SitesBLAST
Comparing WP_068333577.1 NCBI__GCF_001650345.1:WP_068333577.1 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)
5j7iB Crystal structure of a geobacillus thermoglucosidasius acetylating aldehyde dehydrogenase in complex with adp (see paper)
46% identity, 80% coverage: 1:451/563 of query aligns to 3:452/456 of 5j7iB
5j7iC Crystal structure of a geobacillus thermoglucosidasius acetylating aldehyde dehydrogenase in complex with adp (see paper)
46% identity, 80% coverage: 1:451/563 of query aligns to 2:451/455 of 5j7iC
8uhwB The structure of the clostridium thermocellum adhe spirosome
44% identity, 80% coverage: 7:457/563 of query aligns to 1:453/859 of 8uhwB
Sites not aligning to the query:
7bvpA Adhe spirosome in extended conformation (see paper)
44% identity, 76% coverage: 16:444/563 of query aligns to 12:444/869 of 7bvpA
- binding nicotinamide-adenine-dinucleotide: P112 (= P116), T113 (≠ S117), H139 (= H143), G194 (= G198), G195 (= G199), M198 (= M202), V212 (≠ G216), G213 (= G217), A214 (≠ P218), C246 (= C250), E335 (= E340), L337 (= L342), H367 (= H372), T418 (= T418), L419 (= L419)
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)
44% identity, 76% coverage: 16:444/563 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
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)
44% identity, 76% coverage: 16:444/563 of query aligns to 12:444/891 of P0A9Q7
- IVPTTN 110:115 (≠ LVPSTN 114:119) binding NAD(+)
- G195 (= G199) binding NAD(+)
- G213 (= G217) binding NAD(+)
- A267 (≠ I271) 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 (= E340) binding NAD(+)
- K358 (≠ E363) modified: N6-acetyllysine
- L419 (= L419) binding NAD(+)
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 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)
44% identity, 76% coverage: 16:444/563 of query aligns to 12:444/891 of P0A9Q8
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
8cekA Succinyl-coa reductase from clostridium kluyveri (sucd) with NADPH (see paper)
37% identity, 77% coverage: 14:446/563 of query aligns to 4:434/449 of 8cekA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P106 (= P116), I107 (≠ S117), H133 (= H143), P134 (= P144), T185 (= T197), G186 (= G198), G187 (= G199), R190 (≠ M202), V204 (≠ G216), C238 (= C250), E328 (= E340), L407 (= L419)
8cejC Succinyl-coa reductase from clostridium kluyveri (sucd) with mesaconyl-c1-coa (see paper)
37% identity, 77% coverage: 14:446/563 of query aligns to 4:434/449 of 8cejC
- binding Mesaconyl Coenzme A: K66 (≠ A76), P106 (= P116), T108 (= T118), N109 (= N119), A131 (≠ S141), P132 (= P142), H133 (= H143), P134 (= P144), R169 (≠ M179), G189 (= G201), R190 (≠ M202), I237 (= I249), C238 (= C250), S239 (≠ A251), T391 (≠ A403), G394 (= G406), T405 (≠ L417), L407 (= L419)
8cejA Succinyl-coa reductase from clostridium kluyveri (sucd) with mesaconyl-c1-coa (see paper)
37% identity, 77% coverage: 14:446/563 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)
31% identity, 72% coverage: 2:405/563 of query aligns to 4:395/435 of 4c3sA
- active site: T110 (= T118), A208 (≠ G216), C242 (= C250)
- binding nicotinamide-adenine-dinucleotide: I106 (≠ L114), T107 (≠ V115), P108 (= P116), C109 (≠ S117), H135 (= H143), L171 (≠ M179), T189 (= T197), G190 (= G198), G191 (= G199), V194 (≠ M202), A208 (≠ G216), G209 (= G217), C242 (= C250), E330 (= E340), M332 (≠ L342), H360 (= H372)
Sites not aligning to the query:
5dbvA Structure of a c269a mutant of propionaldehyde dehydrogenase from the clostridium phytofermentans fucose utilisation bacterial microcompartment (see paper)
31% identity, 72% coverage: 2:405/563 of query aligns to 3:391/431 of 5dbvA
- active site: T109 (= T118), G208 (= G217), A241 (≠ C250)
- binding coenzyme a: I105 (≠ L114), C108 (≠ S117), N132 (≠ S141), P133 (= P142), H134 (= H143), G189 (= G198), G190 (= G199), V193 (≠ M202), A241 (≠ C250), K245 (≠ Q254), R290 (≠ P299), E326 (= E340), M328 (≠ L342)
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)
31% identity, 66% coverage: 10:380/563 of query aligns to 34:397/464 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.
