SitesBLAST

1 modified: Initiator methionine, Removed
267 A→T: Shows aerobic growth ability on ethanol. Shows 5-6 fold increase in acetaldehyde dehydrogenase activity, but does not affect ethanol dehydrogenase activity. Shows decreased thermal enzyme stability and increased sensitivity to MCO damage. Shows increased protein stability and resistance to MCO; when associated with K-568.
335 binding
358 modified: N6-acetyllysine
419 binding
446:449 mutation Missing: Can form dimers, but does not assemble into long filaments. Strongly affects ALDH activity, but not ADH activity.
487 binding
519 binding
546:550 binding
568 E→K: Partially restores protein stability and resistance to MCO damage; when associated with T-267.
610 binding
619 binding
653 binding
657 binding
670 mutation F->A,E,V: Disrupts spirosome formation. Affects the forward activity of ALDH.
723 binding
737 binding

P0A9Q8 Bifunctional aldehyde-alcohol dehydrogenase AdhE; Alcohol dehydrogenase E; EC 1.2.1.10; EC 1.1.1.1 from Escherichia coli O157:H7 (see paper)
27% identity, 34% coverage: 116:258/420 of query aligns to 103:246/891 of P0A9Q8

query
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P0A9Q8

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Sites not aligning to the query:

487 binding
519 binding
546:550 binding
597:598 binding
638 binding
653 binding
657 binding
723 binding
737 binding

7bvpA Adhe spirosome in extended conformation (see paper)
27% identity, 34% coverage: 116:258/420 of query aligns to 103:246/869 of 7bvpA

query
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7bvpA

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binding nicotinamide-adenine-dinucleotide: P112 (≠ Y124), T113 (≠ E125), H139 (≠ G150), G194 (= G206), G195 (= G207), M198 (≠ L210), V212 (≠ G225), G213 (= G226), A214 (≠ I227), C246 (= C258)

Sites not aligning to the query:

binding nicotinamide-adenine-dinucleotide: 335, 337, 367, 418, 419, 487, 489, 519, 547, 550, 597, 598, 601, 610, 619, 646, 737
binding zinc ion: 653, 657, 723, 737

6tqmA Escherichia coli adhe structure in its compact conformation (see paper)
27% identity, 34% coverage: 116:258/420 of query aligns to 103:246/869 of 6tqmA

query
sites
6tqmA

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Sites not aligning to the query:

6gvsA Engineered glycolyl-coa reductase comprising 8 mutations with bound NADP+ (see paper)
31% identity, 35% coverage: 105:249/420 of query aligns to 94:237/441 of 6gvsA

query
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6gvsA

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binding nadp nicotinamide-adenine-dinucleotide phosphate: P113 (≠ E125), T114 (≠ A126), H140 (≠ G150), R176 (= R186), T194 (≠ R205), G195 (= G206), G196 (= G207), L199 (= L210), A213 (≠ G225), G214 (= G226), A215 (≠ I227)

Sites not aligning to the query:

binding nadp nicotinamide-adenine-dinucleotide phosphate: 247, 336, 366, 412

Query Sequence

>6938396 FitnessBrowser__SB2B:6938396
MDAQAYLLQLGQAAKSSGFALANLGVMAKNRLLGRVAAELKSAFDEILAANAKDVAAARA
SGLGDAMVDRLLLNDDRLKGIIADIDNVISLADPIGEEFDSRLLDNGMRLCRRRVPLGVI
GVIYEARPNVTVEIAVLALKTGNAVILRGGKETLESNLALAAAIRRALAGEGLPEDCVQL
IDNPDRALVTGLLKLDKFVDMIVPRGGQGLQRLCAEQATIPVILGGIGICHLYLDRDADI
SRAANVIINAKVQRPTVCNALDTLLIHRDKLDWLPTLARALQQQGVKLVACEQSLGALAA
AGIEAEAASDESFGTEWLSLTLGVKVVADIDEAIAHIRHYSSGHSEAILTDNLAAATHFM
NEVNSAAVYLNASTRFTDGGQFGFGAEVAVSTQKLHARGPMGLEALTTYKWLGVGDYSCR

Or try a new SitesBLAST search

SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory