NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1374091081|ref|WP_107167579|]
View 

MULTISPECIES: GTP cyclohydrolase II [Pectobacterium]

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

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ribA PRK00393
GTP cyclohydrolase II RibA;
1-195 1.44e-151

GTP cyclohydrolase II RibA;


:

Pssm-ID: 234745  Cd Length: 197  Bit Score: 417.71  E-value: 1.44e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081   1 MQLKRVAEAKLPTPWGDFLMVGFEEIATGHDHLALVYGDISGSVPVLARVHSECLTGDALFSLRCDCGFQLEAALGHIAE 80
Cdd:PRK00393    1 MQLKRVAEAKLPTPWGDFLMVGFEELATGKEHVALVFGDISGTEPVLVRVHSECLTGDALFSLRCDCGFQLEAALERIAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081  81 EGRGVLLYHRQEGRNIGLLNKIRAYALQDLGADTVEANHQLGFAADERDFTLCADMFKLLGVDEVRLLTNNPQKVKILNE 160
Cdd:PRK00393   81 EGRGILLYLRQEGRGIGLLNKIRAYALQDQGLDTVEANHQLGFAADERDYTLAADMLKALGVKKVRLLTNNPKKVEALTE 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1374091081 161 AGINIVERVPLIVGRNPKNENYLATKAAKMGHMLD 195
Cdd:PRK00393  161 AGINIVERVPLIVGRNPHNEHYLKTKAEKMGHLLS 195
 
Name Accession Description Interval E-value
ribA PRK00393
GTP cyclohydrolase II RibA;
1-195 1.44e-151

GTP cyclohydrolase II RibA;


Pssm-ID: 234745  Cd Length: 197  Bit Score: 417.71  E-value: 1.44e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081   1 MQLKRVAEAKLPTPWGDFLMVGFEEIATGHDHLALVYGDISGSVPVLARVHSECLTGDALFSLRCDCGFQLEAALGHIAE 80
Cdd:PRK00393    1 MQLKRVAEAKLPTPWGDFLMVGFEELATGKEHVALVFGDISGTEPVLVRVHSECLTGDALFSLRCDCGFQLEAALERIAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081  81 EGRGVLLYHRQEGRNIGLLNKIRAYALQDLGADTVEANHQLGFAADERDFTLCADMFKLLGVDEVRLLTNNPQKVKILNE 160
Cdd:PRK00393   81 EGRGILLYLRQEGRGIGLLNKIRAYALQDQGLDTVEANHQLGFAADERDYTLAADMLKALGVKKVRLLTNNPKKVEALTE 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1374091081 161 AGINIVERVPLIVGRNPKNENYLATKAAKMGHMLD 195
Cdd:PRK00393  161 AGINIVERVPLIVGRNPHNEHYLKTKAEKMGHLLS 195
ribA TIGR00505
GTP cyclohydrolase II; Several members of the family are bifunctional, involving both ribA and ...
 4-194 2.87e-117

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: 330.59  E-value: 2.87e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081   4 KRVAEAKLPTPWGDFLMVGFEEIATGHDHLALVYGDISGSVPVLARVHSECLTGDALFSLRCDCGFQLEAALGHIAEEGR 83
Cdd:TIGR00505   1 ERVAEAKLPTPYGDFYMVGFEEPATGKDHVALVKGDISAHTDVLVRIHSECLTGDALHSLRCDCGFQLEAALKQIAEEGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081  84 GVLLYHRQEGRNIGLLNKIRAYALQDLGADTVEANHQLGFAADERDFTLCADMFKLLGVDEVRLLTNNPQKVKILNEAGI 163
Cdd:TIGR00505  81 GVLIYLRQEGRGIGLINKLRAYALQDKGYDTVQANLMLGFPADERDFSLCADILEDLGVKKVRLLTNNPKKIEILKKAGI 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1374091081 164 NIVERVPLIVGRNPKNENYLATKAAKMGHML 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 1.36e-114

