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Conserved domains on  [gi|490241267|ref|WP_004139521|]
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MULTISPECIES: GTP cyclohydrolase II [Klebsiella]

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;
1-195 1.35e-155

GTP cyclohydrolase II RibA;


:

Pssm-ID: 234745  Cd Length: 197  Bit Score: 427.72  E-value: 1.35e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267   1 MQLKRVAEAKLPTPWGDFLMVGFEELATGQDHVALVFGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAE 80
Cdd:PRK00393   1 MQLKRVAEAKLPTPWGDFLMVGFEELATGKEHVALVFGDISGTEPVLVRVHSECLTGDALFSLRCDCGFQLEAALERIAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267  81 EGRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVDQVRLLTNNPKKVEILTE 160
Cdd:PRK00393  81 EGRGILLYLRQEGRGIGLLNKIRAYALQDQGLDTVEANHQLGFAADERDYTLAADMLKALGVKKVRLLTNNPKKVEALTE 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 490241267 161 AGINIVERVPLIVGRNPKNAHYLDTKAAKMGHLLS 195
Cdd:PRK00393 161 AGINIVERVPLIVGRNPHNEHYLKTKAEKMGHLLS 195
 
Name Accession Description Interval E-value
ribA PRK00393
GTP cyclohydrolase II RibA;
1-195 1.35e-155

GTP cyclohydrolase II RibA;


Pssm-ID: 234745  Cd Length: 197  Bit Score: 427.72  E-value: 1.35e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267   1 MQLKRVAEAKLPTPWGDFLMVGFEELATGQDHVALVFGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAE 80
Cdd:PRK00393   1 MQLKRVAEAKLPTPWGDFLMVGFEELATGKEHVALVFGDISGTEPVLVRVHSECLTGDALFSLRCDCGFQLEAALERIAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267  81 EGRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVDQVRLLTNNPKKVEILTE 160
Cdd:PRK00393  81 EGRGILLYLRQEGRGIGLLNKIRAYALQDQGLDTVEANHQLGFAADERDYTLAADMLKALGVKKVRLLTNNPKKVEALTE 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 490241267 161 AGINIVERVPLIVGRNPKNAHYLDTKAAKMGHLLS 195
Cdd:PRK00393 161 AGINIVERVPLIVGRNPHNEHYLKTKAEKMGHLLS 195
ribA TIGR00505
GTP cyclohydrolase II; Several members of the family are bifunctional, involving both ribA and ...
 4-194 9.73e-121

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: 339.45  E-value: 9.73e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267    4 KRVAEAKLPTPWGDFLMVGFEELATGQDHVALVFGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAEEGR 83
Cdd:TIGR00505   1 ERVAEAKLPTPYGDFYMVGFEEPATGKDHVALVKGDISAHTDVLVRIHSECLTGDALHSLRCDCGFQLEAALKQIAEEGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267   84 GILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVDQVRLLTNNPKKVEILTEAGI 163
Cdd:TIGR00505  81 GVLIYLRQEGRGIGLINKLRAYALQDKGYDTVQANLMLGFPADERDFSLCADILEDLGVKKVRLLTNNPKKIEILKKAGI 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 490241267  164 NIVERVPLIVGRNPKNAHYLDTKAAKMGHLL 194
Cdd:TIGR00505 161 NIVERVPLIVGRNENNEGYLDTKAEKMGHLL 191
GTP_cyclohydro2 cd00641
GTP cyclohydrolase II (RibA). GTP cyclohydrolase II catalyzes the conversion of GTP to 2, ...
 2-194 6.01e-119

