SitesBLAST
Comparing BWI76_RS20790 BWI76_RS20790 aldehyde dehydrogenase 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)
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)
46% identity, 100% coverage: 1:466/467 of query aligns to 1:463/464 of Q9XDN1
- 1:10 (vs. 1:10, 30% identical) mutation Missing: Much less protein associates with BMCs, no effect on enzyme activity.
- 1:14 (vs. 1:14, 29% identical) mutation Missing: Much less protein associates with BMCs, no effect on enzyme activity.
- 1:18 (vs. 1:17, 22% identical) Targets protein to the BMC
- 2:18 (vs. 2:17, 18% identical) mutation Missing: No longer interacts with PduA.
- E7 (= E7) mutation to A: Substantially decreased protein levels in BMCs, no change in enzyme activity.
- I10 (≠ V10) mutation to A: Substantially decreased protein levels in BMCs, no change in enzyme activity.
- L14 (= L14) mutation to A: Substantially decreased protein levels in BMCs, no change in enzyme activity.
4c3sA Structure of a propionaldehyde dehydrogenase from the clostridium phytofermentans fucose utilisation bacterial microcompartment (see paper)
44% identity, 94% coverage: 29:466/467 of query aligns to 1:434/435 of 4c3sA
- active site: T110 (= T136), A208 (= A235), C242 (= C269)
- binding nicotinamide-adenine-dinucleotide: I106 (≠ V132), T107 (= T133), P108 (= P134), C109 (≠ S135), H135 (= H161), L171 (≠ I197), T189 (= T215), G190 (= G216), G191 (= G217), V194 (= V220), A208 (= A235), G209 (= G236), C242 (= C269), E330 (= E362), M332 (= M364), H360 (= H392), T405 (= T437), I406 (= I438)
5jfmA Crystal structure of rhodopseudomonas palustris propionaldehyde dehydrogenase with bound propionyl-coa (see paper)
46% identity, 93% coverage: 31:466/467 of query aligns to 4:438/439 of 5jfmA
- active site: T113 (= T136), A211 (= A235), C245 (= C269)
- binding propionyl Coenzyme A: I109 (≠ V132), T110 (= T133), T113 (= T136), N114 (= N137), S136 (≠ A159), P137 (= P160), H138 (= H161), I174 (= I197), T192 (= T215), G193 (= G216), G194 (= G217), P244 (≠ I268), C245 (= C269)
5jfmB Crystal structure of rhodopseudomonas palustris propionaldehyde dehydrogenase with bound propionyl-coa (see paper)
46% identity, 93% coverage: 31:466/467 of query aligns to 17:451/452 of 5jfmB
- active site: T126 (= T136), A224 (= A235), C258 (= C269)
- binding coenzyme a: I122 (≠ V132), P124 (= P134), T125 (≠ S135), T126 (= T136), N127 (= N137), P150 (= P160), H151 (= H161), S186 (≠ D196), I187 (= I197), T190 (≠ A200), T205 (= T215), G206 (= G216), G207 (= G217), T308 (≠ R323)
5jflA Crystal structure of rhodopseudomonas palustris propionaldehyde dehydrogenase with bound NAD+ (see paper)
46% identity, 93% coverage: 31:466/467 of query aligns to 5:439/440 of 5jflA
- active site: T114 (= T136), A212 (= A235), C246 (= C269)
- binding nicotinamide-adenine-dinucleotide: I110 (≠ V132), T111 (= T133), P112 (= P134), T113 (≠ S135), T114 (= T136), H139 (= H161), I175 (= I197), T193 (= T215), G194 (= G216), I198 (≠ V220), A212 (= A235), G213 (= G236), A214 (= A237), C246 (= C269), E335 (= E362), H365 (= H392), F409 (≠ M436), T410 (= T437), I411 (= I438)
6gvsA Engineered glycolyl-coa reductase comprising 8 mutations with bound NADP+ (see paper)
