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Conserved domains on  [gi|500492068|ref|WP_011946292|]
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bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II [Legionella pneumophila]

Protein Classification

RibA family protein( domain architecture ID 10002769)

RibA family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RibA COG0807
GTP cyclohydrolase II [Coenzyme transport and metabolism]; GTP cyclohydrolase II is part of ...
 4-400 0e+00

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: 589.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068   4 SLATIEEAVATLKAGKMIILMDDEDRENEGDLVIAAEHATPEAINFMSRLGCGLICLPMAEELIDKLQLPMMARHNKSPY 83
Cdd:COG0807    2 LLSSIEEIIEDIRAGKMVILVDDEDRENEGDLIMAAEFVTPEAINFMARHGRGLICLTLTEERCEQLLLPLMVNNNGTPF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068  84 GTAFTVSIEAANGVSTGISARDRARTIQVAIDPKSGPSDIISPGHVFPLRARKRGVLERPGQTEGSVDLVRLAGLTPAAV 163
Cdd:COG0807   82 GTAFTVSIEAAEGVTTGISAADRARTIQAAVAPDAKPEDLVQPGHIFPLRAQPGGVLVRAGHTEAAVDLARLAGLEPAGV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 164 ICEIINEDGTMSRRDELALFSKKHQIPLVTIKDLINYRIRHENLINPVATTQIPLEEnGVFTMTVFENQIDSGEHFVLVK 243
Cdd:COG0807  162 ICEIMNEDGTMARLPDLEEFAKEHGLKIGTIADLIAYRLRNESLVERVAEARLPTEF-GEFRLHAYRDTIDGQEHLALVK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 244 PPLYGNQVPLVRIHSECITGDVFGSRKCDCGKQLELSLSQIGAEG-GILIYLRQEGRGIGLANKLKAYALQEQGFDTVDA 322
Cdd:COG0807  241 GDPDPDEPVLVRVHSECLTGDVFGSLRCDCGWQLEAALKRIAEEGrGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEA 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500492068 323 NLELGLPADDRDYAVAYQILKYLGVDALRLLTNNPLKIASLERYGIKITQRIPLEIKPSRENHSYLKTKKIKLGHLLA 400
Cdd:COG0807  321 NLALGFPADLRDYGIGAQILRDLGVRKMRLLTNNPRKVVGLEGYGLEVVERVPLEVGPNPHNERYLRTKRDKMGHLLD 398
 
Name Accession Description Interval E-value
RibA COG0807
GTP cyclohydrolase II [Coenzyme transport and metabolism]; GTP cyclohydrolase II is part of ...
 4-400 0e+00

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: 589.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068   4 SLATIEEAVATLKAGKMIILMDDEDRENEGDLVIAAEHATPEAINFMSRLGCGLICLPMAEELIDKLQLPMMARHNKSPY 83
Cdd:COG0807    2 LLSSIEEIIEDIRAGKMVILVDDEDRENEGDLIMAAEFVTPEAINFMARHGRGLICLTLTEERCEQLLLPLMVNNNGTPF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068  84 GTAFTVSIEAANGVSTGISARDRARTIQVAIDPKSGPSDIISPGHVFPLRARKRGVLERPGQTEGSVDLVRLAGLTPAAV 163
Cdd:COG0807   82 GTAFTVSIEAAEGVTTGISAADRARTIQAAVAPDAKPEDLVQPGHIFPLRAQPGGVLVRAGHTEAAVDLARLAGLEPAGV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 164 ICEIINEDGTMSRRDELALFSKKHQIPLVTIKDLINYRIRHENLINPVATTQIPLEEnGVFTMTVFENQIDSGEHFVLVK 243
Cdd:COG0807  162 ICEIMNEDGTMARLPDLEEFAKEHGLKIGTIADLIAYRLRNESLVERVAEARLPTEF-GEFRLHAYRDTIDGQEHLALVK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 244 PPLYGNQVPLVRIHSECITGDVFGSRKCDCGKQLELSLSQIGAEG-GILIYLRQEGRGIGLANKLKAYALQEQGFDTVDA 322
Cdd:COG0807  241 GDPDPDEPVLVRVHSECLTGDVFGSLRCDCGWQLEAALKRIAEEGrGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEA 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500492068 323 NLELGLPADDRDYAVAYQILKYLGVDALRLLTNNPLKIASLERYGIKITQRIPLEIKPSRENHSYLKTKKIKLGHLLA 400
Cdd:COG0807  321 NLALGFPADLRDYGIGAQILRDLGVRKMRLLTNNPRKVVGLEGYGLEVVERVPLEVGPNPHNERYLRTKRDKMGHLLD 398
PRK09311 PRK09311
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
4-399 0e+00

