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Conserved domains on  [gi|269788766|gb|ACZ40908|]
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GTP cyclohydrolase II [Sphaerobacter thermophilus DSM 20745]

Protein Classification

GTP cyclohydrolase II( domain architecture ID 10791939)

GTP cyclohydrolase II catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate

CATH:  3.40.50.10990
EC:  3.5.4.25
Gene Ontology:  GO:0005525|GO:0003935|GO:0009231|GO:0046872|GO:0042803
PubMed:  16115872|11301327
SCOP:  4003211

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ribA PRK00393
GTP cyclohydrolase II RibA;
17-209 1.09e-116

GTP cyclohydrolase II RibA;


:

Pssm-ID: 234745  Cd Length: 197  Bit Score: 330.65  E-value: 1.09e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  17 IQIAAEADLPTRFGRFRAVAFNDVHDEREHAAFVRGDVRGAEGVLVRLHSECLTGDAIGSLRCDCRDQLEAALRLLGQSE 96
Cdd:PRK00393   3 LKRVAEAKLPTPWGDFLMVGFEELATGKEHVALVFGDISGTEPVLVRVHSECLTGDALFSLRCDCGFQLEAALERIAEEG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  97 RGVLLYLRQEGRGIGLTNKIRAYALQDRGLDTVDANLALGFHDDEREYGAAARMLAALGVRSIRLLTNNPAKIEDLARHG 176
Cdd:PRK00393  83 RGILLYLRQEGRGIGLLNKIRAYALQDQGLDTVEANHQLGFAADERDYTLAADMLKALGVKKVRLLTNNPKKVEALTEAG 162

                        170       180       190
                 ....*....|....*....|....*....|...
gi 269788766 177 VRIVERVPLVIPPNEYNRFYLETKARRSHHMLE 209
Cdd:PRK00393 163 INIVERVPLIVGRNPHNEHYLKTKAEKMGHLLS 195
 
Name Accession Description Interval E-value
ribA PRK00393
GTP cyclohydrolase II RibA;
17-209 1.09e-116

GTP cyclohydrolase II RibA;


Pssm-ID: 234745  Cd Length: 197  Bit Score: 330.65  E-value: 1.09e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  17 IQIAAEADLPTRFGRFRAVAFNDVHDEREHAAFVRGDVRGAEGVLVRLHSECLTGDAIGSLRCDCRDQLEAALRLLGQSE 96
Cdd:PRK00393   3 LKRVAEAKLPTPWGDFLMVGFEELATGKEHVALVFGDISGTEPVLVRVHSECLTGDALFSLRCDCGFQLEAALERIAEEG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  97 RGVLLYLRQEGRGIGLTNKIRAYALQDRGLDTVDANLALGFHDDEREYGAAARMLAALGVRSIRLLTNNPAKIEDLARHG 176
Cdd:PRK00393  83 RGILLYLRQEGRGIGLLNKIRAYALQDQGLDTVEANHQLGFAADERDYTLAADMLKALGVKKVRLLTNNPKKVEALTEAG 162

                        170       180       190
                 ....*....|....*....|....*....|...
gi 269788766 177 VRIVERVPLVIPPNEYNRFYLETKARRSHHMLE 209
Cdd:PRK00393 163 INIVERVPLIVGRNPHNEHYLKTKAEKMGHLLS 195
GTP_cyclohydro2 cd00641
GTP cyclohydrolase II (RibA). GTP cyclohydrolase II catalyzes the conversion of GTP to 2, ...
 17-208 2.39e-113

GTP cyclohydrolase II (RibA). GTP cyclohydrolase II catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5' phosphate, formate, pyrophosphate (APy), and GMP in the biosynthetic pathway of riboflavin. Riboflavin is the precursor molecule for the synthesis of the coenzymes flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) which are essential to cell metabolism. The enzyme is present in plants and numerous pathogenic bacteria, especially gram negative organisms, who are dependent on endogenous synthesis of the vitamin because they lack an appropriate uptake system. For animals and humans, which lack this biosynthetic pathway, riboflavin is the essential vitamin B2. GTP cyclohydrolase II requires magnesium ions for activity and has a bound catalytic zinc. The functionally active form is thought to be a homodimer. A paralogous protein is encoded in the genome of Streptomyces coelicolor, which converts GTP to 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (FAPy), an activity that has otherwise been reported for unrelated GTP cyclohydrolases III.


