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Conserved domains on  [gi|663523389|gb|AIF13644|]
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bifunctional riboflavin biosynthesis protein RibAB (ribBA) [uncultured marine group II/III euryarchaeote KM3_63_C07]

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

EC:  3.5.4.25
Gene Symbol:  ribA
Gene Ontology:  GO:0005525|GO:0003935|GO:0009231|GO:0046872
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;
11-203 3.97e-109

GTP cyclohydrolase II RibA;


:

Pssm-ID: 234745  Cd Length: 197  Bit Score: 311.00  E-value: 3.97e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389  11 VDVPADARLPTSYGDFRIRVFHEASTGLDHVALTLGDMSGPDPVLVRVHSECLTGDAFSSLRCDCGAQLAAAMKQIQDVG 90
Cdd:PRK00393   3 LKRVAEAKLPTPWGDFLMVGFEELATGKEHVALVFGDISGTEPVLVRVHSECLTGDALFSLRCDCGFQLEAALERIAEEG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389  91 WGCIVYLRQEGRGIGLHAKIQAYNLQDQGADTLDANLMLGHPADARDYGIASEILAAIGIESVCLLTNNPDKVLQLAGNG 170
Cdd:PRK00393  83 RGILLYLRQEGRGIGLLNKIRAYALQDQGLDTVEANHQLGFAADERDYTLAADMLKALGVKKVRLLTNNPKKVEALTEAG 162

                        170       180       190
                 ....*....|....*....|....*....|...
gi 663523389 171 ANIVERMPLVVGVGDQNIEYLTTKIDRMGHDID 203
Cdd:PRK00393 163 INIVERVPLIVGRNPHNEHYLKTKAEKMGHLLS 195
 
Name Accession Description Interval E-value
ribA PRK00393
GTP cyclohydrolase II RibA;
11-203 3.97e-109

GTP cyclohydrolase II RibA;


Pssm-ID: 234745  Cd Length: 197  Bit Score: 311.00  E-value: 3.97e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389  11 VDVPADARLPTSYGDFRIRVFHEASTGLDHVALTLGDMSGPDPVLVRVHSECLTGDAFSSLRCDCGAQLAAAMKQIQDVG 90
Cdd:PRK00393   3 LKRVAEAKLPTPWGDFLMVGFEELATGKEHVALVFGDISGTEPVLVRVHSECLTGDALFSLRCDCGFQLEAALERIAEEG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389  91 WGCIVYLRQEGRGIGLHAKIQAYNLQDQGADTLDANLMLGHPADARDYGIASEILAAIGIESVCLLTNNPDKVLQLAGNG 170
Cdd:PRK00393  83 RGILLYLRQEGRGIGLLNKIRAYALQDQGLDTVEANHQLGFAADERDYTLAADMLKALGVKKVRLLTNNPKKVEALTEAG 162

                        170       180       190
                 ....*....|....*....|....*....|...
gi 663523389 171 ANIVERMPLVVGVGDQNIEYLTTKIDRMGHDID 203
Cdd:PRK00393 163 INIVERVPLIVGRNPHNEHYLKTKAEKMGHLLS 195
GTP_cyclohydro2 cd00641
GTP cyclohydrolase II (RibA). GTP cyclohydrolase II catalyzes the conversion of GTP to 2, ...
 10-202 2.12e-104

