Align Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; EC 1.8.1.4 (characterized)
to candidate 203771 SO4702 glutathione reductase (NCBI ptt file)
Query= SwissProt::P85207 (461 letters) >FitnessBrowser__MR1:203771 Length = 451 Score = 201 bits (512), Expect = 3e-56 Identities = 152/452 (33%), Positives = 228/452 (50%), Gaps = 24/452 (5%) Query: 4 YDLIVIGTGPGGYPAAIRGAQLGLKVLAVEAAEVGGVCLNVGCIPTKAL---LHAAETVH 60 +D I +G G GG +A R A G KVL +EA VGG C+NVGC+P K + H AE ++ Sbjct: 5 FDYICLGAGSGGIASANRAAMRGAKVLLIEAKHVGGTCVNVGCVPKKVMWYGAHIAEAMN 64 Query: 61 HLKGAEGFGLKAKPELDLKKLGAWRDGVVKKLTGGVAGLLKGNKVELLRGFARFKGPREI 120 GF + + D L R+ + ++ NKV LL G+ RF I Sbjct: 65 LYAKDYGFDVSVN-KFDWNTLVNSREAYIGRIHEAYGRGFTNNKVTLLNGYGRFVNGNTI 123 Query: 121 EVNGETYGAQSFIIATGSEPM--PLKGFPFGEDVWDSTRALRVEEGIPKRLLVIGGGAVG 178 EVNGE Y A +IATG P + G +G D D ALR + PKR+ V+G G + Sbjct: 124 EVNGEHYTADHILIATGGAPTIPNIPGAEYGIDS-DGFFALREQ---PKRVAVVGAGYIA 179 Query: 179 LELGQIYHRLGSEVTLIEYMPEILPAGDRETAALLRKALEKEGLKVRTGTKAVGYEKK-Q 237 +E+ + H LGSE L L D L A++ EG + T + K Sbjct: 180 VEVAGVLHALGSETHLFVRKHAPLRNFDPMLIDALVDAMKTEGPTLHTNSVPQSVVKNAD 239 Query: 238 DGLHVLLEAAQGGSQEEIVVDKILVAVGRRPRTEGLGLEKAGVKVDERGFIQVNARMETS 297 D L + LE + E + VD ++ A+GR P T +GLE V++D +G++ +A+ T+ Sbjct: 240 DSLTLNLE-----NGESVTVDCLIWAIGRSPATGNIGLENTEVQLDSKGYVITDAQQNTT 294 Query: 298 APGVYAIGDV-ARPPLLAHKAMKEGLVAAENA--AGKNALFDF-QVPSVVYTGPEWAGVG 353 G+Y +GD+ A L A+K G + +E A +A D+ Q+P+VV++ P +G Sbjct: 295 HKGIYCVGDIMAGGVELTPVAVKAGRLLSERLFNAMSDAKMDYSQIPTVVFSHPPIGTMG 354 Query: 354 LTEEEARKAGY---NVKVGKFPFSASGRALTLGGAEGLIKVVGDAETDLLLGVFVVGPQA 410 LTE EAR A Y NVKV F++ A+T +K+V + D ++G+ +G Sbjct: 355 LTEPEAR-AQYGDGNVKVYTSSFTSMYTAVTSHRQACKMKLVCAGKEDKVVGIHGIGFGM 413 Query: 411 GELIAEATLALEMGATVSDLGLTIHPHPTLSE 442 E++ +A++MGAT +D + HPT +E Sbjct: 414 DEILQGFGVAMKMGATKADFDAVVAIHPTGAE 445 Lambda K H 0.316 0.138 0.395 Gapped Lambda K H 0.267 0.0410 0.140 Matrix: BLOSUM62 Gap Penalties: Existence: 11, Extension: 1 Number of Sequences: 1 Number of Hits to DB: 548 Number of extensions: 37 Number of successful extensions: 6 Number of sequences better than 1.0e-02: 1 Number of HSP's gapped: 1 Number of HSP's successfully gapped: 1 Length of query: 461 Length of database: 451 Length adjustment: 33 Effective length of query: 428 Effective length of database: 418 Effective search space: 178904 Effective search space used: 178904 Neighboring words threshold: 11 Window for multiple hits: 40 X1: 16 ( 7.3 bits) X2: 38 (14.6 bits) X3: 64 (24.7 bits) S1: 41 (21.6 bits) S2: 51 (24.3 bits)
This GapMind analysis is from Sep 17 2021. The underlying query database was built on Sep 17 2021.
Each pathway is defined by a set of rules based on individual steps or genes. Candidates for each step are identified by using ublast (a fast alternative to protein BLAST) against a database of manually-curated proteins (most of which are experimentally characterized) or by using HMMer with enzyme models (usually from TIGRFam). Ublast hits may be split across two different proteins.
A candidate for a step is "high confidence" if either:
Otherwise, a candidate is "medium confidence" if either:
Other blast hits with at least 50% coverage are "low confidence."
Steps with no high- or medium-confidence candidates may be considered "gaps." For the typical bacterium that can make all 20 amino acids, there are 1-2 gaps in amino acid biosynthesis pathways. For diverse bacteria and archaea that can utilize a carbon source, there is a complete high-confidence catabolic pathway (including a transporter) just 38% of the time, and there is a complete medium-confidence pathway 63% of the time. Gaps may be due to:
GapMind relies on the predicted proteins in the genome and does not search the six-frame translation. In most cases, you can search the six-frame translation by clicking on links to Curated BLAST for each step definition (in the per-step page).
For more information, see the paper from 2019 on GapMind for amino acid biosynthesis, the paper from 2022 on GapMind for carbon sources, or view the source code.
If you notice any errors or omissions in the step descriptions, or any questionable results, please let us know
by Morgan Price, Arkin group, Lawrence Berkeley National Laboratory