Pssm-ID: 238348 [Multi-domain]  Cd Length: 193  Bit Score: 322.14  E-value: 2.39e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  17 IQIAAEADLPTRFGRFRAVAFNDVHDEREHAAFVRGDVRGAEGVLVRLHSECLTGDAIGSLRCDCRDQLEAALRLLGQSE 96
Cdd:cd00641    2 VEKVAEAPLPTRFGDFRIVAFEDTDDGKEHVALVKGDPADGEPVLVRVHSECLTGDVFGSLRCDCGPQLEEALEEIAEEG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  97 RGVLLYLRQEGRGIGLTNKIRAYALQDRGLDTVDANLALGFHDDEREYGAAARMLAALGVRSIRLLTNNPAKIEDLARHG 176
Cdd:cd00641   82 GGVLLYLRQEGRGIGLANKLRAYALQDQGLDTVEANEALGFPADARDYGLAAQILRDLGIKSVRLLTNNPDKIDALEGYG 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 269788766 177 VRIVERVPLVIPPNEYNRFYLETKARRSHHML 208
Cdd:cd00641  162 IEVVERVPLEVEPNEENKGYLKTKRDKMGHLL 193
RibA COG0807
GTP cyclohydrolase II [Coenzyme transport and metabolism]; GTP cyclohydrolase II is part of ...
 17-209 2.92e-103

GTP cyclohydrolase II [Coenzyme transport and metabolism]; GTP cyclohydrolase II is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 440570 [Multi-domain]  Cd Length: 398  Bit Score: 304.20  E-value: 2.92e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  17 IQIAAEADLPTRFGRFRAVAFNDVHDEREHAAFVRGDVRGAEGVLVRLHSECLTGDAIGSLRCDCRDQLEAALRLLGQSE 96
Cdd:COG0807  206 VERVAEARLPTEFGEFRLHAYRDTIDGQEHLALVKGDPDPDEPVLVRVHSECLTGDVFGSLRCDCGWQLEAALKRIAEEG 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  97 RGVLLYLRQEGRGIGLTNKIRAYALQDRGLDTVDANLALGFHDDEREYGAAARMLAALGVRSIRLLTNNPAKIEDLARHG 176
Cdd:COG0807  286 RGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADLRDYGIGAQILRDLGVRKMRLLTNNPRKVVGLEGYG 365

                        170       180       190
                 ....*....|....*....|....*....|...
gi 269788766 177 VRIVERVPLVIPPNEYNRFYLETKARRSHHMLE 209
Cdd:COG0807  366 LEVVERVPLEVGPNPHNERYLRTKRDKMGHLLD 398
ribA TIGR00505
GTP cyclohydrolase II; Several members of the family are bifunctional, involving both ribA and ...
 18-208 6.36e-87

GTP cyclohydrolase II; Several members of the family are bifunctional, involving both ribA and ribB function. In these cases, ribA tends to be on the C-terminal end of the protein and ribB tends to be on the N-terminal. The function of archaeal members of the family has not been demonstrated and is assigned tentatively. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]


