SitesBLAST
Comparing BWI76_RS03590 FitnessBrowser__Koxy:BWI76_RS03590 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
5j7iC Crystal structure of a geobacillus thermoglucosidasius acetylating aldehyde dehydrogenase in complex with adp (see paper)
49% identity, 84% coverage: 5:452/533 of query aligns to 5:451/455 of 5j7iC
5j7iB Crystal structure of a geobacillus thermoglucosidasius acetylating aldehyde dehydrogenase in complex with adp (see paper)
49% identity, 84% coverage: 5:452/533 of query aligns to 6:452/456 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)
46% identity, 80% coverage: 17:445/533 of query aligns to 12:444/891 of P0A9Q7
- IVPTTN 110:115 (≠ LVPSTN 115:120) binding
- G195 (= G200) binding
- G213 (= G218) binding
- A267 (≠ E272) 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 (= E341) binding
- K358 (≠ E364) modified: N6-acetyllysine
- L419 (= L420) 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)
46% identity, 80% coverage: 17:445/533 of query aligns to 12:444/891 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)
46% identity, 80% coverage: 17:445/533 of query aligns to 12:444/869 of 7bvpA
- binding nicotinamide-adenine-dinucleotide: P112 (= P117), T113 (≠ S118), H139 (= H144), G194 (= G199), G195 (= G200), M198 (= M203), V212 (≠ G217), G213 (= G218), A214 (≠ P219), C246 (= C251), E335 (= E341), L337 (= L343), H367 (= H373), T418 (= T419), L419 (= L420)
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)
46% identity, 80% coverage: 17:445/533 of query aligns to 12:444/869 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
8cekA Succinyl-coa reductase from clostridium kluyveri (sucd) with NADPH (see paper)
36% identity, 81% coverage: 15:447/533 of query aligns to 4:434/449 of 8cekA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P106 (= P117), I107 (≠ S118), H133 (= H144), P134 (= P145), T185 (= T198), G186 (= G199), G187 (= G200), R190 (≠ M203), V204 (≠ G217), C238 (= C251), E328 (= E341), L407 (= L420)
8cejC Succinyl-coa reductase from clostridium kluyveri (sucd) with mesaconyl-c1-coa (see paper)
36% identity, 81% coverage: 15:447/533 of query aligns to 4:434/449 of 8cejC
- binding Mesaconyl Coenzme A: K66 (≠ A77), P106 (= P117), T108 (= T119), N109 (= N120), A131 (≠ S142), P132 (= P143), H133 (= H144), P134 (= P145), R169 (≠ L180), G189 (= G202), R190 (≠ M203), I237 (= I250), C238 (= C251), S239 (≠ A252), T391 (≠ A404), G394 (= G407), T405 (≠ L418), L407 (= L420)
8cejA Succinyl-coa reductase from clostridium kluyveri (sucd) with mesaconyl-c1-coa (see paper)
36% identity, 81% coverage: 15:447/533 of query aligns to 4:434/449 of 8cejA
4c3sA Structure of a propionaldehyde dehydrogenase from the clostridium phytofermentans fucose utilisation bacterial microcompartment (see paper)
32% identity, 76% coverage: 7:412/533 of query aligns to 1:403/435 of 4c3sA
- active site: T110 (= T119), A208 (≠ G217), C242 (= C251)
- binding nicotinamide-adenine-dinucleotide: I106 (≠ L115), T107 (≠ V116), P108 (= P117), C109 (≠ S118), H135 (= H144), L171 (= L180), T189 (= T198), G190 (= G199), G191 (= G200), V194 (≠ M203), A208 (≠ G217), G209 (= G218), C242 (= C251), E330 (= E341), M332 (≠ L343), H360 (= H373)
Sites not aligning to the query:
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)
34% identity, 65% coverage: 37:381/533 of query aligns to 60:397/464 of Q9XDN1
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.
- 7 E→A: Substantially decreased protein levels in BMCs, no change in enzyme activity.
