view test-data/cd00003.smp @ 21:7538e2bfcd41 draft

v0.2.00, for NCBI BLAST+ 2.5.0 via bioconda or tool_dependencies.xml
author peterjc
date Wed, 19 Apr 2017 05:27:19 -0400
parents 2fe07f50a41e
children
line wrap: on
line source

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 {
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