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Conserved domains on  [gi|66932968|ref|NP_001019195|]
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GTP cyclohydrolase 1 isoform 1 [Homo sapiens]

Protein Classification

GTP cyclohydrolase I( domain architecture ID 10089848)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GTP_cyclohydro1 cd00642
GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin ...
66-250 6.38e-124

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: 349.76  E-value: 6.38e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968  66 LNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDEDHDEMVIVKDIDMFSMCEHHL 145
Cdd:cd00642   1 ERLEKIAAAVREILELLGEDPNREGLLETPERVAKAYQEITSGYDQALNDPKNTAIFDEDHDEMVIVKDITLFSMCEHHL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968 146 VPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEATHMCMVMRGVQKMNSKT 225
Cdd:cd00642  81 VPFYGKVHIAYIPKDKVIGLSKLARIVEFFSRRLQVQERLTKQIAVAIQEILGPQGVAVVIEATHMCMVMRGVRKPGSKT 160
                       170       180
                ....*....|....*....|....*
gi 66932968 226 VTSTMLGVFREDPKTREEFLTLIRS 250
Cdd:cd00642 161 VTSAMLGVFKEDPKTREEFLRLIRK 185
 
Name Accession Description Interval E-value
GTP_cyclohydro1 cd00642
GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin ...
66-250 6.38e-124

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: 349.76  E-value: 6.38e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968  66 LNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDEDHDEMVIVKDIDMFSMCEHHL 145
Cdd:cd00642   1 ERLEKIAAAVREILELLGEDPNREGLLETPERVAKAYQEITSGYDQALNDPKNTAIFDEDHDEMVIVKDITLFSMCEHHL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968 146 VPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEATHMCMVMRGVQKMNSKT 225
Cdd:cd00642  81 VPFYGKVHIAYIPKDKVIGLSKLARIVEFFSRRLQVQERLTKQIAVAIQEILGPQGVAVVIEATHMCMVMRGVRKPGSKT 160
                       170       180
                ....*....|....*....|....*
gi 66932968 226 VTSTMLGVFREDPKTREEFLTLIRS 250
Cdd:cd00642 161 VTSAMLGVFKEDPKTREEFLRLIRK 185
FolE COG0302
GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the ...
64-250 6.64e-113

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: 321.66  E-value: 6.64e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968  64 NELNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNdAIFDEDHDEMVIVKDIDMFSMCEH 143
Cdd:COG0302   1 DEPDREEIEAAVREILEALGEDPDREGLLDTPKRVAKAYEELFSGYDQDPAEVLN-TTFEEGYDEMVLVKDIEFYSMCEH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968 144 HLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEATHMCMVMRGVQKMNS 223
Cdd:COG0302  80 HLLPFFGKAHVAYIPNGKVVGLSKLARLVDVFARRPQVQERLTAQIADALQEVLGPRGVAVVIEAEHMCMTMRGVRKPGS 159
                       170       180
                ....*....|....*....|....*..
gi 66932968 224 KTVTSTMLGVFREDPKTREEFLTLIRS 250
Cdd:COG0302 160 STVTSAMRGVFREDPATRAEFLSLIRG 186
folE PRK09347
GTP cyclohydrolase I; Provisional
71-250 4.37e-107

GTP cyclohydrolase I; Provisional


Pssm-ID: 236472 [Multi-domain]  Cd Length: 188  Bit Score: 307.09  E-value: 4.37e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968   71 LAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDED-HDEMVIVKDIDMFSMCEHHLVPFV 149
Cdd:PRK09347   8 IEEAVREILEALGEDPDREGLLDTPKRVAKMYEELFSGYANDPKEVLNKTFEEEMgYDEMVLVKDITFYSMCEHHLLPFI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968  150 GKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTST 229
Cdd:PRK09347  88 GKAHVAYIPKGKVIGLSKIARIVDFFARRPQVQERLTAQIADALQEILGPRGVAVVIEAEHMCMTMRGVRKPGSKTVTSA 167
                        170       180
                 ....*....|....*....|.
gi 66932968  230 MLGVFREDPKTREEFLTLIRS 250
Cdd:PRK09347 168 LRGLFKTDPATRAEFLSLIRH 188
GTP_cyclohydroI pfam01227
GTP cyclohydrolase I; This family includes GTP cyclohydrolase enzymes and a family of related ...
71-247 1.32e-105

