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Conserved domains on  [gi|489201322|ref|WP_003110510|]
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MULTISPECIES: GTP cyclohydrolase II [Pseudomonas]

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;
1-196 3.84e-140

GTP cyclohydrolase II RibA;


:

Pssm-ID: 234745  Cd Length: 197  Bit Score: 389.20  E-value: 3.84e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322   1 MSVVFVAASKLPTPFGEFTMHGFLDEESGKEHVALSMGDIADGAPVLGRLHSECLTGDALFSLRCDCGFQLEGALAAIAE 80
Cdd:PRK00393   1 MQLKRVAEAKLPTPWGDFLMVGFEELATGKEHVALVFGDISGTEPVLVRVHSECLTGDALFSLRCDCGFQLEAALERIAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322  81 EGRGVLLYLRQEGRGIGLLNKIRAYELQDGGADTVEANLQLGFGADQRDYAMCQPMLAHLGVSSLRLMTNNPRKVKALES 160
Cdd:PRK00393  81 EGRGILLYLRQEGRGIGLLNKIRAYALQDQGLDTVEANHQLGFAADERDYTLAADMLKALGVKKVRLLTNNPKKVEALTE 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489201322 161 YAITVAERVPLQKGLNKHNRRYLATKAGKLGHMLGS 196
Cdd:PRK00393 161 AGINIVERVPLIVGRNPHNEHYLKTKAEKMGHLLSL 196
 
Name Accession Description Interval E-value
ribA PRK00393
GTP cyclohydrolase II RibA;
1-196 3.84e-140

GTP cyclohydrolase II RibA;


Pssm-ID: 234745  Cd Length: 197  Bit Score: 389.20  E-value: 3.84e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322   1 MSVVFVAASKLPTPFGEFTMHGFLDEESGKEHVALSMGDIADGAPVLGRLHSECLTGDALFSLRCDCGFQLEGALAAIAE 80
Cdd:PRK00393   1 MQLKRVAEAKLPTPWGDFLMVGFEELATGKEHVALVFGDISGTEPVLVRVHSECLTGDALFSLRCDCGFQLEAALERIAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322  81 EGRGVLLYLRQEGRGIGLLNKIRAYELQDGGADTVEANLQLGFGADQRDYAMCQPMLAHLGVSSLRLMTNNPRKVKALES 160
Cdd:PRK00393  81 EGRGILLYLRQEGRGIGLLNKIRAYALQDQGLDTVEANHQLGFAADERDYTLAADMLKALGVKKVRLLTNNPKKVEALTE 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489201322 161 YAITVAERVPLQKGLNKHNRRYLATKAGKLGHMLGS 196
Cdd:PRK00393 161 AGINIVERVPLIVGRNPHNEHYLKTKAEKMGHLLSL 196
GTP_cyclohydro2 cd00641
GTP cyclohydrolase II (RibA). GTP cyclohydrolase II catalyzes the conversion of GTP to 2, ...
 2-194 4.66e-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: 322.91  E-value: 4.66e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322   2 SVVFVAASKLPTPFGEFTMHGFLDEESGKEHVALSMGDIADGAPVLGRLHSECLTGDALFSLRCDCGFQLEGALAAIAEE 81
Cdd:cd00641    1 LVEKVAEAPLPTRFGDFRIVAFEDTDDGKEHVALVKGDPADGEPVLVRVHSECLTGDVFGSLRCDCGPQLEEALEEIAEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322  82 GRGVLLYLRQEGRGIGLLNKIRAYELQDGGADTVEANLQLGFGADQRDYAMCQPMLAHLGVSSLRLMTNNPRKVKALESY 161
Cdd:cd00641   81 GGGVLLYLRQEGRGIGLANKLRAYALQDQGLDTVEANEALGFPADARDYGLAAQILRDLGIKSVRLLTNNPDKIDALEGY 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 489201322 162 AITVAERVPLQKGLNKHNRRYLATKAGKLGHML 194
Cdd:cd00641  161 GIEVVERVPLEVEPNEENKGYLKTKRDKMGHLL 193
RibA COG0807
GTP cyclohydrolase II [Coenzyme transport and metabolism]; GTP cyclohydrolase II is part of ...
 3-194 2.18e-113

