SitesBLAST
Comparing AO356_28450 FitnessBrowser__pseudo5_N2C3_1:AO356_28450 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)
1pz1A Structure of NADPH-dependent family 11 aldo-keto reductase akr11b(holo) (see paper)
35% identity, 97% coverage: 1:326/335 of query aligns to 1:319/333 of 1pz1A
- active site: D52 (= D56), Y57 (= Y61), K90 (≠ D94), Q93 (≠ K98), H125 (= H131)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), W21 (= W21), Q175 (= Q186), Y203 (= Y214), G204 (≠ S215), L206 (= L217), R208 (≠ S219), K214 (≠ S225), G280 (= G293), R282 (= R295), Q286 (= Q299)
P80874 Aldo-keto reductase YhdN; AKR11B; General stress protein 69; GSP69; EC 1.1.1.- from Bacillus subtilis (strain 168) (see paper)
35% identity, 97% coverage: 1:326/335 of query aligns to 1:319/331 of P80874
P46336 Aldo-keto reductase IolS; AKR11A; Vegetative protein 147; VEG147; EC 1.1.1.- from Bacillus subtilis (strain 168) (see paper)
34% identity, 94% coverage: 1:316/335 of query aligns to 1:302/310 of P46336
1pz0A Structure of NADPH-dependent family 11 aldo-keto reductase akr11a(holo) (see paper)
33% identity, 97% coverage: 2:326/335 of query aligns to 1:311/311 of 1pz0A
- active site: D52 (= D56), Y57 (= Y61), N91 (≠ G89), H124 (= H131)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: H124 (= H131), Q174 (= Q186), Y202 (= Y214), F203 (≠ S215), P204 (≠ T216), L205 (= L217), S207 (= S219), G208 (= G220), A211 (≠ S223), K213 (≠ S225)
P77256 NADH-specific methylglyoxal reductase; AKR11B2; EC 1.1.1.- from Escherichia coli (strain K12) (see paper)
32% identity, 93% coverage: 1:312/335 of query aligns to 1:310/326 of P77256
- D232 (≠ E229) mutation D->A,E: Converts the protein into an enzyme with dual specificity, i.e. that is able to use both NADPH and NADH as cosubstrates.
Q3L181 Perakine reductase; EC 1.1.1.317 from Rauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum) (see paper)
28% identity, 97% coverage: 1:325/335 of query aligns to 1:311/337 of Q3L181
- D52 (= D56) mutation to A: 99% loss of activity.
- Y57 (= Y61) mutation to A: 99% loss of activity.
- K84 (= K88) mutation to A: Total loss of activity.
- H126 (= H131) mutation to A: 98% loss of activity.
5danA Crystal structure of a novel aldo keto reductase tm1743 from thermotoga maritima in complex with NADP+
32% identity, 95% coverage: 1:317/335 of query aligns to 1:268/274 of 5danA
- active site: D53 (= D56), Y58 (= Y61), K84 (= K98), H117 (= H131)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), T20 (= T20), W21 (= W21), D53 (= D56), Y58 (= Y61), H117 (= H131), Q169 (= Q186), Y198 (= Y214), S199 (= S215), P200 (≠ T216), L201 (= L217), R203 (≠ S219), Y226 (≠ A274), I242 (= I291), P243 (≠ V292), K244 (≠ G293), G246 (≠ R295), R247 (= R296), H250 (≠ Q299), E253 (≠ G302), N254 (≠ L303)
6kiyA Crystal structure of a thermostable aldo-keto reductase tm1743 in complex with inhibitor epalrestat (see paper)
32% identity, 95% coverage: 1:317/335 of query aligns to 2:269/275 of 6kiyA
- binding {5-[(2E)-2-methyl-3-phenylprop-2-en-1-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl}acetic acid: W22 (= W21), Y59 (= Y61), W87 (≠ I100), H118 (= H131), R204 (≠ S219)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G19), T21 (= T20), W22 (= W21), Y59 (= Y61), H118 (= H131), N149 (= N167), Q170 (= Q186), Y199 (= Y214), S200 (= S215), P201 (≠ T216), L202 (= L217), R204 (≠ S219), T205 (≠ G220), Y227 (≠ A274), I243 (= I291), P244 (≠ V292), K245 (≠ G293), G247 (≠ R295), R248 (= R296), H251 (≠ Q299), E254 (≠ G302), N255 (≠ L303)
6kikA Crystal structure of a thermostable aldo-keto reductase tm1743 in complex with inhibitor tolrestat (see paper)
32% identity, 95% coverage: 1:317/335 of query aligns to 2:269/275 of 6kikA
1lqaA Tas protein from escherichia coli in complex with NADPH (see paper)
30% identity, 95% coverage: 1:319/335 of query aligns to 1:334/346 of 1lqaA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), M21 (≠ W21), D48 (= D56), Y53 (= Y61), H132 (= H131), N180 (= N167), Q205 (= Q186), Y233 (= Y214), S234 (= S215), L236 (= L217), F238 (≠ S219), G239 (= G220), T242 (≠ S223), K244 (≠ E229), A254 (≠ W239), R255 (= R240), G308 (= G293), T310 (≠ R295), Q314 (= Q299), N318 (≠ L303)
P0A9T4 Protein tas from Escherichia coli (strain K12) (see paper)
30% identity, 95% coverage: 1:319/335 of query aligns to 1:334/346 of P0A9T4
