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Conserved domains on  [gi|1733043988|gb|TYT19101|]
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GTP cyclohydrolase II [Klebsiella pneumoniae]

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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
ribA PRK00393
GTP cyclohydrolase II RibA;
1-197 5.38e-155

GTP cyclohydrolase II RibA;


:

Pssm-ID: 234745  Cd Length: 197  Bit Score: 426.18  E-value: 5.38e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988   1 MQLKRVAEAKLPTPWGDFLMVGFEELATGQDHVALVYGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAE 80
Cdd:PRK00393    1 MQLKRVAEAKLPTPWGDFLMVGFEELATGKEHVALVFGDISGTEPVLVRVHSECLTGDALFSLRCDCGFQLEAALERIAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988  81 EGRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVEQVRLLTNNPKKVEILTE 160
Cdd:PRK00393   81 EGRGILLYLRQEGRGIGLLNKIRAYALQDQGLDTVEANHQLGFAADERDYTLAADMLKALGVKKVRLLTNNPKKVEALTE 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1733043988 161 AGINIVERVPLIVGRNPKNAHYLDTKAAKMGHLLNSK 197
Cdd:PRK00393  161 AGINIVERVPLIVGRNPHNEHYLKTKAEKMGHLLSLD 197
 
Name Accession Description Interval E-value
ribA PRK00393
GTP cyclohydrolase II RibA;
1-197 5.38e-155

GTP cyclohydrolase II RibA;


Pssm-ID: 234745  Cd Length: 197  Bit Score: 426.18  E-value: 5.38e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988   1 MQLKRVAEAKLPTPWGDFLMVGFEELATGQDHVALVYGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAE 80
Cdd:PRK00393    1 MQLKRVAEAKLPTPWGDFLMVGFEELATGKEHVALVFGDISGTEPVLVRVHSECLTGDALFSLRCDCGFQLEAALERIAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988  81 EGRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVEQVRLLTNNPKKVEILTE 160
Cdd:PRK00393   81 EGRGILLYLRQEGRGIGLLNKIRAYALQDQGLDTVEANHQLGFAADERDYTLAADMLKALGVKKVRLLTNNPKKVEALTE 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1733043988 161 AGINIVERVPLIVGRNPKNAHYLDTKAAKMGHLLNSK 197
Cdd:PRK00393  161 AGINIVERVPLIVGRNPHNEHYLKTKAEKMGHLLSLD 197
ribA TIGR00505
GTP cyclohydrolase II; Several members of the family are bifunctional, involving both ribA and ...
 4-194 4.70e-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: 340.60  E-value: 4.70e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988   4 KRVAEAKLPTPWGDFLMVGFEELATGQDHVALVYGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAEEGR 83
Cdd:TIGR00505   1 ERVAEAKLPTPYGDFYMVGFEEPATGKDHVALVKGDISAHTDVLVRIHSECLTGDALHSLRCDCGFQLEAALKQIAEEGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988  84 GILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVEQVRLLTNNPKKVEILTEAGI 163
Cdd:TIGR00505  81 GVLIYLRQEGRGIGLINKLRAYALQDKGYDTVQANLMLGFPADERDFSLCADILEDLGVKKVRLLTNNPKKIEILKKAGI 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1733043988 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 5.79e-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: 335.24  E-value: 5.79e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988   2 QLKRVAEAKLPTPWGDFLMVGFEELATGQDHVALVYGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAEE 81
Cdd:cd00641     1 LVEKVAEAPLPTRFGDFRIVAFEDTDDGKEHVALVKGDPADGEPVLVRVHSECLTGDVFGSLRCDCGPQLEEALEEIAEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988  82 GRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVEQVRLLTNNPKKVEILTEA 161
Cdd:cd00641    81 GGGVLLYLRQEGRGIGLANKLRAYALQDQGLDTVEANEALGFPADARDYGLAAQILRDLGIKSVRLLTNNPDKIDALEGY 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1733043988 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 9.28e-118

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: 339.64  E-value: 9.28e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988   3 LKRVAEAKLPTPWGDFLMVGFEELATGQDHVALVYGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAEEG 82
Cdd:COG0807   206 VERVAEARLPTEFGEFRLHAYRDTIDGQEHLALVKGDPDPDEPVLVRVHSECLTGDVFGSLRCDCGWQLEAALKRIAEEG 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988  83 RGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVEQVRLLTNNPKKVEILTEAG 162
Cdd:COG0807   286 RGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADLRDYGIGAQILRDLGVRKMRLLTNNPRKVVGLEGYG 365