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: 328.85  E-value: 2.18e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322   3 VVFVAASKLPTPFGEFTMHGFLDEESGKEHVALSMGDIADGAPVLGRLHSECLTGDALFSLRCDCGFQLEGALAAIAEEG 82
Cdd:COG0807  206 VERVAEARLPTEFGEFRLHAYRDTIDGQEHLALVKGDPDPDEPVLVRVHSECLTGDVFGSLRCDCGWQLEAALKRIAEEG 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322  83 RGVLLYLRQEGRGIGLLNKIRAYELQDGGADTVEANLQLGFGADQRDYAMCQPMLAHLGVSSLRLMTNNPRKVKALESYA 162
Cdd:COG0807  286 RGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADLRDYGIGAQILRDLGVRKMRLLTNNPRKVVGLEGYG 365

                        170       180       190
                 ....*....|....*....|....*....|..
gi 489201322 163 ITVAERVPLQKGLNKHNRRYLATKAGKLGHML 194
Cdd:COG0807  366 LEVVERVPLEVGPNPHNERYLRTKRDKMGHLL 397
ribA TIGR00505
GTP cyclohydrolase II; Several members of the family are bifunctional, involving both ribA and ...
 6-194 1.55e-95

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: 276.27  E-value: 1.55e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322    6 VAASKLPTPFGEFTMHGFLDEESGKEHVALSMGDIADGAPVLGRLHSECLTGDALFSLRCDCGFQLEGALAAIAEEGRGV 85
Cdd:TIGR00505   3 VAEAKLPTPYGDFYMVGFEEPATGKDHVALVKGDISAHTDVLVRIHSECLTGDALHSLRCDCGFQLEAALKQIAEEGRGV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322   86 LLYLRQEGRGIGLLNKIRAYELQDGGADTVEANLQLGFGADQRDYAMCQPMLAHLGVSSLRLMTNNPRKVKALESYAITV 165
Cdd:TIGR00505  83 LIYLRQEGRGIGLINKLRAYALQDKGYDTVQANLMLGFPADERDFSLCADILEDLGVKKVRLLTNNPKKIEILKKAGINI 162

                         170       180
                  ....*....|....*....|....*....
gi 489201322  166 AERVPLQKGLNKHNRRYLATKAGKLGHML 194
Cdd:TIGR00505 163 VERVPLIVGRNENNEGYLDTKAEKMGHLL 191
GTP_cyclohydro2 pfam00925
GTP cyclohydrolase II; GTP cyclohydrolase II catalyzes the first committed step in the ...
 49-170 3.06e-74

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: 219.64  E-value: 3.06e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322   49 RLHSECLTGDALFSLRCDCGFQLEGALAAIAEEGRGVLLYLRQEGRGIGLLNKIRAYELQDGGADTVEANLQLGFGADQR 128
Cdd:pfam00925   2 RVHSECLTGDVLGSLRCDCGEQLEAALRAIAEEGRGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADLR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 489201322  129 DYAMCQPMLAHLGVSSLRLMTNNPRKVKALESYAITVAERVP 170
Cdd:pfam00925  82 DYGIGAQILRDLGVKKIRLLTNNPRKIVGLEGYGLEVVERVP 123
 
Name Accession Description Interval E-value
ribA PRK00393
GTP cyclohydrolase II RibA;
1-196 3.84e-140

GTP cyclohydrolase II RibA;