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


Pssm-ID: 181774 [Multi-domain]  Cd Length: 402  Bit Score: 589.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068   4 SLATIEEAVATLKAGKMIILMDDEDRENEGDLVIAAEHATPEAINFMSRLGCGLICLPMAEELIDKLQLPMMARHNKSPY 83
Cdd:PRK09311   3 MFDSIEEAIADIAAGKAVIVVDDEDRENEGDLIFAAEKATPELVAFMVRHTSGYVCVPLTEEDADRLDLPPMVAHNQDSH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068  84 GTAFTVSIEAANGVSTGISARDRARTIQVAIDPKSGPSDIISPGHVFPLRARKRGVLERPGQTEGSVDLVRLAGLTPAAV 163
Cdd:PRK09311  83 GTAFTVSVDAANGVTTGISAADRATTIRLLADPASKPADFTRPGHVFPLRAKPGGVLRRAGHTEAAVDLARLAGLQPAGV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 164 ICEIINEDGTMSRRDELALFSKKHQIPLVTIKDLINYRIRHENLINPVATTQIPLeENGVFTMTVFENQIDSGEHFVLVK 243
Cdd:PRK09311 163 ICEIVNEDGTMARVPELRVFADEHDLALITIADLIAYRRRHEKLVEREVEARLPT-RFGEFRAIGYTSILDGKEHVALVK 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 244 PPLYGNQVPLVRIHSECITGDVFGSRKCDCGKQLELSLSQIGAEG-GILIYLR-QEGRGIGLANKLKAYALQEQGFDTVD 321
Cdd:PRK09311 242 GDIGDGEDVLVRVHSECLTGDVFGSRRCDCGPQLDAALAQIAEEGrGVVLYMRgQEGRGIGLLHKLRAYQLQDEGYDTVD 321

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500492068 322 ANLELGLPADDRDYAVAYQILKYLGVDALRLLTNNPLKIASLERYGIKITQRIPLEIKPSRENHSYLKTKKIKLGHLL 399
Cdd:PRK09311 322 ANLKLGFPADARDYGIGAQILVDLGVRSMRLLTNNPRKIAGLQGYGLHVTERVPLPVRANEENERYLRTKRDRMGHDL 399
DHBP_synthase pfam00926
3,4-dihydroxy-2-butanone 4-phosphate synthase; 3,4-Dihydroxy-2-butanone 4-phosphate is ...
 9-200 6.08e-125

3,4-dihydroxy-2-butanone 4-phosphate synthase; 3,4-Dihydroxy-2-butanone 4-phosphate is biosynthesized from ribulose 5-phosphate and serves as the biosynthetic precursor for the xylene ring of riboflavin. Sometimes found as a bifunctional enzyme with pfam00925.


Pssm-ID: 460001  Cd Length: 192  Bit Score: 358.61  E-value: 6.08e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068    9 EEAVATLKAGKMIILMDDEDRENEGDLVIAAEHATPEAINFMSRLGCGLICLPMAEELIDKLQLPMMARHNKSPYGTAFT 88
Cdd:pfam00926   1 EEAIEALRAGKPVIVVDDEDRENEGDLIIAAEFVTPEAINFMARHGSGLICVPLTEERADRLGLPPMVANNTDRHGTAFT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068   89 VSIEAANGVSTGISARDRARTIQVAIDPKSGPSDIISPGHVFPLRARKRGVLERPGQTEGSVDLVRLAGLTPAAVICEII 168
Cdd:pfam00926  81 VSVDAREGTTTGISAADRALTIRALADPGAKPEDFRRPGHVFPLRAREGGVLERAGHTEAAVDLARLAGLKPAGVICEIL 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 500492068  169 NEDGTMSRRDELALFSKKHQIPLVTIKDLINY 200
Cdd:pfam00926 161 NDDGTMARLPDLREFAKKHGLKIITIADLIAY 192
GTP_cyclohydro2 cd00641
GTP cyclohydrolase II (RibA). GTP cyclohydrolase II catalyzes the conversion of GTP to 2, ...
 207-399 5.93e-110

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: 320.60  E-value: 5.93e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 207 LINPVATTQIPLEEnGVFTMTVFENQIDSGEHFVLVKPPLYGNQVPLVRIHSECITGDVFGSRKCDCGKQLELSLSQIGA 286
Cdd:cd00641    1 LVEKVAEAPLPTRF-GDFRIVAFEDTDDGKEHVALVKGDPADGEPVLVRVHSECLTGDVFGSLRCDCGPQLEEALEEIAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 287 EG-GILIYLRQEGRGIGLANKLKAYALQEQGFDTVDANLELGLPADDRDYAVAYQILKYLGVDALRLLTNNPLKIASLER 365
Cdd:cd00641   80 EGgGVLLYLRQEGRGIGLANKLRAYALQDQGLDTVEANEALGFPADARDYGLAAQILRDLGIKSVRLLTNNPDKIDALEG 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 500492068 366 YGIKITQRIPLEIKPSRENHSYLKTKKIKLGHLL 399
Cdd:cd00641  160 YGIEVVERVPLEVEPNEENKGYLKTKRDKMGHLL 193
ribB TIGR00506
3,4-dihydroxy-2-butanone 4-phosphate synthase; Several members of the family are bifunctional, ...
 8-201 4.74e-94

3,4-dihydroxy-2-butanone 4-phosphate synthase; 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. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]


Pssm-ID: 273108  Cd Length: 199  Bit Score: 280.42  E-value: 4.74e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068    8 IEEAVATLKAGKMIILMDDEDRENEGDLVIAAEHATPEAINFMSRLGCGLICLPMAEELIDKLQLPMMARHNKSPYGTAF 87
Cdd:TIGR00506   5 VEEALEALKKGEIVLVYDDEDRENEGDLIVAAEFITPEQIAFMRRHAGGLICVAITPDIADKLDLPPMVDINTSASGTAS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068   88 TVSIEAANG-VSTGISARDRARTIQVAIDPKSGPSDIISPGHVFPLRARKRGVLERPGQTEGSVDLVRLAGLTPAAVICE 166
Cdd:TIGR00506  85 TFTITVAHRkTFTGISANDRALTIRAALADVVKPSDFRRPGHVFPLRAADGGVLTRGGHTEASVDLAELAGLKPAGVICE 164