Pssm-ID: 129596 [Multi-domain]  Cd Length: 191  Bit Score: 255.47  E-value: 6.36e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766   18 QIAAEADLPTRFGRFRAVAFNDVHDEREHAAFVRGDVRGAEGVLVRLHSECLTGDAIGSLRCDCRDQLEAALRLLGQSER 97
Cdd:TIGR00505   1 ERVAEAKLPTPYGDFYMVGFEEPATGKDHVALVKGDISAHTDVLVRIHSECLTGDALHSLRCDCGFQLEAALKQIAEEGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766   98 GVLLYLRQEGRGIGLTNKIRAYALQDRGLDTVDANLALGFHDDEREYGAAARMLAALGVRSIRLLTNNPAKIEDLARHGV 177
Cdd:TIGR00505  81 GVLIYLRQEGRGIGLINKLRAYALQDKGYDTVQANLMLGFPADERDFSLCADILEDLGVKKVRLLTNNPKKIEILKKAGI 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 269788766  178 RIVERVPLVIPPNEYNRFYLETKARRSHHML 208
Cdd:TIGR00505 161 NIVERVPLIVGRNENNEGYLDTKAEKMGHLL 191
GTP_cyclohydro2 pfam00925
GTP cyclohydrolase II; GTP cyclohydrolase II catalyzes the first committed step in the ...
 62-184 5.20e-71

GTP cyclohydrolase II; GTP cyclohydrolase II catalyzes the first committed step in the biosynthesis of riboflavin.


Pssm-ID: 460000 [Multi-domain]  Cd Length: 123  Bit Score: 212.32  E-value: 5.20e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766   62 VRLHSECLTGDAIGSLRCDCRDQLEAALRLLGQSERGVLLYLRQEGRGIGLTNKIRAYALQDRGLDTVDANLALGFHDDE 141
Cdd:pfam00925   1 VRVHSECLTGDVLGSLRCDCGEQLEAALRAIAEEGRGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 269788766  142 REYGAAARMLAALGVRSIRLLTNNPAKIEDLARHGVRIVERVP 184
Cdd:pfam00925  81 RDYGIGAQILRDLGVKKIRLLTNNPRKIVGLEGYGLEVVERVP 123
 
Name Accession Description Interval E-value
ribA PRK00393
GTP cyclohydrolase II RibA;
17-209 1.09e-116

GTP cyclohydrolase II RibA;


Pssm-ID: 234745  Cd Length: 197  Bit Score: 330.65  E-value: 1.09e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  17 IQIAAEADLPTRFGRFRAVAFNDVHDEREHAAFVRGDVRGAEGVLVRLHSECLTGDAIGSLRCDCRDQLEAALRLLGQSE 96
Cdd:PRK00393   3 LKRVAEAKLPTPWGDFLMVGFEELATGKEHVALVFGDISGTEPVLVRVHSECLTGDALFSLRCDCGFQLEAALERIAEEG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  97 RGVLLYLRQEGRGIGLTNKIRAYALQDRGLDTVDANLALGFHDDEREYGAAARMLAALGVRSIRLLTNNPAKIEDLARHG 176
Cdd:PRK00393  83 RGILLYLRQEGRGIGLLNKIRAYALQDQGLDTVEANHQLGFAADERDYTLAADMLKALGVKKVRLLTNNPKKVEALTEAG 162

                        170       180       190
                 ....*....|....*....|....*....|...
gi 269788766 177 VRIVERVPLVIPPNEYNRFYLETKARRSHHMLE 209
Cdd:PRK00393 163 INIVERVPLIVGRNPHNEHYLKTKAEKMGHLLS 195
GTP_cyclohydro2 cd00641
GTP cyclohydrolase II (RibA). GTP cyclohydrolase II catalyzes the conversion of GTP to 2, ...
 17-208 2.39e-113

GTP cyclohydrolase II (RibA). GTP cyclohydrolase II catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5' phosphate, formate, pyrophosphate (APy), and GMP in the biosynthetic pathway of riboflavin. Riboflavin is the precursor molecule for the synthesis of the coenzymes flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) which are essential to cell metabolism. The enzyme is present in plants and numerous pathogenic bacteria, especially gram negative organisms, who are dependent on endogenous synthesis of the vitamin because they lack an appropriate uptake system. For animals and humans, which lack this biosynthetic pathway, riboflavin is the essential vitamin B2. GTP cyclohydrolase II requires magnesium ions for activity and has a bound catalytic zinc. The functionally active form is thought to be a homodimer. A paralogous protein is encoded in the genome of Streptomyces coelicolor, which converts GTP to 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (FAPy), an activity that has otherwise been reported for unrelated GTP cyclohydrolases III.


