Align 3-oxoadipyl-CoA thiolase; EC 2.3.1.174 (characterized, see rationale)
to candidate Ac3H11_1916 3-ketoacyl-CoA thiolase (EC 2.3.1.16) @ Acetyl-CoA acetyltransferase (EC 2.3.1.9)
Query= uniprot:A0A2Z5MFE9 (400 letters) >FitnessBrowser__acidovorax_3H11:Ac3H11_1916 Length = 399 Score = 295 bits (756), Expect = 1e-84 Identities = 184/413 (44%), Positives = 243/413 (58%), Gaps = 32/413 (7%) Query: 1 MNDAYICDAIRTPIGRYG-GALKDVRADDLGAVPIKALIQRNPGVDWRAVDDVIYGCANQ 59 + DAYI A RTPIGR G G K+ R DDL IK+ + + P +D +A++D I GC+ Sbjct: 6 VQDAYIVAATRTPIGRSGRGYFKNTRPDDLLVAAIKSAMLQVPTLDPKAIEDAIIGCSFP 65 Query: 60 AGEDNRNVARMSALLAGLPADAP--GATINRLCGSGMDAVGTAARAIKAGEAQLMIAGGV 117 GE N+AR++ GL + P G T+NR C SG+ A+ AA I+ GEA ++IAGG Sbjct: 66 EGEQGMNMARIAV---GLAFNHPVGGVTVNRFCASGITALQMAADRIRVGEADVLIAGGA 122 Query: 118 ESMTRAPFVMGKAASAFTRQAEIHDTTIGWRFVNPLMKRQYGVDSMPETAENVAEQFGIS 177 ESM+ P MG +F + D +G + M TAE VA+Q+ IS Sbjct: 123 ESMSLVP--MGGNKPSFNAEVFARDEDVGIAY------------GMGLTAEKVAQQWKIS 168 Query: 178 RADQDAFALASQQKAARAQRDGTLAQEIVGVEIAQKK-----GDAIR----VTLDEHPR- 227 R QDAFAL S +A +AQ+ G EI E+ ++ G+ + V+LDE PR Sbjct: 169 REAQDAFALESHLRAIKAQKAGEFTDEITPFEVVERSPNLATGEVVEKRRTVSLDEGPRP 228 Query: 228 ETSLESLARLKGVVRPDGTVTAGNASGVNDGACALLIASQQAAEQYGLRRRARVVGMATA 287 +TSLE LA+LK V G+VTAGN+S +DGA AL++AS++A +Q+GL AR V A Sbjct: 229 DTSLEGLAKLKPVFAARGSVTAGNSSQTSDGAGALIVASEKAVKQFGLTPLARFVSYAAR 288 Query: 288 GVEPRIMGIGPAPATQKLLRQLGMTLDQLDVIELNEAFASQGLAVLRMLGLRDDDPRVNP 347 GV P IMGIGP A LR G+ D + ELNEAFA+Q LAV+ LGL + VNP Sbjct: 289 GVPPEIMGIGPIEAIPAALRYAGLKSDDIGWYELNEAFAAQSLAVINTLGL--NPANVNP 346 Query: 348 NGGAIALGHPLGASGARLVTTALHQLERSNGRFALCTMCIGVGQGIALVIERL 400 GGAIALGHPLGA+GA T +H L R ++ + TMC+G GQG A +IE L Sbjct: 347 MGGAIALGHPLGATGAIRAATVVHALRRHKLKYGMVTMCVGTGQGAAGIIEAL 399 Lambda K H 0.319 0.134 0.386 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: 444 Number of extensions: 26 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: 400 Length of database: 399 Length adjustment: 31 Effective length of query: 369 Effective length of database: 368 Effective search space: 135792 Effective search space used: 135792 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 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