Pssm-ID: 234745  Cd Length: 197  Bit Score: 389.20  E-value: 3.84e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322   1 MSVVFVAASKLPTPFGEFTMHGFLDEESGKEHVALSMGDIADGAPVLGRLHSECLTGDALFSLRCDCGFQLEGALAAIAE 80
Cdd:PRK00393   1 MQLKRVAEAKLPTPWGDFLMVGFEELATGKEHVALVFGDISGTEPVLVRVHSECLTGDALFSLRCDCGFQLEAALERIAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322  81 EGRGVLLYLRQEGRGIGLLNKIRAYELQDGGADTVEANLQLGFGADQRDYAMCQPMLAHLGVSSLRLMTNNPRKVKALES 160
Cdd:PRK00393  81 EGRGILLYLRQEGRGIGLLNKIRAYALQDQGLDTVEANHQLGFAADERDYTLAADMLKALGVKKVRLLTNNPKKVEALTE 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489201322 161 YAITVAERVPLQKGLNKHNRRYLATKAGKLGHMLGS 196
Cdd:PRK00393 161 AGINIVERVPLIVGRNPHNEHYLKTKAEKMGHLLSL 196
GTP_cyclohydro2 cd00641
GTP cyclohydrolase II (RibA). GTP cyclohydrolase II catalyzes the conversion of GTP to 2, ...
 2-194 4.66e-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: 322.91  E-value: 4.66e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322   2 SVVFVAASKLPTPFGEFTMHGFLDEESGKEHVALSMGDIADGAPVLGRLHSECLTGDALFSLRCDCGFQLEGALAAIAEE 81
Cdd:cd00641    1 LVEKVAEAPLPTRFGDFRIVAFEDTDDGKEHVALVKGDPADGEPVLVRVHSECLTGDVFGSLRCDCGPQLEEALEEIAEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322  82 GRGVLLYLRQEGRGIGLLNKIRAYELQDGGADTVEANLQLGFGADQRDYAMCQPMLAHLGVSSLRLMTNNPRKVKALESY 161
Cdd:cd00641   81 GGGVLLYLRQEGRGIGLANKLRAYALQDQGLDTVEANEALGFPADARDYGLAAQILRDLGIKSVRLLTNNPDKIDALEGY 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 489201322 162 AITVAERVPLQKGLNKHNRRYLATKAGKLGHML 194
Cdd:cd00641  161 GIEVVERVPLEVEPNEENKGYLKTKRDKMGHLL 193
RibA COG0807
GTP cyclohydrolase II [Coenzyme transport and metabolism]; GTP cyclohydrolase II is part of ...
 3-194 2.18e-113

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: 328.85  E-value: 2.18e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322   3 VVFVAASKLPTPFGEFTMHGFLDEESGKEHVALSMGDIADGAPVLGRLHSECLTGDALFSLRCDCGFQLEGALAAIAEEG 82
Cdd:COG0807  206 VERVAEARLPTEFGEFRLHAYRDTIDGQEHLALVKGDPDPDEPVLVRVHSECLTGDVFGSLRCDCGWQLEAALKRIAEEG 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322  83 RGVLLYLRQEGRGIGLLNKIRAYELQDGGADTVEANLQLGFGADQRDYAMCQPMLAHLGVSSLRLMTNNPRKVKALESYA 162
Cdd:COG0807  286 RGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADLRDYGIGAQILRDLGVRKMRLLTNNPRKVVGLEGYG 365

                        170       180       190
                 ....*....|....*....|....*....|..
gi 489201322 163 ITVAERVPLQKGLNKHNRRYLATKAGKLGHML 194
Cdd:COG0807  366 LEVVERVPLEVGPNPHNERYLRTKRDKMGHLL 397
PRK09311 PRK09311
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
3-194 4.17e-99

