Mercurial > repos > devteam > ncbi_blast_plus
view test-data/cd00003.smp @ 24:c877294f8025 draft
Fixed tool_dependencies.xml
| author | peterjc |
|---|---|
| date | Mon, 09 Jul 2018 10:08:16 -0400 |
| parents | 2fe07f50a41e |
| children |
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PssmWithParameters ::= { pssm { isProtein TRUE, numRows 28, numColumns 234, byRow FALSE, query seq { id { general { db "CDD", tag id 237977 } }, descr { title "cd00003, PNPsynthase, Pyridoxine 5'-phosphate (PNP) synthase domain; pyridoxal 5'-phosphate is the active form of vitamin B6 that acts as an essential, ubiquitous coenzyme in amino acid metabolism. In bacteria, formation of pyridoxine 5'-phosphate is a step in the biosynthesis of vitamin B6. PNP synthase, a homooctameric enzyme, catalyzes the final step in PNP biosynthesis, the condensation of 1-amino-acetone 3-phosphate and 1-deoxy-D-xylulose 5-phosphate. PNP synthase adopts a TIM barrel topology, intersubunit contacts are mediated by three ''extra'' helices, generating a tetramer of symmetric dimers with shared active sites; the open state has been proposed to accept substrates and to release products, while most of the catalytic events are likely to occur in the closed state; a hydrophilic channel running through the center of the barrel was identified as the essential structural feature that enables PNP synthase to release water molecules produced during the reaction from the closed, solvent-shielded active site." }, inst { repr raw, mol aa, length 234, seq-data ncbieaa "RLGVNIDHVATLRNARGTNYPDPVEAALLAEKAGADGITVHLREDRRHIQDR DVRLLRELVRTELNLEMAPTEEMLEIALEVKPHQVTLVPEKREELTTEGGLDVAGQAEKLKPIIERLKDAGIRVSLFI DPDPEQIEAAKEVGADRVELHTGPYANAYDKAEREAELERIAKAAKLARELGLGVNAGHGLNYENVKPIAKIPGIAEL NIGHAIISRALFVGLEEAVREMKDLI" } }, intermediateData { weightedResFreqsPerPos { { 0, 10, 0 }, { 575880368388257, 10, -16 }, { 0, 10, 0 }, { 0, 10, 0 }, { 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