Align Bifunctional chorismate mutase/prephenate dehydratase; Chorismate mutase-prephenate dehydratase; P-protein; EC 5.4.99.5; EC 4.2.1.51 (characterized)
to candidate WP_028583168.1 G494_RS0101895 prephenate dehydratase
Query= SwissProt::P27603 (365 letters) >NCBI__GCF_000429965.1:WP_028583168.1 Length = 365 Score = 263 bits (672), Expect = 5e-75 Identities = 137/363 (37%), Positives = 216/363 (59%), Gaps = 6/363 (1%) Query: 1 MSEADQLKALRVRIDSLDERILDLISERARCAQEVARVKTASWPKAEEAVFYRPEREAWV 60 M + + +R RID++D IL+L+ ER CA+ + ++K + + + P+RE + Sbjct: 1 MDQRADISQVRNRIDAIDNTILELLKERLECAKSIGKLKNET-----KRAKWDPQRELEI 55 Query: 61 LKHIMELNKGPLDNEEMARLFREIMSSCLALEQPLRVAYLGPEGTFSQAAALKHFGHSVI 120 + + E N+ ++ + +F EI+++C ++ VAYLGPE TF+ A +K+FG S Sbjct: 56 YQRLREHNQEIFPDKALHAIFHEIITTCRLSQRKAIVAYLGPEATFTHQAGVKYFGQSAA 115 Query: 121 SKPMAAIDEVFREVVAGAVNFGVVPVENSTEGAVNHTLDSFLEHDIVICGEVELRIHHHL 180 +P+ +I EVF+EV V +G+VPVENS EGAV LDSFL +++ ICGE++L I H+L Sbjct: 116 YRPLESIVEVFQEVEKERVQYGIVPVENSIEGAVTSCLDSFLNYNVQICGELQLPITHNL 175 Query: 181 LVGETTKTDRITRIYSHAQSLAQCRKWLDAHYPNVERVAVSSNADAAKRVKSEWNSAAIA 240 V + + I + SHAQ LAQCR+WL + P + V S AA+ + AIA Sbjct: 176 -VCRSGNIEDIKTVASHAQGLAQCREWLAKNMPGTPTLPVFSTGAAAEMAAEDPEIGAIA 234 Query: 241 GDMAAQLYGLSKLAEKIEDRPVNSTRFLIIGSQEVPPTGDDKTSIIVSMRNKPGALHELL 300 +A Y L + + IED N+TRFL++G + +G DKTS+++ + N+PGAL+E+L Sbjct: 235 SSLAVTTYDLQVVVKGIEDYQGNTTRFLVLGKKSPQKSGADKTSVLLGLINRPGALNEIL 294 Query: 301 MPFHSNGIDLTRIETRPSRSGKWTYVFFIDCMGHHQDPLIKNVLEKIGHEAVALKVLGSY 360 + IDL +IE+RP++ +W Y+FF+D +GH DP+I + + LGSY Sbjct: 295 TILSAKNIDLAKIESRPTKGKQWKYLFFLDMIGHMDDPVIHEACNILKQICAYFEWLGSY 354 Query: 361 PKA 363 P+A Sbjct: 355 PRA 357 Lambda K H 0.319 0.133 0.390 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: 340 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: 365 Length of database: 365 Length adjustment: 30 Effective length of query: 335 Effective length of database: 335 Effective search space: 112225 Effective search space used: 112225 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: 49 (23.5 bits)
Align candidate WP_028583168.1 G494_RS0101895 (prephenate dehydratase)
to HMM PF01817 (CM_2)
# hmmsearch :: search profile(s) against a sequence database # HMMER 3.3.1 (Jul 2020); http://hmmer.org/ # Copyright (C) 2020 Howard Hughes Medical Institute. # Freely distributed under the BSD open source license. # - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - # query HMM file: ../tmp/path.aa/PF01817.25.hmm # target sequence database: /tmp/gapView.1300753.genome.faa # - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - Query: CM_2 [M=79] Accession: PF01817.25 Description: Chorismate mutase type II Scores for complete sequences (score includes all domains): --- full sequence --- --- best 1 domain --- -#dom- E-value score bias E-value score bias exp N Sequence Description ------- ------ ----- ------- ------ ----- ---- -- -------- ----------- 2e-23 68.9 1.7 3.7e-23 68.1 1.7 1.5 1 NCBI__GCF_000429965.1:WP_028583168.1 Domain annotation for each sequence (and alignments): >> NCBI__GCF_000429965.1:WP_028583168.1 # score bias c-Evalue i-Evalue hmmfrom hmm to alifrom ali to envfrom env to acc --- ------ ----- --------- --------- ------- ------- ------- ------- ------- ------- ---- 1 ! 68.1 1.7 3.7e-23 3.7e-23 1 78 [. 11 87 .. 11 88 .. 0.96 Alignments for each domain: == domain 1 score: 68.1 bits; conditional E-value: 3.7e-23 CM_2 1 RkeIdeiDrelleLlaeRmelakeiaeyKkenglpvldpeReeevlerlregaeelgldpeavekifreiisesr 75 R++Id+iD+ +leLl+eR+e+ak i+++K e++ + dp+Re e+ +rlre+ +++ ++++a+ +if+eii +r NCBI__GCF_000429965.1:WP_028583168.1 11 RNRIDAIDNTILELLKERLECAKSIGKLKNETKRAKWDPQRELEIYQRLREH-NQEIFPDKALHAIFHEIITTCR 84 99*************************************************5.4789*****************9 PP CM_2 76 alQ 78 Q NCBI__GCF_000429965.1:WP_028583168.1 85 LSQ 87 888 PP Internal pipeline statistics summary: ------------------------------------- Query model(s): 1 (79 nodes) Target sequences: 1 (365 residues searched) Passed MSV filter: 1 (1); expected 0.0 (0.02) Passed bias filter: 1 (1); expected 0.0 (0.02) Passed Vit filter: 1 (1); expected 0.0 (0.001) Passed Fwd filter: 1 (1); expected 0.0 (1e-05) Initial search space (Z): 1 [actual number of targets] Domain search space (domZ): 1 [number of targets reported over threshold] # CPU time: 0.00u 0.00s 00:00:00.00 Elapsed: 00:00:00.00 # Mc/sec: 15.69 // [ok]
This GapMind analysis is from Jul 25 2024. The underlying query database was built on Jul 25 2024.
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:
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