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: 334.85  E-value: 6.01e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267   2 QLKRVAEAKLPTPWGDFLMVGFEELATGQDHVALVFGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAEE 81
Cdd:cd00641    1 LVEKVAEAPLPTRFGDFRIVAFEDTDDGKEHVALVKGDPADGEPVLVRVHSECLTGDVFGSLRCDCGPQLEEALEEIAEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267  82 GRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVDQVRLLTNNPKKVEILTEA 161
Cdd:cd00641   81 GGGVLLYLRQEGRGIGLANKLRAYALQDQGLDTVEANEALGFPADARDYGLAAQILRDLGIKSVRLLTNNPDKIDALEGY 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 490241267 162 GINIVERVPLIVGRNPKNAHYLDTKAAKMGHLL 194
Cdd:cd00641  161 GIEVVERVPLEVEPNEENKGYLKTKRDKMGHLL 193
RibA COG0807
GTP cyclohydrolase II [Coenzyme transport and metabolism]; GTP cyclohydrolase II is part of ...
 3-195 4.48e-117

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: 337.71  E-value: 4.48e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267   3 LKRVAEAKLPTPWGDFLMVGFEELATGQDHVALVFGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAEEG 82
Cdd:COG0807  206 VERVAEARLPTEFGEFRLHAYRDTIDGQEHLALVKGDPDPDEPVLVRVHSECLTGDVFGSLRCDCGWQLEAALKRIAEEG 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267  83 RGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVDQVRLLTNNPKKVEILTEAG 162
Cdd:COG0807  286 RGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADLRDYGIGAQILRDLGVRKMRLLTNNPRKVVGLEGYG 365

                        170       180       190
                 ....*....|....*....|....*....|...
gi 490241267 163 INIVERVPLIVGRNPKNAHYLDTKAAKMGHLLS 195
Cdd:COG0807  366 LEVVERVPLEVGPNPHNERYLRTKRDKMGHLLD 398
GTP_cyclohydro2 pfam00925
GTP cyclohydrolase II; GTP cyclohydrolase II catalyzes the first committed step in the ...
 49-170 1.67e-72

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: 215.01  E-value: 1.67e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267   49 RVHSECLTGDALFSLRCDCGFQLEAALSHIAEEGRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADER 128
Cdd:pfam00925   2 RVHSECLTGDVLGSLRCDCGEQLEAALRAIAEEGRGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADLR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 490241267  129 DFTLCADMFKLLNVDQVRLLTNNPKKVEILTEAGINIVERVP 170
Cdd:pfam00925  82 DYGIGAQILRDLGVKKIRLLTNNPRKIVGLEGYGLEVVERVP 123
 
Name Accession Description Interval E-value
ribA PRK00393
GTP cyclohydrolase II RibA;
1-195 1.35e-155

GTP cyclohydrolase II RibA;


Pssm-ID: 234745  Cd Length: 197  Bit Score: 427.72  E-value: 1.35e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267   1 MQLKRVAEAKLPTPWGDFLMVGFEELATGQDHVALVFGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAE 80
Cdd:PRK00393   1 MQLKRVAEAKLPTPWGDFLMVGFEELATGKEHVALVFGDISGTEPVLVRVHSECLTGDALFSLRCDCGFQLEAALERIAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267  81 EGRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVDQVRLLTNNPKKVEILTE 160
Cdd:PRK00393  81 EGRGILLYLRQEGRGIGLLNKIRAYALQDQGLDTVEANHQLGFAADERDYTLAADMLKALGVKKVRLLTNNPKKVEALTE 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 490241267 161 AGINIVERVPLIVGRNPKNAHYLDTKAAKMGHLLS 195
Cdd:PRK00393 161 AGINIVERVPLIVGRNPHNEHYLKTKAEKMGHLLS 195
ribA TIGR00505
GTP cyclohydrolase II; Several members of the family are bifunctional, involving both ribA and ...
 4-194 9.73e-121

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: 339.45  E-value: 9.73e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267    4 KRVAEAKLPTPWGDFLMVGFEELATGQDHVALVFGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAEEGR 83
Cdd:TIGR00505   1 ERVAEAKLPTPYGDFYMVGFEEPATGKDHVALVKGDISAHTDVLVRIHSECLTGDALHSLRCDCGFQLEAALKQIAEEGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267   84 GILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVDQVRLLTNNPKKVEILTEAGI 163
Cdd:TIGR00505  81 GVLIYLRQEGRGIGLINKLRAYALQDKGYDTVQANLMLGFPADERDFSLCADILEDLGVKKVRLLTNNPKKIEILKKAGI 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 490241267  164 NIVERVPLIVGRNPKNAHYLDTKAAKMGHLL 194
Cdd:TIGR00505 161 NIVERVPLIVGRNENNEGYLDTKAEKMGHLL 191
GTP_cyclohydro2 cd00641
GTP cyclohydrolase II (RibA). GTP cyclohydrolase II catalyzes the conversion of GTP to 2, ...
 2-194 6.01e-119