45% identity, 93% coverage: 31:466/467 of query aligns to 6:440/441 of 6gvsA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P113 (= P134), T114 (≠ S135), H140 (= H161), R176 (≠ I197), T194 (= T215), G195 (= G216), G196 (= G217), L199 (≠ V220), A213 (= A235), G214 (= G236), A215 (= A237), C247 (= C269), E336 (= E362), H366 (= H392), I412 (= I438)
5dbvA Structure of a c269a mutant of propionaldehyde dehydrogenase from the clostridium phytofermentans fucose utilisation bacterial microcompartment (see paper)
43% identity, 94% coverage: 30:466/467 of query aligns to 1:430/431 of 5dbvA
- active site: T109 (= T136), G208 (= G236), A241 (≠ C269)
- binding coenzyme a: I105 (≠ V132), C108 (≠ S135), N132 (≠ A159), P133 (= P160), H134 (= H161), G189 (= G216), G190 (= G217), V193 (= V220), A241 (≠ C269), K245 (= K273), R290 (= R323), E326 (= E362), M328 (= M364)
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)
36% identity, 72% coverage: 74:408/467 of query aligns to 49:380/891 of P0A9Q7
- IVPTTN 110:115 (≠ VTPSTN 132:137) binding
- G195 (= G217) binding
- G213 (= G236) binding
- A267 (≠ E290) 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 (= E362) binding
- K358 (≠ Q385) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 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)
36% identity, 72% coverage: 74:408/467 of query aligns to 49:380/891 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)
36% identity, 72% coverage: 74:408/467 of query aligns to 49:380/869 of 7bvpA
- binding nicotinamide-adenine-dinucleotide: P112 (= P134), T113 (≠ S135), H139 (= H161), G194 (= G216), G195 (= G217), M198 (≠ V220), V212 (≠ A235), G213 (= G236), A214 (= A237), C246 (= C269), E335 (= E362), L337 (≠ M364), H367 (= H392)
Sites not aligning to the query:
- binding nicotinamide-adenine-dinucleotide: 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)
36% identity, 72% coverage: 74:408/467 of query aligns to 49:380/869 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
5j7iC Crystal structure of a geobacillus thermoglucosidasius acetylating aldehyde dehydrogenase in complex with adp (see paper)
31% identity, 84% coverage: 36:427/467 of query aligns to 18:408/455 of 5j7iC
5j7iB Crystal structure of a geobacillus thermoglucosidasius acetylating aldehyde dehydrogenase in complex with adp (see paper)
31% identity, 84% coverage: 36:427/467 of query aligns to 19:409/456 of 5j7iB
8cekA Succinyl-coa reductase from clostridium kluyveri (sucd) with NADPH (see paper)
29% identity, 86% coverage: 35:437/467 of query aligns to 2:405/449 of 8cekA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P106 (= P134), I107 (≠ S135), H133 (= H161), P134 (= P162), T185 (= T215), G186 (= G216), G187 (= G217), R190 (≠ V220), V204 (≠ A235), C238 (= C269), E328 (= E362)
Sites not aligning to the query:
8cejC Succinyl-coa reductase from clostridium kluyveri (sucd) with mesaconyl-c1-coa (see paper)
29% identity, 86% coverage: 35:437/467 of query aligns to 2:405/449 of 8cejC
- binding Mesaconyl Coenzme A: K66 (vs. gap), P106 (= P134), T108 (= T136), N109 (= N137), A131 (= A159), P132 (= P160), H133 (= H161), P134 (= P162), R169 (≠ I197), G189 (≠ A219), R190 (≠ V220), I237 (= I268), C238 (= C269), S239 (≠ A270), T391 (≠ I423), G394 (≠ L426), T405 (= T437)