5jfmB Crystal structure of rhodopseudomonas palustris propionaldehyde dehydrogenase with bound propionyl-coa (see paper)
30% identity, 64% coverage: 51:409/563 of query aligns to 62:413/452 of 5jfmB
- active site: T126 (= T118), A224 (≠ G216), C258 (= C250)
- binding coenzyme a: I122 (≠ L114), P124 (= P116), T125 (≠ S117), T126 (= T118), N127 (= N119), P150 (= P142), H151 (= H143), S186 (≠ T178), I187 (≠ M179), T190 (= T182), T205 (= T197), G206 (= G198), G207 (= G199), T308 (≠ P299)
5jflA Crystal structure of rhodopseudomonas palustris propionaldehyde dehydrogenase with bound NAD+ (see paper)
30% identity, 64% coverage: 51:409/563 of query aligns to 50:401/440 of 5jflA
- active site: T114 (= T118), A212 (≠ G216), C246 (= C250)
- binding nicotinamide-adenine-dinucleotide: I110 (≠ L114), T111 (≠ V115), P112 (= P116), T113 (≠ S117), T114 (= T118), H139 (= H143), I175 (≠ M179), T193 (= T197), G194 (= G198), I198 (≠ M202), A212 (≠ G216), G213 (= G217), A214 (≠ P218), C246 (= C250), E335 (≠ K341), H365 (= H372)
Sites not aligning to the query:
5jfmA Crystal structure of rhodopseudomonas palustris propionaldehyde dehydrogenase with bound propionyl-coa (see paper)
30% identity, 64% coverage: 51:409/563 of query aligns to 49:400/439 of 5jfmA
- active site: T113 (= T118), A211 (≠ G216), C245 (= C250)
- binding propionyl Coenzyme A: I109 (≠ L114), T110 (≠ V115), T113 (= T118), N114 (= N119), S136 (= S141), P137 (= P142), H138 (= H143), I174 (≠ M179), T192 (= T197), G193 (= G198), G194 (= G199), P244 (≠ I249), C245 (= C250)
6gvsA Engineered glycolyl-coa reductase comprising 8 mutations with bound NADP+ (see paper)
30% identity, 59% coverage: 51:383/563 of query aligns to 51:375/441 of 6gvsA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P113 (= P116), T114 (≠ S117), H140 (= H143), R176 (≠ M179), T194 (= T197), G195 (= G198), G196 (= G199), L199 (≠ M202), A213 (≠ G216), G214 (= G217), A215 (≠ P218), C247 (= C250), E336 (≠ K341), H366 (= H372)
Sites not aligning to the query:
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
25% identity, 31% coverage: 97:271/563 of query aligns to 128:302/494 of 5izdA
- active site: N149 (≠ T118), K172 (≠ S141), E247 (≠ G216), C281 (= C250)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (= L114), T146 (≠ V115), W148 (≠ S117), K172 (≠ S141), P173 (= P142), S174 (≠ H143), S175 (≠ P144), R204 (≠ L177), G205 (≠ T178), G209 (≠ T182), D210 (≠ E183), G225 (= G198), S226 (vs. gap), T229 (vs. gap)
Sites not aligning to the query:
Q9H2A2 2-aminomuconic semialdehyde dehydrogenase; Aldehyde dehydrogenase 12; Aldehyde dehydrogenase family 8 member A1; EC 1.2.1.32 from Homo sapiens (Human) (see paper)
24% identity, 47% coverage: 10:271/563 of query aligns to 47:308/487 of Q9H2A2
- R109 (≠ K69) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (≠ T118) mutation to A: Complete loss of activity.
Sites not aligning to the query:
- 451 R→A: Complete loss of activity.
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
29% identity, 31% coverage: 107:280/563 of query aligns to 143:313/486 of 4pxlA
- active site: N154 (≠ T118), K177 (≠ S141), E253 (vs. gap), C287 (= C250)
- binding nicotinamide-adenine-dinucleotide: I150 (≠ L114), V151 (= V115), P152 (= P116), W153 (≠ S117), K177 (≠ S141), E180 (≠ P144), G210 (≠ T178), G214 (≠ T182), A215 (≠ E183), F228 (≠ A196), G230 (= G198), S231 (vs. gap), V234 (vs. gap), E253 (vs. gap), G255 (= G216), C287 (= C250)
Sites not aligning to the query:
Query Sequence
>WP_068333577.1 NCBI__GCF_001650345.1:WP_068333577.1
MMLDKDLQSIQAARELVKNAKNAQRQFAKLSQQQVDKIVAHIAAEAARHAEPLAKAAHEE
TGFGRWQDKVLKNLFASTQVHEHIRDMKTVGIIADDSANKVMDVGVPLGVITALVPSTNP
TSTIFYKTLIALKAGNAIIFSPHPNAKVCSQQAIEVVKRAAQEAGAPAGIVDGVTLLTMQ
ATETLMKSKDVSLILATGGEGMVRAAYASGTPTISGGPGNGPAFIERSANVPQAVKDIIT
SKTFDNGVICASEQSIIVERCIYDQVHQELIRQGAYLMNEQESEKLAALLLRPNGMINPE
MVGQCALTVAQKAGFSVPAHTTVLVSPQTTVSPKNPYSREKLCPVLGLYVEEDWHTACAR
VMELLTNEGMGHTLVIHTQNTDIVREFALEKPVFRMLVNTPAALGGIGATSNLTPALTLG
CGALGGGSSSDNVGPMNLLNVRKVGYGVRSIEELRQPTAPAASVSAATVPACEPSYTSYQ
EPAPVAPAATNKPVSIFEDTRFTGGSPAATAPVATTSNGDDRFTSTAAPIAPANDTVKHD
ACNDISEAQVEQIIKQVMGRMAS
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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