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 500492068  167 IINEDGTMSRRDELALFSKKHQIPLVTIKDLINYR 201
Cdd:TIGR00506 165 MMNDDGTMARKPELMEYAKKHNLKLISIEDLIEYR 199
 
Name Accession Description Interval E-value
RibA COG0807
GTP cyclohydrolase II [Coenzyme transport and metabolism]; GTP cyclohydrolase II is part of ...
 4-400 0e+00

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: 589.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068   4 SLATIEEAVATLKAGKMIILMDDEDRENEGDLVIAAEHATPEAINFMSRLGCGLICLPMAEELIDKLQLPMMARHNKSPY 83
Cdd:COG0807    2 LLSSIEEIIEDIRAGKMVILVDDEDRENEGDLIMAAEFVTPEAINFMARHGRGLICLTLTEERCEQLLLPLMVNNNGTPF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068  84 GTAFTVSIEAANGVSTGISARDRARTIQVAIDPKSGPSDIISPGHVFPLRARKRGVLERPGQTEGSVDLVRLAGLTPAAV 163
Cdd:COG0807   82 GTAFTVSIEAAEGVTTGISAADRARTIQAAVAPDAKPEDLVQPGHIFPLRAQPGGVLVRAGHTEAAVDLARLAGLEPAGV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 164 ICEIINEDGTMSRRDELALFSKKHQIPLVTIKDLINYRIRHENLINPVATTQIPLEEnGVFTMTVFENQIDSGEHFVLVK 243
Cdd:COG0807  162 ICEIMNEDGTMARLPDLEEFAKEHGLKIGTIADLIAYRLRNESLVERVAEARLPTEF-GEFRLHAYRDTIDGQEHLALVK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 244 PPLYGNQVPLVRIHSECITGDVFGSRKCDCGKQLELSLSQIGAEG-GILIYLRQEGRGIGLANKLKAYALQEQGFDTVDA 322
Cdd:COG0807  241 GDPDPDEPVLVRVHSECLTGDVFGSLRCDCGWQLEAALKRIAEEGrGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEA 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500492068 323 NLELGLPADDRDYAVAYQILKYLGVDALRLLTNNPLKIASLERYGIKITQRIPLEIKPSRENHSYLKTKKIKLGHLLA 400
Cdd:COG0807  321 NLALGFPADLRDYGIGAQILRDLGVRKMRLLTNNPRKVVGLEGYGLEVVERVPLEVGPNPHNERYLRTKRDKMGHLLD 398
PRK09311 PRK09311
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
4-399 0e+00

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


Pssm-ID: 181774 [Multi-domain]  Cd Length: 402  Bit Score: 589.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068   4 SLATIEEAVATLKAGKMIILMDDEDRENEGDLVIAAEHATPEAINFMSRLGCGLICLPMAEELIDKLQLPMMARHNKSPY 83
Cdd:PRK09311   3 MFDSIEEAIADIAAGKAVIVVDDEDRENEGDLIFAAEKATPELVAFMVRHTSGYVCVPLTEEDADRLDLPPMVAHNQDSH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068  84 GTAFTVSIEAANGVSTGISARDRARTIQVAIDPKSGPSDIISPGHVFPLRARKRGVLERPGQTEGSVDLVRLAGLTPAAV 163
Cdd:PRK09311  83 GTAFTVSVDAANGVTTGISAADRATTIRLLADPASKPADFTRPGHVFPLRAKPGGVLRRAGHTEAAVDLARLAGLQPAGV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 164 ICEIINEDGTMSRRDELALFSKKHQIPLVTIKDLINYRIRHENLINPVATTQIPLeENGVFTMTVFENQIDSGEHFVLVK 243
Cdd:PRK09311 163 ICEIVNEDGTMARVPELRVFADEHDLALITIADLIAYRRRHEKLVEREVEARLPT-RFGEFRAIGYTSILDGKEHVALVK 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 244 PPLYGNQVPLVRIHSECITGDVFGSRKCDCGKQLELSLSQIGAEG-GILIYLR-QEGRGIGLANKLKAYALQEQGFDTVD 321
Cdd:PRK09311 242 GDIGDGEDVLVRVHSECLTGDVFGSRRCDCGPQLDAALAQIAEEGrGVVLYMRgQEGRGIGLLHKLRAYQLQDEGYDTVD 321

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500492068 322 ANLELGLPADDRDYAVAYQILKYLGVDALRLLTNNPLKIASLERYGIKITQRIPLEIKPSRENHSYLKTKKIKLGHLL 399
Cdd:PRK09311 322 ANLKLGFPADARDYGIGAQILVDLGVRSMRLLTNNPRKIAGLQGYGLHVTERVPLPVRANEENERYLRTKRDRMGHDL 399
PRK09319 PRK09319
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase RibB/GTP cyclohydrolase II RibA;
7-399 0e+00

