NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|145349380|ref|XP_001419113|]
View 

predicted protein [Ostreococcus lucimarinus CCE9901]

Protein Classification

PLN02831 family protein( domain architecture ID 11477181)

PLN02831 family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLN02831 PLN02831
Bifunctional GTP cyclohydrolase II/ 3,4-dihydroxy-2-butanone-4-phosphate synthase
 57-485 0e+00

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


:

Pssm-ID: 215445 [Multi-domain]  Cd Length: 450  Bit Score: 772.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380  57 DPDAPTAGFAAVADALEDVAKGKFVVVLDDEDRENEGDLIGAADKMTAESLAFMIRHTSGLVCVSLEDSRADALDLPLMV 136
Cdd:PLN02831  27 DPDRPTEGFSSIAEALEDIRQGKFVVVVDDEDRENEGDLIMAASLVTPEAMAFLVKHGSGIVCVSMKGEDLDRLRLPLMV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 137 DSQSNKDAMKTAFTVSVDLAT-STTGISASERAMTINALGSDETTAAAFVRPGHVFPLRYRAGGVLKRAGHTEAAVDLAR 215
Cdd:PLN02831 107 PSKENEEKMATAFTVTVDAKHgTTTGVSASDRAKTILALASPDSKPEDFRRPGHIFPLRYREGGVLKRAGHTEAAVDLAV 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 216 MAGSSPVGVLCEIVNDEDGSMARLPQLKVFAEKHGLKMVLISDMIRYRRAREKMVERTAVARLPTEYGNFTCVSYKNTLD 295
Cdd:PLN02831 187 LAGLPPVGVLCEIVNDEDGSMARLPQLRKFAEEHGLKIISIADLIRYRRKREKLVERTAVARLPTKWGLFTAYCYRSKLD 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 296 GHEHVAFLYGEHeGDvsgavGEDMLVRVHSECLTGDIFKSARCDCGNQLDMAMRRIAGEGKGCIVYLRGQEGRGIGLGHK 375
Cdd:PLN02831 267 GIEHIAFVKGDI-GD-----GQDVLVRVHSECLTGDIFGSARCDCGNQLALAMQLIEKAGRGVLVYLRGHEGRGIGLGHK 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 376 LRAYNLQDEGRDTVQANEDLGFPADTREYGVGAQILQDLGVTSLRLMTNNPAKYNGLSGYGLKVTGRVPLFAPVTMENKR 455
Cdd:PLN02831 341 LRAYNLQDEGRDTVEANEELGLPVDSREYGIGAQILRDLGVRTMRLMTNNPAKYTGLKGYGLAVVGRVPLLTPITKENKR 420

                        410       420       430
                 ....*....|....*....|....*....|
gi 145349380 456 YIDTKRMKMGHLFEMLEGVEPSQAESEQKP 485
Cdd:PLN02831 421 YLETKRTKMGHVYGSDLGGHVSGLESAETN 450
 
Name Accession Description Interval E-value
PLN02831 PLN02831
Bifunctional GTP cyclohydrolase II/ 3,4-dihydroxy-2-butanone-4-phosphate synthase
 57-485 0e+00

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


Pssm-ID: 215445 [Multi-domain]  Cd Length: 450  Bit Score: 772.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380  57 DPDAPTAGFAAVADALEDVAKGKFVVVLDDEDRENEGDLIGAADKMTAESLAFMIRHTSGLVCVSLEDSRADALDLPLMV 136
Cdd:PLN02831  27 DPDRPTEGFSSIAEALEDIRQGKFVVVVDDEDRENEGDLIMAASLVTPEAMAFLVKHGSGIVCVSMKGEDLDRLRLPLMV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 137 DSQSNKDAMKTAFTVSVDLAT-STTGISASERAMTINALGSDETTAAAFVRPGHVFPLRYRAGGVLKRAGHTEAAVDLAR 215
Cdd:PLN02831 107 PSKENEEKMATAFTVTVDAKHgTTTGVSASDRAKTILALASPDSKPEDFRRPGHIFPLRYREGGVLKRAGHTEAAVDLAV 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 216 MAGSSPVGVLCEIVNDEDGSMARLPQLKVFAEKHGLKMVLISDMIRYRRAREKMVERTAVARLPTEYGNFTCVSYKNTLD 295
Cdd:PLN02831 187 LAGLPPVGVLCEIVNDEDGSMARLPQLRKFAEEHGLKIISIADLIRYRRKREKLVERTAVARLPTKWGLFTAYCYRSKLD 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 296 GHEHVAFLYGEHeGDvsgavGEDMLVRVHSECLTGDIFKSARCDCGNQLDMAMRRIAGEGKGCIVYLRGQEGRGIGLGHK 375
Cdd:PLN02831 267 GIEHIAFVKGDI-GD-----GQDVLVRVHSECLTGDIFGSARCDCGNQLALAMQLIEKAGRGVLVYLRGHEGRGIGLGHK 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 376 LRAYNLQDEGRDTVQANEDLGFPADTREYGVGAQILQDLGVTSLRLMTNNPAKYNGLSGYGLKVTGRVPLFAPVTMENKR 455
Cdd:PLN02831 341 LRAYNLQDEGRDTVEANEELGLPVDSREYGIGAQILRDLGVRTMRLMTNNPAKYTGLKGYGLAVVGRVPLLTPITKENKR 420