- 10 I→A: Substantially decreased protein levels in BMCs, no change in enzyme activity.
- 14 L→A: Substantially decreased protein levels in BMCs, no change in enzyme activity.
5dbvA Structure of a c269a mutant of propionaldehyde dehydrogenase from the clostridium phytofermentans fucose utilisation bacterial microcompartment (see paper)
32% identity, 74% coverage: 18:412/533 of query aligns to 11:399/431 of 5dbvA
- active site: T109 (= T119), G208 (= G218), A241 (≠ C251)
- binding coenzyme a: I105 (≠ L115), C108 (≠ S118), N132 (≠ S142), P133 (= P143), H134 (= H144), G189 (= G199), G190 (= G200), V193 (≠ M203), A241 (≠ C251), K245 (≠ Q255), R290 (≠ P300), E326 (= E341), M328 (≠ L343)
5jfmB Crystal structure of rhodopseudomonas palustris propionaldehyde dehydrogenase with bound propionyl-coa (see paper)
32% identity, 67% coverage: 52:410/533 of query aligns to 62:413/452 of 5jfmB
- active site: T126 (= T119), A224 (≠ G217), C258 (= C251)
- binding coenzyme a: I122 (≠ L115), P124 (= P117), T125 (≠ S118), T126 (= T119), N127 (= N120), P150 (= P143), H151 (= H144), S186 (≠ T179), I187 (≠ L180), T190 (= T183), T205 (= T198), G206 (= G199), G207 (= G200), T308 (≠ P300)
5jfmA Crystal structure of rhodopseudomonas palustris propionaldehyde dehydrogenase with bound propionyl-coa (see paper)
32% identity, 67% coverage: 52:410/533 of query aligns to 49:400/439 of 5jfmA
- active site: T113 (= T119), A211 (≠ G217), C245 (= C251)
- binding propionyl Coenzyme A: I109 (≠ L115), T110 (≠ V116), T113 (= T119), N114 (= N120), S136 (= S142), P137 (= P143), H138 (= H144), I174 (≠ L180), T192 (= T198), G193 (= G199), G194 (= G200), P244 (≠ I250), C245 (= C251)
5jflA Crystal structure of rhodopseudomonas palustris propionaldehyde dehydrogenase with bound NAD+ (see paper)
32% identity, 67% coverage: 52:410/533 of query aligns to 50:401/440 of 5jflA
- active site: T114 (= T119), A212 (≠ G217), C246 (= C251)
- binding nicotinamide-adenine-dinucleotide: I110 (≠ L115), T111 (≠ V116), P112 (= P117), T113 (≠ S118), T114 (= T119), H139 (= H144), I175 (≠ L180), T193 (= T198), G194 (= G199), I198 (≠ M203), A212 (≠ G217), G213 (= G218), A214 (≠ P219), C246 (= C251), E335 (≠ K342), H365 (= H373)
Sites not aligning to the query:
6gvsA Engineered glycolyl-coa reductase comprising 8 mutations with bound NADP+ (see paper)
33% identity, 62% coverage: 52:381/533 of query aligns to 51:374/441 of 6gvsA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P113 (= P117), T114 (≠ S118), H140 (= H144), R176 (≠ L180), T194 (= T198), G195 (= G199), G196 (= G200), L199 (≠ M203), A213 (≠ G217), G214 (= G218), A215 (≠ P219), C247 (= C251), E336 (≠ K342), H366 (= H373)
Sites not aligning to the query:
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
28% identity, 36% coverage: 100:291/533 of query aligns to 130:322/494 of 5izdA
