GapMind for catabolism of small carbon sources

 

Alignments for a candidate for TM0027 in Herbaspirillum seropedicae SmR1

Align TM0027, component of β-glucoside porter (Conners et al., 2005). Binds cellobiose, laminaribiose (Nanavati et al. 2006). Regulated by cellobiose-responsive repressor BglR (characterized)
to candidate HSERO_RS07880 HSERO_RS07880 peptide ABC transporter substrate-binding protein

Query= TCDB::Q9WXN4
         (268 letters)



>FitnessBrowser__HerbieS:HSERO_RS07880
          Length = 330

 Score =  165 bits (417), Expect = 1e-45
 Identities = 101/267 (37%), Positives = 160/267 (59%), Gaps = 13/267 (4%)

Query: 4   LVVKNLTKIFSLGFFSKRRIEAVKNVSFEVKEKEIVSLVGESGSGKTTTAKMILRLLPP- 62
           L V+NL   F   F  +  + AV +VS  V    I+ LVGESGSGK+ T   IL ++   
Sbjct: 6   LEVRNLRTHF---FTPEGVLPAVDDVSLSVGRGRILGLVGESGSGKSVTGFSILGMVDAP 62

Query: 63  ---TSGEIYFEGKDIWKDIKDRESLVEFR-RKVHAVFQDPFASYNPFYPVERTLWQAISL 118
                GEI F+G+D+ +   D+ SL E +  ++  +FQDP  + NP   VE  +  A+  
Sbjct: 63  GRIVGGEILFQGRDLVR--MDKTSLRELQGNRIAMIFQDPMMTLNPVLKVEAQMVDAV-- 118

Query: 119 LENKPSNKKEALELIKESLFRVGI-DPKDVLGKYPHQISGGQKQRIMIARCWILRPLLIV 177
           L +   ++++A EL +++L  +GI  P++ L  YPHQ+SGG +QR+ IA   + +P LI+
Sbjct: 119 LAHSKVSRQQARELARDTLGMMGIASPEERLQAYPHQLSGGMRQRVAIAIAMLHKPDLII 178

Query: 178 ADEPTSMIDASSRGGIIKLLEELREEQGTSIIFITHDLGLAYYVSDNIFVMKNGEIVERG 237
           ADEPT+ +D + +  I+  +++L  + GT++I+ITHDL +   ++D + VM  G IVE+G
Sbjct: 179 ADEPTTALDVTIQAQILSEVQKLARQHGTALIWITHDLSVVAGLADEVAVMYAGRIVEQG 238

Query: 238 HPDKVVLEPTHEYTKLLVGSIPKLYRK 264
             D V+  P H YT+ L+GS+P   R+
Sbjct: 239 SVDAVLDAPLHPYTQGLIGSLPSNNRR 265


Lambda     K      H
   0.319    0.139    0.397 

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: 199
Number of extensions: 12
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: 268
Length of database: 330
Length adjustment: 26
Effective length of query: 242
Effective length of database: 304
Effective search space:    73568
Effective search space used:    73568
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 (21.7 bits)
S2: 48 (23.1 bits)

This GapMind analysis is from Sep 17 2021. The underlying query database was built on Sep 17 2021.

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About GapMind

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