Pssm-ID: 238348 [Multi-domain]  Cd Length: 193  Bit Score: 322.14  E-value: 2.39e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  17 IQIAAEADLPTRFGRFRAVAFNDVHDEREHAAFVRGDVRGAEGVLVRLHSECLTGDAIGSLRCDCRDQLEAALRLLGQSE 96
Cdd:cd00641    2 VEKVAEAPLPTRFGDFRIVAFEDTDDGKEHVALVKGDPADGEPVLVRVHSECLTGDVFGSLRCDCGPQLEEALEEIAEEG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  97 RGVLLYLRQEGRGIGLTNKIRAYALQDRGLDTVDANLALGFHDDEREYGAAARMLAALGVRSIRLLTNNPAKIEDLARHG 176
Cdd:cd00641   82 GGVLLYLRQEGRGIGLANKLRAYALQDQGLDTVEANEALGFPADARDYGLAAQILRDLGIKSVRLLTNNPDKIDALEGYG 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 269788766 177 VRIVERVPLVIPPNEYNRFYLETKARRSHHML 208
Cdd:cd00641  162 IEVVERVPLEVEPNEENKGYLKTKRDKMGHLL 193
RibA COG0807
GTP cyclohydrolase II [Coenzyme transport and metabolism]; GTP cyclohydrolase II is part of ...
 17-209 2.92e-103

GTP cyclohydrolase II [Coenzyme transport and metabolism]; GTP cyclohydrolase II is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 440570 [Multi-domain]  Cd Length: 398  Bit Score: 304.20  E-value: 2.92e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  17 IQIAAEADLPTRFGRFRAVAFNDVHDEREHAAFVRGDVRGAEGVLVRLHSECLTGDAIGSLRCDCRDQLEAALRLLGQSE 96
Cdd:COG0807  206 VERVAEARLPTEFGEFRLHAYRDTIDGQEHLALVKGDPDPDEPVLVRVHSECLTGDVFGSLRCDCGWQLEAALKRIAEEG 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  97 RGVLLYLRQEGRGIGLTNKIRAYALQDRGLDTVDANLALGFHDDEREYGAAARMLAALGVRSIRLLTNNPAKIEDLARHG 176
Cdd:COG0807  286 RGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADLRDYGIGAQILRDLGVRKMRLLTNNPRKVVGLEGYG 365

                        170       180       190
                 ....*....|....*....|....*....|...
gi 269788766 177 VRIVERVPLVIPPNEYNRFYLETKARRSHHMLE 209
Cdd:COG0807  366 LEVVERVPLEVGPNPHNERYLRTKRDKMGHLLD 398
PRK09311 PRK09311
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
20-210 1.86e-94

bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;


Pssm-ID: 181774 [Multi-domain]  Cd Length: 402  Bit Score: 281.79  E-value: 1.86e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  20 AAEADLPTRFGRFRAVAFNDVHDEREHAAFVRGDVRGAEGVLVRLHSECLTGDAIGSLRCDCRDQLEAALRLLGQSERGV 99
Cdd:PRK09311 210 EVEARLPTRFGEFRAIGYTSILDGKEHVALVKGDIGDGEDVLVRVHSECLTGDVFGSRRCDCGPQLDAALAQIAEEGRGV 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766 100 LLYLR-QEGRGIGLTNKIRAYALQDRGLDTVDANLALGFHDDEREYGAAARMLAALGVRSIRLLTNNPAKIEDLARHGVR 178
Cdd:PRK09311 290 VLYMRgQEGRGIGLLHKLRAYQLQDEGYDTVDANLKLGFPADARDYGIGAQILVDLGVRSMRLLTNNPRKIAGLQGYGLH 369

