SitesBLAST
Comparing 7026457 FitnessBrowser__ANA3:7026457 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)
4gieA Crystal structure of prostaglandin f synthase from trypanosoma cruzi bound to NADP (see paper)
38% identity, 93% coverage: 17:277/280 of query aligns to 23:285/288 of 4gieA
- active site: D55 (= D48), Y60 (= Y53), K85 (= K78), H118 (= H111)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G29 (= G23), V30 (≠ T24), W31 (≠ F25), D55 (= D48), Y60 (= Y53), K85 (= K78), H118 (= H111), W119 (= W112), S147 (= S143), N148 (= N144), Q169 (= Q166), W195 (≠ Y192), S196 (≠ M193), P197 (= P194), L198 (≠ F195), G199 (≠ A196), S200 (≠ Y197), G201 (= G198), L207 (= L201), A224 (= A218), I239 (= I233), P240 (= P234), K241 (≠ S235), S242 (= S236), T243 (= T237), R247 (≠ N241), E250 (≠ S244), N251 (= N245)
4fziA Crystal structure of prostaglandin f synthase from trypanosoma cruzi (see paper)
38% identity, 93% coverage: 17:277/280 of query aligns to 12:274/277 of 4fziA
1vbjA The crystal structure of prostaglandin f synthase from trypanosoma brucei
34% identity, 92% coverage: 17:274/280 of query aligns to 20:273/281 of 1vbjA
- active site: D52 (= D48), Y57 (= Y53), K82 (= K78), H115 (= H111)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G26 (= G23), M27 (≠ T24), W28 (≠ F25), D52 (= D48), Y57 (= Y53), K82 (= K78), H115 (= H111), W116 (= W112), S144 (= S143), N145 (= N144), Q166 (= Q166), W192 (≠ Y192), S193 (≠ M193), P194 (= P194), L195 (≠ F195), G196 (≠ A196), Q197 (≠ Y197), G198 (= G198), V201 (≠ L201), A218 (= A218), I233 (= I233), P234 (= P234), K235 (≠ S235), S236 (= S236), G237 (≠ T237), N238 (≠ K238), R241 (≠ N241), E244 (≠ S244), N245 (= N245)
Q9GV41 9,11-endoperoxide prostaglandin H2 reductase; Prostaglandin F2-alpha synthase; EC 1.1.1.- from Trypanosoma brucei brucei
34% identity, 92% coverage: 17:274/280 of query aligns to 15:268/276 of Q9GV41
P14065 Glycerol 2-dehydrogenase (NADP(+)); Galactose-inducible crystallin-like protein 1; EC 1.1.1.156 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
34% identity, 93% coverage: 17:277/280 of query aligns to 20:307/312 of P14065
- Q29 (≠ R26) mutation to K: Decreases catalytic activity.
- Y56 (= Y53) mutation to L: Loss of catalytic activity.
- K264 (≠ S235) mutation to R: Decreases catalytic activity.
- N267 (≠ K238) mutation to Q: Decreases catalytic activity.
- R270 (≠ N241) mutation R->H,Y,K: Decreases catalytic activity.