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: 299.03  E-value: 2.12e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389  10 LVDVPADARLPTSYGDFRIRVFHEASTGLDHVALTLGDMSGPDPVLVRVHSECLTGDAFSSLRCDCGAQLAAAMKQIQDV 89
Cdd:cd00641    1 LVEKVAEAPLPTRFGDFRIVAFEDTDDGKEHVALVKGDPADGEPVLVRVHSECLTGDVFGSLRCDCGPQLEEALEEIAEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389  90 GWGCIVYLRQEGRGIGLHAKIQAYNLQDQGADTLDANLMLGHPADARDYGIASEILAAIGIESVCLLTNNPDKVLQLAGN 169
Cdd:cd00641   81 GGGVLLYLRQEGRGIGLANKLRAYALQDQGLDTVEANEALGFPADARDYGLAAQILRDLGIKSVRLLTNNPDKIDALEGY 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 663523389 170 GANIVERMPLVVGVGDQNIEYLTTKIDRMGHDI 202
Cdd:cd00641  161 GIEVVERVPLEVEPNEENKGYLKTKRDKMGHLL 193
RibA COG0807
GTP cyclohydrolase II [Coenzyme transport and metabolism]; GTP cyclohydrolase II is part of ...
 9-203 2.05e-101

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: 298.81  E-value: 2.05e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389   9 ELVDVPADARLPTSYGDFRIRVFHEASTGLDHVALTLGDMSGPDPVLVRVHSECLTGDAFSSLRCDCGAQLAAAMKQIQD 88
Cdd:COG0807  204 SLVERVAEARLPTEFGEFRLHAYRDTIDGQEHLALVKGDPDPDEPVLVRVHSECLTGDVFGSLRCDCGWQLEAALKRIAE 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389  89 VGWGCIVYLRQEGRGIGLHAKIQAYNLQDQGADTLDANLMLGHPADARDYGIASEILAAIGIESVCLLTNNPDKVLQLAG 168
Cdd:COG0807  284 EGRGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADLRDYGIGAQILRDLGVRKMRLLTNNPRKVVGLEG 363

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 663523389 169 NGANIVERMPLVVGVGDQNIEYLTTKIDRMGHDID 203
Cdd:COG0807  364 YGLEVVERVPLEVGPNPHNERYLRTKRDKMGHLLD 398
ribA TIGR00505
GTP cyclohydrolase II; Several members of the family are bifunctional, involving both ribA and ...
 15-200 4.38e-89

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: 260.10  E-value: 4.38e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389   15 ADARLPTSYGDFRIRVFHEASTGLDHVALTLGDMSGPDPVLVRVHSECLTGDAFSSLRCDCGAQLAAAMKQIQDVGWGCI 94
Cdd:TIGR00505   4 AEAKLPTPYGDFYMVGFEEPATGKDHVALVKGDISAHTDVLVRIHSECLTGDALHSLRCDCGFQLEAALKQIAEEGRGVL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389   95 VYLRQEGRGIGLHAKIQAYNLQDQGADTLDANLMLGHPADARDYGIASEILAAIGIESVCLLTNNPDKVLQLAGNGANIV 174
Cdd:TIGR00505  84 IYLRQEGRGIGLINKLRAYALQDKGYDTVQANLMLGFPADERDFSLCADILEDLGVKKVRLLTNNPKKIEILKKAGINIV 163

                         170       180
                  ....*....|....*....|....*.
gi 663523389  175 ERMPLVVGVGDQNIEYLTTKIDRMGH 200
Cdd:TIGR00505 164 ERVPLIVGRNENNEGYLDTKAEKMGH 189
GTP_cyclohydro2 pfam00925
GTP cyclohydrolase II; GTP cyclohydrolase II catalyzes the first committed step in the ...
 56-178 1.54e-68

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: 205.38  E-value: 1.54e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389   56 VRVHSECLTGDAFSSLRCDCGAQLAAAMKQIQDVGWGCIVYLRQEGRGIGLHAKIQAYNLQDQGADTLDANLMLGHPADA 135
Cdd:pfam00925   1 VRVHSECLTGDVLGSLRCDCGEQLEAALRAIAEEGRGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 663523389  136 RDYGIASEILAAIGIESVCLLTNNPDKVLQLAGNGANIVERMP 178
Cdd:pfam00925  81 RDYGIGAQILRDLGVKKIRLLTNNPRKIVGLEGYGLEVVERVP 123
 
