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Conserved domains on  [gi|686561641|gb|AIQ72334|]
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GTP cyclohydrolase [Paenibacillus odorifer]

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 ...
13-196 1.22e-115

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: 326.28  E-value: 1.22e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  13 AENREQIEYHVEKILELIGEDTGREGLLETPARVTRMYEEIFGGYSIDPREALGVTFDESHEELVIVKDIVYYSQCEHHM 92
Cdd:COG0302    2 EPDREEIEAAVREILEALGEDPDREGLLDTPKRVAKAYEELFSGYDQDPAEVLNTTFEEGYDEMVLVKDIEFYSMCEHHL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  93 APFFGKVHIGYIPSGRIAGLSKLARLVEAVSRRLQVQERITAQIADIMTEVLGPHGVMVVVEGEHLCMCARGVKKPGSKT 172
Cdd:COG0302   82 LPFFGKAHVAYIPNGKVVGLSKLARLVDVFARRPQVQERLTAQIADALQEVLGPRGVAVVIEAEHMCMTMRGVRKPGSST 161
                        170       180
                 ....*....|....*....|....
gi 686561641 173 VTMATRGVFREDAAARAEFLSLIK 196
Cdd:COG0302  162 VTSAMRGVFREDPATRAEFLSLIR 185
 
Name Accession Description Interval E-value
FolE COG0302
GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the ...
13-196 1.22e-115

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: 326.28  E-value: 1.22e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  13 AENREQIEYHVEKILELIGEDTGREGLLETPARVTRMYEEIFGGYSIDPREALGVTFDESHEELVIVKDIVYYSQCEHHM 92
Cdd:COG0302    2 EPDREEIEAAVREILEALGEDPDREGLLDTPKRVAKAYEELFSGYDQDPAEVLNTTFEEGYDEMVLVKDIEFYSMCEHHL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  93 APFFGKVHIGYIPSGRIAGLSKLARLVEAVSRRLQVQERITAQIADIMTEVLGPHGVMVVVEGEHLCMCARGVKKPGSKT 172
Cdd:COG0302   82 LPFFGKAHVAYIPNGKVVGLSKLARLVDVFARRPQVQERLTAQIADALQEVLGPRGVAVVIEAEHMCMTMRGVRKPGSST 161
                        170       180
                 ....*....|....*....|....
gi 686561641 173 VTMATRGVFREDAAARAEFLSLIK 196
Cdd:COG0302  162 VTSAMRGVFREDPATRAEFLSLIR 185
folE PRK09347
GTP cyclohydrolase I; Provisional
13-196 2.16e-108

GTP cyclohydrolase I; Provisional


Pssm-ID: 236472 [Multi-domain]  Cd Length: 188  Bit Score: 308.24  E-value: 2.16e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  13 AENREQIEYHVEKILELIGEDTGREGLLETPARVTRMYEEIFGGYSIDPREALGVTFDES--HEELVIVKDIVYYSQCEH 90
Cdd:PRK09347   2 EPDKEKIEEAVREILEALGEDPDREGLLDTPKRVAKMYEELFSGYANDPKEVLNKTFEEEmgYDEMVLVKDITFYSMCEH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  91 HMAPFFGKVHIGYIPSGRIAGLSKLARLVEAVSRRLQVQERITAQIADIMTEVLGPHGVMVVVEGEHLCMCARGVKKPGS 170
Cdd:PRK09347  82 HLLPFIGKAHVAYIPKGKVIGLSKIARIVDFFARRPQVQERLTAQIADALQEILGPRGVAVVIEAEHMCMTMRGVRKPGS 161
                        170       180
                 ....*....|....*....|....*.
gi 686561641 171 KTVTMATRGVFREDAAARAEFLSLIK 196
Cdd:PRK09347 162 KTVTSALRGLFKTDPATRAEFLSLIR 187
GTP_cyclohydroI pfam01227
GTP cyclohydrolase I; This family includes GTP cyclohydrolase enzymes and a family of related ...
19-194 6.77e-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: 296.36  E-value: 6.77e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641   19 IEYHVEKILELIGEDTGREGLLETPARVTRMYEEIFGGYSIDPREALGVTFDESHEELVIVKDIVYYSQCEHHMAPFFGK 98
Cdd:pfam01227   1 IEEAVREILEAIGEDPDREGLLETPKRVAKMYEELFSGYHEDPEKVLKATFEEGYDEMVLVKDIEFYSMCEHHLLPFFGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641   99 VHIGYIPSGRIAGLSKLARLVEAVSRRLQVQERITAQIADIMTEVLGPHGVMVVVEGEHLCMCARGVKKPGSKTVTMATR 178
Cdd:pfam01227  81 AHVAYIPNGKVIGLSKIARIVDIFARRLQVQERLTAQIADALQEILKPRGVAVVIEAEHLCMTMRGVRKPGSKTVTSAFR 160
                         170
                  ....*....|....*.
gi 686561641  179 GVFREDAAARAEFLSL 194
Cdd:pfam01227 161 GVFKTDPALRAEFLAL 176
GTP_cyclohydro1 cd00642
GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin ...
14-196 1.35e-90