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: 324.07  E-value: 1.36e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081   2 QLKRVAEAKLPTPWGDFLMVGFEEIATGHDHLALVYGDISGSVPVLARVHSECLTGDALFSLRCDCGFQLEAALGHIAEE 81
Cdd:cd00641     1 LVEKVAEAPLPTRFGDFRIVAFEDTDDGKEHVALVKGDPADGEPVLVRVHSECLTGDVFGSLRCDCGPQLEEALEEIAEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081  82 GRGVLLYHRQEGRNIGLLNKIRAYALQDLGADTVEANHQLGFAADERDFTLCADMFKLLGVDEVRLLTNNPQKVKILNEA 161
Cdd:cd00641    81 GGGVLLYLRQEGRGIGLANKLRAYALQDQGLDTVEANEALGFPADARDYGLAAQILRDLGIKSVRLLTNNPDKIDALEGY 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1374091081 162 GINIVERVPLIVGRNPKNENYLATKAAKMGHML 194
Cdd:cd00641   161 GIEVVERVPLEVEPNEENKGYLKTKRDKMGHLL 193
RibA COG0807
GTP cyclohydrolase II [Coenzyme transport and metabolism]; GTP cyclohydrolase II is part of ...
 3-195 1.27e-112

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: 326.54  E-value: 1.27e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081   3 LKRVAEAKLPTPWGDFLMVGFEEIATGHDHLALVYGDISGSVPVLARVHSECLTGDALFSLRCDCGFQLEAALGHIAEEG 82
Cdd:COG0807   206 VERVAEARLPTEFGEFRLHAYRDTIDGQEHLALVKGDPDPDEPVLVRVHSECLTGDVFGSLRCDCGWQLEAALKRIAEEG 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081  83 RGVLLYHRQEGRNIGLLNKIRAYALQDLGADTVEANHQLGFAADERDFTLCADMFKLLGVDEVRLLTNNPQKVKILNEAG 162
Cdd:COG0807   286 RGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADLRDYGIGAQILRDLGVRKMRLLTNNPRKVVGLEGYG 365

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1374091081 163 INIVERVPLIVGRNPKNENYLATKAAKMGHMLD 195
Cdd:COG0807   366 LEVVERVPLEVGPNPHNERYLRTKRDKMGHLLD 398
GTP_cyclohydro2 pfam00925
GTP cyclohydrolase II; GTP cyclohydrolase II catalyzes the first committed step in the ...
 49-170 1.16e-70

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: 210.39  E-value: 1.16e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081  49 RVHSECLTGDALFSLRCDCGFQLEAALGHIAEEGRGVLLYHRQEGRNIGLLNKIRAYALQDLGADTVEANHQLGFAADER 128
Cdd:pfam00925   2 RVHSECLTGDVLGSLRCDCGEQLEAALRAIAEEGRGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADLR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1374091081 129 DFTLCADMFKLLGVDEVRLLTNNPQKVKILNEAGINIVERVP 170
Cdd:pfam00925  82 DYGIGAQILRDLGVKKIRLLTNNPRKIVGLEGYGLEVVERVP 123
 
Name Accession Description Interval E-value
ribA PRK00393
GTP cyclohydrolase II RibA;
1-195 1.44e-151

GTP cyclohydrolase II RibA;


Pssm-ID: 234745  Cd Length: 197  Bit Score: 417.71  E-value: 1.44e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081   1 MQLKRVAEAKLPTPWGDFLMVGFEEIATGHDHLALVYGDISGSVPVLARVHSECLTGDALFSLRCDCGFQLEAALGHIAE 80
Cdd:PRK00393    1 MQLKRVAEAKLPTPWGDFLMVGFEELATGKEHVALVFGDISGTEPVLVRVHSECLTGDALFSLRCDCGFQLEAALERIAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081  81 EGRGVLLYHRQEGRNIGLLNKIRAYALQDLGADTVEANHQLGFAADERDFTLCADMFKLLGVDEVRLLTNNPQKVKILNE 160
Cdd:PRK00393   81 EGRGILLYLRQEGRGIGLLNKIRAYALQDQGLDTVEANHQLGFAADERDYTLAADMLKALGVKKVRLLTNNPKKVEALTE 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1374091081 161 AGINIVERVPLIVGRNPKNENYLATKAAKMGHMLD 195
Cdd:PRK00393  161 AGINIVERVPLIVGRNPHNEHYLKTKAEKMGHLLS 195
ribA TIGR00505
GTP cyclohydrolase II; Several members of the family are bifunctional, involving both ribA and ...
 4-194 2.87e-117

