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_043766422.1 U743_RS06095 prephenate dehydratase
Query= SwissProt::P27603 (365 letters) >NCBI__GCF_000733765.1:WP_043766422.1 Length = 368 Score = 337 bits (864), Expect = 3e-97 Identities = 180/364 (49%), Positives = 235/364 (64%), Gaps = 9/364 (2%) Query: 5 DQLKALRVRIDSLDERILDLISERARCAQEVARVKTASWPKAEEAVFYRPEREAWVLKHI 64 D+L R RID+LD I + + ERAR AQEV +K + ++ YRP REA VLK Sbjct: 4 DRLSQARSRIDALDAEIQERVVERARVAQEVRDIKREAGDLSDH---YRPAREAQVLKAA 60 Query: 65 MELNKG---PLDNEEMARLFREIMSSCLALEQPLRVAYLGPEGTFSQAAALKHFGHSVIS 121 +E NK PL M + REIMS+CLALE PL V+YLGPEGT++Q+A KHFGH V + Sbjct: 61 VERNKALGSPLSQAAMTSIMREIMSACLALESPLSVSYLGPEGTYTQSAVYKHFGHQVST 120 Query: 122 KPMAAIDEVFREVVAGAVNFGVVPVENSTEGAVNHTLDSFLEHDIVICGEVELRIHHHLL 181 + AID++FR+V +G +GVVPVENSTEG V+ TLD L + ICGEV L +HHHLL Sbjct: 121 RVAPAIDDIFRDVESGTAAYGVVPVENSTEGVVSSTLDLLLATPLSICGEVMLPVHHHLL 180 Query: 182 VGETTKTDRITRIYSHAQSLAQCRKWLDAHYPNVERVAVSSNADAAKRVKSEWNSAAIAG 241 G RI +Y+H QS AQCR+WLD + PN R ++SN AA+RV AAIA Sbjct: 181 SGHEDMA-RIDVVYAHPQSFAQCRRWLDNNLPNTPREPMASNGAAARRVAETKRGAAIAS 239 Query: 242 DMAAQLYGLSKLAEKIEDRPVNSTRFLIIGSQEVPPTGDDKTSIIVS--MRNKPGALHEL 299 A LYGL++LA IED P N+TRFL+IG Q+ PTG D+TS++ S +PGAL L Sbjct: 240 AAAGVLYGLNELAANIEDDPNNTTRFLVIGRQQPEPTGADRTSLVCSAPQGGEPGALFSL 299 Query: 300 LMPFHSNGIDLTRIETRPSRSGKWTYVFFIDCMGHHQDPLIKNVLEKIGHEAVALKVLGS 359 L PF G++L++IE+RPSR W Y F++D GH DP + V++ + + K+LGS Sbjct: 300 LEPFAQAGVNLSKIESRPSRRAAWDYNFYLDLDGHQADPKVGAVIDDVRSRSAFFKILGS 359 Query: 360 YPKA 363 YP+A Sbjct: 360 YPRA 363 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: 372 Number of extensions: 16 Number of successful extensions: 5 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: 368 Length adjustment: 30 Effective length of query: 335 Effective length of database: 338 Effective search space: 113230 Effective search space used: 113230 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_043766422.1 U743_RS06095 (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.2415394.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 ------- ------ ----- ------- ------ ----- ---- -- -------- ----------- 1.3e-19 56.7 2.5 2.8e-19 55.6 2.5 1.6 1 NCBI__GCF_000733765.1:WP_043766422.1 Domain annotation for each sequence (and alignments): >> NCBI__GCF_000733765.1:WP_043766422.1 # score bias c-Evalue i-Evalue hmmfrom hmm to alifrom ali to envfrom env to acc --- ------ ----- --------- --------- ------- ------- ------- ------- ------- ------- ---- 1 ! 55.6 2.5 2.8e-19 2.8e-19 1 78 [. 10 91 .. 10 92 .. 0.92 Alignments for each domain: == domain 1 score: 55.6 bits; conditional E-value: 2.8e-19 CM_2 1 RkeIdeiDrelleLlaeRmelakeiaeyKkengl..pvldpeReeevlerlre..gaeelgldpeavekifreii 71 R++Id++D+e+ e eR+++a+e+ +K+e+g + ++p+Re++vl+ + e +a l++ a+++i+rei+ NCBI__GCF_000733765.1:WP_043766422.1 10 RSRIDALDAEIQERVVERARVAQEVRDIKREAGDlsDHYRPAREAQVLKAAVErnKALGSPLSQAAMTSIMREIM 84 99****************************9998767****************6645455799************ PP CM_2 72 sesralQ 78 s+++al+ NCBI__GCF_000733765.1:WP_043766422.1 85 SACLALE 91 ****998 PP Internal pipeline statistics summary: ------------------------------------- Query model(s): 1 (79 nodes) Target sequences: 1 (368 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: 17.02 // [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