- 234:244 (vs. 215:229, 33% identical) binding
8hw0A The structure of akr6d1
30% identity, 91% coverage: 1:305/335 of query aligns to 1:299/329 of 8hw0A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), W21 (= W21), Q27 (≠ A34), D49 (= D56), Y54 (= Y61), R123 (≠ W132), S152 (= S166), Q178 (vs. gap), W207 (≠ Y214), S208 (= S215), P209 (≠ T216), L210 (= L217), S212 (= S219), K218 (≠ S225), S227 (≠ R230), R228 (≠ I231), I285 (= I291), G287 (= G293), S289 (≠ R295), Q293 (= Q299), D296 (≠ G302), N297 (≠ L303)
3v0sA Crystal structure of perakine reductase, founder member of a novel akr subfamily with unique conformational changes during NADPH binding (see paper)
26% identity, 99% coverage: 1:332/335 of query aligns to 1:286/287 of 3v0sA
- active site: D45 (= D56), Y50 (= Y61), G87 (≠ A99), H119 (= H131)
- binding 2'-monophosphoadenosine-5'-diphosphate: S198 (= S215), P199 (≠ T216), I200 (≠ L217), G201 (≠ Q218), L204 (= L221), P246 (≠ V292), G247 (= G293), T248 (≠ A294), T249 (≠ R295), N253 (≠ Q299), N256 (≠ G302), N257 (≠ L303)
8jwmB Crystal structure of akrtyl-NADP-tylosin complex (see paper)
30% identity, 97% coverage: 1:324/335 of query aligns to 1:320/331 of 8jwmB
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), M21 (≠ W21), D48 (= D56), Y53 (= Y61), N161 (= N167), Q186 (= Q186), W214 (≠ Y214), S215 (= S215), P216 (≠ T216), L217 (= L217), G219 (≠ S219), G220 (= G220), R235 (= R240), R236 (≠ K241), A237 (= A242), I287 (= I291), G289 (= G293), R291 (= R295), Q295 (= Q299), S298 (≠ G302)
- binding tylosin: Y53 (= Y61), W55 (≠ L63), H130 (= H131), C192 (≠ L192), E193 (≠ M193), R195 (≠ D195), G240 (vs. gap), R241 (= R243), Q250 (≠ R251), E253 (≠ A254), Q254 (≠ N255), R257 (≠ L258), E317 (≠ P321), I318 (≠ F322), P320 (= P324)
Q9P7U2 Putative aryl-alcohol dehydrogenase C977.14c; EC 1.1.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
28% identity, 96% coverage: 6:325/335 of query aligns to 12:345/351 of Q9P7U2
- S113 (≠ T87) modified: Phosphoserine
8jwkD The second purified state crystal structure of akrtyl (see paper)
28% identity, 97% coverage: 1:324/335 of query aligns to 1:303/314 of 8jwkD
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), M21 (≠ W21), D48 (= D56), Y53 (= Y61), H130 (= H131), Q186 (= Q186), W214 (≠ Y214), S215 (= S215), P216 (≠ T216), L217 (= L217), I270 (= I291), G272 (= G293), R274 (= R295), Q278 (= Q299), S281 (≠ G302)
6ow0B Crystal structure of mithramycin 3-side chain keto-reductase mtmw in complex with NAD+ and peg (see paper)
29% identity, 96% coverage: 1:323/335 of query aligns to 1:292/301 of 6ow0B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), L21 (≠ W21), Y50 (= Y61), H117 (= H131), S147 (= S166), Y200 (= Y214), F201 (≠ S215), L203 (= L217), Q205 (≠ S219), T209 (≠ S223), Q268 (= Q299), N272 (≠ L303)
6ow0A Crystal structure of mithramycin 3-side chain keto-reductase mtmw in complex with NAD+ and peg (see paper)
29% identity, 95% coverage: 1:319/335 of query aligns to 1:312/323 of 6ow0A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), L21 (≠ W21), D49 (= D56), Y54 (= Y61), S151 (= S166), Y204 (= Y214), F205 (≠ S215), L207 (= L217), Q209 (≠ S219), G210 (= G220), T213 (≠ S223), K215 (≠ S225), R227 (= R240), V284 (≠ I291), G286 (= G293), Q292 (= Q299), N296 (≠ L303)
8jwoL Crystal structure of akrtyl-tylosin complex (see paper)
28% identity, 97% coverage: 1:324/335 of query aligns to 1:300/311 of 8jwoL
7wf3C Composite map of human kv1.3 channel in apo state with beta subunits (see paper)
28% identity, 95% coverage: 6:323/335 of query aligns to 9:322/328 of 7wf3C
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G22 (= G19), R156 (≠ N167), W210 (≠ Y214), S211 (= S215), P212 (≠ T216), L213 (= L217), C215 (≠ S219), K221 (≠ S225), R231 (≠ I231), Q296 (= Q299), E299 (≠ G302), N300 (≠ L303)
Query Sequence
>AO356_28450 FitnessBrowser__pseudo5_N2C3_1:AO356_28450
MQKNRLGSSDLLISPIGLGTWAIAGTGWEYSWGAQDDEDSLGALEYAVERGVNWIDTAAV
YGLGHAEQLVGQLLRRLPASQRPLVFTKGSLVWDPVTKAISHSLAPRSLLAEVEASLRRL
QVETIDLYQIHWPAFPADGSSEGLEKALSALATAREQGKIRAIGVSNFDVAQLKRAQAVT
EIVSLQPPYSALMRDIEQDVLPFCEQAGMGVLAYSTLQSGLLSGSMTRERIAQLPDDDWR
KARSADFQEPRLSANLALVEVLAGIGERHGVSAAAVAIAWVLRKPVVTGAIVGARRRGQV
DGLIAGAQLRLSAEEIEEIRPFLPVGMGTNVPGNA
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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