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: 334.85  E-value: 6.01e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267   2 QLKRVAEAKLPTPWGDFLMVGFEELATGQDHVALVFGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAEE 81
Cdd:cd00641    1 LVEKVAEAPLPTRFGDFRIVAFEDTDDGKEHVALVKGDPADGEPVLVRVHSECLTGDVFGSLRCDCGPQLEEALEEIAEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267  82 GRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVDQVRLLTNNPKKVEILTEA 161
Cdd:cd00641   81 GGGVLLYLRQEGRGIGLANKLRAYALQDQGLDTVEANEALGFPADARDYGLAAQILRDLGIKSVRLLTNNPDKIDALEGY 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 490241267 162 GINIVERVPLIVGRNPKNAHYLDTKAAKMGHLL 194
Cdd:cd00641  161 GIEVVERVPLEVEPNEENKGYLKTKRDKMGHLL 193
RibA COG0807
GTP cyclohydrolase II [Coenzyme transport and metabolism]; GTP cyclohydrolase II is part of ...
 3-195 4.48e-117

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: 337.71  E-value: 4.48e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267   3 LKRVAEAKLPTPWGDFLMVGFEELATGQDHVALVFGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAEEG 82
Cdd:COG0807  206 VERVAEARLPTEFGEFRLHAYRDTIDGQEHLALVKGDPDPDEPVLVRVHSECLTGDVFGSLRCDCGWQLEAALKRIAEEG 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267  83 RGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVDQVRLLTNNPKKVEILTEAG 162
Cdd:COG0807  286 RGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADLRDYGIGAQILRDLGVRKMRLLTNNPRKVVGLEGYG 365

                        170       180       190
                 ....*....|....*....|....*....|...
gi 490241267 163 INIVERVPLIVGRNPKNAHYLDTKAAKMGHLLS 195
Cdd:COG0807  366 LEVVERVPLEVGPNPHNERYLRTKRDKMGHLLD 398
PRK09311 PRK09311
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
2-194 1.46e-92

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


Pssm-ID: 181774 [Multi-domain]  Cd Length: 402  Bit Score: 275.63  E-value: 1.46e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267   2 QLKRVAEAKLPTPWGDFLMVGFEELATGQDHVALVFGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAEE 81
Cdd:PRK09311 206 LVEREVEARLPTRFGEFRAIGYTSILDGKEHVALVKGDIGDGEDVLVRVHSECLTGDVFGSRRCDCGPQLDAALAQIAEE 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267  82 GRGILLYHR-QEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVDQVRLLTNNPKKVEILTE 160
Cdd:PRK09311 286 GRGVVLYMRgQEGRGIGLLHKLRAYQLQDEGYDTVDANLKLGFPADARDYGIGAQILVDLGVRSMRLLTNNPRKIAGLQG 365

                        170       180       190
                 ....*....|....*....|....*....|....
gi 490241267 161 AGINIVERVPLIVGRNPKNAHYLDTKAAKMGHLL 194
Cdd:PRK09311 366 YGLHVTERVPLPVRANEENERYLRTKRDRMGHDL 399
PRK09319 PRK09319
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase RibB/GTP cyclohydrolase II RibA;
4-196 1.44e-82

