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Conserved domains on  [gi|119601057|gb|EAW80651|]
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GTP cyclohydrolase 1 (dopa-responsive dystonia), isoform CRA_d [Homo sapiens]

Protein Classification

tunnelling fold family protein( domain architecture ID 365)

Tunnelling fold (T-fold) family protein such as dihydroneopterin-triphosphate epimerase (DHNTPE), dihydroneopterin aldolase (DHNA) , GTP cyclohydrolase I (GTPCH-1), 6-pyrovoyl tetrahydropterin synthetase (PTPS), and uricase (UO,uroate/urate oxidase)

PubMed:  10737935
SCOP:  3000283

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TFold super family cl00263
Tunnelling fold (T-fold). The five known T-folds are found in five different enzymes with ...
 66-209 4.99e-93

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.


The actual alignment was detected with superfamily member cd00642:

Pssm-ID: 469697 [Multi-domain]  Cd Length: 185  Bit Score: 269.64  E-value: 4.99e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601057  66 LNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDEDHDEMVIVKDIDMFSMCEHHL 145
Cdd:cd00642    1 ERLEKIAAAVREILELLGEDPNREGLLETPERVAKAYQEITSGYDQALNDPKNTAIFDEDHDEMVIVKDITLFSMCEHHL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119601057 146 VPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEAT 209
Cdd:cd00642   81 VPFYGKVHIAYIPKDKVIGLSKLARIVEFFSRRLQVQERLTKQIAVAIQEILGPQGVAVVIEAT 144
 
Name Accession Description Interval E-value
GTP_cyclohydro1 cd00642
GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin ...
 66-209 4.99e-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: 4.99e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601057  66 LNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDEDHDEMVIVKDIDMFSMCEHHL 145
Cdd:cd00642    1 ERLEKIAAAVREILELLGEDPNREGLLETPERVAKAYQEITSGYDQALNDPKNTAIFDEDHDEMVIVKDITLFSMCEHHL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119601057 146 VPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEAT 209
Cdd:cd00642   81 VPFYGKVHIAYIPKDKVIGLSKLARIVEFFSRRLQVQERLTKQIAVAIQEILGPQGVAVVIEAT 144
FolE COG0302
GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the ...
 64-209 2.11e-82

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: 242.69  E-value: 2.11e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601057  64 NELNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNdAIFDEDHDEMVIVKDIDMFSMCEH 143
Cdd:COG0302    1 DEPDREEIEAAVREILEALGEDPDREGLLDTPKRVAKAYEELFSGYDQDPAEVLN-TTFEEGYDEMVLVKDIEFYSMCEH 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119601057 144 HLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEAT 209
Cdd:COG0302   80 HLLPFFGKAHVAYIPNGKVVGLSKLARLVDVFARRPQVQERLTAQIADALQEVLGPRGVAVVIEAE 145
folE PRK09347
GTP cyclohydrolase I; Provisional
 71-209 7.91e-78

GTP cyclohydrolase I; Provisional


Pssm-ID: 236472 [Multi-domain]  Cd Length: 188  Bit Score: 231.20  E-value: 7.91e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601057  71 LAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDED-HDEMVIVKDIDMFSMCEHHLVPFV 149
Cdd:PRK09347   8 IEEAVREILEALGEDPDREGLLDTPKRVAKMYEELFSGYANDPKEVLNKTFEEEMgYDEMVLVKDITFYSMCEHHLLPFI 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601057 150 GKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEAT 209
Cdd:PRK09347  88 GKAHVAYIPKGKVIGLSKIARIVDFFARRPQVQERLTAQIADALQEILGPRGVAVVIEAE 147
GTP_cyclohydroI pfam01227
GTP cyclohydrolase I; This family includes GTP cyclohydrolase enzymes and a family of related ...
 71-209 9.39e-78

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: 230.49  E-value: 9.39e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601057   71 LAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNdAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVG 150
Cdd:pfam01227   1 IEEAVREILEAIGEDPDREGLLETPKRVAKMYEELFSGYHEDPEKVLK-ATFEEGYDEMVLVKDIEFYSMCEHHLLPFFG 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 119601057  151 KVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEAT 209
Cdd:pfam01227  80 KAHVAYIPNGKVIGLSKIARIVDIFARRLQVQERLTAQIADALQEILKPRGVAVVIEAE 138
folE TIGR00063
GTP cyclohydrolase I; alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) ...
 71-209 5.49e-72