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: 330.59  E-value: 2.87e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081   4 KRVAEAKLPTPWGDFLMVGFEEIATGHDHLALVYGDISGSVPVLARVHSECLTGDALFSLRCDCGFQLEAALGHIAEEGR 83
Cdd:TIGR00505   1 ERVAEAKLPTPYGDFYMVGFEEPATGKDHVALVKGDISAHTDVLVRIHSECLTGDALHSLRCDCGFQLEAALKQIAEEGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081  84 GVLLYHRQEGRNIGLLNKIRAYALQDLGADTVEANHQLGFAADERDFTLCADMFKLLGVDEVRLLTNNPQKVKILNEAGI 163
Cdd:TIGR00505  81 GVLIYLRQEGRGIGLINKLRAYALQDKGYDTVQANLMLGFPADERDFSLCADILEDLGVKKVRLLTNNPKKIEILKKAGI 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1374091081 164 NIVERVPLIVGRNPKNENYLATKAAKMGHML 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 1.36e-114

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: 324.07  E-value: 1.36e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081   2 QLKRVAEAKLPTPWGDFLMVGFEEIATGHDHLALVYGDISGSVPVLARVHSECLTGDALFSLRCDCGFQLEAALGHIAEE 81
Cdd:cd00641     1 LVEKVAEAPLPTRFGDFRIVAFEDTDDGKEHVALVKGDPADGEPVLVRVHSECLTGDVFGSLRCDCGPQLEEALEEIAEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081  82 GRGVLLYHRQEGRNIGLLNKIRAYALQDLGADTVEANHQLGFAADERDFTLCADMFKLLGVDEVRLLTNNPQKVKILNEA 161
Cdd:cd00641    81 GGGVLLYLRQEGRGIGLANKLRAYALQDQGLDTVEANEALGFPADARDYGLAAQILRDLGIKSVRLLTNNPDKIDALEGY 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1374091081 162 GINIVERVPLIVGRNPKNENYLATKAAKMGHML 194
Cdd:cd00641   161 GIEVVERVPLEVEPNEENKGYLKTKRDKMGHLL 193
RibA COG0807
GTP cyclohydrolase II [Coenzyme transport and metabolism]; GTP cyclohydrolase II is part of ...
 3-195 1.27e-112

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: 326.54  E-value: 1.27e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081   3 LKRVAEAKLPTPWGDFLMVGFEEIATGHDHLALVYGDISGSVPVLARVHSECLTGDALFSLRCDCGFQLEAALGHIAEEG 82
Cdd:COG0807   206 VERVAEARLPTEFGEFRLHAYRDTIDGQEHLALVKGDPDPDEPVLVRVHSECLTGDVFGSLRCDCGWQLEAALKRIAEEG 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081  83 RGVLLYHRQEGRNIGLLNKIRAYALQDLGADTVEANHQLGFAADERDFTLCADMFKLLGVDEVRLLTNNPQKVKILNEAG 162
Cdd:COG0807   286 RGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADLRDYGIGAQILRDLGVRKMRLLTNNPRKVVGLEGYG 365

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1374091081 163 INIVERVPLIVGRNPKNENYLATKAAKMGHMLD 195
Cdd:COG0807   366 LEVVERVPLEVGPNPHNERYLRTKRDKMGHLLD 398
PRK09311 PRK09311
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
2-195 1.28e-91

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


Pssm-ID: 181774 [Multi-domain]  Cd Length: 402  Bit Score: 273.32  E-value: 1.28e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081   2 QLKRVAEAKLPTPWGDFLMVGFEEIATGHDHLALVYGDISGSVPVLARVHSECLTGDALFSLRCDCGFQLEAALGHIAEE 81
Cdd:PRK09311  206 LVEREVEARLPTRFGEFRAIGYTSILDGKEHVALVKGDIGDGEDVLVRVHSECLTGDVFGSRRCDCGPQLDAALAQIAEE 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081  82 GRGVLLYHR-QEGRNIGLLNKIRAYALQDLGADTVEANHQLGFAADERDFTLCADMFKLLGVDEVRLLTNNPQKVKILNE 160
Cdd:PRK09311  286 GRGVVLYMRgQEGRGIGLLHKLRAYQLQDEGYDTVDANLKLGFPADARDYGIGAQILVDLGVRSMRLLTNNPRKIAGLQG 365

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1374091081 161 AGINIVERVPLIVGRNPKNENYLATKAAKMGHMLD 195
Cdd:PRK09311  366 YGLHVTERVPLPVRANEENERYLRTKRDRMGHDLD 400
PRK09319 PRK09319
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase RibB/GTP cyclohydrolase II RibA;
4-195 1.30e-81

