Align LL-diaminopimelate aminotransferase; DAP-AT; DAP-aminotransferase; LL-DAP-aminotransferase; EC 2.6.1.83 (uncharacterized)
to candidate Ac3H11_1602 Aspartate aminotransferase (EC 2.6.1.1)
Query= curated2:B1I544 (392 letters) >lcl|FitnessBrowser__acidovorax_3H11:Ac3H11_1602 Aspartate aminotransferase (EC 2.6.1.1) Length = 408 Score = 178 bits (451), Expect = 3e-49 Identities = 130/401 (32%), Positives = 194/401 (48%), Gaps = 21/401 (5%) Query: 2 SFVEAKRIRNLPPYLFARIEQLIADKKAQGVDVISLGIGDPDVPTPDHIIEAAEKELKIP 61 +F A R+ + R+ Q K QG VI LG+G+PD TP HI+EAA++ + Sbjct: 9 AFRAADRLGAIGVSEIVRLTQEANQLKRQGQPVIVLGLGEPDFDTPAHILEAAQQAMARG 68 Query: 62 ANHQYPSSAGMPAYRRAVADWYARRFGVELDPQREVVSLIGSKEGIAHLPWCFVDPGDVV 121 H Y G + A+ + G++ E+ + G+K+ + + V+PGD V Sbjct: 69 ETH-YTVLDGTAELKAAIQHKFKHYNGLDFQ-LNEITAGAGAKQILYNALMASVNPGDEV 126 Query: 122 LVPDPGYPVYAGGTILAGGIPHPVPLTAGNGFLPDLAAIPAETARRAKVMFINYPNNPTG 181 ++P P + YA ++AGG+P VP T NGF + A R + +FIN P+NP+G Sbjct: 127 ILPAPYWTSYADMVLIAGGVPVVVPCTEANGFRITPEQLEAAITPRTRWVFINSPSNPSG 186 Query: 182 AVASKEFFARVVDFAREYG-ILVCHDAAYSEIAFDG--YRPPSFLEVAGAREVGIEFHSV 238 A S E V++ + + + D Y I +DG + P+ + + R+ + + V Sbjct: 187 AAYSAEQLRPVLEVVERHPQVWLLADDIYEHILYDGRAFATPAAV-LPSLRDRTLTVNGV 245 Query: 239 SKTYNMTGWRAGWAAGNAGAVEALGRLKSNLDSGVFQVVQYAAIAALNGPQDGVQSLCEM 298 SK Y MTGWR G+ AG + A+ ++S S + Q AA+AAL GPQD V+ C+ Sbjct: 246 SKAYAMTGWRLGYGAGPKALIAAMAVVQSQATSCPSSISQAAAVAALTGPQDVVRERCQA 305 Query: 299 YRERRDLVVDTLN-DLGWRLTRPRATFYIWA--------PVPAG---HDASSFAEMVLEK 346 +++RRDLVV LN G R P FY +A P G + F +L + Sbjct: 306 FQDRRDLVVAALNVSPGLRCRVPEGAFYTFASCEGALGRTTPGGLLLRTDADFCAYLLRE 365 Query: 347 AGVVITPGTGYGTYGEGYFRISLTLPTPRLVEAMERL-RGC 386 V + PG G YFRIS T L EA R+ R C Sbjct: 366 HHVAVVPGGVLGL--APYFRISYAASTADLQEACARIQRAC 404 Lambda K H 0.321 0.139 0.430 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: 318 Number of extensions: 13 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: 392 Length of database: 408 Length adjustment: 31 Effective length of query: 361 Effective length of database: 377 Effective search space: 136097 Effective search space used: 136097 Neighboring words threshold: 11 Window for multiple hits: 40 X1: 16 ( 7.4 bits) X2: 38 (14.6 bits) X3: 64 (24.7 bits) S1: 41 (21.8 bits) S2: 50 (23.9 bits)
This GapMind analysis is from Aug 03 2021. The underlying query database was built on Aug 03 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, or see changes to Amino acid biosynthesis since the publication.
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