                        410       420       430
                 ....*....|....*....|....*....|
gi 145349380 456 YIDTKRMKMGHLFEMLEGVEPSQAESEQKP 485
Cdd:PLN02831 421 YLETKRTKMGHVYGSDLGGHVSGLESAETN 450
RibA COG0807
GTP cyclohydrolase II [Coenzyme transport and metabolism]; GTP cyclohydrolase II is part of ...
 65-469 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: 557.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380  65 FAAVADALEDVAKGKFVVVLDDEDRENEGDLIGAADKMTAESLAFMIRHTSGLVCVSLEDSRADALDLPLMVDSqsNKDA 144
Cdd:COG0807    3 LSSIEEIIEDIRAGKMVILVDDEDRENEGDLIMAAEFVTPEAINFMARHGRGLICLTLTEERCEQLLLPLMVNN--NGTP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 145 MKTAFTVSVDLAT-STTGISASERAMTINALGSDETTAAAFVRPGHVFPLRYRAGGVLKRAGHTEAAVDLARMAGSSPVG 223
Cdd:COG0807   81 FGTAFTVSIEAAEgVTTGISAADRARTIQAAVAPDAKPEDLVQPGHIFPLRAQPGGVLVRAGHTEAAVDLARLAGLEPAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 224 VLCEIVNDeDGSMARLPQLKVFAEKHGLKMVLISDMIRYRRAREKMVERTAVARLPTEYGNFTCVSYKNTLDGHEHVAFL 303
Cdd:COG0807  161 VICEIMNE-DGTMARLPDLEEFAKEHGLKIGTIADLIAYRLRNESLVERVAEARLPTEFGEFRLHAYRDTIDGQEHLALV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 304 YGEHEGDvsgavgEDMLVRVHSECLTGDIFKSARCDCGNQLDMAMRRIAGEGKGCIVYLRgQEGRGIGLGHKLRAYNLQD 383
Cdd:COG0807  240 KGDPDPD------EPVLVRVHSECLTGDVFGSLRCDCGWQLEAALKRIAEEGRGVLVYLR-QEGRGIGLLNKLRAYALQD 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 384 EGRDTVQANEDLGFPADTREYGVGAQILQDLGVTSLRLMTNNPAKYNGLSGYGLKVTGRVPLFAPVTMENKRYIDTKRMK 463
Cdd:COG0807  313 QGLDTVEANLALGFPADLRDYGIGAQILRDLGVRKMRLLTNNPRKVVGLEGYGLEVVERVPLEVGPNPHNERYLRTKRDK 392


                 ....*.
gi 145349380 464 MGHLFE 469
Cdd:COG0807  393 MGHLLD 398
DHBP_synthase pfam00926
3,4-dihydroxy-2-butanone 4-phosphate synthase; 3,4-Dihydroxy-2-butanone 4-phosphate is ...
 70-262 4.69e-112

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: 328.95  E-value: 4.69e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380   70 DALEDVAKGKFVVVLDDEDRENEGDLIGAADKMTAESLAFMIRHTSGLVCVSLEDSRADALDLPLMVdsQSNKDAMKTAF 149
Cdd:pfam00926   2 EAIEALRAGKPVIVVDDEDRENEGDLIIAAEFVTPEAINFMARHGSGLICVPLTEERADRLGLPPMV--ANNTDRHGTAF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380  150 TVSVDLATS-TTGISASERAMTINALGSDETTAAAFVRPGHVFPLRYRAGGVLKRAGHTEAAVDLARMAGSSPVGVLCEI 228
Cdd:pfam00926  80 TVSVDAREGtTTGISAADRALTIRALADPGAKPEDFRRPGHVFPLRAREGGVLERAGHTEAAVDLARLAGLKPAGVICEI 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 145349380  229 VNDeDGSMARLPQLKVFAEKHGLKMVLISDMIRY 262
Cdd:pfam00926 160 LND-DGTMARLPDLREFAKKHGLKIITIADLIAY 192
GTP_cyclohydro2 cd00641
GTP cyclohydrolase II (RibA). GTP cyclohydrolase II catalyzes the conversion of GTP to 2, ...
 269-468 7.40e-105

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: 310.59  E-value: 7.40e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 269 MVERTAVARLPTEYGNFTCVSYKNTLDGHEHVAFLYGEHEGDvsgavgEDMLVRVHSECLTGDIFKSARCDCGNQLDMAM 348
Cdd:cd00641    1 LVEKVAEAPLPTRFGDFRIVAFEDTDDGKEHVALVKGDPADG------EPVLVRVHSECLTGDVFGSLRCDCGPQLEEAL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 349 RRIAGEGKGCIVYLRgQEGRGIGLGHKLRAYNLQDEGRDTVQANEDLGFPADTREYGVGAQILQDLGVTSLRLMTNNPAK 428
Cdd:cd00641   75 EEIAEEGGGVLLYLR-QEGRGIGLANKLRAYALQDQGLDTVEANEALGFPADARDYGLAAQILRDLGIKSVRLLTNNPDK 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 145349380 429 YNGLSGYGLKVTGRVPLFAPVTMENKRYIDTKRMKMGHLF 468
Cdd:cd00641  154 IDALEGYGIEVVERVPLEVEPNEENKGYLKTKRDKMGHLL 193
ribB TIGR00506
3,4-dihydroxy-2-butanone 4-phosphate synthase; Several members of the family are bifunctional, ...
 65-263 4.53e-83

