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 3607842 Dshi_1250 ABC transporter related (RefSeq)
Query= TCDB::Q9X103 (369 letters) >FitnessBrowser__Dino:3607842 Length = 351 Score = 300 bits (768), Expect = 4e-86 Identities = 171/364 (46%), Positives = 229/364 (62%), Gaps = 21/364 (5%) Query: 3 MAQVVLENVTKVYENKVVAVKNANLVVEDKEFVVLLGPSGCGKTTTLRMIAGLEEITDGK 62 M+ + L K Y V V +L + D EF V +GPSGCGK+T LRMIAGLEE ++G Sbjct: 1 MSGITLRGAVKRYGETQV-VHGVDLSIADGEFCVFVGPSGCGKSTLLRMIAGLEETSEGS 59 Query: 63 IYIDGKVVNDVEPKDRDIAMVFQNYALYPHMTVYENMAFGLKLRKYPKDEIDRRVREAAK 122 I+I + V ++P +R +AMVFQ YALYPHMTV ENM FGLK+ PK EI +V A++ Sbjct: 60 IHIGARDVTRLDPSERGVAMVFQTYALYPHMTVAENMGFGLKMNGVPKAEIKAKVAAASE 119 Query: 123 ILGIENLLDRKPRQLSGGQRQRVAVGRAIVRNPKVFLFDEPLSNLDAKLRVQMRSELKKL 182 IL +++ L RKP+ LSGGQRQRVA+GRAIVR P+VFLFDEPLSNLDA+LRV+MR E+ +L Sbjct: 120 ILKLDDYLARKPKALSGGQRQRVAIGRAIVRGPEVFLFDEPLSNLDAELRVEMRVEIARL 179 Query: 183 HHRLQATIIYVTHDQVEAMTMADKIVVMKDGEIQQIGTPHEIYNSPANVFVAGFIGSPPM 242 H + AT+IYVTHDQVEAMT+ADKIVV++ G ++Q+G P E+Y P NVFVAGFIGSP M Sbjct: 180 HKEIGATMIYVTHDQVEAMTLADKIVVLRAGRVEQVGAPLELYRDPDNVFVAGFIGSPAM 239 Query: 243 NFVNARVVRGEGGLWIQASGF-KVKVPKEFEDKLANYIDKEIIFGIRPEDIYDKLFALAP 301 NF++ R+ + +G + VP A + G+RP+ I AL P Sbjct: 240 NFLDGRIENDA----VHLAGLPPLPVPG------AAGRSGPVTVGVRPQHI-----ALEP 284 Query: 302 SPENTITGVVDVVEPLGSETILHVKVGD-DLIVASVNPRTQAKEEQKIDLVLDMTRMHAF 360 + + V++ E LG + L+++ D + E + L L R+ F Sbjct: 285 GGDGYL---VELTESLGGVSYLYLRGADGSRLTVEAGEEDPIAEGTPVGLSLAPDRVMLF 341 Query: 361 DKET 364 + ET Sbjct: 342 EAET 345 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: 323 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: 369 Length of database: 351 Length adjustment: 29 Effective length of query: 340 Effective length of database: 322 Effective search space: 109480 Effective search space used: 109480 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)
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:
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