Name Accession Description Interval E-value
ribA PRK00393
GTP cyclohydrolase II RibA;
11-203 3.97e-109

GTP cyclohydrolase II RibA;


Pssm-ID: 234745  Cd Length: 197  Bit Score: 311.00  E-value: 3.97e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389  11 VDVPADARLPTSYGDFRIRVFHEASTGLDHVALTLGDMSGPDPVLVRVHSECLTGDAFSSLRCDCGAQLAAAMKQIQDVG 90
Cdd:PRK00393   3 LKRVAEAKLPTPWGDFLMVGFEELATGKEHVALVFGDISGTEPVLVRVHSECLTGDALFSLRCDCGFQLEAALERIAEEG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389  91 WGCIVYLRQEGRGIGLHAKIQAYNLQDQGADTLDANLMLGHPADARDYGIASEILAAIGIESVCLLTNNPDKVLQLAGNG 170
Cdd:PRK00393  83 RGILLYLRQEGRGIGLLNKIRAYALQDQGLDTVEANHQLGFAADERDYTLAADMLKALGVKKVRLLTNNPKKVEALTEAG 162

                        170       180       190
                 ....*....|....*....|....*....|...
gi 663523389 171 ANIVERMPLVVGVGDQNIEYLTTKIDRMGHDID 203
Cdd:PRK00393 163 INIVERVPLIVGRNPHNEHYLKTKAEKMGHLLS 195
GTP_cyclohydro2 cd00641
GTP cyclohydrolase II (RibA). GTP cyclohydrolase II catalyzes the conversion of GTP to 2, ...
 10-202 2.12e-104

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: 299.03  E-value: 2.12e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389  10 LVDVPADARLPTSYGDFRIRVFHEASTGLDHVALTLGDMSGPDPVLVRVHSECLTGDAFSSLRCDCGAQLAAAMKQIQDV 89
Cdd:cd00641    1 LVEKVAEAPLPTRFGDFRIVAFEDTDDGKEHVALVKGDPADGEPVLVRVHSECLTGDVFGSLRCDCGPQLEEALEEIAEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389  90 GWGCIVYLRQEGRGIGLHAKIQAYNLQDQGADTLDANLMLGHPADARDYGIASEILAAIGIESVCLLTNNPDKVLQLAGN 169
Cdd:cd00641   81 GGGVLLYLRQEGRGIGLANKLRAYALQDQGLDTVEANEALGFPADARDYGLAAQILRDLGIKSVRLLTNNPDKIDALEGY 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 663523389 170 GANIVERMPLVVGVGDQNIEYLTTKIDRMGHDI 202
Cdd:cd00641  161 GIEVVERVPLEVEPNEENKGYLKTKRDKMGHLL 193
RibA COG0807
GTP cyclohydrolase II [Coenzyme transport and metabolism]; GTP cyclohydrolase II is part of ...
 9-203 2.05e-101

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: 298.81  E-value: 2.05e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389   9 ELVDVPADARLPTSYGDFRIRVFHEASTGLDHVALTLGDMSGPDPVLVRVHSECLTGDAFSSLRCDCGAQLAAAMKQIQD 88
Cdd:COG0807  204 SLVERVAEARLPTEFGEFRLHAYRDTIDGQEHLALVKGDPDPDEPVLVRVHSECLTGDVFGSLRCDCGWQLEAALKRIAE 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389  89 VGWGCIVYLRQEGRGIGLHAKIQAYNLQDQGADTLDANLMLGHPADARDYGIASEILAAIGIESVCLLTNNPDKVLQLAG 168
Cdd:COG0807  284 EGRGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADLRDYGIGAQILRDLGVRKMRLLTNNPRKVVGLEG 363

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 663523389 169 NGANIVERMPLVVGVGDQNIEYLTTKIDRMGHDID 203
Cdd:COG0807  364 YGLEVVERVPLEVGPNPHNERYLRTKRDKMGHLLD 398
PRK09311 PRK09311
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
10-204 7.67e-92