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


Pssm-ID: 181774 [Multi-domain]  Cd Length: 402  Bit Score: 292.58  E-value: 4.17e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322   3 VVFVAASKLPTPFGEFTMHGFLDEESGKEHVALSMGDIADGAPVLGRLHSECLTGDALFSLRCDCGFQLEGALAAIAEEG 82
Cdd:PRK09311 207 VEREVEARLPTRFGEFRAIGYTSILDGKEHVALVKGDIGDGEDVLVRVHSECLTGDVFGSRRCDCGPQLDAALAQIAEEG 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322  83 RGVLLYLR-QEGRGIGLLNKIRAYELQDGGADTVEANLQLGFGADQRDYAMCQPMLAHLGVSSLRLMTNNPRKVKALESY 161
Cdd:PRK09311 287 RGVVLYMRgQEGRGIGLLHKLRAYQLQDEGYDTVDANLKLGFPADARDYGIGAQILVDLGVRSMRLLTNNPRKIAGLQGY 366

                        170       180       190
                 ....*....|....*....|....*....|...
gi 489201322 162 AITVAERVPLQKGLNKHNRRYLATKAGKLGHML 194
Cdd:PRK09311 367 GLHVTERVPLPVRANEENERYLRTKRDRMGHDL 399
ribA TIGR00505
GTP cyclohydrolase II; Several members of the family are bifunctional, involving both ribA and ...
 6-194 1.55e-95

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: 276.27  E-value: 1.55e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322    6 VAASKLPTPFGEFTMHGFLDEESGKEHVALSMGDIADGAPVLGRLHSECLTGDALFSLRCDCGFQLEGALAAIAEEGRGV 85
Cdd:TIGR00505   3 VAEAKLPTPYGDFYMVGFEEPATGKDHVALVKGDISAHTDVLVRIHSECLTGDALHSLRCDCGFQLEAALKQIAEEGRGV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322   86 LLYLRQEGRGIGLLNKIRAYELQDGGADTVEANLQLGFGADQRDYAMCQPMLAHLGVSSLRLMTNNPRKVKALESYAITV 165
Cdd:TIGR00505  83 LIYLRQEGRGIGLINKLRAYALQDKGYDTVQANLMLGFPADERDFSLCADILEDLGVKKVRLLTNNPKKIEILKKAGINI 162

                         170       180
                  ....*....|....*....|....*....
gi 489201322  166 AERVPLQKGLNKHNRRYLATKAGKLGHML 194
Cdd:TIGR00505 163 VERVPLIVGRNENNEGYLDTKAEKMGHLL 191
PRK09319 PRK09319
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase RibB/GTP cyclohydrolase II RibA;
5-194 1.07e-88

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


Pssm-ID: 236465 [Multi-domain]  Cd Length: 555  Bit Score: 270.67  E-value: 1.07e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322   5 FV---AASKLPTPFGEFTMHGFLDEESGKEHVALSMGDIAD--GAPVLGRLHSECLTGDALFSLRCDCGFQLEGALAAIA 79
Cdd:PRK09319 209 FVyreAVAKLPSQFGQFQAYGYRNELDGSEHVALVKGDPANfkDEPVLVRMHSECLTGDAFGSLRCDCRMQLEAALKMIE 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322  80 EEGRGVLLYLRQEGRGIGLLNKIRAYELQDGGADTVEANLQLGFGADQRDYAMCQPMLAHLGVSSLRLMTNNPRKVKALE 159
Cdd:PRK09319 289 NEGEGVVVYLRQEGRGIGLINKLKAYSLQDGGLDTVEANERLGFPADLRNYGVGAQILNDLGIKRLRLITNNPRKIAGLG 368

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 489201322 160 SYAITVAERVPLQKGLNKHNRRYLATKAGKLGHML 194
Cdd:PRK09319 369 GYGLEVVDRVPLLIEANDYNAEYLATKAEKLGHLL 403
PRK09318 PRK09318
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
7-194 4.41e-80