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


Pssm-ID: 236465 [Multi-domain]  Cd Length: 555  Bit Score: 518.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068   7 TIEEAVATLKAGKMIILMDDEDRENEGDLVIAAEHATPEAINFMSRLGCGLICLPMAEELIDKLQLPMMARHNKSPYGTA 86
Cdd:PRK09319   7 SIDDALAAIRNGECVVVVDDENRENEGDLICAAQFATPEMINFMATEARGLICLAMTGERLDELDLPLMVDRNTDSNQTA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068  87 FTVSIEAA--NGVSTGISARDRARTIQVAIDPKSGPSDIISPGHVFPLRARKRGVLERPGQTEGSVDLVRLAGLTPAAVI 164
Cdd:PRK09319  87 FTVSIDAGpeLGVSTGISAEDRARTIQVAINPDTKPEDLRRPGHIFPLRAKEGGVLKRAGHTEAAVDLARLAGLYPAGVI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 165 CEIINEDGTMSRRDELALFSKKHQIPLVTIKDLINYRIRHENLINPVATTQIPlEENGVFTMTVFENQIDSGEHFVLVK- 243
Cdd:PRK09319 167 CEIQNPDGSMARLPELKEYAKQHGLKLISIADLISYRLQNERFVYREAVAKLP-SQFGQFQAYGYRNELDGSEHVALVKg 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 244 -PPLYGNQVPLVRIHSECITGDVFGSRKCDCGKQLELSLSQIGAEG-GILIYLRQEGRGIGLANKLKAYALQEQGFDTVD 321
Cdd:PRK09319 246 dPANFKDEPVLVRMHSECLTGDAFGSLRCDCRMQLEAALKMIENEGeGVVVYLRQEGRGIGLINKLKAYSLQDGGLDTVE 325

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500492068 322 ANLELGLPADDRDYAVAYQILKYLGVDALRLLTNNPLKIASLERYGIKITQRIPLEIKPSRENHSYLKTKKIKLGHLL 399
Cdd:PRK09319 326 ANERLGFPADLRNYGVGAQILNDLGIKRLRLITNNPRKIAGLGGYGLEVVDRVPLLIEANDYNAEYLATKAEKLGHLL 403
PLN02831 PLN02831
Bifunctional GTP cyclohydrolase II/ 3,4-dihydroxy-2-butanone-4-phosphate synthase
 6-402 3.27e-171

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


Pssm-ID: 215445 [Multi-domain]  Cd Length: 450  Bit Score: 486.13  E-value: 3.27e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068   6 ATIEEAVATLKAGKMIILMDDEDRENEGDLVIAAEHATPEAINFMSRLGCGLICLPMAEELIDKLQLPMMARH--NKSPY 83
Cdd:PLN02831  36 SSIAEALEDIRQGKFVVVVDDEDRENEGDLIMAASLVTPEAMAFLVKHGSGIVCVSMKGEDLDRLRLPLMVPSkeNEEKM 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068  84 GTAFTVSIEAANGVSTGISARDRARTIQVAIDPKSGPSDIISPGHVFPLRARKRGVLERPGQTEGSVDLVRLAGLTPAAV 163
Cdd:PLN02831 116 ATAFTVTVDAKHGTTTGVSASDRAKTILALASPDSKPEDFRRPGHIFPLRYREGGVLKRAGHTEAAVDLAVLAGLPPVGV 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 164 ICEIIN-EDGTMSRRDELALFSKKHQIPLVTIKDLINYRIRHENLINPVATTQIPLEeNGVFTMTVFENQIDSGEHFVLV 242
Cdd:PLN02831 196 LCEIVNdEDGSMARLPQLRKFAEEHGLKIISIADLIRYRRKREKLVERTAVARLPTK-WGLFTAYCYRSKLDGIEHIAFV 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 243 KPPLYGNQVPLVRIHSECITGDVFGSRKCDCGKQLELSLSQIGAEG-GILIYLR-QEGRGIGLANKLKAYALQEQGFDTV 320
Cdd:PLN02831 275 KGDIGDGQDVLVRVHSECLTGDIFGSARCDCGNQLALAMQLIEKAGrGVLVYLRgHEGRGIGLGHKLRAYNLQDEGRDTV 354

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 321 DANLELGLPADDRDYAVAYQILKYLGVDALRLLTNNPLKIASLERYGIKITQRIPLEIKPSRENHSYLKTKKIKLGHLLA 400
Cdd:PLN02831 355 EANEELGLPVDSREYGIGAQILRDLGVRTMRLMTNNPAKYTGLKGYGLAVVGRVPLLTPITKENKRYLETKRTKMGHVYG 434


                 ..
gi 500492068 401 ID 402
Cdd:PLN02831 435 SD 436
RibB COG0108
3,4-dihydroxy-2-butanone 4-phosphate synthase [Coenzyme transport and metabolism]; 3, ...
 4-203 2.64e-134

3,4-dihydroxy-2-butanone 4-phosphate synthase [Coenzyme transport and metabolism]; 3,4-dihydroxy-2-butanone 4-phosphate synthase is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 439878  Cd Length: 201  Bit Score: 382.84  E-value: 2.64e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068   4 SLATIEEAVATLKAGKMIILMDDEDRENEGDLVIAAEHATPEAINFMSRLGCGLICLPMAEELIDKLQLPMMARHNKSPY 83
Cdd:COG0108    2 SLSSIEEAIEALRAGKMVIVVDDEDRENEGDLIIAAEFVTPEAINFMARHGRGLICLPLTEERADRLGLPPMVDRNTDPY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068  84 GTAFTVSIEAANGVSTGISARDRARTIQVAIDPKSGPSDIISPGHVFPLRARKRGVLERPGQTEGSVDLVRLAGLTPAAV 163
Cdd:COG0108   82 GTAFTVSVDAREGVTTGISAADRALTIRALADPDAKPEDFVRPGHVFPLRARPGGVLERAGHTEAAVDLARLAGLKPAGV 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 500492068 164 ICEIINEDGTMSRRDELALFSKKHQIPLVTIKDLINYRIR 203
Cdd:COG0108  162 ICEIMNDDGTMARLPDLEEFAKKHGLKIITIADLIAYRRR 201
PRK14019 PRK14019
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
4-377 1.66e-132