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


Pssm-ID: 181774 [Multi-domain]  Cd Length: 402  Bit Score: 274.47  E-value: 7.67e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389  10 LVDVPADARLPTSYGDFRIRVFHEASTGLDHVALTLGDMSGPDPVLVRVHSECLTGDAFSSLRCDCGAQLAAAMKQIQDV 89
Cdd:PRK09311 206 LVEREVEARLPTRFGEFRAIGYTSILDGKEHVALVKGDIGDGEDVLVRVHSECLTGDVFGSRRCDCGPQLDAALAQIAEE 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389  90 GWGCIVYLR-QEGRGIGLHAKIQAYNLQDQGADTLDANLMLGHPADARDYGIASEILAAIGIESVCLLTNNPDKVLQLAG 168
Cdd:PRK09311 286 GRGVVLYMRgQEGRGIGLLHKLRAYQLQDEGYDTVDANLKLGFPADARDYGIGAQILVDLGVRSMRLLTNNPRKIAGLQG 365

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 663523389 169 NGANIVERMPLVVGVGDQNIEYLTTKIDRMGHDIDD 204
Cdd:PRK09311 366 YGLHVTERVPLPVRANEENERYLRTKRDRMGHDLDL 401
ribA TIGR00505
GTP cyclohydrolase II; Several members of the family are bifunctional, involving both ribA and ...
 15-200 4.38e-89

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: 260.10  E-value: 4.38e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389   15 ADARLPTSYGDFRIRVFHEASTGLDHVALTLGDMSGPDPVLVRVHSECLTGDAFSSLRCDCGAQLAAAMKQIQDVGWGCI 94
Cdd:TIGR00505   4 AEAKLPTPYGDFYMVGFEEPATGKDHVALVKGDISAHTDVLVRIHSECLTGDALHSLRCDCGFQLEAALKQIAEEGRGVL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389   95 VYLRQEGRGIGLHAKIQAYNLQDQGADTLDANLMLGHPADARDYGIASEILAAIGIESVCLLTNNPDKVLQLAGNGANIV 174
Cdd:TIGR00505  84 IYLRQEGRGIGLINKLRAYALQDKGYDTVQANLMLGFPADERDFSLCADILEDLGVKKVRLLTNNPKKIEILKKAGINIV 163

                         170       180
                  ....*....|....*....|....*.
gi 663523389  175 ERMPLVVGVGDQNIEYLTTKIDRMGH 200
Cdd:TIGR00505 164 ERVPLIVGRNENNEGYLDTKAEKMGH 189
PRK09319 PRK09319
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase RibB/GTP cyclohydrolase II RibA;
15-207 4.08e-76

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


Pssm-ID: 236465 [Multi-domain]  Cd Length: 555  Bit Score: 238.70  E-value: 4.08e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389  15 ADARLPTSYGDFRIRVFHEASTGLDHVALTLGDMS--GPDPVLVRVHSECLTGDAFSSLRCDCGAQLAAAMKQIQDVGWG 92
Cdd:PRK09319 214 AVAKLPSQFGQFQAYGYRNELDGSEHVALVKGDPAnfKDEPVLVRMHSECLTGDAFGSLRCDCRMQLEAALKMIENEGEG 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389  93 CIVYLRQEGRGIGLHAKIQAYNLQDQGADTLDANLMLGHPADARDYGIASEILAAIGIESVCLLTNNPDKVLQLAGNGAN 172
Cdd:PRK09319 294 VVVYLRQEGRGIGLINKLKAYSLQDGGLDTVEANERLGFPADLRNYGVGAQILNDLGIKRLRLITNNPRKIAGLGGYGLE 373

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 663523389 173 IVERMPLVVGVGDQNIEYLTTKIDRMGHDIDDARL 207
Cdd:PRK09319 374 VVDRVPLLIEANDYNAEYLATKAEKLGHLLLQTYL 408
PLN02831 PLN02831
Bifunctional GTP cyclohydrolase II/ 3,4-dihydroxy-2-butanone-4-phosphate synthase
 8-200 2.45e-74