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


Pssm-ID: 236464 [Multi-domain]  Cd Length: 387  Bit Score: 243.87  E-value: 4.41e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322   7 AASKLPTPFGEFTMHGFLDEESGKEHVALSMGDIadGAPVLGRLHSECLTGDALFSLRCDCGFQLEGALAAIAEEGrGVL 86
Cdd:PRK09318 196 AEAKLPTDYGEFEIVSFENHLDGKEHVAIVKEPL--GEVPLVRIHSECVTGDTLSSLRCDCGSQLANFLRMISKEG-GIL 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322  87 LYLRQEGRGIGLLNKIRAYELQDGGADTVEANLQLGFGADQRDYAMCQPMLAHLGVSSLRLMTNNPRKVKALESYAITVA 166
Cdd:PRK09318 273 IYLRQEGRGIGLSNKIKAYELQDKGLDTVEANRALGFKEDERDYAAAFQILKALGIEKVRLLTNNPRKTKALEKYGIEVV 352

                        170       180
                 ....*....|....*....|....*...
gi 489201322 167 ERVPLQKGLNKHNRRYLATKAGKLGHML 194
Cdd:PRK09318 353 ETVPLYGEVTKYNRFYLKTKVEKLGHKL 380
PLN02831 PLN02831
Bifunctional GTP cyclohydrolase II/ 3,4-dihydroxy-2-butanone-4-phosphate synthase
 3-205 1.84e-79

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


Pssm-ID: 215445 [Multi-domain]  Cd Length: 450  Bit Score: 244.23  E-value: 1.84e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322   3 VVFVAASKLPTPFGEFTMHGFLDEESGKEHVALSMGDIADGAPVLGRLHSECLTGDALFSLRCDCGFQLEGALAAIAEEG 82
Cdd:PLN02831 241 VERTAVARLPTKWGLFTAYCYRSKLDGIEHIAFVKGDIGDGQDVLVRVHSECLTGDIFGSARCDCGNQLALAMQLIEKAG 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322  83 RGVLLYLR-QEGRGIGLLNKIRAYELQDGGADTVEANLQLGFGADQRDYAMCQPMLAHLGVSSLRLMTNNPRKVKALESY 161
Cdd:PLN02831 321 RGVLVYLRgHEGRGIGLGHKLRAYNLQDEGRDTVEANEELGLPVDSREYGIGAQILRDLGVRTMRLMTNNPAKYTGLKGY 400

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 489201322 162 AITVAERVPLQKGLNKHNRRYLATKAGKLGHMLGSLHQGEAETT 205
Cdd:PLN02831 401 GLAVVGRVPLLTPITKENKRYLETKRTKMGHVYGSDLGGHVSGL 444
GTP_cyclohydro2 pfam00925
GTP cyclohydrolase II; GTP cyclohydrolase II catalyzes the first committed step in the ...
 49-170 3.06e-74

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: 219.64  E-value: 3.06e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322   49 RLHSECLTGDALFSLRCDCGFQLEGALAAIAEEGRGVLLYLRQEGRGIGLLNKIRAYELQDGGADTVEANLQLGFGADQR 128
Cdd:pfam00925   2 RVHSECLTGDVLGSLRCDCGEQLEAALRAIAEEGRGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADLR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 489201322  129 DYAMCQPMLAHLGVSSLRLMTNNPRKVKALESYAITVAERVP 170
Cdd:pfam00925  82 DYGIGAQILRDLGVKKIRLLTNNPRKIVGLEGYGLEVVERVP 123
PRK08815 PRK08815
GTP cyclohydrolase II RibA;
27-194 9.75e-55

GTP cyclohydrolase II RibA;


Pssm-ID: 236340 [Multi-domain]  Cd Length: 375  Bit Score: 178.41  E-value: 9.75e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322  27 ESGKEHVALSMGDIADGAPVLGRLHSECLTGDALFSLRCDCGFQLEGALAAIAEEGRGVLLYLRQEGRGIGLLNKIRAYE 106
Cdd:PRK08815 198 VAQRDQVAIVVGQPDLSSAVPVRVHSSCLTGDLFGSLKCDCGDQLRHGLAKLKELGGGVLLYLDQEGRGNGIAAKMRAYG 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322 107 LQDGGADTVEANLQLGFGADQRDYAMCQPMLAHLGVSSLRLMTNNPRKVKALESYAITVAERVPLQKGLNKHNRRYLATK 186
Cdd:PRK08815 278 YQHAGLDTIDADAQLGFGPDERRYGSAVAMLRGLGITRVRLLTNNPTKAERLRAAGIEVEDRIRVTGRITAENERYLRTK 357


