SitesBLAST
Comparing CA265_RS00955 FitnessBrowser__Pedo557:CA265_RS00955 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)
1pz1A Structure of NADPH-dependent family 11 aldo-keto reductase akr11b(holo) (see paper)
39% identity, 92% coverage: 1:300/327 of query aligns to 1:286/333 of 1pz1A
- active site: D52 (= D52), Y57 (= Y57), K90 (≠ D89), Q93 (≠ N92), H125 (= H142)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), W21 (≠ F21), Q175 (= Q192), Y203 (= Y220), G204 (≠ S221), L206 (≠ M223), R208 (= R225), K214 (= K231), G280 (= G294), R282 (= R296), Q286 (= Q300)
P80874 Aldo-keto reductase YhdN; AKR11B; General stress protein 69; GSP69; EC 1.1.1.- from Bacillus subtilis (strain 168) (see paper)
39% identity, 92% coverage: 1:300/327 of query aligns to 1:286/331 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, 98% coverage: 1:321/327 of query aligns to 1:306/310 of P46336
1pz0A Structure of NADPH-dependent family 11 aldo-keto reductase akr11a(holo) (see paper)
34% identity, 97% coverage: 5:321/327 of query aligns to 4:305/311 of 1pz0A
- active site: D52 (= D52), Y57 (= Y57), N91 (≠ E97), H124 (= H142)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: H124 (= H142), Q174 (= Q192), Y202 (= Y220), F203 (≠ S221), P204 (= P222), L205 (≠ M223), S207 (≠ R225), G208 (= G226), A211 (≠ S229), K213 (= K231)
6ow0A Crystal structure of mithramycin 3-side chain keto-reductase mtmw in complex with NAD+ and peg (see paper)
31% identity, 99% coverage: 1:325/327 of query aligns to 1:317/323 of 6ow0A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), L21 (≠ F21), D49 (= D52), Y54 (= Y57), S151 (= S172), Y204 (= Y220), F205 (≠ S221), L207 (≠ M223), Q209 (≠ R225), G210 (= G226), T213 (≠ S229), K215 (= K231), R227 (≠ H243), V284 (≠ L292), G286 (= G294), Q292 (= Q300), N296 (= N304)
P77256 NADH-specific methylglyoxal reductase; AKR11B2; EC 1.1.1.- from Escherichia coli (strain K12) (see paper)
32% identity, 96% coverage: 1:313/327 of query aligns to 1:310/326 of P77256
- D232 (≠ K235) 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.
6ow0B Crystal structure of mithramycin 3-side chain keto-reductase mtmw in complex with NAD+ and peg (see paper)
31% identity, 99% coverage: 1:325/327 of query aligns to 1:293/301 of 6ow0B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), L21 (≠ F21), Y50 (= Y57), H117 (= H142), S147 (= S172), Y200 (= Y220), F201 (≠ S221), L203 (≠ M223), Q205 (≠ R225), T209 (≠ S229), Q268 (= Q300), N272 (= N304)
Q3L181 Perakine reductase; EC 1.1.1.317 from Rauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum) (see paper)
32% identity, 98% coverage: 1:320/327 of query aligns to 1:305/337 of Q3L181
- D52 (= D52) mutation to A: 99% loss of activity.
- Y57 (= Y57) mutation to A: 99% loss of activity.
- K84 (= K83) mutation to A: Total loss of activity.
- H126 (= H142) mutation to A: 98% loss of activity.