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


Pssm-ID: 236465 [Multi-domain]  Cd Length: 555  Bit Score: 254.49  E-value: 1.44e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267   4 KRVAEAKLPTPWGDFLMVGFEELATGQDHVALVFGDIS--GQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAEE 81
Cdd:PRK09319 211 YREAVAKLPSQFGQFQAYGYRNELDGSEHVALVKGDPAnfKDEPVLVRMHSECLTGDAFGSLRCDCRMQLEAALKMIENE 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267  82 GRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVDQVRLLTNNPKKVEILTEA 161
Cdd:PRK09319 291 GEGVVVYLRQEGRGIGLINKLKAYSLQDGGLDTVEANERLGFPADLRNYGVGAQILNDLGIKRLRLITNNPRKIAGLGGY 370

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 490241267 162 GINIVERVPLIVGRNPKNAHYLDTKAAKMGHLLSQ 196
Cdd:PRK09319 371 GLEVVDRVPLLIEANDYNAEYLATKAEKLGHLLLQ 405
PRK09318 PRK09318
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
2-195 4.39e-76

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


Pssm-ID: 236464 [Multi-domain]  Cd Length: 387  Bit Score: 233.09  E-value: 4.39e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267   2 QLKRV-AEAKLPTPWGDFLMVGFEELATGQDHVALV---FGDIsgqspVLARVHSECLTGDALFSLRCDCGFQLEAALSH 77
Cdd:PRK09318 190 QLIKVkAEAKLPTDYGEFEIVSFENHLDGKEHVAIVkepLGEV-----PLVRIHSECVTGDTLSSLRCDCGSQLANFLRM 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267  78 IAEEGrGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVDQVRLLTNNPKKVEI 157
Cdd:PRK09318 265 ISKEG-GILIYLRQEGRGIGLSNKIKAYELQDKGLDTVEANRALGFKEDERDYAAAFQILKALGIEKVRLLTNNPRKTKA 343

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 490241267 158 LTEAGINIVERVPLIVGRNPKNAHYLDTKAAKMGHLLS 195
Cdd:PRK09318 344 LEKYGIEVVETVPLYGEVTKYNRFYLKTKVEKLGHKLE 381
GTP_cyclohydro2 pfam00925
GTP cyclohydrolase II; GTP cyclohydrolase II catalyzes the first committed step in the ...
 49-170 1.67e-72

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: 215.01  E-value: 1.67e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267   49 RVHSECLTGDALFSLRCDCGFQLEAALSHIAEEGRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADER 128
Cdd:pfam00925   2 RVHSECLTGDVLGSLRCDCGEQLEAALRAIAEEGRGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADLR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 490241267  129 DFTLCADMFKLLNVDQVRLLTNNPKKVEILTEAGINIVERVP 170
Cdd:pfam00925  82 DYGIGAQILRDLGVKKIRLLTNNPRKIVGLEGYGLEVVERVP 123
PLN02831 PLN02831
Bifunctional GTP cyclohydrolase II/ 3,4-dihydroxy-2-butanone-4-phosphate synthase
 4-193 5.64e-71

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


Pssm-ID: 215445 [Multi-domain]  Cd Length: 450  Bit Score: 221.89  E-value: 5.64e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267   4 KRVAEAKLPTPWGDFLMVGFEELATGQDHVALVFGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAEEGR 83
Cdd:PLN02831 242 ERTAVARLPTKWGLFTAYCYRSKLDGIEHIAFVKGDIGDGQDVLVRVHSECLTGDIFGSARCDCGNQLALAMQLIEKAGR 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267  84 GILLYHR-QEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVDQVRLLTNNPKKVEILTEAG 162
Cdd:PLN02831 322 GVLVYLRgHEGRGIGLGHKLRAYNLQDEGRDTVEANEELGLPVDSREYGIGAQILRDLGVRTMRLMTNNPAKYTGLKGYG 401

                        170       180       190
                 ....*....|....*....|....*....|.
gi 490241267 163 INIVERVPLIVGRNPKNAHYLDTKAAKMGHL 193
Cdd:PLN02831 402 LAVVGRVPLLTPITKENKRYLETKRTKMGHV 432
PRK08815 PRK08815
GTP cyclohydrolase II RibA;
12-194 6.96e-59

GTP cyclohydrolase II RibA;