                 ....*...
gi 489201322 187 AGKLGHML 194
Cdd:PRK08815 358 ADRAGHAL 365
PRK14019 PRK14019
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
6-170 1.73e-16

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


Pssm-ID: 237587 [Multi-domain]  Cd Length: 367  Bit Score: 76.54  E-value: 1.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322   6 VAASKLPTPFGEFTMHGFLDEESGKEHVALSMGDIADGAPVLGRLHSECLTGDALFSLRCDCGFQLEGALAAIAEEGRGV 85
Cdd:PRK14019 209 VAERPMQTAHGEFRLVAYRDKPSGSTHLALVKGTICPDEETLVRVHEPLSVLDLLEVGQPTHSWSLDAAMAAIAEAGSGV 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322  86 LLYLRQEGRGIGLLNKIRAyelQDGGADTVEANlqlgfgADQRDYAMCQPMLAHLGVSSLRLMTnNPRKVKALESYAITV 165
Cdd:PRK14019 289 VVLLNCGDDGEHLLDRFRA---EEAAAALKRRP------VDYRTYGIGAQILRDLGVGKMRLLS-SPRKFPSMSGFGLEV 358


                 ....*
gi 489201322 166 AERVP 170
Cdd:PRK14019 359 TGYVP 363
PRK12485 PRK12485
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
2-172 5.19e-08

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


Pssm-ID: 171535 [Multi-domain]  Cd Length: 369  Bit Score: 51.89  E-value: 5.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322   2 SVVFVAASKLPTPFGEFTMHGFLDEESGKEHVALSMGDIADGAPVLGRLHsecltgdALFSLRCDCGFQLEG-------- 73
Cdd:PRK12485 205 TIKRIGERELPTVHGTFRLVTYEDRIEGGVHMAMVMGDIRREQPTLVRVH-------VIDPLRDLVGAEYAGpanwtlwa 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322  74 ALAAIAEEGRGVLLYLRQEGRGIGLLNKI-------RAYELQDGGADTveanlQLGFGADqrdyamcqpMLAHLGVSSLR 146
Cdd:PRK12485 278 ALQKVAEEGHGVVVVLANHESSQALLERIpqltqppRQYQRSQSRIYS-----EVGTGAQ---------ILQDLGVGKLR 343

                        170       180
                 ....*....|....*....|....*.
gi 489201322 147 LMtNNPRKVKALESYAITVAERVPLQ 172
Cdd:PRK12485 344 HL-GPPLKYAGLTGYDLEVVESIPFP 368
PRK07198 PRK07198
GTP cyclohydrolase II;
37-171 7.69e-05

GTP cyclohydrolase II;


Pssm-ID: 235959 [Multi-domain]  Cd Length: 418  Bit Score: 42.72  E-value: 7.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322  37 MGDIADGA----PVLGRLHSECLTGDALFSLRCDCGFQL----EGALAAIAEEGRGVLLYLRQEGRGIGLLNKIRAY--- 105
Cdd:PRK07198 227 FGDVTDLAdpetELTCRVHDECNGSDVFGSDICTCRPYLthgiEECIRGAQRGGVGLIVYNRKEGRALGEVTKFLVYnar 306

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201322 106 ELQDGG--ADTVEANLQLGFGA-DQRDYAMCQPMLAHLGVSSL-RLMTNNPRKVKALESYAITVAERVPL 171
Cdd:PRK07198 307 KRQVGGdtAATYFARTECVAGVqDMRFQELMPDVLHWLGIRRIhRLVSMSNMKYDAITGSGIEVGERVPI 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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