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1733043988 163 INIVERVPLIVGRNPKNAHYLDTKAAKMGHLLN 195
Cdd:COG0807   366 LEVVERVPLEVGPNPHNERYLRTKRDKMGHLLD 398
GTP_cyclohydro2 pfam00925
GTP cyclohydrolase II; GTP cyclohydrolase II catalyzes the first committed step in the ...
 49-170 5.21e-73

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: 216.17  E-value: 5.21e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988  49 RVHSECLTGDALFSLRCDCGFQLEAALSHIAEEGRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADER 128
Cdd:pfam00925   2 RVHSECLTGDVLGSLRCDCGEQLEAALRAIAEEGRGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADLR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1733043988 129 DFTLCADMFKLLNVEQVRLLTNNPKKVEILTEAGINIVERVP 170
Cdd:pfam00925  82 DYGIGAQILRDLGVKKIRLLTNNPRKIVGLEGYGLEVVERVP 123
 
Name Accession Description Interval E-value
ribA PRK00393
GTP cyclohydrolase II RibA;
1-197 5.38e-155

GTP cyclohydrolase II RibA;


Pssm-ID: 234745  Cd Length: 197  Bit Score: 426.18  E-value: 5.38e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988   1 MQLKRVAEAKLPTPWGDFLMVGFEELATGQDHVALVYGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAE 80
Cdd:PRK00393    1 MQLKRVAEAKLPTPWGDFLMVGFEELATGKEHVALVFGDISGTEPVLVRVHSECLTGDALFSLRCDCGFQLEAALERIAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988  81 EGRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVEQVRLLTNNPKKVEILTE 160
Cdd:PRK00393   81 EGRGILLYLRQEGRGIGLLNKIRAYALQDQGLDTVEANHQLGFAADERDYTLAADMLKALGVKKVRLLTNNPKKVEALTE 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1733043988 161 AGINIVERVPLIVGRNPKNAHYLDTKAAKMGHLLNSK 197
Cdd:PRK00393  161 AGINIVERVPLIVGRNPHNEHYLKTKAEKMGHLLSLD 197
ribA TIGR00505
GTP cyclohydrolase II; Several members of the family are bifunctional, involving both ribA and ...
 4-194 4.70e-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: 340.60  E-value: 4.70e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988   4 KRVAEAKLPTPWGDFLMVGFEELATGQDHVALVYGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAEEGR 83
Cdd:TIGR00505   1 ERVAEAKLPTPYGDFYMVGFEEPATGKDHVALVKGDISAHTDVLVRIHSECLTGDALHSLRCDCGFQLEAALKQIAEEGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988  84 GILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVEQVRLLTNNPKKVEILTEAGI 163
Cdd:TIGR00505  81 GVLIYLRQEGRGIGLINKLRAYALQDKGYDTVQANLMLGFPADERDFSLCADILEDLGVKKVRLLTNNPKKIEILKKAGI 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1733043988 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 5.79e-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: 335.24  E-value: 5.79e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988   2 QLKRVAEAKLPTPWGDFLMVGFEELATGQDHVALVYGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAEE 81
Cdd:cd00641     1 LVEKVAEAPLPTRFGDFRIVAFEDTDDGKEHVALVKGDPADGEPVLVRVHSECLTGDVFGSLRCDCGPQLEEALEEIAEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988  82 GRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVEQVRLLTNNPKKVEILTEA 161
Cdd:cd00641    81 GGGVLLYLRQEGRGIGLANKLRAYALQDQGLDTVEANEALGFPADARDYGLAAQILRDLGIKSVRLLTNNPDKIDALEGY 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1733043988 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 9.28e-118

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: 339.64  E-value: 9.28e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988   3 LKRVAEAKLPTPWGDFLMVGFEELATGQDHVALVYGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAEEG 82
Cdd:COG0807   206 VERVAEARLPTEFGEFRLHAYRDTIDGQEHLALVKGDPDPDEPVLVRVHSECLTGDVFGSLRCDCGWQLEAALKRIAEEG 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988  83 RGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVEQVRLLTNNPKKVEILTEAG 162
Cdd:COG0807   286 RGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADLRDYGIGAQILRDLGVRKMRLLTNNPRKVVGLEGYG 365

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1733043988 163 INIVERVPLIVGRNPKNAHYLDTKAAKMGHLLN 195
Cdd:COG0807   366 LEVVERVPLEVGPNPHNERYLRTKRDKMGHLLD 398
PRK09311 PRK09311
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
2-195 7.48e-94

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


Pssm-ID: 181774 [Multi-domain]  Cd Length: 402  Bit Score: 279.09  E-value: 7.48e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988   2 QLKRVAEAKLPTPWGDFLMVGFEELATGQDHVALVYGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAEE 81
Cdd:PRK09311  206 LVEREVEARLPTRFGEFRAIGYTSILDGKEHVALVKGDIGDGEDVLVRVHSECLTGDVFGSRRCDCGPQLDAALAQIAEE 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988  82 GRGILLYHR-QEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVEQVRLLTNNPKKVEILTE 160
Cdd:PRK09311  286 GRGVVLYMRgQEGRGIGLLHKLRAYQLQDEGYDTVDANLKLGFPADARDYGIGAQILVDLGVRSMRLLTNNPRKIAGLQG 365

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1733043988 161 AGINIVERVPLIVGRNPKNAHYLDTKAAKMGHLLN 195
Cdd:PRK09311  366 YGLHVTERVPLPVRANEENERYLRTKRDRMGHDLD 400
PRK09319 PRK09319
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase RibB/GTP cyclohydrolase II RibA;
4-196 1.65e-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: 1.65e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988   4 KRVAEAKLPTPWGDFLMVGFEELATGQDHVALVYGDIS--GQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAEE 81
Cdd:PRK09319  211 YREAVAKLPSQFGQFQAYGYRNELDGSEHVALVKGDPAnfKDEPVLVRMHSECLTGDAFGSLRCDCRMQLEAALKMIENE 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988  82 GRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVEQVRLLTNNPKKVEILTEA 161
Cdd:PRK09319  291 GEGVVVYLRQEGRGIGLINKLKAYSLQDGGLDTVEANERLGFPADLRNYGVGAQILNDLGIKRLRLITNNPRKIAGLGGY 370

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1733043988 162 GINIVERVPLIVGRNPKNAHYLDTKAAKMGHLLNS 196
Cdd:PRK09319  371 GLEVVDRVPLLIEANDYNAEYLATKAEKLGHLLLQ 405
PRK09318 PRK09318
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
2-200 7.81e-76

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


Pssm-ID: 236464 [Multi-domain]  Cd Length: 387  Bit Score: 232.70  E-value: 7.81e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988   2 QLKRV-AEAKLPTPWGDFLMVGFEELATGQDHVALV---YGDIsgqspVLARVHSECLTGDALFSLRCDCGFQLEAALSH 77
Cdd:PRK09318  190 QLIKVkAEAKLPTDYGEFEIVSFENHLDGKEHVAIVkepLGEV-----PLVRIHSECVTGDTLSSLRCDCGSQLANFLRM 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988  78 IAEEGrGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVEQVRLLTNNPKKVEI 157
Cdd:PRK09318  265 ISKEG-GILIYLRQEGRGIGLSNKIKAYELQDKGLDTVEANRALGFKEDERDYAAAFQILKALGIEKVRLLTNNPRKTKA 343

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1733043988 158 LTEAGINIVERVPLIVGRNPKNAHYLDTKAAKMGHLLNSKPTE 200
Cdd:PRK09318  344 LEKYGIEVVETVPLYGEVTKYNRFYLKTKVEKLGHKLELREVN 386
GTP_cyclohydro2 pfam00925
GTP cyclohydrolase II; GTP cyclohydrolase II catalyzes the first committed step in the ...
 49-170 5.21e-73

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: 216.17  E-value: 5.21e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988  49 RVHSECLTGDALFSLRCDCGFQLEAALSHIAEEGRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADER 128
Cdd:pfam00925   2 RVHSECLTGDVLGSLRCDCGEQLEAALRAIAEEGRGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADLR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1733043988 129 DFTLCADMFKLLNVEQVRLLTNNPKKVEILTEAGINIVERVP 170
Cdd:pfam00925  82 DYGIGAQILRDLGVKKIRLLTNNPRKIVGLEGYGLEVVERVP 123
PLN02831 PLN02831
Bifunctional GTP cyclohydrolase II/ 3,4-dihydroxy-2-butanone-4-phosphate synthase
 4-197 2.80e-72

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


Pssm-ID: 215445 [Multi-domain]  Cd Length: 450  Bit Score: 225.35  E-value: 2.80e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988   4 KRVAEAKLPTPWGDFLMVGFEELATGQDHVALVYGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAEEGR 83
Cdd:PLN02831  242 ERTAVARLPTKWGLFTAYCYRSKLDGIEHIAFVKGDIGDGQDVLVRVHSECLTGDIFGSARCDCGNQLALAMQLIEKAGR 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988  84 GILLYHR-QEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVEQVRLLTNNPKKVEILTEAG 162
Cdd:PLN02831  322 GVLVYLRgHEGRGIGLGHKLRAYNLQDEGRDTVEANEELGLPVDSREYGIGAQILRDLGVRTMRLMTNNPAKYTGLKGYG 401

