Align Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 (characterized)
to candidate Ac3H11_4615 Mercuric ion reductase (EC 1.16.1.1)
Query= SwissProt::P11959 (470 letters) >FitnessBrowser__acidovorax_3H11:Ac3H11_4615 Length = 561 Score = 228 bits (580), Expect = 5e-64 Identities = 153/456 (33%), Positives = 241/456 (52%), Gaps = 12/456 (2%) Query: 9 ETETLVVGAGPGGYVAAIRAAQLGQKVTIVEKGNLGGVCLNVGCIPSKALISASHRYEQA 68 + + V+G+G AA++A + G VT++E+G +GG C+N+GC+PSK +I A+H Sbjct: 98 QLQIAVIGSGGAAMAAALKAVEQGAHVTLIERGTIGGTCVNIGCVPSKIMIRAAHIAHLR 157 Query: 69 KHSE-EMGIKAENVTIDFAKVQEWKASVVKKLTGG-VEGLLKGNK-VEIVKGEAYFVDAN 125 + S + GI A ID +K+ + ++V +L EG+L N + ++ GEA F D Sbjct: 158 RESPFDGGITATVPAIDRSKLLAQQQALVDELRHAKYEGILDSNSAITVLHGEARFKDDQ 217 Query: 126 TVRV-VNGDSAQTYTFKNAIIATGSRPI--ELPNFKFSNRILDSTGALNLGEVPKSLVVI 182 +V V +N + F ++ATG+ P +P K S ST AL VP+ L VI Sbjct: 218 SVVVRLNEGGERVVMFDRCLVATGASPAVPPIPGLKESP-YWTSTEALVSETVPERLAVI 276 Query: 183 GGGYIGIELGTAYANFGTKVTILEGAGEILSGFEKQMAAIIKKRLKKKGVEVVTNALAKG 242 G + +EL A+A G++VTIL + + + + + +G+ V+ + A Sbjct: 277 GSSVVALELAQAFARLGSQVTIL-ARRTLFFREDPAIGEAVTDAFRAEGITVLEHTQASQ 335 Query: 243 AEEREDGVTVTYEANGETKTIDADYVLVTVGRRPNTDELGLEQIGIKMTNRGLIEVDQQC 302 +T +GE I AD +LV GR PNT L L+ G+ + +G I +D+ Sbjct: 336 VAHVNREFVLT-TGHGE---IRADKLLVATGRTPNTRSLALDAAGVTVNAQGAIVIDKGM 391 Query: 303 RTSVPNIFAIGDIVPGPALAHKASYEGKVAAEAIAGHPSAVDYVAIPAVVFSDPECASVG 362 RTS P+I+A GD P + A+ G AA + G +A+D A+PAVVF+DP+ A+VG Sbjct: 392 RTSTPHIYAAGDCADQPQFVYVAAAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVG 451 Query: 363 YFEQQAKDEGIDVIAAKFPFAANGRALALNDTDGFLKLVVRKEDGVIIGAQIIGPNASDM 422 Y E +A +GI+ + RALA DT GF+KLV+ + G +IG Q + P A ++ Sbjct: 452 YSEAEAHHDGIETDSRTLTLDNVPRALANFDTRGFIKLVIEEGSGRLIGVQAVAPEAGEL 511 Query: 423 IAELGLAIEAGMTAEDIALTIHAHPTLGEIAMEAAE 458 I LAI MT +++A + + T+ E AA+ Sbjct: 512 IQTAVLAIRNRMTVQELADQLFPYLTMVEGLKLAAQ 547 Lambda K H 0.316 0.135 0.376 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: 569 Number of extensions: 30 Number of successful extensions: 3 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: 470 Length of database: 561 Length adjustment: 35 Effective length of query: 435 Effective length of database: 526 Effective search space: 228810 Effective search space used: 228810 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: 52 (24.6 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