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


Pssm-ID: 237587 [Multi-domain]  Cd Length: 367  Bit Score: 384.70  E-value: 1.66e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068   4 SLATIEEAVATLKAGKMIILMDDEDRENEGDLVIAAEHATPEAINFMSRLGCGLICLPMAEELIDKLQLPMMARHNKSPY 83
Cdd:PRK14019   2 TLASIEEIIADIRAGRMVILVDEEDRENEGDLVMAAEFVTPEAINFMAKHGRGLICLTLTEERCEQLGLPLMTYRNGTQY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068  84 GTAFTVSIEAANGVSTGISARDRARTIQVAIDPKSGPSDIISPGHVFPLRARKRGVLERPGQTEGSVDLVRLAGLTPAAV 163
Cdd:PRK14019  82 GTNFTVSIEAAEGVTTGISAADRARTIQAAVARDAKPEDIVQPGHIFPLMAQPGGVLVRAGHTEAGCDLAALAGLTPAAV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 164 ICEIINEDGTMSRRDELALFSKKHQIPLVTIKDLINYRIRHENLINPVAttQIPLE-ENGVFTMTVFENQIDSGEHFVLV 242
Cdd:PRK14019 162 ICEIMKDDGTMARLPDLEEFAKEHGLKIGTIADLIHYRSRTESIVERVA--ERPMQtAHGEFRLVAYRDKPSGSTHLALV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 243 KPPLYGNQVPLVRIHSECITGDVFGSRKCDCGKQLELSLSQIGAEGGILIYLrqegrgigLANKLKAYALQEQGFDTVDA 322
Cdd:PRK14019 240 KGTICPDEETLVRVHEPLSVLDLLEVGQPTHSWSLDAAMAAIAEAGSGVVVL--------LNCGDDGEHLLDRFRAEEAA 311

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 500492068 323 NLELGLPADDRDYAVAYQILKYLGVDALRLLTnNPLKIASLERYGIKITQRIPLE 377
Cdd:PRK14019 312 AALKRRPVDYRTYGIGAQILRDLGVGKMRLLS-SPRKFPSMSGFGLEVTGYVPMP 365
DHBP_synthase pfam00926
3,4-dihydroxy-2-butanone 4-phosphate synthase; 3,4-Dihydroxy-2-butanone 4-phosphate is ...
 9-200 6.08e-125

3,4-dihydroxy-2-butanone 4-phosphate synthase; 3,4-Dihydroxy-2-butanone 4-phosphate is biosynthesized from ribulose 5-phosphate and serves as the biosynthetic precursor for the xylene ring of riboflavin. Sometimes found as a bifunctional enzyme with pfam00925.


Pssm-ID: 460001  Cd Length: 192  Bit Score: 358.61  E-value: 6.08e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068    9 EEAVATLKAGKMIILMDDEDRENEGDLVIAAEHATPEAINFMSRLGCGLICLPMAEELIDKLQLPMMARHNKSPYGTAFT 88
Cdd:pfam00926   1 EEAIEALRAGKPVIVVDDEDRENEGDLIIAAEFVTPEAINFMARHGSGLICVPLTEERADRLGLPPMVANNTDRHGTAFT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068   89 VSIEAANGVSTGISARDRARTIQVAIDPKSGPSDIISPGHVFPLRARKRGVLERPGQTEGSVDLVRLAGLTPAAVICEII 168
Cdd:pfam00926  81 VSVDAREGTTTGISAADRALTIRALADPGAKPEDFRRPGHVFPLRAREGGVLERAGHTEAAVDLARLAGLKPAGVICEIL 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 500492068  169 NEDGTMSRRDELALFSKKHQIPLVTIKDLINY 200
Cdd:pfam00926 161 NDDGTMARLPDLREFAKKHGLKIITIADLIAY 192
PRK09318 PRK09318
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
8-401 9.50e-124

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


Pssm-ID: 236464 [Multi-domain]  Cd Length: 387  Bit Score: 362.90  E-value: 9.50e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068   8 IEEAVATLKAGKMIILMDDEdRENEGDLVIAAEHATPEAINFMSRLGCGLICLPMAEELIDK---LQLPmmarhnkSPYG 84
Cdd:PRK09318   1 MEELREAFLEGKPVILIDRN-RENEADFVYPAQIITEEVVNFFLSYGKGLLCLTADEEDLLKrgfFKLP-------SNGG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068  85 -TAFTVSIEAANGvsTGISARDRARTIQvAIDPKSGPSDIISPGHVFPLRARkrGVLERPGQTEGSVDLVRLAGLTPAAV 163
Cdd:PRK09318  73 eTNFFIPVDYGTG--TGISASERALTCR-KLAEGLYVHEFRYPGHVTLLGGI--GFNRRRGHTEASLELSELLGFKRYAV 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 164 ICEIINEDGTMSRRDELALFSKKHQIPLVTIKDLINYRIRHENLINPVATTQIPlEENGVFTMTVFENQIDSGEHFVLVK 243
Cdd:PRK09318 148 IVEILDEKGDSHDLDYVLKLAEKFSLPVLEIDDVWKEFVRRKQLIKVKAEAKLP-TDYGEFEIVSFENHLDGKEHVAIVK 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 244 PPLYGnqVPLVRIHSECITGDVFGSRKCDCGKQLELSLSQIGAEGGILIYLRQEGRGIGLANKLKAYALQEQGFDTVDAN 323
Cdd:PRK09318 227 EPLGE--VPLVRIHSECVTGDTLSSLRCDCGSQLANFLRMISKEGGILIYLRQEGRGIGLSNKIKAYELQDKGLDTVEAN 304