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


Pssm-ID: 236465 [Multi-domain]  Cd Length: 555  Bit Score: 252.18  E-value: 1.30e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081   4 KRVAEAKLPTPWGDFLMVGFEEIATGHDHLALVYGDIS--GSVPVLARVHSECLTGDALFSLRCDCGFQLEAALGHIAEE 81
Cdd:PRK09319  211 YREAVAKLPSQFGQFQAYGYRNELDGSEHVALVKGDPAnfKDEPVLVRMHSECLTGDAFGSLRCDCRMQLEAALKMIENE 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081  82 GRGVLLYHRQEGRNIGLLNKIRAYALQDLGADTVEANHQLGFAADERDFTLCADMFKLLGVDEVRLLTNNPQKVKILNEA 161
Cdd:PRK09319  291 GEGVVVYLRQEGRGIGLINKLKAYSLQDGGLDTVEANERLGFPADLRNYGVGAQILNDLGIKRLRLITNNPRKIAGLGGY 370

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1374091081 162 GINIVERVPLIVGRNPKNENYLATKAAKMGHMLD 195
Cdd:PRK09319  371 GLEVVDRVPLLIEANDYNAEYLATKAEKLGHLLL 404
PRK09318 PRK09318
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
2-197 4.76e-74

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


Pssm-ID: 236464 [Multi-domain]  Cd Length: 387  Bit Score: 228.08  E-value: 4.76e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081   2 QLKRV-AEAKLPTPWGDFLMVGFEEIATGHDHLALV---YGDIsgsvpVLARVHSECLTGDALFSLRCDCGFQLEAALGH 77
Cdd:PRK09318  190 QLIKVkAEAKLPTDYGEFEIVSFENHLDGKEHVAIVkepLGEV-----PLVRIHSECVTGDTLSSLRCDCGSQLANFLRM 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081  78 IAEEGrGVLLYHRQEGRNIGLLNKIRAYALQDLGADTVEANHQLGFAADERDFTLCADMFKLLGVDEVRLLTNNPQKVKI 157
Cdd:PRK09318  265 ISKEG-GILIYLRQEGRGIGLSNKIKAYELQDKGLDTVEANRALGFKEDERDYAAAFQILKALGIEKVRLLTNNPRKTKA 343

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1374091081 158 LNEAGINIVERVPLIVGRNPKNENYLATKAAKMGHMLDMK 197
Cdd:PRK09318  344 LEKYGIEVVETVPLYGEVTKYNRFYLKTKVEKLGHKLELR 383
PLN02831 PLN02831
Bifunctional GTP cyclohydrolase II/ 3,4-dihydroxy-2-butanone-4-phosphate synthase
 4-197 1.73e-72

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


Pssm-ID: 215445 [Multi-domain]  Cd Length: 450  Bit Score: 225.74  E-value: 1.73e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081   4 KRVAEAKLPTPWGDFLMVGFEEIATGHDHLALVYGDISGSVPVLARVHSECLTGDALFSLRCDCGFQLEAALGHIAEEGR 83
Cdd:PLN02831  242 ERTAVARLPTKWGLFTAYCYRSKLDGIEHIAFVKGDIGDGQDVLVRVHSECLTGDIFGSARCDCGNQLALAMQLIEKAGR 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081  84 GVLLYHR-QEGRNIGLLNKIRAYALQDLGADTVEANHQLGFAADERDFTLCADMFKLLGVDEVRLLTNNPQKVKILNEAG 162
Cdd:PLN02831  322 GVLVYLRgHEGRGIGLGHKLRAYNLQDEGRDTVEANEELGLPVDSREYGIGAQILRDLGVRTMRLMTNNPAKYTGLKGYG 401

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1374091081 163 INIVERVPLIVGRNPKNENYLATKAAKMGHMLDMK 197
Cdd:PLN02831  402 LAVVGRVPLLTPITKENKRYLETKRTKMGHVYGSD 436
GTP_cyclohydro2 pfam00925
GTP cyclohydrolase II; GTP cyclohydrolase II catalyzes the first committed step in the ...
 49-170 1.16e-70

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: 210.39  E-value: 1.16e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081  49 RVHSECLTGDALFSLRCDCGFQLEAALGHIAEEGRGVLLYHRQEGRNIGLLNKIRAYALQDLGADTVEANHQLGFAADER 128
Cdd:pfam00925   2 RVHSECLTGDVLGSLRCDCGEQLEAALRAIAEEGRGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADLR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1374091081 129 DFTLCADMFKLLGVDEVRLLTNNPQKVKILNEAGINIVERVP 170
Cdd:pfam00925  82 DYGIGAQILRDLGVKKIRLLTNNPRKIVGLEGYGLEVVERVP 123
PRK08815 PRK08815
GTP cyclohydrolase II RibA;
31-196 1.90e-59

