|
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
|
|
|