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_012536421.1 AFE_RS04210 prephenate dehydratase
Query= SwissProt::P27603 (365 letters) >NCBI__GCF_000021485.1:WP_012536421.1 Length = 358 Score = 350 bits (898), Expect = e-101 Identities = 185/359 (51%), Positives = 245/359 (68%), Gaps = 6/359 (1%) Query: 6 QLKALRVRIDSLDERILDLISERARCAQEVARVKTASWPKAEEAVFYRPEREAWVLKHIM 65 +L ALR ID +D++ L L+ ER R AQ+V VK A A E FY P+RE+ +L+ +M Sbjct: 5 ELAALRKAIDQVDQQFLQLLGERGRLAQQVGAVKQA----AGEVNFYHPDRESEILRRVM 60 Query: 66 ELNKGPLDNEEMARLFREIMSSCLALEQPLRVAYLGPEGTFSQAAALKHFGHSVISKPMA 125 N GP +E++A +FREI+S+ LALEQPL+VAYLGP GTFSQ AA KHFG + + +P A Sbjct: 61 ADNPGPFSSEQVAIIFREIISAGLALEQPLQVAYLGPAGTFSQIAAQKHFGRAAVLQPTA 120 Query: 126 AIDEVFREVVAGAVNFGVVPVENSTEGAVNHTLDSFLEHDIVICGEVELRIHHHLLVGET 185 I E+FR V + FGVVPVENSTEG+VN +LD L++ + ICGEV+LRI H+L+ Sbjct: 121 GIAEIFRLVDSDQARFGVVPVENSTEGSVNLSLDLLLDYPLQICGEVQLRIVHNLVAKVP 180 Query: 186 TKTDRITRIYSHAQSLAQCRKWLDAHYPNVERVAVSSNADAAKRVKSEWNSAAIAGDMAA 245 T R R+Y H Q+ AQCR+WL H P E V V+SNA AA+R ++ + +AI+ +AA Sbjct: 181 ISTVR--RVYVHYQTRAQCRQWLATHLPQAELVDVASNAVAAERAATDADGSAISTTLAA 238 Query: 246 QLYGLSKLAEKIEDRPVNSTRFLIIGSQEVPPTGDDKTSIIVSMRNKPGALHELLMPFHS 305 + YGL L IED P N+TRFLIIG PTG+DKTS++V+ N+PG+LH LL P Sbjct: 239 EAYGLDILVAGIEDNPENTTRFLIIGKIHTRPTGNDKTSLVVAGANRPGSLHALLSPLAD 298 Query: 306 NGIDLTRIETRPSRSGKWTYVFFIDCMGHHQDPLIKNVLEKIGHEAVALKVLGSYPKAV 364 GI LTRIE+RP+RS W YVF++D +GH QD I VL+ + +A + LGSYP+AV Sbjct: 299 AGISLTRIESRPARSAIWEYVFYLDLLGHCQDAAIAPVLDVLAQQASFCRCLGSYPRAV 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: 341 Number of extensions: 16 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: 358 Length adjustment: 29 Effective length of query: 336 Effective length of database: 329 Effective search space: 110544 Effective search space used: 110544 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_012536421.1 AFE_RS04210 (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.3398010.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 ------- ------ ----- ------- ------ ----- ---- -- -------- ----------- 4.2e-27 80.6 0.1 7.9e-27 79.7 0.1 1.5 1 NCBI__GCF_000021485.1:WP_012536421.1 Domain annotation for each sequence (and alignments): >> NCBI__GCF_000021485.1:WP_012536421.1 # score bias c-Evalue i-Evalue hmmfrom hmm to alifrom ali to envfrom env to acc --- ------ ----- --------- --------- ------- ------- ------- ------- ------- ------- ---- 1 ! 79.7 0.1 7.9e-27 7.9e-27 1 76 [] 6 80 .. 6 80 .. 0.98 Alignments for each domain: == domain 1 score: 79.7 bits; conditional E-value: 7.9e-27 TIGR01807 1 LkelRnkiDaiDdrildLlseRaklakavgelKkksaseaviYRPeREaavlrrlkelnkGpLdqeavarifrEi 75 L++lR++iD +D++ l+Ll eR +la++vg +K++ a e +Y P+RE +lrr++ n+Gp +e+va ifrEi NCBI__GCF_000021485.1:WP_012536421.1 6 LAALRKAIDQVDQQFLQLLGERGRLAQQVGAVKQA-AGEVNFYHPDRESEILRRVMADNPGPFSSEQVAIIFREI 79 789********************************.99999*********************************9 PP TIGR01807 76 m 76 + NCBI__GCF_000021485.1:WP_012536421.1 80 I 80 7 PP Internal pipeline statistics summary: ------------------------------------- Query model(s): 1 (76 nodes) Target sequences: 1 (358 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: 21.76 // [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