GTP cyclohydrolase II RibA;


Pssm-ID: 236340 [Multi-domain]  Cd Length: 375  Bit Score: 190.35  E-value: 1.90e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081  31 DHLALVYG--DISGSVPVlaRVHSECLTGDALFSLRCDCGFQLEAALGHIAEEGRGVLLYHRQEGRNIGLLNKIRAYALQ 108
Cdd:PRK08815  202 DQVAIVVGqpDLSSAVPV--RVHSSCLTGDLFGSLKCDCGDQLRHGLAKLKELGGGVLLYLDQEGRGNGIAAKMRAYGYQ 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081 109 DLGADTVEANHQLGFAADERDFTLCADMFKLLGVDEVRLLTNNPQKVKILNEAGINIVERVPLIVGRNPKNENYLATKAA 188
Cdd:PRK08815  280 HAGLDTIDADAQLGFGPDERRYGSAVAMLRGLGITRVRLLTNNPTKAERLRAAGIEVEDRIRVTGRITAENERYLRTKAD 359


                  ....*...
gi 1374091081 189 KMGHMLDM 196
Cdd:PRK08815  360 RAGHALDV 367
PRK14019 PRK14019
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
3-170 2.68e-17

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


Pssm-ID: 237587 [Multi-domain]  Cd Length: 367  Bit Score: 78.47  E-value: 2.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081   3 LKRVAEAKLPTPWGDFLMVGFEEIATGHDHLALVYGDISGSVPVLARVHSECLTGDALFSLRCDCGFQLEAALGHIAEEG 82
Cdd:PRK14019  206 VERVAERPMQTAHGEFRLVAYRDKPSGSTHLALVKGTICPDEETLVRVHEPLSVLDLLEVGQPTHSWSLDAAMAAIAEAG 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081  83 RGV-LLYHRQEGrnigllnkirAYALQDLGADTVEANHQLGFAADERDFTLCADMFKLLGVDEVRLLTnNPQKVKILNEA 161
Cdd:PRK14019  286 SGVvVLLNCGDD----------GEHLLDRFRAEEAAAALKRRPVDYRTYGIGAQILRDLGVGKMRLLS-SPRKFPSMSGF 354


                  ....*....
gi 1374091081 162 GINIVERVP 170
Cdd:PRK14019  355 GLEVTGYVP 363
PRK12485 PRK12485
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
3-102 6.76e-09

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


Pssm-ID: 171535 [Multi-domain]  Cd Length: 369  Bit Score: 54.58  E-value: 6.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081   3 LKRVAEAKLPTPWGDFLMVGFEEIATGHDHLALVYGDISGSVPVLARVHseclTGDALFSL-----RCDCGFQLEAALGH 77
Cdd:PRK12485  206 IKRIGERELPTVHGTFRLVTYEDRIEGGVHMAMVMGDIRREQPTLVRVH----VIDPLRDLvgaeyAGPANWTLWAALQK 281

                          90       100
                  ....*....|....*....|....*
gi 1374091081  78 IAEEGRGVLLYHRQEGRNIGLLNKI 102
Cdd:PRK12485  282 VAEEGHGVVVVLANHESSQALLERI 306
PRK07198 PRK07198
GTP cyclohydrolase II;
36-171 8.92e-09

GTP cyclohydrolase II;


Pssm-ID: 235959 [Multi-domain]  Cd Length: 418  Bit Score: 53.89  E-value: 8.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374091081  36 VYGDIS----GSVPVLARVHSECLTGDALFSLRCDCgfqlEAALGHIAEE--------GRGVLLYHRQEGRNIGLLNKIR 103
Cdd:PRK07198  226 IFGDVTdladPETELTCRVHDECNGSDVFGSDICTC----RPYLTHGIEEcirgaqrgGVGLIVYNRKEGRALGEVTKFL 301

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1374091081 104 AYAL--QDLGADTVEANhqlgFA--------ADERDFTLCADMFKLLGVDEV-RLLTNNPQKVKILNEAGINIVERVPL 171
Cdd:PRK07198  302 VYNArkRQVGGDTAATY----FArtecvagvQDMRFQELMPDVLHWLGIRRIhRLVSMSNMKYDAITGSGIEVGERVPI 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH