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 GFF4122 HP15_4062 spermidine/putrescine ABC transporter, ATP-binding protein
Query= TCDB::Q9X103 (369 letters) >FitnessBrowser__Marino:GFF4122 Length = 373 Score = 255 bits (651), Expect = 2e-72 Identities = 139/337 (41%), Positives = 212/337 (62%), Gaps = 13/337 (3%) Query: 1 MRMAQVVLENVTKVYENKVVAVKNANLVVEDKEFVVLLGPSGCGKTTTLRMIAGLEEITD 60 M+ + L N++K + K V + +L + D EF+ LLGPSGCGKTT LR++AG E + Sbjct: 1 MKQTLLSLSNLSKQFGGKTV-LDGLDLEIYDGEFITLLGPSGCGKTTLLRLMAGFEHPDE 59 Query: 61 GKIYIDGKVVNDVEPKDRDIAMVFQNYALYPHMTVYENMAFGLKLRKYPKDEIDRRVREA 120 G I + G+ + P++R + VFQ+YAL+PHM+V++N+A+GLK+ K PKDEI +RV EA Sbjct: 60 GTITLAGENLTHTAPENRPLNTVFQHYALFPHMSVFDNVAYGLKMEKRPKDEIRQRVDEA 119 Query: 121 AKILGIENLLDRKPRQLSGGQRQRVAVGRAIVRNPKVFLFDEPLSNLDAKLRVQMRSELK 180 ++ +++ RKP QLSGGQ+QRVA+ RA+V+ P++ L DEPLS LD KLR M+ ELK Sbjct: 120 LAMVQLQDFARRKPHQLSGGQQQRVAIARAVVKRPRLLLLDEPLSALDYKLRRTMQVELK 179 Query: 181 KLHHRLQATIIYVTHDQVEAMTMADKIVVMKDGEIQQIGTPHEIYNSPANVFVAGFIGSP 240 +L L T ++VTHDQ EA++M+D++VV+KDG +QQ+GTP E+Y PAN+F A F+G Sbjct: 180 RLQRELGITFVFVTHDQEEALSMSDRVVVLKDGLVQQLGTPREVYERPANLFTARFVGE- 238 Query: 241 PMNFVNARVVR-GEGGLWIQASGFKVKVPKEFEDKLANYIDKEIIFGIRPEDIYDKLFAL 299 NF V +G + + G K + + ++ + +RPEDI L Sbjct: 239 -TNFFPGTVESVQDGSIKVDVFGLKRTLRR---PDFPVQAEQSLHVLLRPEDIR----VL 290 Query: 300 APSPENTITGVVDVVEPLGS--ETILHVKVGDDLIVA 334 P EN + G + GS ++++H+ G +++ + Sbjct: 291 EPDDENGVAGKIVERNYKGSTLDSVIHLADGTEVLAS 327 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: 369 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: 373 Length adjustment: 30 Effective length of query: 339 Effective length of database: 343 Effective search space: 116277 Effective search space used: 116277 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