd Length: 259  Bit Score: 195.85  E-value: 5.86e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619  28 EEAVR-VLLRWAGENPAREGLLDTPKRVAKAYRELFAGYELNVQDVLGTTF--EEVGGYDDVVLVRDIPFFSHCEHHMVP 104
Cdd:PTZ00484   77 ESARRkILKSLEGEDPDRDGLKKTPKRVAKALEFLTKGYHMSVEEVIKKALfkVEPKNNDEMVKVRDIDIFSLCEHHLLP 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619 105 IVGKAHVAYLPAGRVLGLSKIARVVEIFGRRLQTQENMTAQIARSIEETLKPRGVAVMIDAEHMCMSMRGVNKQGSTTLT 184
Cdd:PTZ00484  157 FEGECTIGYIPNKKVLGLSKFARIIEIFSRRLQVQERLTQQIANALQKYLKPMGVAVVIVASHMCMNMRGVQKHDASTTT 236
                         170       180
                  ....*....|....*....|..
gi 2324468619 185 TSFTGTFKNDPAEQVRFMTMVR 206
Cdd:PTZ00484  237 SAYLGVFRSDPKLRAEFFSLIK 258
PLN03044 PLN03044
GTP cyclohydrolase I; Provisional
28-177 6.67e-60

GTP cyclohydrolase I; Provisional


Pssm-ID: 215549 [Multi-domain]  Cd Length: 188  Bit Score: 185.85  E-value: 6.67e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619  28 EEAVRVLLRWAGENPAREGLLDTPKRVAKAYRELFAGYELNVQDVLGTT-FEE---VGGYDDVVLVRDIPFFSHCEHHMV 103
Cdd:PLN03044    2 EQAVRTILECLGEDVEREGLLDTPKRVAKALLFMTQGYDQDPEVVLGTAlFHEpevHDGHEEMVVVRDIDIHSTCEETMV 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2324468619 104 PIVGKAHVAYLP-AGRVLGLSKIARVVEIFGRRLQTQENMTAQIARSIEETLKPRGVAVMIDAEHMCMSMRGVNK 177
Cdd:PLN03044   82 PFTGRIHVGYIPnAGVILGLSKLARIAEVYARRLQTQERLTRQIADAIVESVEPLGVMVVVEAAHFCMVMRGVEK 156
PLN02531 PLN02531
GTP cyclohydrolase I
28-168 1.63e-43

GTP cyclohydrolase I


Pssm-ID: 215290 [Multi-domain]  Cd Length: 469  Bit Score: 151.46  E-value: 1.63e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619  28 EEAVRVLLRWAGENPAREGLLDTPKRVAKAYRELFAGYELNVQDVLGTT-FEEVGGYDDV---------VLVRDIPFFSH 97
Cdd:PLN02531   36 ESAVKVLLQGLGEDVNREGLKKTPLRVAKALREATRGYKQSAKDIVGGAlFPEAGLDDGVghgggcgglVVVRDLDLFSY 115
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2324468619  98 CEHHMVPIVGKAHVAYLPAG-RVLGLSKIARVVEIFGRRLQTQENMTAQIARSIEETLKPRGVAVMIDAEHM 168
Cdd:PLN02531  116 CESCLLPFQVKCHIGYVPSGqRVVGLSKLSRVAEVFAKRLQDPQRLADEICSALHHGIKPAGVAVVLECSHI 187
PLN02531 PLN02531
GTP cyclohydrolase I
22-177 5.82e-30

GTP cyclohydrolase I


Pssm-ID: 215290 [Multi-domain]  Cd Length: 469  Bit Score: 114.87  E-value: 5.82e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619  22 PSQAEAEEAVRVLLRWAGENPAREGLLDTPKRVAK------AYRELFAGYELNVQdvlGTTFEEVGGY------DDVVLV 89
Cdd:PLN02531  264 EPNPAMVSAVESILRSLGEDPLRKELVLTPSRFVRwllnstQGSRMGRNLEMKLN---GFACEKMDPLhanlneKTMHTE 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619  90 RDIPFFSHCEHHMVPIVGKAHVAYLPAGRV------LGLSKIARVVEIFGRRLQTQENMTAQIARSIEETLKPrGVAVMI 163
Cdd:PLN02531  341 LNLPFWSQCEHHLLPFYGVVHVGYFCAEGGrgnrnpISRSLLQSIVHFYGFRLQVQERLTRQIAETVSSLLGG-DVMVVV 419
                         170
                  ....*....|....
gi 2324468619 164 DAEHMCMSMRGVNK 177
Cdd:PLN02531  420 EASHTCMISRGVEK 433
TFold cd00651
Tunnelling fold (T-fold). The five known T-folds are found in five different enzymes with ...
84-177 9.33e-08

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: 48.98  E-value: 9.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324468619  84 DDVVLVRDIPFFSHC----EHHMVPIVGKAHVAYLPAGRV----------LGLSKIARVVEIFGRRLQTQENMTAQIARS 149
Cdd:cd00651     1 TDGVRVKDLLKVTRLgfvtLERTVGQIFEVDVTLSWDGKKaaasddvatdTVYNTIYRLAKEYVEGSQLIERLAEEIAYL 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 2324468619 150 IEETLKPRGVAVMI--DAEHMCMSMRGVNK 177
Cdd:cd00651    81 IAEHFLSSVAEVKVeeKKPHAVIPDRGVFK 110
 
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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