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: 263.09  E-value: 1.35e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  14 ENREQIEYHVEKILELIGEDTGREGLLETPARVTRMYEEIFGGYSIDPREAL-GVTFDESHEELVIVKDIVYYSQCEHHM 92
Cdd:cd00642    1 ERLEKIAAAVREILELLGEDPNREGLLETPERVAKAYQEITSGYDQALNDPKnTAIFDEDHDEMVIVKDITLFSMCEHHL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  93 APFFGKVHIGYIPSGRIAGLSKLARLVEAVSRRLQVQERITAQIADIMTEVLGPHGVMVVVEGEHLCMCARGVKKPGSKT 172
Cdd:cd00642   81 VPFYGKVHIAYIPKDKVIGLSKLARIVEFFSRRLQVQERLTKQIAVAIQEILGPQGVAVVIEATHMCMVMRGVRKPGSKT 160
                        170       180
                 ....*....|....*....|....
gi 686561641 173 VTMATRGVFREDAAARAEFLSLIK 196
Cdd:cd00642  161 VTSAMLGVFKEDPKTREEFLRLIR 184
folE TIGR00063
GTP cyclohydrolase I; alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) ...
19-196 6.36e-87

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: 253.53  E-value: 6.36e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641   19 IEYHVEKILELIGEDTGREGLLETPARVTRMYEEIFGGYSIDPREAL-GVTFDESHEELVIVKDIVYYSQCEHHMAPFFG 97
Cdd:TIGR00063   1 IAGAMREILELIGEDLNREGLLETPKRVAKMYVEIFSGYDYANFPKItLAIFQEKHDEMVLVRDITFTSTCEHHLVPFDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641   98 KVHIGYIPSGRIAGLSKLARLVEAVSRRLQVQERITAQIADIMTEVLGPHGVMVVVEGEHLCMCARGVKKPGSKTVTMAT 177
Cdd:TIGR00063  81 KAHVAYIPKDKVIGLSKIARIVEFFARRPQVQERLTQQIAEALQEILEPNGVAVVVEATHMCMKMRGIRKPGSATVTSAL 160
                         170
                  ....*....|....*....
gi 686561641  178 RGVFREDAAARAEFLSLIK 196
Cdd:TIGR00063 161 GGLFKSDQKTRAEFLRLVR 179
 
Name Accession Description Interval E-value
FolE COG0302
GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the ...
13-196 1.22e-115

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: 326.28  E-value: 1.22e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  13 AENREQIEYHVEKILELIGEDTGREGLLETPARVTRMYEEIFGGYSIDPREALGVTFDESHEELVIVKDIVYYSQCEHHM 92
Cdd:COG0302    2 EPDREEIEAAVREILEALGEDPDREGLLDTPKRVAKAYEELFSGYDQDPAEVLNTTFEEGYDEMVLVKDIEFYSMCEHHL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  93 APFFGKVHIGYIPSGRIAGLSKLARLVEAVSRRLQVQERITAQIADIMTEVLGPHGVMVVVEGEHLCMCARGVKKPGSKT 172
Cdd:COG0302   82 LPFFGKAHVAYIPNGKVVGLSKLARLVDVFARRPQVQERLTAQIADALQEVLGPRGVAVVIEAEHMCMTMRGVRKPGSST 161
                        170       180
                 ....*....|....*....|....
gi 686561641 173 VTMATRGVFREDAAARAEFLSLIK 196
Cdd:COG0302  162 VTSAMRGVFREDPATRAEFLSLIR 185
folE PRK09347
GTP cyclohydrolase I; Provisional
13-196 2.16e-108