                        170       180       190
                 ....*....|....*....|....*....|..
gi 269788766 179 IVERVPLVIPPNEYNRFYLETKARRSHHMLEW 210
Cdd:PRK09311 370 VTERVPLPVRANEENERYLRTKRDRMGHDLDL 401
ribA TIGR00505
GTP cyclohydrolase II; Several members of the family are bifunctional, involving both ribA and ...
 18-208 6.36e-87

GTP cyclohydrolase II; Several members of the family are bifunctional, involving both ribA and ribB function. In these cases, ribA tends to be on the C-terminal end of the protein and ribB tends to be on the N-terminal. The function of archaeal members of the family has not been demonstrated and is assigned tentatively. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]


Pssm-ID: 129596 [Multi-domain]  Cd Length: 191  Bit Score: 255.47  E-value: 6.36e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766   18 QIAAEADLPTRFGRFRAVAFNDVHDEREHAAFVRGDVRGAEGVLVRLHSECLTGDAIGSLRCDCRDQLEAALRLLGQSER 97
Cdd:TIGR00505   1 ERVAEAKLPTPYGDFYMVGFEEPATGKDHVALVKGDISAHTDVLVRIHSECLTGDALHSLRCDCGFQLEAALKQIAEEGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766   98 GVLLYLRQEGRGIGLTNKIRAYALQDRGLDTVDANLALGFHDDEREYGAAARMLAALGVRSIRLLTNNPAKIEDLARHGV 177
Cdd:TIGR00505  81 GVLIYLRQEGRGIGLINKLRAYALQDKGYDTVQANLMLGFPADERDFSLCADILEDLGVKKVRLLTNNPKKIEILKKAGI 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 269788766  178 RIVERVPLVIPPNEYNRFYLETKARRSHHML 208
Cdd:TIGR00505 161 NIVERVPLIVGRNENNEGYLDTKAEKMGHLL 191
PRK09319 PRK09319
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase RibB/GTP cyclohydrolase II RibA;
21-209 1.31e-86

bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase RibB/GTP cyclohydrolase II RibA;


Pssm-ID: 236465 [Multi-domain]  Cd Length: 555  Bit Score: 266.43  E-value: 1.31e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  21 AEADLPTRFGRFRAVAFNDVHDEREHAAFVRGDVR--GAEGVLVRLHSECLTGDAIGSLRCDCRDQLEAALRLLGQSERG 98
Cdd:PRK09319 214 AVAKLPSQFGQFQAYGYRNELDGSEHVALVKGDPAnfKDEPVLVRMHSECLTGDAFGSLRCDCRMQLEAALKMIENEGEG 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  99 VLLYLRQEGRGIGLTNKIRAYALQDRGLDTVDANLALGFHDDEREYGAAARMLAALGVRSIRLLTNNPAKIEDLARHGVR 178
Cdd:PRK09319 294 VVVYLRQEGRGIGLINKLKAYSLQDGGLDTVEANERLGFPADLRNYGVGAQILNDLGIKRLRLITNNPRKIAGLGGYGLE 373

                        170       180       190
                 ....*....|....*....|....*....|.
gi 269788766 179 IVERVPLVIPPNEYNRFYLETKARRSHHMLE 209
Cdd:PRK09319 374 VVDRVPLLIEANDYNAEYLATKAEKLGHLLL 404
PRK09318 PRK09318
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
17-209 2.44e-82

bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;


Pssm-ID: 236464 [Multi-domain]  Cd Length: 387  Bit Score: 250.42  E-value: 2.44e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  17 IQIAAEADLPTRFGRFRAVAFNDVHDEREHAAFVR---GDVrgaegVLVRLHSECLTGDAIGSLRCDCRDQLEAALRLLG 93
Cdd:PRK09318 192 IKVKAEAKLPTDYGEFEIVSFENHLDGKEHVAIVKeplGEV-----PLVRIHSECVTGDTLSSLRCDCGSQLANFLRMIS 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  94 QsERGVLLYLRQEGRGIGLTNKIRAYALQDRGLDTVDANLALGFHDDEREYGAAARMLAALGVRSIRLLTNNPAKIEDLA 173
Cdd:PRK09318 267 K-EGGILIYLRQEGRGIGLSNKIKAYELQDKGLDTVEANRALGFKEDERDYAAAFQILKALGIEKVRLLTNNPRKTKALE 345