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


Pssm-ID: 215445 [Multi-domain]  Cd Length: 450  Bit Score: 231.13  E-value: 2.45e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389   8 NELVDVPADARLPTSYGDFRIRVFHEASTGLDHVALTLGDMSGPDPVLVRVHSECLTGDAFSSLRCDCGAQLAAAMKQIQ 87
Cdd:PLN02831 238 EKLVERTAVARLPTKWGLFTAYCYRSKLDGIEHIAFVKGDIGDGQDVLVRVHSECLTGDIFGSARCDCGNQLALAMQLIE 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389  88 DVGWGCIVYLR-QEGRGIGLHAKIQAYNLQDQGADTLDANLMLGHPADARDYGIASEILAAIGIESVCLLTNNPDKVLQL 166
Cdd:PLN02831 318 KAGRGVLVYLRgHEGRGIGLGHKLRAYNLQDEGRDTVEANEELGLPVDSREYGIGAQILRDLGVRTMRLMTNNPAKYTGL 397

                        170       180       190
                 ....*....|....*....|....*....|....
gi 663523389 167 AGNGANIVERMPLVVGVGDQNIEYLTTKIDRMGH 200
Cdd:PLN02831 398 KGYGLAVVGRVPLLTPITKENKRYLETKRTKMGH 431
PRK09318 PRK09318
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
8-208 1.20e-71

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


Pssm-ID: 236464 [Multi-domain]  Cd Length: 387  Bit Score: 222.30  E-value: 1.20e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389   8 NELVDVPADARLPTSYGDFRIRVFHEASTGLDHVALTLGDMSgpDPVLVRVHSECLTGDAFSSLRCDCGAQLAAAMKQIQ 87
Cdd:PRK09318 189 KQLIKVKAEAKLPTDYGEFEIVSFENHLDGKEHVAIVKEPLG--EVPLVRIHSECVTGDTLSSLRCDCGSQLANFLRMIS 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389  88 DVGwGCIVYLRQEGRGIGLHAKIQAYNLQDQGADTLDANLMLGHPADARDYGIASEILAAIGIESVCLLTNNPDKVLQLA 167
Cdd:PRK09318 267 KEG-GILIYLRQEGRGIGLSNKIKAYELQDKGLDTVEANRALGFKEDERDYAAAFQILKALGIEKVRLLTNNPRKTKALE 345

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 663523389 168 GNGANIVERMPLVVGVGDQNIEYLTTKIDRMGHDIDDARLN 208
Cdd:PRK09318 346 KYGIEVVETVPLYGEVTKYNRFYLKTKVEKLGHKLELREVN 386
GTP_cyclohydro2 pfam00925
GTP cyclohydrolase II; GTP cyclohydrolase II catalyzes the first committed step in the ...
 56-178 1.54e-68

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: 205.38  E-value: 1.54e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389   56 VRVHSECLTGDAFSSLRCDCGAQLAAAMKQIQDVGWGCIVYLRQEGRGIGLHAKIQAYNLQDQGADTLDANLMLGHPADA 135
Cdd:pfam00925   1 VRVHSECLTGDVLGSLRCDCGEQLEAALRAIAEEGRGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 663523389  136 RDYGIASEILAAIGIESVCLLTNNPDKVLQLAGNGANIVERMP 178
Cdd:pfam00925  81 RDYGIGAQILRDLGVKKIRLLTNNPRKIVGLEGYGLEVVERVP 123
PRK08815 PRK08815
GTP cyclohydrolase II RibA;
39-203 4.14e-50

GTP cyclohydrolase II RibA;


