Align Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; EC 1.8.1.4 (characterized)
to candidate PfGW456L13_2924 Glutathione reductase (EC 1.8.1.7)
Query= SwissProt::P85207 (461 letters) >FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2924 Length = 452 Score = 251 bits (640), Expect = 5e-71 Identities = 162/445 (36%), Positives = 241/445 (54%), Gaps = 14/445 (3%) Query: 4 YDLIVIGTGPGGYPAAIRGAQLGLKVLAVEAAEVGGVCLNVGCIPTKALLHAAETVHHLK 63 +DL VIG G GG AA A G KV E+ +GG C+NVGC+P K L++ A + Sbjct: 5 FDLYVIGAGSGGVRAARFAAGFGAKVAVAESRYLGGTCVNVGCVPKKLLVYGAHFAEDFE 64 Query: 64 GAEGFGLKA-KPELDLKKLGAWRDGVVKKLTGGVAGLLKGNKVELLRGFARFKGPREIEV 122 A GFG + + D L A +D + +L G LL + V L G A+ P ++E+ Sbjct: 65 QASGFGWGLDEAQFDWPTLIANKDREINRLNGIYRNLLVNSGVTLHEGHAKIVDPHQVEI 124 Query: 123 NGETYGAQSFIIATGSEPMPLKGFPFGEDVWDSTRALRVEEGIPKRLLVIGGGAVGLELG 182 NGE + A++ +IATG P + P E S +A ++E +PKR+LV+GGG + +E Sbjct: 125 NGERFTARNILIATGGWPQ-IPEIPGHEHAISSNQAFFLKE-LPKRVLVVGGGYIAVEFA 182 Query: 183 QIYHRLGSEVTLIEYMPEILPAG-DRETAALLRKALEKEGLKVRTGTKAVGYEKKQDG-L 240 I+H LG++ TL+ Y E+ G D L++ L K G+ ++ +K DG L Sbjct: 183 GIFHGLGAKTTLL-YRGELFLRGFDGSVRKHLQEELTKRGMDLQFNADIERIDKLADGSL 241 Query: 241 HVLLEAAQGGSQEEIVVDKILVAVGRRPRTEGLGLEKAGVKVDERGFIQVNARMETSAPG 300 V L+ + ++ D + A GRRP + LGLE GVK+D +GF++V+ +T+ P Sbjct: 242 KVTLKDGR-----QLEADCVFYATGRRPMLDNLGLENTGVKLDRKGFVEVDELYQTAEPS 296 Query: 301 VYAIGDVARPPLLAHKAMKEGLVAAENAAGKNAL--FDFQ-VPSVVYTGPEWAGVGLTEE 357 + A+GDV L A+ EG+ A D++ +P+ V++ P VGLTEE Sbjct: 297 ILALGDVIGRVQLTPVALAEGMAVARRLFKPEQYRPVDYKMIPTAVFSLPNIGTVGLTEE 356 Query: 358 EARKAGYNVKVGKFPFSASGRALTLGGAEGLIKVVGDAETDLLLGVFVVGPQAGELIAEA 417 EAR+AG+ V+V + F LT L+K+V DA TD +LG +VGP+AGE++ Sbjct: 357 EAREAGHEVQVFESRFRPMKLTLTECQERTLMKLVVDANTDKVLGCHMVGPEAGEIVQGL 416 Query: 418 TLALEMGATVSDLGLTIHPHPTLSE 442 +AL+ GAT D TI HPT +E Sbjct: 417 AIALKAGATKRDFDETIGVHPTAAE 441 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: 514 Number of extensions: 25 Number of successful extensions: 5 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: 452 Length adjustment: 33 Effective length of query: 428 Effective length of database: 419 Effective search space: 179332 Effective search space used: 179332 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