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: 216.16  E-value: 5.49e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601057   71 LAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVG 150
Cdd:TIGR00063   1 IAGAMREILELIGEDLNREGLLETPKRVAKMYVEIFSGYDYANFPKITLAIFQEKHDEMVLVRDITFTSTCEHHLVPFDG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 119601057  151 KVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEAT 209
Cdd:TIGR00063  81 KAHVAYIPKDKVIGLSKIARIVEFFARRPQVQERLTQQIAEALQEILEPNGVAVVVEAT 139
 
Name Accession Description Interval E-value
GTP_cyclohydro1 cd00642
GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin ...
 66-209 4.99e-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: 4.99e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601057  66 LNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDEDHDEMVIVKDIDMFSMCEHHL 145
Cdd:cd00642    1 ERLEKIAAAVREILELLGEDPNREGLLETPERVAKAYQEITSGYDQALNDPKNTAIFDEDHDEMVIVKDITLFSMCEHHL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119601057 146 VPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEAT 209
Cdd:cd00642   81 VPFYGKVHIAYIPKDKVIGLSKLARIVEFFSRRLQVQERLTKQIAVAIQEILGPQGVAVVIEAT 144
FolE COG0302
GTP cyclohydrolase I [Coenzyme transport and metabolism]; GTP cyclohydrolase I is part of the ...
 64-209 2.11e-82

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: 242.69  E-value: 2.11e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601057  64 NELNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNdAIFDEDHDEMVIVKDIDMFSMCEH 143
Cdd:COG0302    1 DEPDREEIEAAVREILEALGEDPDREGLLDTPKRVAKAYEELFSGYDQDPAEVLN-TTFEEGYDEMVLVKDIEFYSMCEH 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119601057 144 HLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEAT 209
Cdd:COG0302   80 HLLPFFGKAHVAYIPNGKVVGLSKLARLVDVFARRPQVQERLTAQIADALQEVLGPRGVAVVIEAE 145
folE PRK09347
GTP cyclohydrolase I; Provisional
 71-209 7.91e-78

GTP cyclohydrolase I; Provisional


Pssm-ID: 236472 [Multi-domain]  Cd Length: 188  Bit Score: 231.20  E-value: 7.91e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601057  71 LAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDED-HDEMVIVKDIDMFSMCEHHLVPFV 149
Cdd:PRK09347   8 IEEAVREILEALGEDPDREGLLDTPKRVAKMYEELFSGYANDPKEVLNKTFEEEMgYDEMVLVKDITFYSMCEHHLLPFI 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601057 150 GKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEAT 209
Cdd:PRK09347  88 GKAHVAYIPKGKVIGLSKIARIVDFFARRPQVQERLTAQIADALQEILGPRGVAVVIEAE 147
GTP_cyclohydroI pfam01227
GTP cyclohydrolase I; This family includes GTP cyclohydrolase enzymes and a family of related ...
 71-209 9.39e-78

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: 230.49  E-value: 9.39e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601057   71 LAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNdAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVG 150
Cdd:pfam01227   1 IEEAVREILEAIGEDPDREGLLETPKRVAKMYEELFSGYHEDPEKVLK-ATFEEGYDEMVLVKDIEFYSMCEHHLLPFFG 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 119601057  151 KVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEAT 209
Cdd:pfam01227  80 KAHVAYIPNGKVIGLSKIARIVDIFARRLQVQERLTAQIADALQEILKPRGVAVVIEAE 138
folE TIGR00063
GTP cyclohydrolase I; alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) ...
 71-209 5.49e-72

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: 216.16  E-value: 5.49e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601057   71 LAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVG 150
Cdd:TIGR00063   1 IAGAMREILELIGEDLNREGLLETPKRVAKMYVEIFSGYDYANFPKITLAIFQEKHDEMVLVRDITFTSTCEHHLVPFDG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 119601057  151 KVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEAT 209
Cdd:TIGR00063  81 KAHVAYIPKDKVIGLSKIARIVEFFARRPQVQERLTQQIAEALQEILEPNGVAVVVEAT 139
PRK12606 PRK12606
GTP cyclohydrolase I; Reviewed
 66-208 9.44e-69

GTP cyclohydrolase I; Reviewed


Pssm-ID: 237149  Cd Length: 201  Bit Score: 208.84  E-value: 9.44e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601057  66 LNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNdAIFDEDHDEMVIVKDIDMFSMCEHHL 145
Cdd:PRK12606  17 FDPPALEAAVRELLEALGEDPDREGLLDTPQRVAKAMQYLCDGYEQDPAEALG-ALFDSDNDEMVIVRDIELYSLCEHHL 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119601057 146 VPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEA 208
Cdd:PRK12606  96 LPFIGVAHVAYLPGGKVLGLSKIARIVDMFARRLQIQENLTRQIATAVVTVTQARGAAVVIEA 158
PTZ00484 PTZ00484
GTP cyclohydrolase I; Provisional
 10-209 1.21e-67