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: 255.38  E-value: 4.53e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380   65 FAAVADALEDVAKGKFVVVLDDEDRENEGDLIGAADKMTAESLAFMIRHTSGLVCVSLEDSRADALDLPLMVDsqSNKDA 144
Cdd:TIGR00506   2 FERVEEALEALKKGEIVLVYDDEDRENEGDLIVAAEFITPEQIAFMRRHAGGLICVAITPDIADKLDLPPMVD--INTSA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380  145 MKTAFTVSVDLA--TSTTGISASERAMTINALGSDETTAAAFVRPGHVFPLRYRAGGVLKRAGHTEAAVDLARMAGSSPV 222
Cdd:TIGR00506  80 SGTASTFTITVAhrKTFTGISANDRALTIRAALADVVKPSDFRRPGHVFPLRAADGGVLTRGGHTEASVDLAELAGLKPA 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 145349380  223 GVLCEIVNDeDGSMARLPQLKVFAEKHGLKMVLISDMIRYR 263
Cdd:TIGR00506 160 GVICEMMND-DGTMARKPELMEYAKKHNLKLISIEDLIEYR 199
 
Name Accession Description Interval E-value
PLN02831 PLN02831
Bifunctional GTP cyclohydrolase II/ 3,4-dihydroxy-2-butanone-4-phosphate synthase
 57-485 0e+00

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


Pssm-ID: 215445 [Multi-domain]  Cd Length: 450  Bit Score: 772.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380  57 DPDAPTAGFAAVADALEDVAKGKFVVVLDDEDRENEGDLIGAADKMTAESLAFMIRHTSGLVCVSLEDSRADALDLPLMV 136
Cdd:PLN02831  27 DPDRPTEGFSSIAEALEDIRQGKFVVVVDDEDRENEGDLIMAASLVTPEAMAFLVKHGSGIVCVSMKGEDLDRLRLPLMV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 137 DSQSNKDAMKTAFTVSVDLAT-STTGISASERAMTINALGSDETTAAAFVRPGHVFPLRYRAGGVLKRAGHTEAAVDLAR 215
Cdd:PLN02831 107 PSKENEEKMATAFTVTVDAKHgTTTGVSASDRAKTILALASPDSKPEDFRRPGHIFPLRYREGGVLKRAGHTEAAVDLAV 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 216 MAGSSPVGVLCEIVNDEDGSMARLPQLKVFAEKHGLKMVLISDMIRYRRAREKMVERTAVARLPTEYGNFTCVSYKNTLD 295
Cdd:PLN02831 187 LAGLPPVGVLCEIVNDEDGSMARLPQLRKFAEEHGLKIISIADLIRYRRKREKLVERTAVARLPTKWGLFTAYCYRSKLD 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 296 GHEHVAFLYGEHeGDvsgavGEDMLVRVHSECLTGDIFKSARCDCGNQLDMAMRRIAGEGKGCIVYLRGQEGRGIGLGHK 375
Cdd:PLN02831 267 GIEHIAFVKGDI-GD-----GQDVLVRVHSECLTGDIFGSARCDCGNQLALAMQLIEKAGRGVLVYLRGHEGRGIGLGHK 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 376 LRAYNLQDEGRDTVQANEDLGFPADTREYGVGAQILQDLGVTSLRLMTNNPAKYNGLSGYGLKVTGRVPLFAPVTMENKR 455
Cdd:PLN02831 341 LRAYNLQDEGRDTVEANEELGLPVDSREYGIGAQILRDLGVRTMRLMTNNPAKYTGLKGYGLAVVGRVPLLTPITKENKR 420

                        410       420       430
                 ....*....|....*....|....*....|
gi 145349380 456 YIDTKRMKMGHLFEMLEGVEPSQAESEQKP 485
Cdd:PLN02831 421 YLETKRTKMGHVYGSDLGGHVSGLESAETN 450
PRK09311 PRK09311
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
62-471 0e+00

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


Pssm-ID: 181774 [Multi-domain]  Cd Length: 402  Bit Score: 650.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380  62 TAGFAAVADALEDVAKGKFVVVLDDEDRENEGDLIGAADKMTAESLAFMIRHTSGLVCVSLEDSRADALDLPLMVDSqsN 141
Cdd:PRK09311   1 MTMFDSIEEAIADIAAGKAVIVVDDEDRENEGDLIFAAEKATPELVAFMVRHTSGYVCVPLTEEDADRLDLPPMVAH--N 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 142 KDAMKTAFTVSVDLATS-TTGISASERAMTINALGSDETTAAAFVRPGHVFPLRYRAGGVLKRAGHTEAAVDLARMAGSS 220
Cdd:PRK09311  79 QDSHGTAFTVSVDAANGvTTGISAADRATTIRLLADPASKPADFTRPGHVFPLRAKPGGVLRRAGHTEAAVDLARLAGLQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 221 PVGVLCEIVNDeDGSMARLPQLKVFAEKHGLKMVLISDMIRYRRAREKMVERTAVARLPTEYGNFTCVSYKNTLDGHEHV 300
Cdd:PRK09311 159 PAGVICEIVNE-DGTMARVPELRVFADEHDLALITIADLIAYRRRHEKLVEREVEARLPTRFGEFRAIGYTSILDGKEHV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 301 AFLYGehegDVSGavGEDMLVRVHSECLTGDIFKSARCDCGNQLDMAMRRIAGEGKGCIVYLRGQEGRGIGLGHKLRAYN 380
Cdd:PRK09311 238 ALVKG----DIGD--GEDVLVRVHSECLTGDVFGSRRCDCGPQLDAALAQIAEEGRGVVLYMRGQEGRGIGLLHKLRAYQ 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 381 LQDEGRDTVQANEDLGFPADTREYGVGAQILQDLGVTSLRLMTNNPAKYNGLSGYGLKVTGRVPLFAPVTMENKRYIDTK 460
Cdd:PRK09311 312 LQDEGYDTVDANLKLGFPADARDYGIGAQILVDLGVRSMRLLTNNPRKIAGLQGYGLHVTERVPLPVRANEENERYLRTK 391