5danA Crystal structure of a novel aldo keto reductase tm1743 from thermotoga maritima in complex with NADP+
30% identity, 98% coverage: 1:321/327 of query aligns to 1:271/274 of 5danA
- active site: D53 (= D52), Y58 (= Y57), K84 (= K83), H117 (= H142)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), T20 (≠ A20), W21 (≠ F21), D53 (= D52), Y58 (= Y57), H117 (= H142), Q169 (= Q192), Y198 (= Y220), S199 (= S221), P200 (= P222), L201 (≠ M223), R203 (= R225), Y226 (≠ A275), I242 (≠ V291), P243 (≠ L292), K244 (≠ A293), G246 (≠ A295), R247 (= R296), H250 (≠ Q300), E253 (≠ S303), N254 (= N304)
6kiyA Crystal structure of a thermostable aldo-keto reductase tm1743 in complex with inhibitor epalrestat (see paper)
30% identity, 98% coverage: 1:321/327 of query aligns to 2:272/275 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 (≠ F21), Y59 (= Y57), W87 (= W88), H118 (= H142), R204 (= R225)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G19), T21 (≠ A20), W22 (≠ F21), Y59 (= Y57), H118 (= H142), N149 (= N173), Q170 (= Q192), Y199 (= Y220), S200 (= S221), P201 (= P222), L202 (≠ M223), R204 (= R225), T205 (≠ G226), Y227 (≠ A275), I243 (≠ V291), P244 (≠ L292), K245 (≠ A293), G247 (≠ A295), R248 (= R296), H251 (≠ Q300), E254 (≠ S303), N255 (= N304)
6kikA Crystal structure of a thermostable aldo-keto reductase tm1743 in complex with inhibitor tolrestat (see paper)
30% identity, 98% coverage: 1:321/327 of query aligns to 2:272/275 of 6kikA
3v0sA Crystal structure of perakine reductase, founder member of a novel akr subfamily with unique conformational changes during NADPH binding (see paper)
31% identity, 98% coverage: 1:320/327 of query aligns to 1:273/287 of 3v0sA
- active site: D45 (= D52), Y50 (= Y57), G87 (≠ N93), H119 (= H142)
- binding 2'-monophosphoadenosine-5'-diphosphate: S198 (= S221), P199 (= P222), I200 (≠ M223), G201 (≠ E224), L204 (= L227), P246 (≠ A293), G247 (= G294), T248 (≠ A295), T249 (≠ R296), N253 (≠ Q300), N256 (≠ S303), N257 (= N304)
4wghA Crystal structure of aldo/keto reductase from klebsiella pneumoniae in complex with NADP and acetate at 1.8 a resolution
29% identity, 94% coverage: 13:321/327 of query aligns to 13:268/283 of 4wghA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), T20 (≠ A20), W21 (≠ F21), D49 (= D52), Y54 (= Y57), N142 (= N173), Q164 (= Q192), Y192 (= Y220), C193 (≠ S221), P194 (= P222), L195 (≠ M223), Q197 (≠ K239), A198 (= A240), R200 (≠ D242), A223 (= A275), I239 (≠ L292), P240 (≠ A293), K241 (≠ G294), A242 (= A295), A243 (≠ R296), S244 (≠ N297), H247 (≠ Q300), N251 (= N304)
6ciaA Crystal structure of aldo-keto reductase from klebsiella pneumoniae in complex with NADPH.
29% identity, 94% coverage: 13:321/327 of query aligns to 14:269/284 of 6ciaA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G20 (= G19), T21 (≠ A20), W22 (≠ F21), D50 (= D52), Y55 (= Y57), H113 (= H142), N143 (= N173), Q165 (= Q192), Y193 (= Y220), C194 (≠ S221), P195 (= P222), L196 (≠ M223), Q198 (≠ K239), A199 (= A240), A224 (= A275), I240 (≠ L292), P241 (≠ A293), K242 (≠ G294), A243 (= A295), A244 (≠ R296), S245 (≠ N297), H248 (≠ Q300), N252 (= N304)
Q9P7U2 Putative aryl-alcohol dehydrogenase C977.14c; EC 1.1.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
29% identity, 98% coverage: 3:321/327 of query aligns to 9:339/351 of Q9P7U2