Pssm-ID: 236340 [Multi-domain]  Cd Length: 375  Bit Score: 166.47  E-value: 4.14e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389  39 DHVALTLG--DMSGPDPVlvRVHSECLTGDAFSSLRCDCGAQLAAAMKQIQDVGWGCIVYLRQEGRGIGLHAKIQAYNLQ 116
Cdd:PRK08815 202 DQVAIVVGqpDLSSAVPV--RVHSSCLTGDLFGSLKCDCGDQLRHGLAKLKELGGGVLLYLDQEGRGNGIAAKMRAYGYQ 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389 117 DQGADTLDANLMLGHPADARDYGIASEILAAIGIESVCLLTNNPDKVLQLAGNGANIVERMPLVVGVGDQNIEYLTTKID 196
Cdd:PRK08815 280 HAGLDTIDADAQLGFGPDERRYGSAVAMLRGLGITRVRLLTNNPTKAERLRAAGIEVEDRIRVTGRITAENERYLRTKAD 359


                 ....*..
gi 663523389 197 RMGHDID 203
Cdd:PRK08815 360 RAGHALD 366
PRK14019 PRK14019
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
6-178 8.67e-16

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


Pssm-ID: 237587 [Multi-domain]  Cd Length: 367  Bit Score: 74.62  E-value: 8.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389   6 SVNE-LVDVPADARLPTSYGDFRIRVFHEASTGLDHVALTLGDMSGPDPVLVRVHSECLTGDAFSSLRCDCGAQLAAAMK 84
Cdd:PRK14019 200 SRTEsIVERVAERPMQTAHGEFRLVAYRDKPSGSTHLALVKGTICPDEETLVRVHEPLSVLDLLEVGQPTHSWSLDAAMA 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389  85 QIQDVGWGCIVYlrqegrgigLHAKIQAYNLQDQGADTLDANLMLGHPADARDYGIASEILAAIGIESVCLLTnNPDKVL 164
Cdd:PRK14019 280 AIAEAGSGVVVL---------LNCGDDGEHLLDRFRAEEAAAALKRRPVDYRTYGIGAQILRDLGVGKMRLLS-SPRKFP 349

                        170
                 ....*....|....
gi 663523389 165 QLAGNGANIVERMP 178
Cdd:PRK14019 350 SMSGFGLEVTGYVP 363
PRK07198 PRK07198
GTP cyclohydrolase II;
47-179 6.05e-08

GTP cyclohydrolase II;


Pssm-ID: 235959 [Multi-domain]  Cd Length: 418  Bit Score: 51.97  E-value: 6.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389  47 DMSGPD-PVLVRVHSECLTGDAFSSLRCDCGAQLAAAMKQI----QDVGWGCIVYLRQEGRGIGLHAKIQAYNL--QDQG 119
Cdd:PRK07198 232 DLADPEtELTCRVHDECNGSDVFGSDICTCRPYLTHGIEECirgaQRGGVGLIVYNRKEGRALGEVTKFLVYNArkRQVG 311

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663523389 120 ADTLDANLM----LGHPADARDYGIASEILAAIGIESVCLLTNNPD-KVLQLAGNGANIVERMPL 179
Cdd:PRK07198 312 GDTAATYFArtecVAGVQDMRFQELMPDVLHWLGIRRIHRLVSMSNmKYDAITGSGIEVGERVPI 376
PRK12485 PRK12485
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
19-97 1.15e-05

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


Pssm-ID: 171535 [Multi-domain]  Cd Length: 369  Bit Score: 45.34  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523389  19 LPTSYGDFRIRVFHEASTGLDHVALTLGDMSGPDPVLVRVHsecltgdAFSSLRCDCGAQ--------LAAAMKQIQDVG 90
Cdd:PRK12485 214 LPTVHGTFRLVTYEDRIEGGVHMAMVMGDIRREQPTLVRVH-------VIDPLRDLVGAEyagpanwtLWAALQKVAEEG 286


                 ....*..
gi 663523389  91 WGCIVYL 97
Cdd:PRK12485 287 HGVVVVL 293
 
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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