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_011372105.1 SUDEN_RS02465 prephenate dehydratase
Query= SwissProt::P27603 (365 letters) >NCBI__GCF_000012965.1:WP_011372105.1 Length = 363 Score = 207 bits (528), Expect = 3e-58 Identities = 134/363 (36%), Positives = 201/363 (55%), Gaps = 16/363 (4%) Query: 7 LKALRVRIDSLDERILDLISERARCAQEVARVKTASWPKAEEAVFYRPEREAWVLKHI-- 64 L+ R ID++D +IL+L+++R + V +K K ++ YRPERE +++ + Sbjct: 4 LEECRDGIDAIDNKILELLNQRMVVVKRVGEIK-----KDSKSAIYRPEREKAIIERLTL 58 Query: 65 MELN-KGPLDNEEMARLFREIMSSCLALEQPLRVAYLGPEGTFSQAAALKHFGHSVISKP 123 +N KG L+ + + +F EI + LE P R+AYLGPEG+F+ AA FG P Sbjct: 59 QSVNDKGLLNQDAIEAIFLEIFAVSRNLELPERIAYLGPEGSFTHQAAESRFGAMSDYMP 118 Query: 124 MAAIDEVFREVVAGAVNFGVVPVENSTEGAVNHTLDSFLEHDIVICGEVELRIHHHLLVG 183 M +I VF+E+ FGVVP+ENS +G V TLD + + I E+ + IH V Sbjct: 119 MRSISHVFKELETKRAKFGVVPIENSRDGVVGETLDLLAKSSVKIVAELYMPIHMS-FVT 177 Query: 184 ETTKTDRITRIYSHAQSLAQCRKWLDAH-YPNVERVAVSSNADAAKRVKSEWNSAAIAGD 242 + K IT+IYS + QCR++L H NVE + V S A AA + ++AAI Sbjct: 178 KAKKISDITKIYSRDKGFGQCREFLQEHNLSNVELIPVESTAKAAILASKDDSAAAICSH 237 Query: 243 MAAQLYGLSKLAEKIEDRPVNSTRFLIIGSQEVPPTGDDKTSIIVSMRN--KPGALHELL 300 +AA+LY + + + +ED + TRF I+ + + DDKTSI+V +++ K G+L L Sbjct: 238 IAAKLYNVPTMFDHVEDSIGSQTRFFILSDFKNEKSYDDKTSILVRLKDSVKAGSLVHFL 297 Query: 301 MPFHSNGIDLTRIETRPSR-SGKWTYVFFIDCMGHHQDPLIKNVLEKIGHEAVALKVLGS 359 F I+L++IE+RPS+ G + Y FFID GH D + VL+K E + LGS Sbjct: 298 QDFEHESINLSKIESRPSKEKGGFEYWFFIDFYGHVDDEKFQKVLQKHKEE---VTWLGS 354 Query: 360 YPK 362 Y K Sbjct: 355 YVK 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: 300 Number of extensions: 19 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: 365 Length of database: 363 Length adjustment: 29 Effective length of query: 336 Effective length of database: 334 Effective search space: 112224 Effective search space used: 112224 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_011372105.1 SUDEN_RS02465 (prephenate dehydratase)
to HMM TIGR01807 (pheA: chorismate mutase (EC 5.4.99.5))
# 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/TIGR01807.hmm # target sequence database: /tmp/gapView.141616.genome.faa # - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - Query: TIGR01807 [M=76] Accession: TIGR01807 Description: CM_P2: chorismate mutase 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 ------- ------ ----- ------- ------ ----- ---- -- -------- ----------- 2.1e-28 84.7 0.9 5.1e-28 83.5 0.9 1.7 1 NCBI__GCF_000012965.1:WP_011372105.1 Domain annotation for each sequence (and alignments): >> NCBI__GCF_000012965.1:WP_011372105.1 # score bias c-Evalue i-Evalue hmmfrom hmm to alifrom ali to envfrom env to acc --- ------ ----- --------- --------- ------- ------- ------- ------- ------- ------- ---- 1 ! 83.5 0.9 5.1e-28 5.1e-28 1 76 [] 4 80 .. 4 80 .. 0.92 Alignments for each domain: == domain 1 score: 83.5 bits; conditional E-value: 5.1e-28 TIGR01807 1 LkelRnkiDaiDdrildLlseRaklakavgelKkksaseaviYRPeREaavlrrl..keln.kGpLdqeavarif 72 L+e R+ iDaiD++il+Ll++R+ ++k+vge+Kk s+++iYRPeRE a++ rl ++ n kG+L+q+a+++if NCBI__GCF_000012965.1:WP_011372105.1 4 LEECRDGIDAIDNKILELLNQRMVVVKRVGEIKKD--SKSAIYRPEREKAIIERLtlQSVNdKGLLNQDAIEAIF 76 789********************************..9999************9733555449************ PP TIGR01807 73 rEim 76 Ei+ NCBI__GCF_000012965.1:WP_011372105.1 77 LEIF 80 **97 PP Internal pipeline statistics summary: ------------------------------------- Query model(s): 1 (76 nodes) Target sequences: 1 (363 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: 17.12 // [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