SitesBLAST
Comparing BPHYT_RS21770 FitnessBrowser__BFirm:BPHYT_RS21770 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
8cekA Succinyl-coa reductase from clostridium kluyveri (sucd) with NADPH (see paper)
34% identity, 94% coverage: 23:473/481 of query aligns to 3:449/449 of 8cekA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P106 (= P128), I107 (≠ S129), H133 (≠ S155), P134 (= P156), T185 (= T208), G186 (= G209), G187 (≠ S210), R190 (≠ N213), V204 (= V227), C238 (= C261), E328 (= E352), L407 (≠ M432)
8cejC Succinyl-coa reductase from clostridium kluyveri (sucd) with mesaconyl-c1-coa (see paper)
34% identity, 94% coverage: 23:473/481 of query aligns to 3:449/449 of 8cejC
- binding Mesaconyl Coenzme A: K66 (= K88), P106 (= P128), T108 (= T130), N109 (= N131), A131 (= A153), P132 (= P154), H133 (≠ S155), P134 (= P156), R169 (≠ K192), G189 (≠ A212), R190 (≠ N213), I237 (≠ S260), C238 (= C261), S239 (= S262), T391 (≠ C415), G394 (= G419), T405 (≠ L430), L407 (≠ M432)
8cejA Succinyl-coa reductase from clostridium kluyveri (sucd) with mesaconyl-c1-coa (see paper)
34% identity, 94% coverage: 23:473/481 of query aligns to 3:449/449 of 8cejA
5j7iC Crystal structure of a geobacillus thermoglucosidasius acetylating aldehyde dehydrogenase in complex with adp (see paper)
35% identity, 92% coverage: 23:463/481 of query aligns to 14:450/455 of 5j7iC
5j7iB Crystal structure of a geobacillus thermoglucosidasius acetylating aldehyde dehydrogenase in complex with adp (see paper)
35% identity, 92% coverage: 23:463/481 of query aligns to 15:451/456 of 5j7iB
P0A9Q7 Bifunctional aldehyde-alcohol dehydrogenase AdhE; Alcohol dehydrogenase E; EC 1.2.1.10; EC 1.1.1.1 from Escherichia coli (strain K12) (see 8 papers)
33% identity, 90% coverage: 26:458/481 of query aligns to 12:445/891 of P0A9Q7
- IVPTTN 110:115 (≠ ITPSTN 126:131) binding
- G195 (≠ S210) binding
- G213 (= G228) binding
- A267 (≠ T282) mutation to 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.
- E335 (= E352) binding
- K358 (≠ S375) modified: N6-acetyllysine
- L419 (≠ M432) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 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)
33% identity, 90% coverage: 26:458/481 of query aligns to 12:445/891 of P0A9Q8
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)
33% identity, 90% coverage: 26:458/481 of query aligns to 12:445/869 of 7bvpA
- binding nicotinamide-adenine-dinucleotide: P112 (= P128), T113 (≠ S129), H139 (≠ S155), G194 (= G209), G195 (≠ S210), M198 (≠ N213), V212 (= V227), G213 (= G228), A214 (= A229), C246 (= C261), E335 (= E352), L337 (= L354), H367 (= H384), T418 (≠ S431), L419 (≠ M432)
Sites not aligning to the query:
- binding nicotinamide-adenine-dinucleotide: 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)
33% identity, 90% coverage: 26:458/481 of query aligns to 12:445/869 of 6tqmA
Sites not aligning to the query:
- binding fe (iii) ion: 653, 657, 723, 737
- binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: 487, 490, 545, 547, 550, 597, 603, 608, 646, 727
Q9XDN1 Propanal dehydrogenase (CoA-propanoylating); Coenzyme-A-acylating propionaldehyde dehydrogenase; Propanediol utilization protein PduP; EC 1.2.1.87 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
29% identity, 79% coverage: 18:395/481 of query aligns to 5:400/464 of Q9XDN1
- E7 (= E20) mutation to A: Substantially decreased protein levels in BMCs, no change in enzyme activity.
- I10 (≠ V23) mutation to A: Substantially decreased protein levels in BMCs, no change in enzyme activity.
- L14 (≠ V27) mutation to A: Substantially decreased protein levels in BMCs, no change in enzyme activity.
Sites not aligning to the query:
- 1:10 mutation Missing: Much less protein associates with BMCs, no effect on enzyme activity.
- 1:14 mutation Missing: Much less protein associates with BMCs, no effect on enzyme activity.
- 1:18 Targets protein to the BMC
- 2:18 mutation Missing: No longer interacts with PduA.
6gvsA Engineered glycolyl-coa reductase comprising 8 mutations with bound NADP+ (see paper)
28% identity, 72% coverage: 56:399/481 of query aligns to 44:381/441 of 6gvsA