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 WP_085123761.1 B9O00_RS16330 ABC transporter ATP-binding protein
Query= TCDB::Q9X103 (369 letters) >NCBI__GCF_900177295.1:WP_085123761.1 Length = 361 Score = 298 bits (763), Expect = 2e-85 Identities = 168/360 (46%), Positives = 227/360 (63%), Gaps = 9/360 (2%) Query: 3 MAQVVLENVTKVYENKVVAVKNANLVVEDKEFVVLLGPSGCGKTTTLRMIAGLEEITDGK 62 M V +++ K + + VA+++ +L V D EF+ LGPSGCGKTTTLRM AGLE T G+ Sbjct: 1 MVSVRYQHLHKAFGDGSVALQDFSLEVADGEFLTFLGPSGCGKTTTLRMTAGLETPTSGE 60 Query: 63 IYIDGKVVNDVEPKDRDIAMVFQNYALYPHMTVYENMAFGLKLRKYPKDEIDRRVREAAK 122 I+ + V D+ P R+IAMVFQ+YALYPHMTV +N+ + L+ + +DE RR A Sbjct: 61 IFFGERPVVDLPPGRRNIAMVFQSYALYPHMTVQQNLEYPLRKQGVARDERARRATALAA 120 Query: 123 ILGIENLLDRKPRQLSGGQRQRVAVGRAIVRNPKVFLFDEPLSNLDAKLRVQMRSELKKL 182 L ++ LL R+P+ LSGGQ+QRVA+GRA++R P+VFL DEPLSNLDA+LR QMR+EL +L Sbjct: 121 TLQLDALLHRRPKHLSGGQQQRVALGRALIREPEVFLLDEPLSNLDAELRTQMRAELIQL 180 Query: 183 HHRLQATIIYVTHDQVEAMTMADKIVVMKDGEIQQIGTPHEIYNSPANVFVAGFIGSPPM 242 H R+ T+IYVTHDQVEAMTM+ +I VM GE+QQ+GTP EIY P N FVA F+GSP M Sbjct: 181 HRRIGRTMIYVTHDQVEAMTMSTRIAVMSKGELQQVGTPLEIYREPRNRFVAAFVGSPAM 240 Query: 243 NFVNARVVRGEGGLWIQASGFKVKVPKEFEDKLANYIDKE-IIFGIRPEDIYDKLFALAP 301 NFV + +G +A+G +V +P +LA ++ GIRPE + +L P Sbjct: 241 NFVEGGIELRDGRAVFRAAGLEVALPDARSARLAGLARASGVLAGIRPEHL-----SLEP 295 Query: 302 SPENTITGVVDVVEPLGSETILHVKVGDDLIVASVNPRTQAKEEQKIDLVLDMTRMHAFD 361 G V VVE +G E I+ + IV A + L +D ++H FD Sbjct: 296 GSGE---GRVLVVEAMGHEDIVTAETPAGRIVVRSAGTATAAAGDLVPLRVDPEKLHLFD 352 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: 329 Number of extensions: 11 Number of successful extensions: 2 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: 361 Length adjustment: 30 Effective length of query: 339 Effective length of database: 331 Effective search space: 112209 Effective search space used: 112209 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 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