Align Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase (EC 2.3.1.168) (characterized)
to candidate 3608573 Dshi_1967 catalytic domain of components of various dehydrogenase complexes (RefSeq)
Query= reanno::Smeli:SMc03203 (426 letters) >FitnessBrowser__Dino:3608573 Length = 433 Score = 238 bits (608), Expect = 2e-67 Identities = 151/429 (35%), Positives = 225/429 (52%), Gaps = 35/429 (8%) Query: 6 IKMPDVGEGVAEAELVEWHVKPGDPVREDMVLAAVMTDKATVEIPSPVTGKVLWLGAEVG 65 + +PD+G+ + +V V GD V E+ L + +DKAT+E+PSPV GKV+ + G Sbjct: 14 VNVPDIGD-FTDVPVVSILVSVGDVVAEEDPLLELESDKATMEVPSPVAGKVVEIKVAEG 72 Query: 66 DTVAVKAPLVRIETAGEAGEAAPDSIPEALAEQVLDEPVAVSSRLEAKAPPQPEKPAPKP 125 DTV+ + L+ + A + A + P A A A AP P AP Sbjct: 73 DTVS-EGTLIMMMEAEDGAAGASEPAPSAPA---------------ASAPAAPSAAAPAA 116 Query: 126 APAPREAPDLSA---KPLASPAVRLRARESGIDLRQVAGTGPAGRITHEDLDLFISRGAE 182 P+ AP A K ASP+VR AR IDL +V GTG GRI ED+ ++ Sbjct: 117 PTDPKPAPVTDAGFGKAHASPSVRAFARSLEIDLSKVNGTGRKGRILREDVTAYLKSSTA 176 Query: 183 PLPAQTGLV---------------RKTAVEEVRMIGLRRRIAEKMSLSTSRIPHITYVEE 227 P PA+ G + VE+V M +++ + S IPH+T+ +E Sbjct: 177 PAPAKGGAASGGMGIPPIPVVDFSKFGPVEDVEMPRIKKISGPALHRSWLNIPHVTHNDE 236 Query: 228 VDMTALEDLRATMNRDRKPEQAKLTILPFLMRALVKTVAEQPGVNATFDDHAGVIHRHAA 287 D+T L+ R M+ K + ++T+L F+++A V + N++ + + A Sbjct: 237 ADITDLDKYRKEMDTQAKEDGYRVTLLSFVIKASVSALKTHWEFNSSIHPDGDKLIKKAF 296 Query: 288 VHIGIATQTPAGLTVPVVRHAEARGIWDCAAELNRLADAARTGTATRDELTGSTITISSL 347 +IG A TP GL VPV++ A+ +G+ + + EL L+ AR G ++ G+T TISSL Sbjct: 297 YNIGFAADTPNGLMVPVIKDADRKGLVEISKELMELSAKARAGELKGPDMQGATFTISSL 356 Query: 348 GAIGGIASTPVINHPEVAIVGVNKIAVRPVWDGAQFVPRKIMNLSSSFDHRVIDGWDAAV 407 G IGG + TP++N PEVAI+G+ + + PVW+G +FVPR + LS S+DHR +DG AA Sbjct: 357 GGIGGTSFTPIVNAPEVAILGLTRSKMAPVWNGEEFVPRLMQPLSLSYDHRAVDGALAAR 416 Query: 408 FVQRLKTLL 416 F LKTLL Sbjct: 417 FCVTLKTLL 425 Lambda K H 0.317 0.133 0.384 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: 442 Number of extensions: 15 Number of successful extensions: 4 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: 426 Length of database: 433 Length adjustment: 32 Effective length of query: 394 Effective length of database: 401 Effective search space: 157994 Effective search space used: 157994 Neighboring words threshold: 11 Window for multiple hits: 40 X1: 16 ( 7.3 bits) X2: 38 (14.6 bits) X3: 64 (24.7 bits) S1: 41 (21.6 bits) S2: 51 (24.3 bits)
This GapMind analysis is from Sep 17 2021. The underlying query database was built on Sep 17 2021.
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 the paper from 2019 on GapMind for amino acid biosynthesis, the paper from 2022 on GapMind for carbon sources, or view the source code.
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