GTP cyclohydrolase I; Provisional


Pssm-ID: 240434  Cd Length: 259  Bit Score: 208.17  E-value: 1.21e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601057  10 AEKPRGARCSNGfpeRD-PPRPGPSRPAEKPPRPEAKSAQPADGWKGERPR-SEEDNELNLPNLAAAYSSILSSL-GENP 86
Cdd:PTZ00484  16 GNEENGDISRNC---RDgDIDNDANLSLLDEDASLGKGRQSNSGPSTESSPtCATLMEEKKGAIESARRKILKSLeGEDP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601057  87 QRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFD---EDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVL 163
Cdd:PTZ00484  93 DRDGLKKTPKRVAKALEFLTKGYHMSVEEVIKKALFKvepKNNDEMVKVRDIDIFSLCEHHLLPFEGECTIGYIPNKKVL 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 119601057 164 GLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEAT 209
Cdd:PTZ00484 173 GLSKFARIIEIFSRRLQVQERLTQQIANALQKYLKPMGVAVVIVAS 218
PLN03044 PLN03044
GTP cyclohydrolase I; Provisional
 71-209 4.10e-61

GTP cyclohydrolase I; Provisional


Pssm-ID: 215549 [Multi-domain]  Cd Length: 188  Bit Score: 188.93  E-value: 4.10e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601057  71 LAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDED-----HDEMVIVKDIDMFSMCEHHL 145
Cdd:PLN03044   1 MEQAVRTILECLGEDVEREGLLDTPKRVAKALLFMTQGYDQDPEVVLGTALFHEPevhdgHEEMVVVRDIDIHSTCEETM 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119601057 146 VPFVGKVHIGYLPNK-QVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEAT 209
Cdd:PLN03044  81 VPFTGRIHVGYIPNAgVILGLSKLARIAEVYARRLQTQERLTRQIADAIVESVEPLGVMVVVEAA 145
PLN02531 PLN02531
GTP cyclohydrolase I
 71-207 8.62e-41

GTP cyclohydrolase I


Pssm-ID: 215290 [Multi-domain]  Cd Length: 469  Bit Score: 144.15  E-value: 8.62e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601057  71 LAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDE---DHDE--------MVIVKDIDMFS 139
Cdd:PLN02531  35 IESAVKVLLQGLGEDVNREGLKKTPLRVAKALREATRGYKQSAKDIVGGALFPEaglDDGVghgggcggLVVVRDLDLFS 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119601057 140 MCEHHLVPFVGKVHIGYLPNKQ-VLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVE 207
Cdd:PLN02531 115 YCESCLLPFQVKCHIGYVPSGQrVVGLSKLSRVAEVFAKRLQDPQRLADEICSALHHGIKPAGVAVVLE 183
PLN02531 PLN02531
GTP cyclohydrolase I
 69-208 5.53e-34

GTP cyclohydrolase I


Pssm-ID: 215290 [Multi-domain]  Cd Length: 469  Bit Score: 126.04  E-value: 5.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601057  69 PNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQ-----ETISDVLNDAIFDEDH-----DEMVIVKDIDMF 138
Cdd:PLN02531 267 PAMVSAVESILRSLGEDPLRKELVLTPSRFVRWLLNSTQGSRmgrnlEMKLNGFACEKMDPLHanlneKTMHTELNLPFW 346

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119601057 139 SMCEHHLVPFVGKVHIGYLPNKQV------LGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALrPAGVGVVVEA 208
Cdd:PLN02531 347 SQCEHHLLPFYGVVHVGYFCAEGGrgnrnpISRSLLQSIVHFYGFRLQVQERLTRQIAETVSSLL-GGDVMVVVEA 421
TFold cd00651
Tunnelling fold (T-fold). The five known T-folds are found in five different enzymes with ...
 127-209 1.50e-13

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: 64.39  E-value: 1.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601057 127 DEMVIVKDIDMFSMC----EHHLVPFVGKVHIGYLPNKQV----------LGLSKLARIVEIYSRRLQVQERLTKQIAVA 192
Cdd:cd00651    1 TDGVRVKDLLKVTRLgfvtLERTVGQIFEVDVTLSWDGKKaaasddvatdTVYNTIYRLAKEYVEGSQLIERLAEEIAYL 80

                         90
                 ....*....|....*..
gi 119601057 193 ITEALRPAGVGVVVEAT 209
Cdd:cd00651   81 IAEHFLSSVAEVKVEEK 97
 
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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