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 269788766 174 RHGVRIVERVPLVIPPNEYNRFYLETKARRSHHMLE 209
Cdd:PRK09318 346 KYGIEVVETVPLYGEVTKYNRFYLKTKVEKLGHKLE 381
PLN02831 PLN02831
Bifunctional GTP cyclohydrolase II/ 3,4-dihydroxy-2-butanone-4-phosphate synthase
 20-207 2.35e-75

Bifunctional GTP cyclohydrolase II/ 3,4-dihydroxy-2-butanone-4-phosphate synthase


Pssm-ID: 215445 [Multi-domain]  Cd Length: 450  Bit Score: 234.60  E-value: 2.35e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  20 AAEADLPTRFGRFRAVAFNDVHDEREHAAFVRGDVRGAEGVLVRLHSECLTGDAIGSLRCDCRDQLEAALRLLGQSERGV 99
Cdd:PLN02831 244 TAVARLPTKWGLFTAYCYRSKLDGIEHIAFVKGDIGDGQDVLVRVHSECLTGDIFGSARCDCGNQLALAMQLIEKAGRGV 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766 100 LLYLR-QEGRGIGLTNKIRAYALQDRGLDTVDANLALGFHDDEREYGAAARMLAALGVRSIRLLTNNPAKIEDLARHGVR 178
Cdd:PLN02831 324 LVYLRgHEGRGIGLGHKLRAYNLQDEGRDTVEANEELGLPVDSREYGIGAQILRDLGVRTMRLMTNNPAKYTGLKGYGLA 403

                        170       180
                 ....*....|....*....|....*....
gi 269788766 179 IVERVPLVIPPNEYNRFYLETKARRSHHM 207
Cdd:PLN02831 404 VVGRVPLLTPITKENKRYLETKRTKMGHV 432
GTP_cyclohydro2 pfam00925
GTP cyclohydrolase II; GTP cyclohydrolase II catalyzes the first committed step in the ...
 62-184 5.20e-71

GTP cyclohydrolase II; GTP cyclohydrolase II catalyzes the first committed step in the biosynthesis of riboflavin.


Pssm-ID: 460000 [Multi-domain]  Cd Length: 123  Bit Score: 212.32  E-value: 5.20e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766   62 VRLHSECLTGDAIGSLRCDCRDQLEAALRLLGQSERGVLLYLRQEGRGIGLTNKIRAYALQDRGLDTVDANLALGFHDDE 141
Cdd:pfam00925   1 VRVHSECLTGDVLGSLRCDCGEQLEAALRAIAEEGRGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 269788766  142 REYGAAARMLAALGVRSIRLLTNNPAKIEDLARHGVRIVERVP 184
Cdd:pfam00925  81 RDYGIGAQILRDLGVKKIRLLTNNPRKIVGLEGYGLEVVERVP 123
PRK08815 PRK08815
GTP cyclohydrolase II RibA;
44-211 1.47e-56

GTP cyclohydrolase II RibA;


Pssm-ID: 236340 [Multi-domain]  Cd Length: 375  Bit Score: 184.19  E-value: 1.47e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  44 REHAAFVRGDVRGAEGVLVRLHSECLTGDAIGSLRCDCRDQLEAALRLLGQSERGVLLYLRQEGRGIGLTNKIRAYALQD 123
Cdd:PRK08815 201 RDQVAIVVGQPDLSSAVPVRVHSSCLTGDLFGSLKCDCGDQLRHGLAKLKELGGGVLLYLDQEGRGNGIAAKMRAYGYQH 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766 124 RGLDTVDANLALGFHDDEREYGAAARMLAALGVRSIRLLTNNPAKIEDLARHGVRIVERVPLVIPPNEYNRFYLETKARR 203
Cdd:PRK08815 281 AGLDTIDADAQLGFGPDERRYGSAVAMLRGLGITRVRLLTNNPTKAERLRAAGIEVEDRIRVTGRITAENERYLRTKADR 360