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1733043988 163 INIVERVPLIVGRNPKNAHYLDTKAAKMGHLLNSK 197
Cdd:PLN02831  402 LAVVGRVPLLTPITKENKRYLETKRTKMGHVYGSD 436
PRK08815 PRK08815
GTP cyclohydrolase II RibA;
12-195 1.97e-59

GTP cyclohydrolase II RibA;


Pssm-ID: 236340 [Multi-domain]  Cd Length: 375  Bit Score: 190.35  E-value: 1.97e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988  12 PTPWGDFLMVGFEELATG---QDHVALVYGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAEEGRGILLY 88
Cdd:PRK08815  180 PVPLRGLGMTEFVVFRGGvaqRDQVAIVVGQPDLSSAVPVRVHSSCLTGDLFGSLKCDCGDQLRHGLAKLKELGGGVLLY 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988  89 HRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVEQVRLLTNNPKKVEILTEAGINIVER 168
Cdd:PRK08815  260 LDQEGRGNGIAAKMRAYGYQHAGLDTIDADAQLGFGPDERRYGSAVAMLRGLGITRVRLLTNNPTKAERLRAAGIEVEDR 339

                         170       180
                  ....*....|....*....|....*..
gi 1733043988 169 VPLIVGRNPKNAHYLDTKAAKMGHLLN 195
Cdd:PRK08815  340 IRVTGRITAENERYLRTKADRAGHALD 366
PRK14019 PRK14019
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
3-170 3.27e-18

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


Pssm-ID: 237587 [Multi-domain]  Cd Length: 367  Bit Score: 81.16  E-value: 3.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988   3 LKRVAEAKLPTPWGDFLMVGFEELATGQDHVALVYGDISGQSPVLARVHSECLTGDALFSLRCDCGFQLEAALSHIAEEG 82
Cdd:PRK14019  206 VERVAERPMQTAHGEFRLVAYRDKPSGSTHLALVKGTICPDEETLVRVHEPLSVLDLLEVGQPTHSWSLDAAMAAIAEAG 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988  83 RG-ILLYHRQEGrnigllnkirAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLNVEQVRLLTnNPKKVEILTEA 161
Cdd:PRK14019  286 SGvVVLLNCGDD----------GEHLLDRFRAEEAAAALKRRPVDYRTYGIGAQILRDLGVGKMRLLS-SPRKFPSMSGF 354


                  ....*....
gi 1733043988 162 GINIVERVP 170
Cdd:PRK14019  355 GLEVTGYVP 363
PRK12485 PRK12485
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
3-102 2.75e-09

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


Pssm-ID: 171535 [Multi-domain]  Cd Length: 369  Bit Score: 55.74  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988   3 LKRVAEAKLPTPWGDFLMVGFEELATGQDHVALVYGDISGQSPVLARVHseclTGDALFSL-----RCDCGFQLEAALSH 77
Cdd:PRK12485  206 IKRIGERELPTVHGTFRLVTYEDRIEGGVHMAMVMGDIRREQPTLVRVH----VIDPLRDLvgaeyAGPANWTLWAALQK 281

                          90       100
                  ....*....|....*....|....*
gi 1733043988  78 IAEEGRGILLYHRQEGRNIGLLNKI 102
Cdd:PRK12485  282 VAEEGHGVVVVLANHESSQALLERI 306
PRK07198 PRK07198
GTP cyclohydrolase II;
23-171 5.84e-09

GTP cyclohydrolase II;


Pssm-ID: 235959 [Multi-domain]  Cd Length: 418  Bit Score: 54.67  E-value: 5.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988  23 FEELATGQD-HVAL---------VYGDIS----GQSPVLARVHSECLTGDALFSLRCDCgfqlEAALSHIAEE------- 81
Cdd:PRK07198  203 FPELVTRPDlEVFLppiggqtvyIFGDVTdladPETELTCRVHDECNGSDVFGSDICTC----RPYLTHGIEEcirgaqr 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733043988  82 -GRGILLYHRQEGRNIGLLNKIRAY-ALQDQ-GYDTVEANhqlgFA--------ADERDFTLCADMFKLLNVEQV-RLLT 149
Cdd:PRK07198  279 gGVGLIVYNRKEGRALGEVTKFLVYnARKRQvGGDTAATY----FArtecvagvQDMRFQELMPDVLHWLGIRRIhRLVS 354

                         170       180
                  ....*....|....*....|..
gi 1733043988 150 NNPKKVEILTEAGINIVERVPL 171
Cdd:PRK07198  355 MSNMKYDAITGSGIEVGERVPI 376
 
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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