- active site: N149 (≠ T119), K172 (≠ S142), E247 (≠ G217), C281 (= C251)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (= L115), T146 (≠ V116), W148 (≠ S118), K172 (≠ S142), P173 (= P143), S174 (≠ H144), S175 (vs. gap), R204 (≠ L178), G205 (≠ T179), G209 (≠ T183), D210 (≠ S184), G225 (= G199), S226 (vs. gap), T229 (vs. gap)
Sites not aligning to the query:
3rhdA Crystal structure of glyceraldehyde-3-phosphate dehydrogenase gapn from methanocaldococcus jannaschii dsm 2661 complexed with NADP
24% identity, 48% coverage: 10:266/533 of query aligns to 24:282/456 of 3rhdA
- active site: N133 (≠ T119), H156 (≠ S142), E233 (≠ I215), C267 (= C251)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I129 (≠ L115), T130 (≠ V116), F132 (≠ S118), H156 (≠ S142), S158 (≠ H144), S159 (≠ P145), K160 (≠ G146), G193 (≠ T179), E194 (≠ L180), G197 (≠ T183), D198 (≠ S184), F211 (≠ A197), S214 (vs. gap), V217 (vs. gap)
Sites not aligning to the query:
6fkuA Structure and function of aldehyde dehydrogenase from thermus thermophilus: an enzyme with an evolutionarily-distinct c-terminal arm (recombinant protein with shortened c-terminal, in complex with NADP) (see paper)
24% identity, 50% coverage: 108:375/533 of query aligns to 148:410/511 of 6fkuA
- active site: N159 (≠ T119), E261 (≠ S216), C295 (= C251)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I155 (≠ L115), T156 (≠ V116), N159 (≠ T119), K182 (≠ S142), S184 (≠ H144), E185 (≠ P145), G214 (vs. gap), G215 (vs. gap), K216 (vs. gap), G220 (≠ S176), Q221 (= Q177), F237 (vs. gap), T238 (vs. gap), G239 (vs. gap), S240 (vs. gap), V243 (vs. gap), E261 (≠ S216), L262 (≠ G217), C295 (= C251), R342 (≠ K305), F343 (≠ T306), E404 (= E369), F406 (≠ L371)
Sites not aligning to the query:
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
31% identity, 31% coverage: 108:270/533 of query aligns to 143:306/486 of 4pxlA
- active site: N154 (≠ T119), K177 (≠ S142), E253 (vs. gap), C287 (= C251)
- binding nicotinamide-adenine-dinucleotide: I150 (≠ L115), V151 (= V116), P152 (= P117), W153 (≠ S118), K177 (≠ S142), E180 (≠ R148), G210 (≠ T179), G214 (≠ T183), A215 (≠ S184), F228 (≠ A197), G230 (= G199), S231 (vs. gap), V234 (vs. gap), E253 (vs. gap), G255 (= G217), C287 (= C251)
Sites not aligning to the query:
Query Sequence
>BWI76_RS03590 FitnessBrowser__Koxy:BWI76_RS03590
MIELDNDLQSRQNARELVRNAKKAQAILATFSQQQIDAIVKNVAQEAAHHAEALAKMAAE
ETGFGNWQDKVLKNRFASLRVYDAIKDMKTVGIIHDDQVQKVMDVGVPLGVICALVPSTN
PTSTVIYKTLIALKAGNAIIFSPHPGARQCSWKAIEIVKRAAEAAGAPAGSVDAISQLTL
EATSELMHSKDVSLILATGGEGMVRAAYASGTPTISGGPGNGPAFIERSADIPHAVKDII
TSKTFDNGVICASEQSIIVERCIYDEVHRELEAQGAYFMNESEAAKMAALLLRPNGTINP
KVVGKTALYLSQMAGFCVPASTRVLIAEQTTVSHTNPYSREKLCPVLGLYVEEDWKAACQ
RVVELLTNEGLGHTLVIHTRNQDVIRQFCLEKPVNRILINTPAALGGIGATTNITPALTL
GCGAVGGGSSSDNVGPMNLLNIRKVGYGVRSIDELRAPGSRPEPQPIIVSPAAGPNRSIF
DDERFNAPAAAATAAHPASADDRFATAAVGAESEINEQNVERVIRQVLERLGK
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