                 ....*...
gi 269788766 204 SHHMLEWD 211
Cdd:PRK08815 361 AGHALDVD 368
PRK14019 PRK14019
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
17-184 6.31e-14

bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;


Pssm-ID: 237587 [Multi-domain]  Cd Length: 367  Bit Score: 69.61  E-value: 6.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  17 IQIAAEADLPTRFGRFRAVAFNDVHDEREHAAFVRGDVRGAEGVLVRLHSECLTGDAIGSLRCDCRDQLEAALRLLGQSE 96
Cdd:PRK14019 206 VERVAERPMQTAHGEFRLVAYRDKPSGSTHLALVKGTICPDEETLVRVHEPLSVLDLLEVGQPTHSWSLDAAMAAIAEAG 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  97 RGVLLYLrqeGRGIGltnkirAYALQDRGLDTVDANLALGFHDDEREYGAAARMLAALGVRSIRLLTnNPAKIEDLARHG 176
Cdd:PRK14019 286 SGVVVLL---NCGDD------GEHLLDRFRAEEAAAALKRRPVDYRTYGIGAQILRDLGVGKMRLLS-SPRKFPSMSGFG 355


                 ....*...
gi 269788766 177 VRIVERVP 184
Cdd:PRK14019 356 LEVTGYVP 363
PRK12485 PRK12485
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
22-185 6.33e-08

bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;


Pssm-ID: 171535 [Multi-domain]  Cd Length: 369  Bit Score: 52.27  E-value: 6.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  22 EADLPTRFGRFRAVAFNDVHDEREHAAFVRGDVRGAEGVLVRLHSECLTGDAIGSLRCDCRD-QLEAALRLLGQSERGVL 100
Cdd:PRK12485 211 ERELPTVHGTFRLVTYEDRIEGGVHMAMVMGDIRREQPTLVRVHVIDPLRDLVGAEYAGPANwTLWAALQKVAEEGHGVV 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766 101 LYLRQEGRGIGLTNKIRAYALQDRGLDTVDANLAlgfhddeREYGAAARMLAALGVRSIRLLtNNPAKIEDLARHGVRIV 180
Cdd:PRK12485 291 VVLANHESSQALLERIPQLTQPPRQYQRSQSRIY-------SEVGTGAQILQDLGVGKLRHL-GPPLKYAGLTGYDLEVV 362


                 ....*
gi 269788766 181 ERVPL 185
Cdd:PRK12485 363 ESIPF 367
PRK07198 PRK07198
GTP cyclohydrolase II;
62-190 8.51e-08

GTP cyclohydrolase II;


Pssm-ID: 235959 [Multi-domain]  Cd Length: 418  Bit Score: 51.97  E-value: 8.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269788766  62 VRLHSECLTGDAIGSLRCDCRDQL----EAALRLLGQSERGVLLYLRQEGRGIGLTNKIRAYALQDR--GLDTVDANlal 135
Cdd:PRK07198 242 CRVHDECNGSDVFGSDICTCRPYLthgiEECIRGAQRGGVGLIVYNRKEGRALGEVTKFLVYNARKRqvGGDTAATY--- 318

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269788766 136 gFHDDEREYGAA-AR-------MLAALGVRSI-RLLTNNPAKIEDLARHGVRIVERVPL---VIPPN 190
Cdd:PRK07198 319 -FARTECVAGVQdMRfqelmpdVLHWLGIRRIhRLVSMSNMKYDAITGSGIEVGERVPIpdeLIPAD 384
 
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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