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500492068 324 LELGLPADDRDYAVAYQILKYLGVDALRLLTNNPLKIASLERYGIKITQRIPLEIKPSRENHSYLKTKKIKLGHLLAI 401
Cdd:PRK09318 305 RALGFKEDERDYAAAFQILKALGIEKVRLLTNNPRKTKALEKYGIEVVETVPLYGEVTKYNRFYLKTKVEKLGHKLEL 382
GTP_cyclohydro2 cd00641
GTP cyclohydrolase II (RibA). GTP cyclohydrolase II catalyzes the conversion of GTP to 2, ...
 207-399 5.93e-110

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: 320.60  E-value: 5.93e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 207 LINPVATTQIPLEEnGVFTMTVFENQIDSGEHFVLVKPPLYGNQVPLVRIHSECITGDVFGSRKCDCGKQLELSLSQIGA 286
Cdd:cd00641    1 LVEKVAEAPLPTRF-GDFRIVAFEDTDDGKEHVALVKGDPADGEPVLVRVHSECLTGDVFGSLRCDCGPQLEEALEEIAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 287 EG-GILIYLRQEGRGIGLANKLKAYALQEQGFDTVDANLELGLPADDRDYAVAYQILKYLGVDALRLLTNNPLKIASLER 365
Cdd:cd00641   80 EGgGVLLYLRQEGRGIGLANKLRAYALQDQGLDTVEANEALGFPADARDYGLAAQILRDLGIKSVRLLTNNPDKIDALEG 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 500492068 366 YGIKITQRIPLEIKPSRENHSYLKTKKIKLGHLL 399
Cdd:cd00641  160 YGIEVVERVPLEVEPNEENKGYLKTKRDKMGHLL 193
ribA PRK00393
GTP cyclohydrolase II RibA;
208-399 1.86e-103

GTP cyclohydrolase II RibA;


Pssm-ID: 234745  Cd Length: 197  Bit Score: 304.07  E-value: 1.86e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 208 INPVATTQIPLEeNGVFTMTVFENQIDSGEHFVLVKPPLYGNQVPLVRIHSECITGDVFGSRKCDCGKQLELSLSQIGAE 287
Cdd:PRK00393   3 LKRVAEAKLPTP-WGDFLMVGFEELATGKEHVALVFGDISGTEPVLVRVHSECLTGDALFSLRCDCGFQLEAALERIAEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 288 G-GILIYLRQEGRGIGLANKLKAYALQEQGFDTVDANLELGLPADDRDYAVAYQILKYLGVDALRLLTNNPLKIASLERY 366
Cdd:PRK00393  82 GrGILLYLRQEGRGIGLLNKIRAYALQDQGLDTVEANHQLGFAADERDYTLAADMLKALGVKKVRLLTNNPKKVEALTEA 161

                        170       180       190
                 ....*....|....*....|....*....|...
gi 500492068 367 GIKITQRIPLEIKPSRENHSYLKTKKIKLGHLL 399
Cdd:PRK00393 162 GINIVERVPLIVGRNPHNEHYLKTKAEKMGHLL 194
PRK09314 PRK09314
bifunctional 3,4-dihydroxy-2-butanone 4-phosphate synthase/GTP cyclohydrolase II;
8-374 2.09e-103

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


Pssm-ID: 181775 [Multi-domain]  Cd Length: 339  Bit Score: 309.60  E-value: 2.09e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068   8 IEEAVATLKAGKMIILMDDEDRENEGDLVIAAEHATPEAINFMSRLGCGLICLPMAEELIDKLQLPMMARHNKSPYGTAF 87
Cdd:PRK09314   6 VEEAIEDIKNGKMLIMVDDEDRENEGDLVYAAIFSTPEKVNFMATHARGLICVSLTKELAKKLELPPMVSKNTSNHETAF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068  88 TVSIEAANGvSTGISARDRARTIQVAIDPKSGPSDIISPGHVFPLRARKRGVLERPGQTEGSVDLVRLAGLTPAAVICEI 167
Cdd:PRK09314  86 TVSIDAKEA-TTGISAFERDMTIKLLADDTSKPSDFVRPGHIFPLIAKDGGVLVRTGHTEGSVDLCKLAGLKPVAVICEI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 168 INEDGTMSRRDELALFSKKHQIPLVTIKDLINYRIRHENLINPVAttqiplEENGVFTMTVFENQI----DSGEHFVLVk 243
Cdd:PRK09314 165 MKEDGTMARRDDLEDFAKKHNLKMIYVSDLVEYRLKNESLIKEEE------KEESEFAGFKAEKYTfldhLQNEHIAFK- 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 244 pplYGN--QVPLVRIHSECITGDVFGSRKCDcgkQLELSLSQIGAEGGILIYLRQEgrgiglanklkayalqeqgfdTVD 321
Cdd:PRK09314 238 ---FGEikLTPNVKFHKIGSDFELLTSDKFS---ELLKAIEYLKKNGGVLIFLNTE---------------------SKE 290