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: 302.91  E-value: 1.32e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968    71 LAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNdAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVG 150
Cdd:pfam01227   1 IEEAVREILEAIGEDPDREGLLETPKRVAKMYEELFSGYHEDPEKVLK-ATFEEGYDEMVLVKDIEFYSMCEHHLLPFFG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968   151 KVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTM 230
Cdd:pfam01227  80 KAHVAYIPNGKVIGLSKIARIVDIFARRLQVQERLTAQIADALQEILKPRGVAVVIEAEHLCMTMRGVRKPGSKTVTSAF 159
                         170
                  ....*....|....*..
gi 66932968   231 LGVFREDPKTREEFLTL 247
Cdd:pfam01227 160 RGVFKTDPALRAEFLAL 176
folE TIGR00063
GTP cyclohydrolase I; alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) ...
71-250 5.22e-100

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: 288.96  E-value: 5.22e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968    71 LAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVG 150
Cdd:TIGR00063   1 IAGAMREILELIGEDLNREGLLETPKRVAKMYVEIFSGYDYANFPKITLAIFQEKHDEMVLVRDITFTSTCEHHLVPFDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968   151 KVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTM 230
Cdd:TIGR00063  81 KAHVAYIPKDKVIGLSKIARIVEFFARRPQVQERLTQQIAEALQEILEPNGVAVVVEATHMCMKMRGIRKPGSATVTSAL 160
                         170       180
                  ....*....|....*....|
gi 66932968   231 LGVFREDPKTREEFLTLIRS 250
Cdd:TIGR00063 161 GGLFKSDQKTRAEFLRLVRH 180
 
Name Accession Description Interval E-value
GTP_cyclohydro1 cd00642
GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin ...
66-250 6.38e-124

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: 349.76  E-value: 6.38e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968  66 LNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDEDHDEMVIVKDIDMFSMCEHHL 145
Cdd:cd00642   1 ERLEKIAAAVREILELLGEDPNREGLLETPERVAKAYQEITSGYDQALNDPKNTAIFDEDHDEMVIVKDITLFSMCEHHL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968 146 VPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEATHMCMVMRGVQKMNSKT 225
Cdd:cd00642  81 VPFYGKVHIAYIPKDKVIGLSKLARIVEFFSRRLQVQERLTKQIAVAIQEILGPQGVAVVIEATHMCMVMRGVRKPGSKT 160
                       170       180
                ....*....|....*....|....*
gi 66932968 226 VTSTMLGVFREDPKTREEFLTLIRS 250
Cdd:cd00642 161 VTSAMLGVFKEDPKTREEFLRLIRK 185
FolE COG0302
GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the ...
64-250 6.64e-113

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: 321.66  E-value: 6.64e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968  64 NELNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNdAIFDEDHDEMVIVKDIDMFSMCEH 143
Cdd:COG0302   1 DEPDREEIEAAVREILEALGEDPDREGLLDTPKRVAKAYEELFSGYDQDPAEVLN-TTFEEGYDEMVLVKDIEFYSMCEH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968 144 HLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEATHMCMVMRGVQKMNS 223
Cdd:COG0302  80 HLLPFFGKAHVAYIPNGKVVGLSKLARLVDVFARRPQVQERLTAQIADALQEVLGPRGVAVVIEAEHMCMTMRGVRKPGS 159
                       170       180
                ....*....|....*....|....*..
gi 66932968 224 KTVTSTMLGVFREDPKTREEFLTLIRS 250
Cdd:COG0302 160 STVTSAMRGVFREDPATRAEFLSLIRG 186
folE PRK09347
GTP cyclohydrolase I; Provisional
71-250 4.37e-107