GTP cyclohydrolase I; Provisional


Pssm-ID: 236472 [Multi-domain]  Cd Length: 188  Bit Score: 308.24  E-value: 2.16e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  13 AENREQIEYHVEKILELIGEDTGREGLLETPARVTRMYEEIFGGYSIDPREALGVTFDES--HEELVIVKDIVYYSQCEH 90
Cdd:PRK09347   2 EPDKEKIEEAVREILEALGEDPDREGLLDTPKRVAKMYEELFSGYANDPKEVLNKTFEEEmgYDEMVLVKDITFYSMCEH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  91 HMAPFFGKVHIGYIPSGRIAGLSKLARLVEAVSRRLQVQERITAQIADIMTEVLGPHGVMVVVEGEHLCMCARGVKKPGS 170
Cdd:PRK09347  82 HLLPFIGKAHVAYIPKGKVIGLSKIARIVDFFARRPQVQERLTAQIADALQEILGPRGVAVVIEAEHMCMTMRGVRKPGS 161
                        170       180
                 ....*....|....*....|....*.
gi 686561641 171 KTVTMATRGVFREDAAARAEFLSLIK 196
Cdd:PRK09347 162 KTVTSALRGLFKTDPATRAEFLSLIR 187
GTP_cyclohydroI pfam01227
GTP cyclohydrolase I; This family includes GTP cyclohydrolase enzymes and a family of related ...
19-194 6.77e-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: 296.36  E-value: 6.77e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641   19 IEYHVEKILELIGEDTGREGLLETPARVTRMYEEIFGGYSIDPREALGVTFDESHEELVIVKDIVYYSQCEHHMAPFFGK 98
Cdd:pfam01227   1 IEEAVREILEAIGEDPDREGLLETPKRVAKMYEELFSGYHEDPEKVLKATFEEGYDEMVLVKDIEFYSMCEHHLLPFFGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641   99 VHIGYIPSGRIAGLSKLARLVEAVSRRLQVQERITAQIADIMTEVLGPHGVMVVVEGEHLCMCARGVKKPGSKTVTMATR 178
Cdd:pfam01227  81 AHVAYIPNGKVIGLSKIARIVDIFARRLQVQERLTAQIADALQEILKPRGVAVVIEAEHLCMTMRGVRKPGSKTVTSAFR 160
                         170
                  ....*....|....*.
gi 686561641  179 GVFREDAAARAEFLSL 194
Cdd:pfam01227 161 GVFKTDPALRAEFLAL 176
GTP_cyclohydro1 cd00642
GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin ...
14-196 1.35e-90

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: 263.09  E-value: 1.35e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  14 ENREQIEYHVEKILELIGEDTGREGLLETPARVTRMYEEIFGGYSIDPREAL-GVTFDESHEELVIVKDIVYYSQCEHHM 92
Cdd:cd00642    1 ERLEKIAAAVREILELLGEDPNREGLLETPERVAKAYQEITSGYDQALNDPKnTAIFDEDHDEMVIVKDITLFSMCEHHL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  93 APFFGKVHIGYIPSGRIAGLSKLARLVEAVSRRLQVQERITAQIADIMTEVLGPHGVMVVVEGEHLCMCARGVKKPGSKT 172
Cdd:cd00642   81 VPFYGKVHIAYIPKDKVIGLSKLARIVEFFSRRLQVQERLTKQIAVAIQEILGPQGVAVVIEATHMCMVMRGVRKPGSKT 160
                        170       180
                 ....*....|....*....|....
gi 686561641 173 VTMATRGVFREDAAARAEFLSLIK 196
Cdd:cd00642  161 VTSAMLGVFKEDPKTREEFLRLIR 184
folE TIGR00063
GTP cyclohydrolase I; alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) ...
19-196 6.36e-87

