Align Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 (characterized)
to candidate HSERO_RS01180 HSERO_RS01180 acetyl-CoA acetyltransferase
Query= SwissProt::P14611 (393 letters) >FitnessBrowser__HerbieS:HSERO_RS01180 Length = 391 Score = 591 bits (1524), Expect = e-173 Identities = 298/392 (76%), Positives = 339/392 (86%), Gaps = 1/392 (0%) Query: 1 MTDVVIVSAARTAVGKFGGSLAKIPAPELGAVVIKAALERAGVKPEQVSEVIMGQVLTAG 60 M DVVIV+A RTA+GKFGG+L+KI A +LGA VIKA L + G+KPE +SEVI+GQVLTAG Sbjct: 1 MDDVVIVAAQRTAIGKFGGALSKIAAADLGAQVIKALLAKTGIKPEAISEVILGQVLTAG 60 Query: 61 SGQNPARQAAIKAGLPAMVPAMTINKVCGSGLKAVMLAANAIMAGDAEIVVAGGQENMSA 120 GQNPARQ+ IK+GLP MVPA + KVCGSGLKAV LAA AI GDA+IV+AGGQENMSA Sbjct: 61 LGQNPARQSVIKSGLPDMVPAFVVGKVCGSGLKAVQLAAQAIRCGDAQIVIAGGQENMSA 120 Query: 121 APHVLPGSRDGFRMGDAKLVDTMIVDGLWDVYNQYHMGITAENVAKEYGITREAQDEFAV 180 +PHVL SRDGFRMGDAKL DTMIVDGLWDVYNQYHMGITAENVAK++ I+RE QD FA Sbjct: 121 SPHVLNNSRDGFRMGDAKLTDTMIVDGLWDVYNQYHMGITAENVAKKFEISREEQDAFAA 180 Query: 181 GSQNKAEAAQKAGKFDEEIVPVLIPQRKGDPVAFKTDEFVRQGATLDSMSGLKPAFDKAG 240 SQNKAEAAQKAGKF +EIVP+ I +K + V F TDEFV+ G T +S++ L+PAFDKAG Sbjct: 181 ASQNKAEAAQKAGKFKDEIVPIEIKGKK-ETVVFDTDEFVKHGVTAESLATLRPAFDKAG 239 Query: 241 TVTAANASGLNDGAAAVVVMSAAKAKELGLTPLATIKSYANAGVDPKVMGMGPVPASKRA 300 TVTA NASG+NDGAAAVVV SA A ELGL LA IK+Y++AG+DP +MGMGPVPAS+ Sbjct: 240 TVTAGNASGINDGAAAVVVTSAKLAAELGLPVLAKIKAYSSAGLDPSIMGMGPVPASQLT 299 Query: 301 LSRAEWTPQDLDLMEINEAFAAQALAVHQQMGWDTSKVNVNGGAIAIGHPIGASGCRILV 360 L +A WTPQDLDLMEINEAFAAQA+AV++QMGWDTSK+NVNGGAIA+GHPIGASGCR+LV Sbjct: 300 LKKAGWTPQDLDLMEINEAFAAQAIAVNKQMGWDTSKINVNGGAIALGHPIGASGCRVLV 359 Query: 361 TLLHEMKRRDAKKGLASLCIGGGMGVALAVER 392 TLLHEM RRDAKKGLASLCIGGGMGVALAVER Sbjct: 360 TLLHEMVRRDAKKGLASLCIGGGMGVALAVER 391 Lambda K H 0.315 0.131 0.369 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: 529 Number of extensions: 18 Number of successful extensions: 2 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: 393 Length of database: 391 Length adjustment: 31 Effective length of query: 362 Effective length of database: 360 Effective search space: 130320 Effective search space used: 130320 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: 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