                        410
                 ....*....|.
gi 145349380 461 RMKMGHLFEML 471
Cdd:PRK09311 392 RDRMGHDLDLL 402
RibA COG0807
GTP cyclohydrolase II [Coenzyme transport and metabolism]; GTP cyclohydrolase II is part of ...
 65-469 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: 557.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380  65 FAAVADALEDVAKGKFVVVLDDEDRENEGDLIGAADKMTAESLAFMIRHTSGLVCVSLEDSRADALDLPLMVDSqsNKDA 144
Cdd:COG0807    3 LSSIEEIIEDIRAGKMVILVDDEDRENEGDLIMAAEFVTPEAINFMARHGRGLICLTLTEERCEQLLLPLMVNN--NGTP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 145 MKTAFTVSVDLAT-STTGISASERAMTINALGSDETTAAAFVRPGHVFPLRYRAGGVLKRAGHTEAAVDLARMAGSSPVG 223
Cdd:COG0807   81 FGTAFTVSIEAAEgVTTGISAADRARTIQAAVAPDAKPEDLVQPGHIFPLRAQPGGVLVRAGHTEAAVDLARLAGLEPAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 224 VLCEIVNDeDGSMARLPQLKVFAEKHGLKMVLISDMIRYRRAREKMVERTAVARLPTEYGNFTCVSYKNTLDGHEHVAFL 303
Cdd:COG0807  161 VICEIMNE-DGTMARLPDLEEFAKEHGLKIGTIADLIAYRLRNESLVERVAEARLPTEFGEFRLHAYRDTIDGQEHLALV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 304 YGEHEGDvsgavgEDMLVRVHSECLTGDIFKSARCDCGNQLDMAMRRIAGEGKGCIVYLRgQEGRGIGLGHKLRAYNLQD 383
Cdd:COG0807  240 KGDPDPD------EPVLVRVHSECLTGDVFGSLRCDCGWQLEAALKRIAEEGRGVLVYLR-QEGRGIGLLNKLRAYALQD 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 384 EGRDTVQANEDLGFPADTREYGVGAQILQDLGVTSLRLMTNNPAKYNGLSGYGLKVTGRVPLFAPVTMENKRYIDTKRMK 463
Cdd:COG0807  313 QGLDTVEANLALGFPADLRDYGIGAQILRDLGVRKMRLLTNNPRKVVGLEGYGLEVVERVPLEVGPNPHNERYLRTKRDK 392


                 ....*.
gi 145349380 464 MGHLFE 469
Cdd:COG0807  393 MGHLLD 398
PRK09319 PRK09319
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase RibB/GTP cyclohydrolase II RibA;
65-469 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: 553.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380  65 FAAVADALEDVAKGKFVVVLDDEDRENEGDLIGAADKMTAESLAFMIRHTSGLVCVSLEDSRADALDLPLMVDSqsNKDA 144
Cdd:PRK09319   5 FDSIDDALAAIRNGECVVVVDDENRENEGDLICAAQFATPEMINFMATEARGLICLAMTGERLDELDLPLMVDR--NTDS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 145 MKTAFTVSVDLATS---TTGISASERAMTINALGSDETTAAAFVRPGHVFPLRYRAGGVLKRAGHTEAAVDLARMAGSSP 221
Cdd:PRK09319  83 NQTAFTVSIDAGPElgvSTGISAEDRARTIQVAINPDTKPEDLRRPGHIFPLRAKEGGVLKRAGHTEAAVDLARLAGLYP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 222 VGVLCEIVNdEDGSMARLPQLKVFAEKHGLKMVLISDMIRYRRAREKMVERTAVARLPTEYGNFTCVSYKNTLDGHEHVA 301
Cdd:PRK09319 163 AGVICEIQN-PDGSMARLPELKEYAKQHGLKLISIADLISYRLQNERFVYREAVAKLPSQFGQFQAYGYRNELDGSEHVA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 302 FLygehEGDVSGAVGEDMLVRVHSECLTGDIFKSARCDCGNQLDMAMRRIAGEGKGCIVYLRgQEGRGIGLGHKLRAYNL 381
Cdd:PRK09319 242 LV----KGDPANFKDEPVLVRMHSECLTGDAFGSLRCDCRMQLEAALKMIENEGEGVVVYLR-QEGRGIGLINKLKAYSL 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 382 QDEGRDTVQANEDLGFPADTREYGVGAQILQDLGVTSLRLMTNNPAKYNGLSGYGLKVTGRVPLFAPVTMENKRYIDTKR 461
Cdd:PRK09319 317 QDGGLDTVEANERLGFPADLRNYGVGAQILNDLGIKRLRLITNNPRKIAGLGGYGLEVVDRVPLLIEANDYNAEYLATKA 396


                 ....*...
gi 145349380 462 MKMGHLFE 469
Cdd:PRK09319 397 EKLGHLLL 404
PRK14019 PRK14019
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
66-444 5.84e-116