Pssm-ID: 236340 [Multi-domain]  Cd Length: 375  Bit Score: 188.81  E-value: 6.96e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267  12 PTPWGDFLMVGFEELATG---QDHVALVFGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAEEGRGILLY 88
Cdd:PRK08815 180 PVPLRGLGMTEFVVFRGGvaqRDQVAIVVGQPDLSSAVPVRVHSSCLTGDLFGSLKCDCGDQLRHGLAKLKELGGGVLLY 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267  89 HRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVDQVRLLTNNPKKVEILTEAGINIVER 168
Cdd:PRK08815 260 LDQEGRGNGIAAKMRAYGYQHAGLDTIDADAQLGFGPDERRYGSAVAMLRGLGITRVRLLTNNPTKAERLRAAGIEVEDR 339

                        170       180
                 ....*....|....*....|....*.
gi 490241267 169 VPLIVGRNPKNAHYLDTKAAKMGHLL 194
Cdd:PRK08815 340 IRVTGRITAENERYLRTKADRAGHAL 365
PRK14019 PRK14019
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
3-170 5.14e-18

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


Pssm-ID: 237587 [Multi-domain]  Cd Length: 367  Bit Score: 80.39  E-value: 5.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267   3 LKRVAEAKLPTPWGDFLMVGFEELATGQDHVALVFGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAEEG 82
Cdd:PRK14019 206 VERVAERPMQTAHGEFRLVAYRDKPSGSTHLALVKGTICPDEETLVRVHEPLSVLDLLEVGQPTHSWSLDAAMAAIAEAG 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267  83 RG-ILLYHRQEGrnigllnkirAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVDQVRLLTnNPKKVEILTEA 161
Cdd:PRK14019 286 SGvVVLLNCGDD----------GEHLLDRFRAEEAAAALKRRPVDYRTYGIGAQILRDLGVGKMRLLS-SPRKFPSMSGF 354


                 ....*....
gi 490241267 162 GINIVERVP 170
Cdd:PRK14019 355 GLEVTGYVP 363
PRK07198 PRK07198
GTP cyclohydrolase II;
23-171 1.15e-09

GTP cyclohydrolase II;


Pssm-ID: 235959 [Multi-domain]  Cd Length: 418  Bit Score: 56.59  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267  23 FEELATGQD-HVAL---------VFGDIS----GQSPVLARVHSECLTGDALFSLRCDCgfqlEAALSHIAEE------- 81
Cdd:PRK07198 203 FPELVTRPDlEVFLppiggqtvyIFGDVTdladPETELTCRVHDECNGSDVFGSDICTC----RPYLTHGIEEcirgaqr 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267  82 -GRGILLYHRQEGRNIGLLNKIRAY-ALQDQ-GYDTVEANhqlgFA--------ADERDFTLCADMFKLLNVDQV-RLLT 149
Cdd:PRK07198 279 gGVGLIVYNRKEGRALGEVTKFLVYnARKRQvGGDTAATY----FArtecvagvQDMRFQELMPDVLHWLGIRRIhRLVS 354

                        170       180
                 ....*....|....*....|..
gi 490241267 150 NNPKKVEILTEAGINIVERVPL 171
Cdd:PRK07198 355 MSNMKYDAITGSGIEVGERVPI 376
PRK12485 PRK12485
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
3-102 1.79e-09

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


Pssm-ID: 171535 [Multi-domain]  Cd Length: 369  Bit Score: 56.12  E-value: 1.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490241267   3 LKRVAEAKLPTPWGDFLMVGFEELATGQDHVALVFGDISGQSPVLARVHseclTGDALFSL-----RCDCGFQLEAALSH 77
Cdd:PRK12485 206 IKRIGERELPTVHGTFRLVTYEDRIEGGVHMAMVMGDIRREQPTLVRVH----VIDPLRDLvgaeyAGPANWTLWAALQK 281

                         90       100
                 ....*....|....*....|....*
gi 490241267  78 IAEEGRGILLYHRQEGRNIGLLNKI 102
Cdd:PRK12485 282 VAEEGHGVVVVLANHESSQALLERI 306
 
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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