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 500492068 322 ANLElglpaddRDYAVAYQILKYLGVDALRLLTNNPLK-IASLERYGIKITQRI 374
Cdd:PRK09314 291 NNQV-------KDYGIGAQILKYLGIKDIKLLSSSEDKeYVGLSGFGLNIVETI 337
PRK12485 PRK12485
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
4-377 1.30e-101

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


Pssm-ID: 171535 [Multi-domain]  Cd Length: 369  Bit Score: 306.12  E-value: 1.30e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068   4 SLATIEEAVATLKAGKMIILMDDEDRENEGDLVIAAEHATPEAINFMSRLGCGLICLPMAEELIDKLQLPMMARHNKSPY 83
Cdd:PRK12485   2 AFNTIEEIIEDYRQGKMVLLVDDEDRENEGDLLLAAERCDAQAINFMAREARGLICLTLTDEHCQRLGLEQMVPSNGSVF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068  84 GTAFTVSIEAANGVSTGISARDRARTIQVAIDPKSGPSDIISPGHVFPLRARKRGVLERPGQTEGSVDLVRLAGLTPAAV 163
Cdd:PRK12485  82 STAFTVSIEAATGVTTGISAADRARTVAAAVAPNARPEDLVQPGHIFPLRAREGGVLTRAGHTEAGCDLARLAGFSPASV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 164 ICEIINEDGTMSRRDELALFSKKHQIPLVTIKDLINYRIRHENLINPVATTQIPlEENGVFTMTVFENQIDSGEHFVLVK 243
Cdd:PRK12485 162 IVEVMNDDGTMARRPDLEVFAAKHGIKIGTIADLIHYRLSTEHTIKRIGERELP-TVHGTFRLVTYEDRIEGGVHMAMVM 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 244 PPLYGNQVPLVRIHSECITGDVFGSRKcdCGKQ---LELSLSQIGAEG-GILIYLRQEGRGIGLANKLKAYALQEQGFDT 319
Cdd:PRK12485 241 GDIRREQPTLVRVHVIDPLRDLVGAEY--AGPAnwtLWAALQKVAEEGhGVVVVLANHESSQALLERIPQLTQPPRQYQR 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 320 VDANL--ELGLPAddrdyavayQILKYLGVDALRLLtNNPLKIASLERYGIKITQRIPLE 377
Cdd:PRK12485 319 SQSRIysEVGTGA---------QILQDLGVGKLRHL-GPPLKYAGLTGYDLEVVESIPFP 368
ribB TIGR00506
3,4-dihydroxy-2-butanone 4-phosphate synthase; Several members of the family are bifunctional, ...
 8-201 4.74e-94

3,4-dihydroxy-2-butanone 4-phosphate synthase; 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. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]


Pssm-ID: 273108  Cd Length: 199  Bit Score: 280.42  E-value: 4.74e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068    8 IEEAVATLKAGKMIILMDDEDRENEGDLVIAAEHATPEAINFMSRLGCGLICLPMAEELIDKLQLPMMARHNKSPYGTAF 87
Cdd:TIGR00506   5 VEEALEALKKGEIVLVYDDEDRENEGDLIVAAEFITPEQIAFMRRHAGGLICVAITPDIADKLDLPPMVDINTSASGTAS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068   88 TVSIEAANG-VSTGISARDRARTIQVAIDPKSGPSDIISPGHVFPLRARKRGVLERPGQTEGSVDLVRLAGLTPAAVICE 166
Cdd:TIGR00506  85 TFTITVAHRkTFTGISANDRALTIRAALADVVKPSDFRRPGHVFPLRAADGGVLTRGGHTEASVDLAELAGLKPAGVICE 164

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 500492068  167 IINEDGTMSRRDELALFSKKHQIPLVTIKDLINYR 201
Cdd:TIGR00506 165 MMNDDGTMARKPELMEYAKKHNLKLISIEDLIEYR 199
ribA TIGR00505
GTP cyclohydrolase II; Several members of the family are bifunctional, involving both ribA and ...
 222-399 5.01e-81

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: 247.00  E-value: 5.01e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068  222 GVFTMTVFENQIDSGEHFVLVKPPLYGNQVPLVRIHSECITGDVFGSRKCDCGKQLELSLSQIGAEG-GILIYLRQEGRG 300
Cdd:TIGR00505  13 GDFYMVGFEEPATGKDHVALVKGDISAHTDVLVRIHSECLTGDALHSLRCDCGFQLEAALKQIAEEGrGVLIYLRQEGRG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068  301 IGLANKLKAYALQEQGFDTVDANLELGLPADDRDYAVAYQILKYLGVDALRLLTNNPLKIASLERYGIKITQRIPLEIKP 380
Cdd:TIGR00505  93 IGLINKLRAYALQDKGYDTVQANLMLGFPADERDFSLCADILEDLGVKKVRLLTNNPKKIEILKKAGINIVERVPLIVGR 172

                         170
                  ....*....|....*....
gi 500492068  381 SRENHSYLKTKKIKLGHLL 399
Cdd:TIGR00505 173 NENNEGYLDTKAEKMGHLL 191
GTP_cyclohydro2 pfam00925
GTP cyclohydrolase II; GTP cyclohydrolase II catalyzes the first committed step in the ...
 254-375 3.20e-69