Sites not aligning to the query:
8cejA Succinyl-coa reductase from clostridium kluyveri (sucd) with mesaconyl-c1-coa (see paper)
29% identity, 86% coverage: 35:437/467 of query aligns to 2:405/449 of 8cejA
Sites not aligning to the query:
7w5nA The crystal structure of the reduced form of gluconobacter oxydans wsh-004 sndh (see paper)
25% identity, 69% coverage: 114:433/467 of query aligns to 135:462/492 of 7w5nA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: W156 (≠ S135), K180 (≠ A159), A182 (≠ K165), T212 (≠ P195), G213 (≠ D196), G217 (≠ A200), F231 (≠ V214), G233 (= G216), S234 (vs. gap), V237 (vs. gap), Q337 (≠ L305), E388 (= E362), F390 (≠ M364)
2esdA Crystal structure of thioacylenzyme intermediate of an NADP dependent aldehyde dehydrogenase (see paper)
27% identity, 59% coverage: 118:391/467 of query aligns to 135:405/474 of 2esdA
- active site: N153 (≠ T136), K176 (≠ A159), A249 (= A235), C283 (= C269), E376 (= E351)
- binding glyceraldehyde-3-phosphate: Y154 (≠ N137), R282 (≠ I268), C283 (= C269), T284 (≠ A270)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: F152 (≠ S135), K176 (≠ A159), P178 (= P162), T179 (≠ A163), G209 (≠ D196), G213 (≠ A200), D214 (≠ Q201), F227 (≠ V214), S230 (≠ G217), I233 (≠ V220), K328 (vs. gap), S329 (vs. gap), Y332 (vs. gap)
Sites not aligning to the query:
Q59931 NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Glyceraldehyde-3-phosphate dehydrogenase [NADP(+)]; Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase; Triosephosphate dehydrogenase; EC 1.2.1.9 from Streptococcus mutans serotype c (strain ATCC 700610 / UA159) (see 3 papers)
27% identity, 59% coverage: 118:391/467 of query aligns to 136:406/475 of Q59931
- S151 (≠ T133) binding
- K177 (≠ A159) binding
- T180 (≠ A163) binding
- D215 (≠ Q201) binding
- 230:251 (vs. 216:236, 18% identical) binding
- E377 (= E362) binding
Sites not aligning to the query:
3rhhD Crystal structure of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from bacillus halodurans c-125 complexed with NADP
27% identity, 63% coverage: 107:402/467 of query aligns to 119:416/480 of 3rhhD
- active site: N155 (≠ T136), K178 (≠ A159), E251 (≠ A234), C285 (= C269), E378 (= E351)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I151 (≠ V132), P153 (= P134), F154 (≠ S135), K178 (≠ A159), P179 (= P160), A180 (= A164), T181 (≠ K165), G211 (≠ D196), G215 (≠ A200), D216 (≠ Q201), F229 (≠ V214), G231 (= G216), G232 (= G217), T235 (≠ V220)
Sites not aligning to the query:
Query Sequence
>BWI76_RS20790 BWI76_RS20790 aldehyde dehydrogenase
MNQQDIEQVVKAVLLKMTDSSKPDSTVHEMGVFASLDDAVAAAKVAQQGLKSVAMRQLAI
HAIREAGEKYARELAELAVSETGMGRVEDKFAKNVAQARGTPGVECLSPQVLTGDNGLTL
IENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAIMLLNQAVI
AAGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTGGEAVVESARKHTNKRLIAAGAGNP
PVVVDETADLARAAQSIVKGASFDNNIICADEKVLIVVDSVADELMRLMEGQQAVKLTAA
QAEQLQPVLLKNIDERGKGTVSRDWVGRDAGKIAAAIGLNVPPQTRLLFVETPASHPFAV
TELMMPVLPVVRVANVDEAIALAVQLEGGCHHTAAMHSRNIDNMNQMANAIDTSIFVKNG
PCIAGLGLGGEGWTTMTITTPTGEGVTSARTFVRLRRCVLVDAFRIV
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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