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


Pssm-ID: 237587 [Multi-domain]  Cd Length: 367  Bit Score: 345.80  E-value: 5.84e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380  66 AAVADALEDVAKGKFVVVLDDEDRENEGDLIGAADKMTAESLAFMIRHTSGLVCVSLEDSRADALDLPLMVdsQSNKDAM 145
Cdd:PRK14019   4 ASIEEIIADIRAGRMVILVDEEDRENEGDLVMAAEFVTPEAINFMAKHGRGLICLTLTEERCEQLGLPLMT--YRNGTQY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 146 KTAFTVSVDLATS-TTGISASERAMTINALGSDETTAAAFVRPGHVFPLRYRAGGVLKRAGHTEAAVDLARMAGSSPVGV 224
Cdd:PRK14019  82 GTNFTVSIEAAEGvTTGISAADRARTIQAAVARDAKPEDIVQPGHIFPLMAQPGGVLVRAGHTEAGCDLAALAGLTPAAV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 225 LCEIVNDeDGSMARLPQLKVFAEKHGLKMVLISDMIRYRRAREKMVERTAVARLPTEYGNFTCVSYKNTLDGHEHVAFLY 304
Cdd:PRK14019 162 ICEIMKD-DGTMARLPDLEEFAKEHGLKIGTIADLIHYRSRTESIVERVAERPMQTAHGEFRLVAYRDKPSGSTHLALVK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 305 GEHEGDvsgavgEDMLVRVHSECLTGDIFKSARCDCGNQLDMAMRRIAGEGKGCIVYlrgqegrgigLGHKLRAYNLQDE 384
Cdd:PRK14019 241 GTICPD------EETLVRVHEPLSVLDLLEVGQPTHSWSLDAAMAAIAEAGSGVVVL----------LNCGDDGEHLLDR 304

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 385 GRDTVQANEDLGFPADTREYGVGAQILQDLGVTSLRLMTnNPAKYNGLSGYGLKVTGRVP 444
Cdd:PRK14019 305 FRAEEAAAALKRRPVDYRTYGIGAQILRDLGVGKMRLLS-SPRKFPSMSGFGLEVTGYVP 363
RibB COG0108
3,4-dihydroxy-2-butanone 4-phosphate synthase [Coenzyme transport and metabolism]; 3, ...
 65-265 4.70e-114

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: 334.30  E-value: 4.70e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380  65 FAAVADALEDVAKGKFVVVLDDEDRENEGDLIGAADKMTAESLAFMIRHTSGLVCVSLEDSRADALDLPLMVDSqsNKDA 144
Cdd:COG0108    3 LSSIEEAIEALRAGKMVIVVDDEDRENEGDLIIAAEFVTPEAINFMARHGRGLICLPLTEERADRLGLPPMVDR--NTDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 145 MKTAFTVSVDLATS-TTGISASERAMTINALGSDETTAAAFVRPGHVFPLRYRAGGVLKRAGHTEAAVDLARMAGSSPVG 223
Cdd:COG0108   81 YGTAFTVSVDAREGvTTGISAADRALTIRALADPDAKPEDFVRPGHVFPLRARPGGVLERAGHTEAAVDLARLAGLKPAG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 145349380 224 VLCEIVNDeDGSMARLPQLKVFAEKHGLKMVLISDMIRYRRA 265
Cdd:COG0108  161 VICEIMND-DGTMARLPDLEEFAKKHGLKIITIADLIAYRRR 201
DHBP_synthase pfam00926
3,4-dihydroxy-2-butanone 4-phosphate synthase; 3,4-Dihydroxy-2-butanone 4-phosphate is ...
 70-262 4.69e-112

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: 328.95  E-value: 4.69e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380   70 DALEDVAKGKFVVVLDDEDRENEGDLIGAADKMTAESLAFMIRHTSGLVCVSLEDSRADALDLPLMVdsQSNKDAMKTAF 149
Cdd:pfam00926   2 EAIEALRAGKPVIVVDDEDRENEGDLIIAAEFVTPEAINFMARHGSGLICVPLTEERADRLGLPPMV--ANNTDRHGTAF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380  150 TVSVDLATS-TTGISASERAMTINALGSDETTAAAFVRPGHVFPLRYRAGGVLKRAGHTEAAVDLARMAGSSPVGVLCEI 228
Cdd:pfam00926  80 TVSVDAREGtTTGISAADRALTIRALADPGAKPEDFRRPGHVFPLRAREGGVLERAGHTEAAVDLARLAGLKPAGVICEI 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 145349380  229 VNDeDGSMARLPQLKVFAEKHGLKMVLISDMIRY 262
Cdd:pfam00926 160 LND-DGTMARLPDLREFAKKHGLKIITIADLIAY 192
PRK09318 PRK09318
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
82-475 2.03e-110