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: 214.24  E-value: 3.20e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068  254 VRIHSECITGDVFGSRKCDCGKQLELSLSQIGAEG-GILIYLRQEGRGIGLANKLKAYALQEQGFDTVDANLELGLPADD 332
Cdd:pfam00925   1 VRVHSECLTGDVLGSLRCDCGEQLEAALRAIAEEGrGVLVYLRQEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPADL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 500492068  333 RDYAVAYQILKYLGVDALRLLTNNPLKIASLERYGIKITQRIP 375
Cdd:pfam00925  81 RDYGIGAQILRDLGVKKIRLLTNNPRKIVGLEGYGLEVVERVP 123
PRK08815 PRK08815
GTP cyclohydrolase II RibA;
8-402 3.46e-61

GTP cyclohydrolase II RibA;


Pssm-ID: 236340 [Multi-domain]  Cd Length: 375  Bit Score: 201.91  E-value: 3.46e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068   8 IEEAVATLKAGKMIILMDDEDRENegdLVIAAEHATPEAINFMSRLGCGLICLPMAEELIDKLQLPmmarhnkspygtaf 87
Cdd:PRK08815  20 CERAAAELRAGRPVLLTDAQGQRR---AVIALDSSTAQSAAAFARAAQGRHYLFLTATRAQVLGLE-------------- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068  88 tvsieAANGVSTGISARDRARTIQVA--IDPKSgpsdiisPGHVFPLRARKRGVLErpgqtegsvdLVRLAGLTPAAVIC 165
Cdd:PRK08815  83 -----APQGARVALPDVDYDRLAALAylRDGRV-------PAPWAPGDALDAGAVE----------IARLALLLPAMVAV 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 166 EIinedgtmsRRDELALFSKKHQIPLVTIKDLINYRIRHENLInpVATTQIPLEENGVFTMTVF---ENQIDsgEHFVLV 242
Cdd:PRK08815 141 PL--------PVHDEAAFAGCQALALADLDAGCATSAAAGYEL--VTRTPVPLRGLGMTEFVVFrggVAQRD--QVAIVV 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 243 KPPLYGNQVPlVRIHSECITGDVFGSRKCDCGKQLELSLSQI-GAEGGILIYLRQEGRGIGLANKLKAYALQEQGFDTVD 321
Cdd:PRK08815 209 GQPDLSSAVP-VRVHSSCLTGDLFGSLKCDCGDQLRHGLAKLkELGGGVLLYLDQEGRGNGIAAKMRAYGYQHAGLDTID 287

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 322 ANLELGLPADDRDYAVAYQILKYLGVDALRLLTNNPLKIASLERYGIKITQRIPLEIKPSRENHSYLKTKKIKLGHLLAI 401
Cdd:PRK08815 288 ADAQLGFGPDERRYGSAVAMLRGLGITRVRLLTNNPTKAERLRAAGIEVEDRIRVTGRITAENERYLRTKADRAGHALDV 367


                 .
gi 500492068 402 D 402
Cdd:PRK08815 368 D 368
PRK05773 PRK05773
3,4-dihydroxy-2-butanone 4-phosphate synthase; Validated
 8-198 9.03e-32

3,4-dihydroxy-2-butanone 4-phosphate synthase; Validated


Pssm-ID: 235601  Cd Length: 219  Bit Score: 119.78  E-value: 9.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068   8 IEEAVATLKAGKMIILMDDEDRENEGDLVIAAEHATPEAINFMSRLGCGLICLPMAEELIDKLQLPMMARHNKS------ 81
Cdd:PRK05773   3 FEEARKALESGIPVLIYDFDGREEEVDMVFYAGAVTWKSIYTLRKNAGGLICYATSNSEGKTLGLNFLAEILKRhelyrk 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068  82 -----PYGT--AFTVSIEAANgVSTGISARDRARTI----QVAIDPKSGPSDII--------SPGHVFPLRArkRGVLER 142
Cdd:PRK05773  83 lvkkpSYGDepAFSLWVNHVK-TKTGISDYDRALTIrelhKVVELAKTNPEEAReefyenfySPGHVPILIG--RGIRER 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 500492068 143 PGQTEGSVDLVRLAGLTPAAVICEIINEDGTMSRRDELAlFSKKHQIPLVTIKDLI 198
Cdd:PRK05773 160 RGHTELSIALAQAAGLEPSAVIAEMLDEKLSLSKEKAKK-IAKNLGFPLVEGKEIF 214
PRK07198 PRK07198
GTP cyclohydrolase II;
251-381 1.00e-07

GTP cyclohydrolase II;


Pssm-ID: 235959 [Multi-domain]  Cd Length: 418  Bit Score: 53.51  E-value: 1.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500492068 251 VPL-VRIHSECITGDVFGSRKCDC------GKQLELSLSQIGAeGGILIYLRQEGRGIGLANKLKAY-ALQEQ-GFDTVD 321
Cdd:PRK07198 238 TELtCRVHDECNGSDVFGSDICTCrpylthGIEECIRGAQRGG-VGLIVYNRKEGRALGEVTKFLVYnARKRQvGGDTAA 316

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500492068 322 ANLElglpaddRDYAVA------YQ-----ILKYLGVDAL-RLLTNNPLKIASLERYGIKITQR--IPLEIKPS 381
Cdd:PRK07198 317 TYFA-------RTECVAgvqdmrFQelmpdVLHWLGIRRIhRLVSMSNMKYDAITGSGIEVGERvpIPDELIPA 383
 
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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