GTP cyclohydrolase I; Provisional


Pssm-ID: 236472 [Multi-domain]  Cd Length: 188  Bit Score: 307.09  E-value: 4.37e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968   71 LAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDED-HDEMVIVKDIDMFSMCEHHLVPFV 149
Cdd:PRK09347   8 IEEAVREILEALGEDPDREGLLDTPKRVAKMYEELFSGYANDPKEVLNKTFEEEMgYDEMVLVKDITFYSMCEHHLLPFI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968  150 GKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTST 229
Cdd:PRK09347  88 GKAHVAYIPKGKVIGLSKIARIVDFFARRPQVQERLTAQIADALQEILGPRGVAVVIEAEHMCMTMRGVRKPGSKTVTSA 167
                        170       180
                 ....*....|....*....|.
gi 66932968  230 MLGVFREDPKTREEFLTLIRS 250
Cdd:PRK09347 168 LRGLFKTDPATRAEFLSLIRH 188
GTP_cyclohydroI pfam01227
GTP cyclohydrolase I; This family includes GTP cyclohydrolase enzymes and a family of related ...
71-247 1.32e-105

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: 302.91  E-value: 1.32e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968    71 LAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNdAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVG 150
Cdd:pfam01227   1 IEEAVREILEAIGEDPDREGLLETPKRVAKMYEELFSGYHEDPEKVLK-ATFEEGYDEMVLVKDIEFYSMCEHHLLPFFG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968   151 KVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTM 230
Cdd:pfam01227  80 KAHVAYIPNGKVIGLSKIARIVDIFARRLQVQERLTAQIADALQEILKPRGVAVVIEAEHLCMTMRGVRKPGSKTVTSAF 159
                         170
                  ....*....|....*..
gi 66932968   231 LGVFREDPKTREEFLTL 247
Cdd:pfam01227 160 RGVFKTDPALRAEFLAL 176
folE TIGR00063
GTP cyclohydrolase I; alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) ...
71-250 5.22e-100

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: 288.96  E-value: 5.22e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968    71 LAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVG 150
Cdd:TIGR00063   1 IAGAMREILELIGEDLNREGLLETPKRVAKMYVEIFSGYDYANFPKITLAIFQEKHDEMVLVRDITFTSTCEHHLVPFDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968   151 KVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTM 230
Cdd:TIGR00063  81 KAHVAYIPKDKVIGLSKIARIVEFFARRPQVQERLTQQIAEALQEILEPNGVAVVVEATHMCMKMRGIRKPGSATVTSAL 160
                         170       180
                  ....*....|....*....|
gi 66932968   231 LGVFREDPKTREEFLTLIRS 250
Cdd:TIGR00063 161 GGLFKSDQKTRAEFLRLVRH 180
PTZ00484 PTZ00484
GTP cyclohydrolase I; Provisional
10-250 4.52e-92

GTP cyclohydrolase I; Provisional


Pssm-ID: 240434  Cd Length: 259  Bit Score: 271.73  E-value: 4.52e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968   10 AEKPRGARCSNGfpeRD-PPRPGPSRPAEKPPRPEAKSAQPADGWKGERPR-SEEDNELNLPNLAAAYSSILSSL-GENP 86
Cdd:PTZ00484  16 GNEENGDISRNC---RDgDIDNDANLSLLDEDASLGKGRQSNSGPSTESSPtCATLMEEKKGAIESARRKILKSLeGEDP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968   87 QRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFD---EDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVL 163
Cdd:PTZ00484  93 DRDGLKKTPKRVAKALEFLTKGYHMSVEEVIKKALFKvepKNNDEMVKVRDIDIFSLCEHHLLPFEGECTIGYIPNKKVL 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968  164 GLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREE 243
Cdd:PTZ00484 173 GLSKFARIIEIFSRRLQVQERLTQQIANALQKYLKPMGVAVVIVASHMCMNMRGVQKHDASTTTSAYLGVFRSDPKLRAE 252

                 ....*..
gi 66932968  244 FLTLIRS 250
Cdd:PTZ00484 253 FFSLIKR 259
PRK12606 PRK12606
GTP cyclohydrolase I; Reviewed
66-248 6.82e-92

GTP cyclohydrolase I; Reviewed


Pssm-ID: 237149  Cd Length: 201  Bit Score: 269.31  E-value: 6.82e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968   66 LNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNdAIFDEDHDEMVIVKDIDMFSMCEHHL 145
Cdd:PRK12606  17 FDPPALEAAVRELLEALGEDPDREGLLDTPQRVAKAMQYLCDGYEQDPAEALG-ALFDSDNDEMVIVRDIELYSLCEHHL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968  146 VPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEATHMCMVMRGVQKMNSKT 225
Cdd:PRK12606  96 LPFIGVAHVAYLPGGKVLGLSKIARIVDMFARRLQIQENLTRQIATAVVTVTQARGAAVVIEAEHLCMMMRGVRKQNSRM 175
                        170       180
                 ....*....|....*....|...
gi 66932968  226 VTSTMLGVFREDPKTREEFLTLI 248
Cdd:PRK12606 176 ITSVMLGAFRDSAQTRNEFLRLI 198
PLN03044 PLN03044
GTP cyclohydrolase I; Provisional
71-249 3.50e-83