P51635 Aldo-keto reductase family 1 member A1; 3-DG-reducing enzyme; Alcohol dehydrogenase [NADP(+)]; Aldehyde reductase; Glucuronate reductase; Glucuronolactone reductase; EC 1.1.1.2; EC 1.1.1.33; EC 1.1.1.372; EC 1.1.1.54; EC 1.1.1.19; EC 1.1.1.20 from Rattus norvegicus (Rat) (see paper)
33% identity, 92% coverage: 17:273/280 of query aligns to 14:301/325 of P51635
- K23 (≠ R26) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K30 (≠ F33) Not glycated
- K34 (≠ L37) Not glycated
- K61 (≠ N64) Not glycated
- K68 (vs. gap) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K80 (= K78) Not glycated
- K85 (≠ N83) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K97 (≠ D95) Not glycated
- K127 (vs. gap) Not glycated
- K134 (≠ E123) Not glycated
- K141 (vs. gap) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K145 (vs. gap) Not glycated
- K153 (= K134) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K157 (≠ R138) Not glycated
- K240 (≠ V212) Not glycated
- K257 (≠ G229) Not glycated
- K263 (≠ S235) Not glycated
- K287 (≠ E259) Not glycated
- K294 (≠ R266) Not glycated
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylthreonine
- 13 Not glycated
- 308 Not glycated
A0QV09 Aldo-keto reductase MSMEG_2407/MSMEI_2346; AKR; AKR5H1; EC 1.1.1.- from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
37% identity, 94% coverage: 17:278/280 of query aligns to 22:280/283 of A0QV09
- G196 (≠ M193) binding
- L198 (≠ F195) binding
- V200 (≠ Y197) binding
- I236 (= I233) binding
- R238 (≠ S235) binding
- S239 (= S236) binding
- A240 (≠ T237) binding
- R244 (≠ N241) binding
- S247 (= S244) binding
- N248 (= N245) binding
- R274 (≠ N272) binding
2wzmA Crystal structure of a mycobacterium aldo-keto reductase in its apo and liganded form (see paper)
37% identity, 94% coverage: 17:278/280 of query aligns to 13:271/274 of 2wzmA
- active site: D44 (= D48), Y49 (= Y53), K74 (= K78), H107 (= H111)
- binding [(2r,3r,4r,5r)-5-(6-amino-9h-purin-9-yl)-3-hydroxy-4-(phosphonooxy)tetrahydrofuran-2-yl]methyl [(2r,3s,4s)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate: G21 (≠ F25), Y186 (= Y192), G187 (≠ M193), P188 (= P194), L189 (≠ F195), G190 (≠ A196), V191 (≠ Y197), G192 (= G198), L195 (= L201), A212 (= A218), I227 (= I233), R229 (≠ S235), S230 (= S236), A231 (≠ T237), R235 (≠ N241), N239 (= N245), R265 (≠ N272)
1a80A Native 2,5-diketo-d-gluconic acid reductase a from corynbacterium sp. Complexed with NADPH (see paper)
39% identity, 89% coverage: 16:265/280 of query aligns to 12:261/277 of 1a80A
- active site: D44 (= D48), Y49 (= Y53), K74 (= K78), H107 (= H111)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G19 (= G23), V20 (≠ T24), F21 (= F25), D44 (= D48), Y49 (= Y53), K74 (= K78), H107 (= H111), S138 (= S143), N139 (= N144), Q160 (= Q166), W186 (≠ Y192), G187 (≠ M193), P188 (= P194), L189 (≠ F195), G190 (≠ A196), Q191 (≠ Y197), F197 (≠ L201), A214 (= A218), F229 (≠ I233), P230 (= P234), K231 (≠ S235), S232 (= S236), V233 (≠ T237), R234 (≠ K238), R237 (≠ N241), E240 (≠ S244), N241 (= N245)
P06632 2,5-diketo-D-gluconic acid reductase A; 2,5-DKG reductase A; 2,5-DKGR A; 25DKGR-A; AKR5C; EC 1.1.1.346 from Corynebacterium sp. (strain ATCC 31090) (see 3 papers)
39% identity, 89% coverage: 16:265/280 of query aligns to 13:262/278 of P06632
- Y50 (= Y53) active site, Proton donor
- H108 (= H111) binding
- 188:242 (vs. 193:245, 35% identical) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1m9hA Corynebacterium 2,5-dkgr a and phe 22 replaced with tyr (f22y), lys 232 replaced with gly (k232g), arg 238 replaced with his (r238h)and ala 272 replaced with gly (a272g)in presence of nadh cofactor (see paper)
39% identity, 89% coverage: 16:265/280 of query aligns to 12:261/277 of 1m9hA
