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 NAD(+)
358 modified: N6-acetyllysine
419 binding NAD(+)
446:449 mutation Missing: Can form dimers, but does not assemble into long filaments. Strongly affects ALDH activity, but not ADH activity.
487 binding NAD(+)
519 binding NAD(+)
546:550 binding NAD(+)
568 E→K: Partially restores protein stability and resistance to MCO damage; when associated with T-267.
610 binding NAD(+)
619 binding NAD(+)
653 binding Fe cation
657 binding Fe cation
670 mutation F->A,E,V: Disrupts spirosome formation. Affects the forward activity of ALDH.
723 binding Fe cation
737 binding Fe cation

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)
26% identity, 36% coverage: 109:257/418 of query aligns to 101:249/891 of P0A9Q8

query
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P0A9Q8

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Sites not aligning to the query:

487 binding NAD(+)
519 binding NAD(+)
546:550 binding NAD(+)
597:598 binding NAD(+)
638 binding NAD(+)
653 binding Fe cation
657 binding Fe cation
723 binding Fe cation
737 binding Fe cation

6gvsA Engineered glycolyl-coa reductase comprising 8 mutations with bound NADP+ (see paper)
25% identity, 44% coverage: 101:283/418 of query aligns to 95:277/441 of 6gvsA

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6gvsA

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binding nadp nicotinamide-adenine-dinucleotide phosphate: P113 (= P123), T114 (≠ N124), H140 (≠ G145), R176 (= R181), T194 (≠ R200), G195 (= G201), G196 (= G202), L199 (= L205), A213 (≠ T220), G214 (= G221), A215 (≠ T222), C247 (= C253)

Sites not aligning to the query:

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

4c3sA Structure of a propionaldehyde dehydrogenase from the clostridium phytofermentans fucose utilisation bacterial microcompartment (see paper)
25% identity, 42% coverage: 108:284/418 of query aligns to 93:278/435 of 4c3sA

query
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4c3sA

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active site: T110 (≠ V125), A208 (≠ T220), C242 (= C253)
binding nicotinamide-adenine-dinucleotide: I106 (≠ S121), T107 (≠ R122), P108 (= P123), C109 (≠ N124), H135 (≠ G145), L171 (≠ R181), T189 (≠ R200), G190 (= G201), G191 (= G202), V194 (≠ L205), A208 (≠ T220), G209 (= G221), C242 (= C253)

Sites not aligning to the query:

binding nicotinamide-adenine-dinucleotide: 330, 332, 360, 405, 406

Query Sequence

>WP_005346465.1 NCBI__GCF_000173975.1:WP_005346465.1
MTTKEILTQAVTAKNAINSADTETKNKALANMADALLAHTDAILEANKQDVEAARGKISD
VMIDRLMLDAGRIEGMAKGIRELIDLDDPAGKVLRTVERPNGIVIEKTAVPMGVIAIIYE
SRPNVTSDAAALCIKSGNVCVLRSGKEAWKSANAVVTALKEGMVKSNLPGEGIQLIEDTS
RESSVELMKAVGYVDLLIPRGGPGLIRSCVENAKVPCIQTGTGICHVYVDESASFEKALQ
IIENAKTSRPSVCNAEEVLLVHSAVAEKFLPLLQKKLVEERKEKGEIPVELRLCDRAAKI
ISGTPAGADDFDTEFLDYILAVKIVDSVEEAVEHISKHSTGHSEAIITESKEAADYFTMR
VDSAAVYVNVSTRFTDGGEFGLGCEMGISTQKLHARGPMGLEELCTYKYIIRGEGQIR

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