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


Pssm-ID: 236464 [Multi-domain]  Cd Length: 387  Bit Score: 332.08  E-value: 2.03e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380  82 VVLDDEDRENEGDLIGAADKMTAESLAFMIRHTSGLVCVSLEDSraDALD-----LPlmvdsqSNKDamKTAFTVSVDLA 156
Cdd:PRK09318  14 VILIDRNRENEADFVYPAQIITEEVVNFFLSYGKGLLCLTADEE--DLLKrgffkLP------SNGG--ETNFFIPVDYG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 157 TsTTGISASERAMTINALgSDETTAAAFVRPGHVFPLRyrAGGVLKRAGHTEAAVDLARMAGSSPVGVLCEIVNDEDGSM 236
Cdd:PRK09318  84 T-GTGISASERALTCRKL-AEGLYVHEFRYPGHVTLLG--GIGFNRRRGHTEASLELSELLGFKRYAVIVEILDEKGDSH 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 237 ARLPQLKvFAEKHGLKMVLISDMIRYRRAREKMVERTAVARLPTEYGNFTCVSYKNTLDGHEHVAFlygehegdVSGAVG 316
Cdd:PRK09318 160 DLDYVLK-LAEKFSLPVLEIDDVWKEFVRRKQLIKVKAEAKLPTDYGEFEIVSFENHLDGKEHVAI--------VKEPLG 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 317 EDMLVRVHSECLTGDIFKSARCDCGNQLDMAMRRIAGEGkGCIVYLRgQEGRGIGLGHKLRAYNLQDEGRDTVQANEDLG 396
Cdd:PRK09318 231 EVPLVRIHSECVTGDTLSSLRCDCGSQLANFLRMISKEG-GILIYLR-QEGRGIGLSNKIKAYELQDKGLDTVEANRALG 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145349380 397 FPADTREYGVGAQILQDLGVTSLRLMTNNPAKYNGLSGYGLKVTGRVPLFAPVTMENKRYIDTKRMKMGHLFEmLEGVE 475
Cdd:PRK09318 309 FKEDERDYAAAFQILKALGIEKVRLLTNNPRKTKALEKYGIEVVETVPLYGEVTKYNRFYLKTKVEKLGHKLE-LREVN 386
GTP_cyclohydro2 cd00641
GTP cyclohydrolase II (RibA). GTP cyclohydrolase II catalyzes the conversion of GTP to 2, ...
 269-468 7.40e-105

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: 310.59  E-value: 7.40e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 269 MVERTAVARLPTEYGNFTCVSYKNTLDGHEHVAFLYGEHEGDvsgavgEDMLVRVHSECLTGDIFKSARCDCGNQLDMAM 348
Cdd:cd00641    1 LVEKVAEAPLPTRFGDFRIVAFEDTDDGKEHVALVKGDPADG------EPVLVRVHSECLTGDVFGSLRCDCGPQLEEAL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 349 RRIAGEGKGCIVYLRgQEGRGIGLGHKLRAYNLQDEGRDTVQANEDLGFPADTREYGVGAQILQDLGVTSLRLMTNNPAK 428
Cdd:cd00641   75 EEIAEEGGGVLLYLR-QEGRGIGLANKLRAYALQDQGLDTVEANEALGFPADARDYGLAAQILRDLGIKSVRLLTNNPDK 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 145349380 429 YNGLSGYGLKVTGRVPLFAPVTMENKRYIDTKRMKMGHLF 468
Cdd:cd00641  154 IDALEGYGIEVVERVPLEVEPNEENKGYLKTKRDKMGHLL 193
PRK09314 PRK09314
bifunctional 3,4-dihydroxy-2-butanone 4-phosphate synthase/GTP cyclohydrolase II;
68-441 1.12e-99

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


Pssm-ID: 181775 [Multi-domain]  Cd Length: 339  Bit Score: 303.05  E-value: 1.12e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380  68 VADALEDVAKGKFVVVLDDEDRENEGDLIGAADKMTAESLAFMIRHTSGLVCVSLEDSRADALDLPLMVDSqsNKDAMKT 147
Cdd:PRK09314   6 VEEAIEDIKNGKMLIMVDDEDRENEGDLVYAAIFSTPEKVNFMATHARGLICVSLTKELAKKLELPPMVSK--NTSNHET 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 148 AFTVSVDLATSTTGISASERAMTINALGSDETTAAAFVRPGHVFPLRYRAGGVLKRAGHTEAAVDLARMAGSSPVGVLCE 227
Cdd:PRK09314  84 AFTVSIDAKEATTGISAFERDMTIKLLADDTSKPSDFVRPGHIFPLIAKDGGVLVRTGHTEGSVDLCKLAGLKPVAVICE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 228 IVNdEDGSMARLPQLKVFAEKHGLKMVLISDMIRYRRAREKMVERtaVARLPTEYGNFTCVSY--KNTLdGHEHVAFLYG 305
Cdd:PRK09314 164 IMK-EDGTMARRDDLEDFAKKHNLKMIYVSDLVEYRLKNESLIKE--EEKEESEFAGFKAEKYtfLDHL-QNEHIAFKFG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 306 EHEgdvsgavgEDMLVRVHS-----ECLTGDIFKSarcdcgnqLDMAMRRIAGEGkGCIVYLRGqegrgiglghklrayn 380
Cdd:PRK09314 240 EIK--------LTPNVKFHKigsdfELLTSDKFSE--------LLKAIEYLKKNG-GVLIFLNT---------------- 286

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145349380 381 lqdegrDTVQANEdlgfpadTREYGVGAQILQDLGVTSLRLMTNNPAK-YNGLSGYGLKVTG 441
Cdd:PRK09314 287 ------ESKENNQ-------VKDYGIGAQILKYLGIKDIKLLSSSEDKeYVGLSGFGLNIVE 335
PRK12485 PRK12485
bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II;
65-445 5.37e-98

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


Pssm-ID: 171535 [Multi-domain]  Cd Length: 369  Bit Score: 299.96  E-value: 5.37e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380  65 FAAVADALEDVAKGKFVVVLDDEDRENEGDLIGAADKMTAESLAFMIRHTSGLVCVSLEDSRADALDLPLMVdsQSNKDA 144
Cdd:PRK12485   3 FNTIEEIIEDYRQGKMVLLVDDEDRENEGDLLLAAERCDAQAINFMAREARGLICLTLTDEHCQRLGLEQMV--PSNGSV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 145 MKTAFTVSVDLATS-TTGISASERAMTINALGSDETTAAAFVRPGHVFPLRYRAGGVLKRAGHTEAAVDLARMAGSSPVG 223
Cdd:PRK12485  81 FSTAFTVSIEAATGvTTGISAADRARTVAAAVAPNARPEDLVQPGHIFPLRAREGGVLTRAGHTEAGCDLARLAGFSPAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 224 VLCEIVNDeDGSMARLPQLKVFAEKHGLKMVLISDMIRYRRAREKMVERTAVARLPTEYGNFTCVSYKNTLDGHEHVAFL 303
Cdd:PRK12485 161 VIVEVMND-DGTMARRPDLEVFAAKHGIKIGTIADLIHYRLSTEHTIKRIGERELPTVHGTFRLVTYEDRIEGGVHMAMV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 304 YGEHEGDvsgavgEDMLVRVHSECLTGDIFKSARCDCGN-QLDMAMRRIAGEGKGCIVYLRGQEG------RGIGLGHKL 376
Cdd:PRK12485 240 MGDIRRE------QPTLVRVHVIDPLRDLVGAEYAGPANwTLWAALQKVAEEGHGVVVVLANHESsqalleRIPQLTQPP 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145349380 377 RAYNlqdEGRDTVQAnedlgfpadtrEYGVGAQILQDLGVTSLRLMtNNPAKYNGLSGYGLKVTGRVPL 445
Cdd:PRK12485 314 RQYQ---RSQSRIYS-----------EVGTGAQILQDLGVGKLRHL-GPPLKYAGLTGYDLEVVESIPF 367
ribA PRK00393
GTP cyclohydrolase II RibA;
269-469 1.54e-96

GTP cyclohydrolase II RibA;


Pssm-ID: 234745  Cd Length: 197  Bit Score: 289.43  E-value: 1.54e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 269 MVERTAVARLPTEYGNFTCVSYKNTLDGHEHVAFLYGEHEGdvsgavGEDMLVRVHSECLTGDIFKSARCDCGNQLDMAM 348
Cdd:PRK00393   2 QLKRVAEAKLPTPWGDFLMVGFEELATGKEHVALVFGDISG------TEPVLVRVHSECLTGDALFSLRCDCGFQLEAAL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 349 RRIAGEGKGCIVYLRgQEGRGIGLGHKLRAYNLQDEGRDTVQANEDLGFPADTREYGVGAQILQDLGVTSLRLMTNNPAK 428
Cdd:PRK00393  76 ERIAEEGRGILLYLR-QEGRGIGLLNKIRAYALQDQGLDTVEANHQLGFAADERDYTLAADMLKALGVKKVRLLTNNPKK 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 145349380 429 YNGLSGYGLKVTGRVPLFAPVTMENKRYIDTKRMKMGHLFE 469
Cdd:PRK00393 155 VEALTEAGINIVERVPLIVGRNPHNEHYLKTKAEKMGHLLS 195
ribB TIGR00506
3,4-dihydroxy-2-butanone 4-phosphate synthase; Several members of the family are bifunctional, ...
 65-263 4.53e-83

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: 255.38  E-value: 4.53e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380   65 FAAVADALEDVAKGKFVVVLDDEDRENEGDLIGAADKMTAESLAFMIRHTSGLVCVSLEDSRADALDLPLMVDsqSNKDA 144
Cdd:TIGR00506   2 FERVEEALEALKKGEIVLVYDDEDRENEGDLIVAAEFITPEQIAFMRRHAGGLICVAITPDIADKLDLPPMVD--INTSA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380  145 MKTAFTVSVDLA--TSTTGISASERAMTINALGSDETTAAAFVRPGHVFPLRYRAGGVLKRAGHTEAAVDLARMAGSSPV 222
Cdd:TIGR00506  80 SGTASTFTITVAhrKTFTGISANDRALTIRAALADVVKPSDFRRPGHVFPLRAADGGVLTRGGHTEASVDLAELAGLKPA 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 145349380  223 GVLCEIVNDeDGSMARLPQLKVFAEKHGLKMVLISDMIRYR 263
Cdd:TIGR00506 160 GVICEMMND-DGTMARKPELMEYAKKHNLKLISIEDLIEYR 199
ribA TIGR00505
GTP cyclohydrolase II; Several members of the family are bifunctional, involving both ribA and ...
 271-467 4.50e-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: 249.70  E-value: 4.50e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380  271 ERTAVARLPTEYGNFTCVSYKNTLDGHEHVAFLYGEHEGDvsgavgEDMLVRVHSECLTGDIFKSARCDCGNQLDMAMRR 350
Cdd:TIGR00505   1 ERVAEAKLPTPYGDFYMVGFEEPATGKDHVALVKGDISAH------TDVLVRIHSECLTGDALHSLRCDCGFQLEAALKQ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380  351 IAGEGKGCIVYLRgQEGRGIGLGHKLRAYNLQDEGRDTVQANEDLGFPADTREYGVGAQILQDLGVTSLRLMTNNPAKYN 430
Cdd:TIGR00505  75 IAEEGRGVLIYLR-QEGRGIGLINKLRAYALQDKGYDTVQANLMLGFPADERDFSLCADILEDLGVKKVRLLTNNPKKIE 153