- S113 (≠ G94) modified: Phosphoserine
8hw0A The structure of akr6d1
30% identity, 99% coverage: 1:325/327 of query aligns to 1:320/329 of 8hw0A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), W21 (≠ F21), Q27 (≠ M27), D49 (= D52), Y54 (= Y57), R123 (≠ W143), S152 (= S172), Q178 (= Q192), W207 (≠ Y220), S208 (= S221), P209 (= P222), L210 (≠ M223), S212 (≠ R225), K218 (= K231), S227 (≠ A240), R228 (≠ D241), I285 (≠ L292), G287 (= G294), S289 (≠ R296), Q293 (= Q300), D296 (≠ S303), N297 (= N304)
6hg6A Clostridium beijerinckii aldo-keto reductase cbei_3974 with NADPH (see paper)
29% identity, 98% coverage: 1:321/327 of query aligns to 12:308/313 of 6hg6A
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G30 (= G19), W32 (≠ F21), D60 (= D52), Y65 (= Y57), H137 (= H142), Q192 (= Q192), F221 (≠ Y220), S222 (= S221), P223 (= P222), L224 (≠ M223), L278 (= L292), I279 (≠ A293), G280 (= G294), Q286 (= Q300), E289 (≠ S303), N290 (= N304)
4aubB The complex structure of the bacterial aldo-keto reductase akr14a1 with NADP and citrate (see paper)
28% identity, 98% coverage: 1:321/327 of query aligns to 11:318/335 of 4aubB
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G29 (= G19), W31 (= W28), D59 (= D52), Y64 (= Y57), H136 (= H142), Q191 (= Q192), F220 (≠ Y220), T221 (≠ S221), P222 (= P222), L223 (≠ M223), Q225 (≠ R225), G226 (= G226), K231 (= K231), R241 (≠ D241), R244 (= R244), L288 (= L292), G290 (= G294), S292 (≠ R296), Q296 (= Q300), E299 (≠ S303), N300 (= N304)
Sites not aligning to the query:
5t79A X-ray crystal structure of a novel aldo-keto reductases for the biocatalytic conversion of 3-hydroxybutanal to 1,3-butanediol (see paper)
28% identity, 99% coverage: 1:324/327 of query aligns to 13:313/315 of 5t79A
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G31 (= G19), W33 (≠ F21), Y66 (= Y57), H138 (= H142), N169 (= N173), Q193 (= Q192), F221 (≠ Y220), S222 (= S221), L224 (≠ M223), G226 (≠ R225), T230 (≠ S229), R232 (≠ K231), S263 (≠ A275), L280 (= L292), G282 (= G294), S284 (≠ R296), Q288 (= Q300)
3eauA Voltage-dependent k+ channel beta subunit in complex with cortisone (see paper)
26% identity, 99% coverage: 3:325/327 of query aligns to 5:322/327 of 3eauA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G21 (= G19), W23 (≠ F21), Q29 (≠ N31), D51 (= D52), Y56 (= Y57), K84 (= K83), S154 (= S172), Q180 (= Q192), W209 (≠ Y220), S210 (= S221), P211 (= P222), L212 (≠ M223), A213 (≠ E224), C214 (≠ R225), G215 (= G226), K220 (= K231), R230 (≠ K235), L287 (= L292), L288 (≠ A293), G289 (= G294), S291 (≠ R296), Q295 (= Q300), E298 (≠ S303), N299 (= N304)
- binding 17,21-dihydroxypregna-1,4-diene-3,11,20-trione: W23 (≠ F21), V55 (≠ F56), Y56 (= Y57), W87 (= W88), N124 (≠ H142), R155 (≠ N173), I174 (vs. gap), I177 (≠ A189), I202 (vs. gap)
Query Sequence
>CA265_RS00955 FitnessBrowser__Pedo557:CA265_RS00955
MEYRKLGNTRLELSAIAYGAFAIGGNMWGGNEKKDSIESVKASIDNGITTIDTAPFYGFG
LSEALIGEAIKGYDRTKIQLLTKFGLVWDGSNNGAGEHFFDAQNDGKAVPIYRYATKASI
IKEVEDSLKRLHTDYIDLLQQHWPDPTTEIDEVMEAMAQLIKDGKILAAGLSNADHALLE
KAAAVNLPASNQVPFSMLNRAIQDDLIPYTLENNIGIIAYSPMERGLLSGKYFEKEKLKA
DDHRNGYFSQFDLDAVKTFLERISPLAKEKNASIAQLVLRWTTLQQGITVVLAGARNAEQ
AVSNAAAMDFEISKEELAFIDGELGKI
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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