GTP cyclohydrolase I; Provisional


Pssm-ID: 215549 [Multi-domain]  Cd Length: 188  Bit Score: 246.71  E-value: 3.50e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968   71 LAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDED-----HDEMVIVKDIDMFSMCEHHL 145
Cdd:PLN03044   1 MEQAVRTILECLGEDVEREGLLDTPKRVAKALLFMTQGYDQDPEVVLGTALFHEPevhdgHEEMVVVRDIDIHSTCEETM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968  146 VPFVGKVHIGYLPNK-QVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEATHMCMVMRGVQKMNSK 224
Cdd:PLN03044  81 VPFTGRIHVGYIPNAgVILGLSKLARIAEVYARRLQTQERLTRQIADAIVESVEPLGVMVVVEAAHFCMVMRGVEKHGAS 160
                        170       180
                 ....*....|....*....|....*
gi 66932968  225 TVTSTMLGVFREDPKTREEFLTLIR 249
Cdd:PLN03044 161 TTTSAVRGCFASNPKLRAEFFRIIR 185
PLN02531 PLN02531
GTP cyclohydrolase I
69-248 2.12e-51

GTP cyclohydrolase I


Pssm-ID: 215290 [Multi-domain]  Cd Length: 469  Bit Score: 173.81  E-value: 2.12e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968   69 PNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQ-----ETISDVLNDAIFDEDH-----DEMVIVKDIDMF 138
Cdd:PLN02531 267 PAMVSAVESILRSLGEDPLRKELVLTPSRFVRWLLNSTQGSRmgrnlEMKLNGFACEKMDPLHanlneKTMHTELNLPFW 346
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968  139 SMCEHHLVPFVGKVHIGYLPNKQV------LGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALrPAGVGVVVEATHMC 212
Cdd:PLN02531 347 SQCEHHLLPFYGVVHVGYFCAEGGrgnrnpISRSLLQSIVHFYGFRLQVQERLTRQIAETVSSLL-GGDVMVVVEASHTC 425
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 66932968  213 MVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLI 248
Cdd:PLN02531 426 MISRGVEKFGSSTATIAVLGRFSSDAKARAMFLQSI 461
PLN02531 PLN02531
GTP cyclohydrolase I
71-211 7.56e-42

GTP cyclohydrolase I


Pssm-ID: 215290 [Multi-domain]  Cd Length: 469  Bit Score: 148.38  E-value: 7.56e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968   71 LAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDE---DHDE--------MVIVKDIDMFS 139
Cdd:PLN02531  35 IESAVKVLLQGLGEDVNREGLKKTPLRVAKALREATRGYKQSAKDIVGGALFPEaglDDGVghgggcggLVVVRDLDLFS 114
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66932968  140 MCEHHLVPFVGKVHIGYLPNKQ-VLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEATHM 211
Cdd:PLN02531 115 YCESCLLPFQVKCHIGYVPSGQrVVGLSKLSRVAEVFAKRLQDPQRLADEICSALHHGIKPAGVAVVLECSHI 187
TFold cd00651
Tunnelling fold (T-fold). The five known T-folds are found in five different enzymes with ...
127-232 1.44e-19

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: 81.34  E-value: 1.44e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932968 127 DEMVIVKDIDMFSMC----EHHLVPFVGKVHIGYLPNKQV----------LGLSKLARIVEIYSRRLQVQERLTKQIAVA 192
Cdd:cd00651   1 TDGVRVKDLLKVTRLgfvtLERTVGQIFEVDVTLSWDGKKaaasddvatdTVYNTIYRLAKEYVEGSQLIERLAEEIAYL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 66932968 193 ITEAL--RPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLG 232
Cdd:cd00651  81 IAEHFlsSVAEVKVEEKKPHAVIPDRGVFKPTDSPGVTIERG 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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