annotate test-data/cd00003.smp @ 18:577d9c12411a draft

v0.1.06, now using BLAST+ 2.2.31

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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