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 145349380  431 GLSGYGLKVTGRVPLFAPVTMENKRYIDTKRMKMGHL 467
Cdd:TIGR00505 154 ILKKAGINIVERVPLIVGRNENNEGYLDTKAEKMGHL 190
GTP_cyclohydro2 pfam00925
GTP cyclohydrolase II; GTP cyclohydrolase II catalyzes the first committed step in the ...
 321-444 1.49e-76

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: 235.43  E-value: 1.49e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380  321 VRVHSECLTGDIFKSARCDCGNQLDMAMRRIAGEGKGCIVYLRgQEGRGIGLGHKLRAYNLQDEGRDTVQANEDLGFPAD 400
Cdd:pfam00925   1 VRVHSECLTGDVLGSLRCDCGEQLEAALRAIAEEGRGVLVYLR-QEGRGIGLLNKLRAYALQDQGLDTVEANLALGFPAD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 145349380  401 TREYGVGAQILQDLGVTSLRLMTNNPAKYNGLSGYGLKVTGRVP 444
Cdd:pfam00925  80 LRDYGIGAQILRDLGVKKIRLLTNNPRKIVGLEGYGLEVVERVP 123
PRK08815 PRK08815
GTP cyclohydrolase II RibA;
209-470 7.05e-48

GTP cyclohydrolase II RibA;


Pssm-ID: 236340 [Multi-domain]  Cd Length: 375  Bit Score: 169.16  E-value: 7.05e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 209 AAVDLARMAGSSPVGVLCEIVNDEDGSMArlpqlkvfaekhGLKMVLISDMIRYRRARE----KMVERTAV---ARLPTE 281
Cdd:PRK08815 123 GAVEIARLALLLPAMVAVPLPVHDEAAFA------------GCQALALADLDAGCATSAaagyELVTRTPVplrGLGMTE 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 282 YgnftcVSYKNTLDGHEHVAFLYGEheGDVSGAVGedmlVRVHSECLTGDIFKSARCDCGNQLDMAMRRIAGEGKGCIVY 361
Cdd:PRK08815 191 F-----VVFRGGVAQRDQVAIVVGQ--PDLSSAVP----VRVHSSCLTGDLFGSLKCDCGDQLRHGLAKLKELGGGVLLY 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 362 LrGQEGRGIGLGHKLRAYNLQDEGRDTVQANEDLGFPADTREYGVGAQILQDLGVTSLRLMTNNPAKYNGLSGYGLKVTG 441
Cdd:PRK08815 260 L-DQEGRGNGIAAKMRAYGYQHAGLDTIDADAQLGFGPDERRYGSAVAMLRGLGITRVRLLTNNPTKAERLRAAGIEVED 338

                        250       260
                 ....*....|....*....|....*....
gi 145349380 442 RVPLFAPVTMENKRYIDTKRMKMGHLFEM 470
Cdd:PRK08815 339 RIRVTGRITAENERYLRTKADRAGHALDV 367
PRK05773 PRK05773
3,4-dihydroxy-2-butanone 4-phosphate synthase; Validated
 68-254 6.35e-17

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


Pssm-ID: 235601  Cd Length: 219  Bit Score: 79.72  E-value: 6.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380  68 VADALEDVAKGKFVVVLDDEDRENEGDLIGAADKMTAESLAFMIRHTSGLVCVSLEDSRADALDLPLMVD----SQSNKD 143
Cdd:PRK05773   3 FEEARKALESGIPVLIYDFDGREEEVDMVFYAGAVTWKSIYTLRKNAGGLICYATSNSEGKTLGLNFLAEilkrHELYRK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 144 AMKT-------AFTVSVDLATSTTGISASERAMTINALG-------SDETTA-----AAFVRPGHVFPLRYRagGVLKRA 204
Cdd:PRK05773  83 LVKKpsygdepAFSLWVNHVKTKTGISDYDRALTIRELHkvvelakTNPEEAreefyENFYSPGHVPILIGR--GIRERR 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 145349380 205 GHTEAAVDLARMAGSSPVGVLCEIVnDEDGSMaRLPQLKVFAEKHGLKMV 254
Cdd:PRK05773 161 GHTELSIALAQAAGLEPSAVIAEML-DEKLSL-SKEKAKKIAKNLGFPLV 208
PRK07198 PRK07198
GTP cyclohydrolase II;
321-445 6.46e-06

GTP cyclohydrolase II;


Pssm-ID: 235959 [Multi-domain]  Cd Length: 418  Bit Score: 48.50  E-value: 6.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145349380 321 VRVHSECLTGDIFKSARCDCGNQL----DMAMRRIAGEGKGCIVYLRgQEGRGIGLGHKLRAYNL--QDEGRDTVQA--- 391
Cdd:PRK07198 242 CRVHDECNGSDVFGSDICTCRPYLthgiEECIRGAQRGGVGLIVYNR-KEGRALGEVTKFLVYNArkRQVGGDTAATyfa 320

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 145349380 392 -NEDLGFPADTREYGVGAQILQDLGVTSL-RLMTNNPAKYNGLSGYGLKVTGRVPL 445
Cdd:PRK07198 321 rTECVAGVQDMRFQELMPDVLHWLGIRRIhRLVSMSNMKYDAITGSGIEVGERVPI 376
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH