Align MalK; aka Sugar ABC transporter, ATP-binding protein, component of The maltose, maltotriose, mannotetraose (MalE1)/maltose, maltotriose, trehalose (MalE2) porter (Nanavati et al., 2005). For MalG1 (823aas) and MalG2 (833aas), the C-terminal transmembrane domain with 6 putative TMSs is preceded by a single N-terminal TMS and a large (600 residue) hydrophilic region showing sequence similarity to MLP1 and 2 (9.A.14; e-12 & e-7) as well as other proteins (characterized)
to candidate GFF5296 PS417_27115 transporter
Query= TCDB::Q9X103 (369 letters) >FitnessBrowser__WCS417:GFF5296 Length = 380 Score = 239 bits (610), Expect = 9e-68 Identities = 141/339 (41%), Positives = 203/339 (59%), Gaps = 22/339 (6%) Query: 6 VVLENVTKVYENKVVAVKNANLVVEDKEFVVLLGPSGCGKTTTLRMIAGLEEITDGKIYI 65 V ++ VTK ++ + +AV + +L ++ E LLG SG GK+T LRM+AG E T+G+IY+ Sbjct: 23 VKIDRVTKKFD-ETIAVDDVSLEIKKGEIFALLGGSGSGKSTLLRMLAGFERPTEGRIYL 81 Query: 66 DGKVVNDVEPKDRDIAMVFQNYALYPHMTVYENMAFGLKLRKYPKDEIDRRVREAAKILG 125 DG+ + D+ P +R I M+FQ+YAL+PHMTV +N+AFGL+ K PK EID RV E K++ Sbjct: 82 DGEDITDMPPYERPINMMFQSYALFPHMTVAQNIAFGLQQDKIPKAEIDARVAEMLKLVQ 141 Query: 126 IENLLDRKPRQLSGGQRQRVAVGRAIVRNPKVFLFDEPLSNLDAKLRVQMRSELKKLHHR 185 + RKP QLSGGQRQRVA+ R++ + PK+ L DEP+ LD KLR QM+ EL ++ R Sbjct: 142 MSQYAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRSQMQLELVEIIER 201 Query: 186 LQATIIYVTHDQVEAMTMADKIVVMKDGEIQQIGTPHEIYNSPANVFVAGFIGSPPMNFV 245 + T + VTHDQ EAMTMA++I +M G I QIG+P +IY +P + V FIG+ +N Sbjct: 202 VGVTCVMVTHDQEEAMTMAERIAIMHLGWIAQIGSPIDIYETPTSRLVCEFIGN--VNIF 259 Query: 246 NARVVRGEGGLWIQASGFKVKVPKEFEDKLANY------IDKEIIFGIRPEDIYDKLFAL 299 + +VV G + +K P D Y DK + + IRPE KL Sbjct: 260 DTQVVDDAEGHAV------LKCPDLDRDIYVGYGIATSVEDKSVTYAIRPE----KLLVT 309 Query: 300 APSP---ENTITGVVDVVEPLGSETILHVKVGDDLIVAS 335 P N +G V + LG ++ +V++ +V S Sbjct: 310 TEMPTCEHNWSSGKVHDIAYLGGHSVFYVELPSGKLVQS 348 Lambda K H 0.319 0.138 0.387 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: 348 Number of extensions: 12 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: 369 Length of database: 380 Length adjustment: 30 Effective length of query: 339 Effective length of database: 350 Effective search space: 118650 Effective search space used: 118650 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: 50 (23.9 bits)
This GapMind analysis is from Apr 09 2024. 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:
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