GapMind for Amino acid biosynthesis

 

Alignments for a candidate for cmutase in Pseudomonas fluorescens GW456-L13

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 PfGW456L13_2176 Chorismate mutase I (EC 5.4.99.5) / Prephenate dehydratase (EC 4.2.1.51)

Query= SwissProt::P27603
         (365 letters)



>FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2176
          Length = 364

 Score =  632 bits (1630), Expect = 0.0
 Identities = 317/365 (86%), Positives = 341/365 (93%), Gaps = 1/365 (0%)

Query: 1   MSEADQLKALRVRIDSLDERILDLISERARCAQEVARVKTASWPKAEEAVFYRPEREAWV 60
           MSE  +LKALR+RID+LDE++L+LISERARCAQEVARVK AS  + E  VFYRPEREA V
Sbjct: 1   MSE-QELKALRLRIDALDEKVLELISERARCAQEVARVKMASLAEGEVPVFYRPEREAQV 59

Query: 61  LKHIMELNKGPLDNEEMARLFREIMSSCLALEQPLRVAYLGPEGTFSQAAALKHFGHSVI 120
           LK +ME N+GPL NEEMARLFREIMSSCLALEQPL+VAYLGPEGTF+QAAA+KHFGH+VI
Sbjct: 60  LKRVMERNQGPLGNEEMARLFREIMSSCLALEQPLKVAYLGPEGTFTQAAAMKHFGHAVI 119

Query: 121 SKPMAAIDEVFREVVAGAVNFGVVPVENSTEGAVNHTLDSFLEHDIVICGEVELRIHHHL 180
           SKPMAAIDEVFREV AGAVNFGVVPVENSTEGAVNHTLDSFLEHD+VICGEVELRIHHHL
Sbjct: 120 SKPMAAIDEVFREVAAGAVNFGVVPVENSTEGAVNHTLDSFLEHDMVICGEVELRIHHHL 179

Query: 181 LVGETTKTDRITRIYSHAQSLAQCRKWLDAHYPNVERVAVSSNADAAKRVKSEWNSAAIA 240
           LVGE TKTD I+RIYSHAQSLAQCRKWLDAHYPNVERVAVSSNA+AAKRVK EWNSAAIA
Sbjct: 180 LVGENTKTDSISRIYSHAQSLAQCRKWLDAHYPNVERVAVSSNAEAAKRVKGEWNSAAIA 239

Query: 241 GDMAAQLYGLSKLAEKIEDRPVNSTRFLIIGSQEVPPTGDDKTSIIVSMRNKPGALHELL 300
           GDMAA LYGL++LAEKIEDRP NSTRFL+IG+QEVPPTGDDKTSIIVSM NKPGALHELL
Sbjct: 240 GDMAAGLYGLTRLAEKIEDRPDNSTRFLMIGNQEVPPTGDDKTSIIVSMSNKPGALHELL 299

Query: 301 MPFHSNGIDLTRIETRPSRSGKWTYVFFIDCMGHHQDPLIKNVLEKIGHEAVALKVLGSY 360
           +PFH NGIDLTRIETRPSRSGKWTYVFFID +GHH+DPL+K VLEKI  EAVALKVLGSY
Sbjct: 300 VPFHDNGIDLTRIETRPSRSGKWTYVFFIDFVGHHRDPLVKGVLEKISQEAVALKVLGSY 359

Query: 361 PKAVL 365
           PKAVL
Sbjct: 360 PKAVL 364


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: 504
Number of extensions: 9
Number of successful extensions: 1
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: 364
Length adjustment: 29
Effective length of query: 336
Effective length of database: 335
Effective search space:   112560
Effective search space used:   112560
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 PfGW456L13_2176 (Chorismate mutase I (EC 5.4.99.5) / Prephenate dehydratase (EC 4.2.1.51))
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.26755.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
    ------- ------ -----    ------- ------ -----   ---- --  --------                                               -----------
      2e-34  104.0   2.8    2.1e-34  103.9   1.3    1.9  2  lcl|FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2176  Chorismate mutase I (EC 5.4.99.5


Domain annotation for each sequence (and alignments):
>> lcl|FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2176  Chorismate mutase I (EC 5.4.99.5) / Prephenate dehydratase (E
   #    score  bias  c-Evalue  i-Evalue hmmfrom  hmm to    alifrom  ali to    envfrom  env to     acc
 ---   ------ ----- --------- --------- ------- -------    ------- -------    ------- -------    ----
   1 !  103.9   1.3   2.1e-34   2.1e-34       1      76 []       6      84 ..       6      84 .. 0.93
   2 ?   -3.0   0.0      0.51      0.51      67      75 ..     125     133 ..     122     134 .. 0.80

  Alignments for each domain:
  == domain 1  score: 103.9 bits;  conditional E-value: 2.1e-34
                                               TIGR01807  1 LkelRnkiDaiDdrildLlseRaklakavgelKkks...aseaviYRPeREaavlrr 54
                                                            Lk+lR +iDa+D+++l+L+seRa++a++v+++K +s    +  v+YRPeREa+vl+r
  lcl|FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2176  6 LKALRLRIDALDEKVLELISERARCAQEVARVKMASlaeGEVPVFYRPEREAQVLKR 62
                                                            799********************************9633333579************ PP

                                               TIGR01807 55 lkelnkGpLdqeavarifrEim 76
                                                            ++e+n+GpL +e++ar+frEim
  lcl|FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2176 63 VMERNQGPLGNEEMARLFREIM 84
                                                            *********************9 PP

  == domain 2  score: -3.0 bits;  conditional E-value: 0.51
                                               TIGR01807  67 avarifrEi 75 
                                                             a++ +frE+
  lcl|FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2176 125 AIDEVFREV 133
                                                             789999998 PP



Internal pipeline statistics summary:
-------------------------------------
Query model(s):                            1  (76 nodes)
Target sequences:                          1  (364 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: 12.15
//
[ok]

This GapMind analysis is from Apr 09 2024. The underlying query database was built on Apr 09 2024.

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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:

where "other" refers to the best ublast hit to a sequence that is not annotated as performing this step (and is not "ignored").

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