- active site: D44 (= D48), Y49 (= Y53), K74 (= K78), H107 (= H111)
- binding nicotinamide-adenine-dinucleotide: G19 (= G23), V20 (≠ T24), Y21 (≠ F25), D44 (= D48), Y49 (= Y53), H107 (= H111), W108 (= W112), S138 (= S143), N139 (= N144), Q160 (= Q166), W186 (≠ Y192), G187 (≠ M193), P188 (= P194), L189 (≠ F195), G190 (≠ A196), Q191 (≠ Y197), F197 (≠ L201), A214 (= A218), F229 (≠ I233), P230 (= P234), G231 (≠ S235), S232 (= S236), H237 (≠ N241), E240 (≠ S244), N241 (= N245)
Q9JII6 Aldo-keto reductase family 1 member A1; Alcohol dehydrogenase [NADP(+)]; Aldehyde reductase; Glucuronate reductase; Glucuronolactone reductase; EC 1.1.1.2; EC 1.1.1.33; EC 1.1.1.372; EC 1.1.1.54; EC 1.1.1.19; EC 1.1.1.20 from Mus musculus (Mouse)
31% identity, 92% coverage: 17:273/280 of query aligns to 14:301/325 of Q9JII6
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylthreonine
P14550 Aldo-keto reductase family 1 member A1; Alcohol dehydrogenase [NADP(+)]; Aldehyde reductase; Glucuronate reductase; Glucuronolactone reductase; EC 1.1.1.2; EC 1.1.1.372; EC 1.1.1.54; EC 1.1.1.19; EC 1.1.1.20 from Homo sapiens (Human) (see 3 papers)
32% identity, 92% coverage: 17:273/280 of query aligns to 14:301/325 of P14550
- Y50 (= Y53) active site, Proton donor; mutation to F: Complete loss of enzymatic activity.; mutation to H: Complete loss of enzymatic activity.
- N52 (= N55) to S: reduced activity towards daunorubicin; dbSNP:rs2229540
- E55 (≠ A58) to D: reduced activity towards daunorubicin; dbSNP:rs6690497
- K80 (= K78) Lowers pKa of active site Tyr; mutation to M: Complete loss of enzymatic activity.
- H113 (= H111) binding ; mutation to Q: Strong decrease in enzymatic activity.
- I299 (≠ A271) mutation to A: No change in enzymatic activity.; mutation to C: No change in enzymatic activity.
- V300 (≠ N272) mutation to C: No change in enzymatic activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3d3fA Crystal structure of yvgn and cofactor NADPH from bacillus subtilis (see paper)
37% identity, 92% coverage: 17:274/280 of query aligns to 16:271/275 of 3d3fA
- active site: D48 (= D48), Y53 (= Y53), K78 (= K78), H111 (= H111)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G22 (= G23), V23 (≠ T24), F24 (= F25), D48 (= D48), Y53 (= Y53), K78 (= K78), H111 (= H111), W112 (= W112), S140 (= S143), N141 (= N144), Q162 (= Q166), W188 (≠ Y192), S189 (≠ M193), P190 (= P194), L191 (≠ F195), M192 (≠ A196), Q193 (≠ Y197), G194 (= G198), L197 (= L201), A214 (= A218), I229 (= I233), P230 (= P234), K231 (≠ S235), S232 (= S236), I233 (≠ T237), K234 (= K238), R237 (≠ N241), E240 (≠ S244), N241 (= N245)
3cv7A Crystal structure of porcine aldehyde reductase ternary complex (see paper)
32% identity, 92% coverage: 17:273/280 of query aligns to 14:301/322 of 3cv7A
- active site: D45 (= D48), Y50 (= Y53), K80 (= K78), H113 (= H111)
- binding 3,5-dichloro-2-hydroxybenzoic acid: W22 (≠ F25), I49 (= I52), Y50 (= Y53), W82 (= W80), H113 (= H111), W114 (= W112)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G23), T21 (= T24), W22 (≠ F25), D45 (= D48), Y50 (= Y53), K80 (= K78), H113 (= H111), S162 (= S143), N163 (= N144), Q184 (= Q166), Y210 (= Y192), S211 (≠ M193), P212 (= P194), L213 (≠ F195), S215 (≠ Y197), D217 (vs. gap), L229 (≠ Q202), A246 (= A218), I261 (= I233), P262 (= P234), K263 (≠ S235), S264 (= S236), V265 (≠ T237), T266 (≠ K238), R269 (≠ N241), Q272 (≠ S244), N273 (= N245)
Sites not aligning to the query:
3h4gA Structure of aldehyde reductase holoenzyme in complex with potent aldose reductase inhibitor fidarestat: implications for inhibitor binding and selectivity (see paper)
33% identity, 92% coverage: 17:273/280 of query aligns to 14:301/320 of 3h4gA