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: 253.53  E-value: 6.36e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641   19 IEYHVEKILELIGEDTGREGLLETPARVTRMYEEIFGGYSIDPREAL-GVTFDESHEELVIVKDIVYYSQCEHHMAPFFG 97
Cdd:TIGR00063   1 IAGAMREILELIGEDLNREGLLETPKRVAKMYVEIFSGYDYANFPKItLAIFQEKHDEMVLVRDITFTSTCEHHLVPFDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641   98 KVHIGYIPSGRIAGLSKLARLVEAVSRRLQVQERITAQIADIMTEVLGPHGVMVVVEGEHLCMCARGVKKPGSKTVTMAT 177
Cdd:TIGR00063  81 KAHVAYIPKDKVIGLSKIARIVEFFARRPQVQERLTQQIAEALQEILEPNGVAVVVEATHMCMKMRGIRKPGSATVTSAL 160
                         170
                  ....*....|....*....
gi 686561641  178 RGVFREDAAARAEFLSLIK 196
Cdd:TIGR00063 161 GGLFKSDQKTRAEFLRLVR 179
PRK12606 PRK12606
GTP cyclohydrolase I; Reviewed
20-195 2.86e-80

GTP cyclohydrolase I; Reviewed


Pssm-ID: 237149  Cd Length: 201  Bit Score: 237.34  E-value: 2.86e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  20 EYHVEKILELIGEDTGREGLLETPARVTRMYEEIFGGYSIDPREALGVTFDESHEELVIVKDIVYYSQCEHHMAPFFGKV 99
Cdd:PRK12606  23 EAAVRELLEALGEDPDREGLLDTPQRVAKAMQYLCDGYEQDPAEALGALFDSDNDEMVIVRDIELYSLCEHHLLPFIGVA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641 100 HIGYIPSGRIAGLSKLARLVEAVSRRLQVQERITAQIADIMTEVLGPHGVMVVVEGEHLCMCARGVKKPGSKTVTMATRG 179
Cdd:PRK12606 103 HVAYLPGGKVLGLSKIARIVDMFARRLQIQENLTRQIATAVVTVTQARGAAVVIEAEHLCMMMRGVRKQNSRMITSVMLG 182
                        170
                 ....*....|....*.
gi 686561641 180 VFREDAAARAEFLSLI 195
Cdd:PRK12606 183 AFRDSAQTRNEFLRLI 198
PTZ00484 PTZ00484
GTP cyclohydrolase I; Provisional
10-196 1.47e-68

GTP cyclohydrolase I; Provisional


Pssm-ID: 240434  Cd Length: 259  Bit Score: 209.71  E-value: 1.47e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  10 GKVAENREQIEYHVEKILE-LIGEDTGREGLLETPARVTRMYEEIFGGYSIDP----REALGVTFDESHEELVIVKDIVY 84
Cdd:PTZ00484  67 TLMEEKKGAIESARRKILKsLEGEDPDRDGLKKTPKRVAKALEFLTKGYHMSVeeviKKALFKVEPKNNDEMVKVRDIDI 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  85 YSQCEHHMAPFFGKVHIGYIPSGRIAGLSKLARLVEAVSRRLQVQERITAQIADIMTEVLGPHGVMVVVEGEHLCMCARG 164
Cdd:PTZ00484 147 FSLCEHHLLPFEGECTIGYIPNKKVLGLSKFARIIEIFSRRLQVQERLTQQIANALQKYLKPMGVAVVIVASHMCMNMRG 226
                        170       180       190
                 ....*....|....*....|....*....|..
gi 686561641 165 VKKPGSKTVTMATRGVFREDAAARAEFLSLIK 196
Cdd:PTZ00484 227 VQKHDASTTTSAYLGVFRSDPKLRAEFFSLIK 258
PLN03044 PLN03044
GTP cyclohydrolase I; Provisional
19-197 4.51e-66

GTP cyclohydrolase I; Provisional


Pssm-ID: 215549 [Multi-domain]  Cd Length: 188  Bit Score: 200.87  E-value: 4.51e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  19 IEYHVEKILELIGEDTGREGLLETPARVTRMYEEIFGGYSIDPREALGVT-FDE-----SHEELVIVKDIVYYSQCEHHM 92
Cdd:PLN03044   1 MEQAVRTILECLGEDVEREGLLDTPKRVAKALLFMTQGYDQDPEVVLGTAlFHEpevhdGHEEMVVVRDIDIHSTCEETM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  93 APFFGKVHIGYIP-SGRIAGLSKLARLVEAVSRRLQVQERITAQIADIMTEVLGPHGVMVVVEGEHLCMCARGVKKPGSK 171
Cdd:PLN03044  81 VPFTGRIHVGYIPnAGVILGLSKLARIAEVYARRLQTQERLTRQIADAIVESVEPLGVMVVVEAAHFCMVMRGVEKHGAS 160
                        170       180
                 ....*....|....*....|....*.
gi 686561641 172 TVTMATRGVFREDAAARAEFLSLIKE 197
Cdd:PLN03044 161 TTTSAVRGCFASNPKLRAEFFRIIRG 186
PLN02531 PLN02531
GTP cyclohydrolase I
7-195 2.83e-47

GTP cyclohydrolase I


Pssm-ID: 215290 [Multi-domain]  Cd Length: 469  Bit Score: 160.71  E-value: 2.83e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641   7 YVNGKVAENREQIEYHVEKILELIGEDTGREGLLETPAR-------------VTRMYEEIFGGYSIDPREALGVTFDEsh 73
Cdd:PLN02531 257 DSSSASPEPNPAMVSAVESILRSLGEDPLRKELVLTPSRfvrwllnstqgsrMGRNLEMKLNGFACEKMDPLHANLNE-- 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  74 EELVIVKDIVYYSQCEHHMAPFFGKVHIGYIP----SGRIAGLSK--LARLVEAVSRRLQVQERITAQIADIMTEVLGPh 147
Cdd:PLN02531 335 KTMHTELNLPFWSQCEHHLLPFYGVVHVGYFCaeggRGNRNPISRslLQSIVHFYGFRLQVQERLTRQIAETVSSLLGG- 413
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 686561641 148 GVMVVVEGEHLCMCARGVKKPGSKTVTMATRGVFREDAAARAEFLSLI 195
Cdd:PLN02531 414 DVMVVVEASHTCMISRGVEKFGSSTATIAVLGRFSSDAKARAMFLQSI 461
PLN02531 PLN02531
GTP cyclohydrolase I
19-196 1.87e-31

GTP cyclohydrolase I


Pssm-ID: 215290 [Multi-domain]  Cd Length: 469  Bit Score: 118.72  E-value: 1.87e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  19 IEYHVEKILELIGEDTGREGLLETPARVTRMYEEIFGGYSIDPREAL-GVTFDESHEE-----------LVIVKDIVYYS 86
Cdd:PLN02531  35 IESAVKVLLQGLGEDVNREGLKKTPLRVAKALREATRGYKQSAKDIVgGALFPEAGLDdgvghgggcggLVVVRDLDLFS 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  87 QCEHHMAPFFGKVHIGYIPSG-RIAGLSKLARLVEAVSRRLQVQERITAQIADIMTEVLGPHGVMVVVEGEHL------C 159
Cdd:PLN02531 115 YCESCLLPFQVKCHIGYVPSGqRVVGLSKLSRVAEVFAKRLQDPQRLADEICSALHHGIKPAGVAVVLECSHIhfpnesL 194
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 686561641 160 MCARGVKKPGSKTVTMATR-GVFR-EDAAARAEFLSLIK 196
Cdd:PLN02531 195 GSLDLSSHQGWVKASVCSGsGVFEdESGNLWEEFVSLLQ 233
TFold cd00651
Tunnelling fold (T-fold). The five known T-folds are found in five different enzymes with ...
75-179 4.66e-09

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: 52.45  E-value: 4.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686561641  75 ELVIVKDIVYYSQC----EHHMAPFFGKVHIGYIPSGRIAG----------LSKLARLVEAVSRRLQVQERITAQIADIM 140
Cdd:cd00651    2 DGVRVKDLLKVTRLgfvtLERTVGQIFEVDVTLSWDGKKAAasddvatdtvYNTIYRLAKEYVEGSQLIERLAEEIAYLI 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 686561641 141 TE--VLGPHGVMVVVEGEHLCMCARGVKKPGSKTVTMATRG 179
Cdd:cd00651   82 AEhfLSSVAEVKVEEKKPHAVIPDRGVFKPTDSPGVTIERG 122
 
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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