SitesBLAST
Comparing 17089 FitnessBrowser__Keio:17089 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)
A0QV10 Aldo-keto reductase MSMEG_2408/MSMEI_2347; EC 1.1.1.- from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
51% identity, 97% coverage: 7:273/275 of query aligns to 5:271/275 of A0QV10
- K262 (= K264) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
3wbwA Crystal structure of gox0644 in complex with NADPH
51% identity, 97% coverage: 5:271/275 of query aligns to 4:267/271 of 3wbwA
- active site: D45 (= D46), Y50 (= Y51), K71 (= K76), H104 (= H107)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G20 (= G21), H104 (= H107), N136 (= N139), W183 (= W186), R184 (≠ S187), P185 (= P188), L186 (= L189), L192 (≠ F197), A209 (= A214), K226 (= K231), S227 (= S232), V228 (= V233), R232 (= R237), E235 (= E240), N236 (= N241)
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)
51% identity, 99% coverage: 1:272/275 of query aligns to 1:276/278 of P06632
- M1 (= M1) modified: Initiator methionine, Removed
- Y50 (= Y51) active site, Proton donor
- H108 (= H107) binding
- 188:242 (vs. 187:241, 49% identical) binding
1a80A Native 2,5-diketo-d-gluconic acid reductase a from corynbacterium sp. Complexed with NADPH (see paper)
51% identity, 98% coverage: 4:272/275 of query aligns to 3:275/277 of 1a80A
- active site: D44 (= D46), Y49 (= Y51), K74 (= K76), H107 (= H107)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G19 (= G21), F21 (≠ W23), D44 (= D46), Y49 (= Y51), H107 (= H107), S138 (≠ C138), Q160 (= Q160), W186 (= W186), G187 (≠ S187), P188 (= P188), L189 (= L189), Q191 (= Q191), A214 (= A214), F229 (≠ I229), K231 (= K231), S232 (= S232), V233 (= V233), R234 (≠ T234), R237 (= R237), E240 (= E240), N241 (= N241)
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)
51% identity, 97% coverage: 7:272/275 of query aligns to 5:275/277 of 1m9hA
- active site: D44 (= D46), Y49 (= Y51), K74 (= K76), H107 (= H107)
- binding nicotinamide-adenine-dinucleotide: G19 (= G21), Y21 (≠ W23), Y49 (= Y51), H107 (= H107), Q160 (= Q160), W186 (= W186), G187 (≠ S187), P188 (= P188), L189 (= L189), Q191 (= Q191), A214 (= A214), F229 (≠ I229), P230 (= P230), G231 (≠ K231), H237 (≠ R237), N241 (= N241)
4gieA Crystal structure of prostaglandin f synthase from trypanosoma cruzi bound to NADP (see paper)
45% identity, 99% coverage: 2:273/275 of query aligns to 10:283/288 of 4gieA
- active site: D55 (= D46), Y60 (= Y51), K85 (= K76), H118 (= H107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G29 (= G21), W31 (= W23), D55 (= D46), Y60 (= Y51), H118 (= H107), W119 (= W108), N148 (= N139), Q169 (= Q160), W195 (= W186), S196 (= S187), P197 (= P188), L198 (= L189), S200 (≠ Q191), L207 (≠ F197), A224 (= A214), I239 (= I229), P240 (= P230), K241 (= K231), S242 (= S232), R247 (= R237), E250 (= E240), N251 (= N241)
4fziA Crystal structure of prostaglandin f synthase from trypanosoma cruzi (see paper)
45% identity, 98% coverage: 5:273/275 of query aligns to 2:272/277 of 4fziA
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)
43% identity, 100% coverage: 2:275/275 of query aligns to 10:282/283 of A0QV09
- G196 (≠ S187) binding
- L198 (= L189) binding
- V200 (≠ Q191) binding
- I236 (= I229) binding
- R238 (≠ K231) binding
- S239 (= S232) binding
- A240 (≠ V233) binding
- R244 (= R237) binding
- S247 (≠ E240) binding
- N248 (= N241) binding
- R274 (≠ G267) binding
2wzmA Crystal structure of a mycobacterium aldo-keto reductase in its apo and liganded form (see paper)
43% identity, 100% coverage: 2:275/275 of query aligns to 1:273/274 of 2wzmA
- active site: D44 (= D46), Y49 (= Y51), K74 (= K76), H107 (= H107)
- 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: Y186 (≠ W186), G187 (≠ S187), P188 (= P188), L189 (= L189), G190 (≠ A190), V191 (≠ Q191), G192 (= G192), L195 (≠ F197), A212 (= A214), I227 (= I229), R229 (≠ K231), S230 (= S232), R235 (= R237), N239 (= N241), R265 (≠ G267)
4g5dA X-ray crystal structure of prostaglandin f synthase from leishmania major friedlin bound to NADPH (see paper)
44% identity, 97% coverage: 5:272/275 of query aligns to 6:280/283 of 4g5dA
- active site: D48 (= D46), Y53 (= Y51), K78 (= K76), H111 (= H107)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G22 (= G21), V23 (= V22), W24 (= W23), D48 (= D46), Y53 (= Y51), H111 (= H107), S148 (≠ C138), N149 (= N139), Q170 (= Q160), W196 (= W186), S197 (= S187), P198 (= P188), L199 (= L189), Q201 (= Q191), G202 (= G192), L205 (≠ F197), I237 (= I229), P238 (= P230), K239 (= K231), S240 (= S232), V241 (= V233), H242 (≠ T234), R245 (= R237), E248 (= E240), N249 (= N241)
Q9GV41 9,11-endoperoxide prostaglandin H2 reductase; Prostaglandin F2-alpha synthase; EC 1.1.1.- from Trypanosoma brucei brucei
42% identity, 99% coverage: 1:273/275 of query aligns to 1:272/276 of Q9GV41
1vbjA The crystal structure of prostaglandin f synthase from trypanosoma brucei
42% identity, 99% coverage: 1:273/275 of query aligns to 6:277/281 of 1vbjA
- active site: D52 (= D46), Y57 (= Y51), K82 (= K76), H115 (= H107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G26 (= G21), M27 (≠ V22), W28 (= W23), D52 (= D46), Y57 (= Y51), H115 (= H107), N145 (= N139), Q166 (= Q160), W192 (= W186), S193 (= S187), P194 (= P188), L195 (= L189), Q197 (= Q191), G198 (= G192), V201 (≠ F197), A218 (= A214), I233 (= I229), K235 (= K231), S236 (= S232), G237 (≠ V233), R241 (= R237), E244 (= E240), N245 (= N241)
1vp5A Crystal structure of 2,5-diketo-d-gluconic acid reductase (tm1009) from thermotoga maritima at 2.40 a resolution
45% identity, 94% coverage: 7:264/275 of query aligns to 5:265/284 of 1vp5A
- active site: D44 (= D46), Y49 (= Y51), K78 (= K76), H111 (= H107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G21), V20 (= V22), F21 (≠ W23), D44 (= D46), Y49 (= Y51), N140 (= N139), Q161 (= Q160), W187 (= W186), G188 (≠ S187), P189 (= P188), F190 (≠ L189), E192 (≠ Q191), F198 (= F197), A215 (= A214), I230 (= I229), K232 (= K231), T233 (≠ S232), V234 (= V233), R238 (= R237), E241 (= E240), N242 (= N241)
3d3fA Crystal structure of yvgn and cofactor NADPH from bacillus subtilis (see paper)
45% identity, 97% coverage: 6:273/275 of query aligns to 7:273/275 of 3d3fA
- active site: D48 (= D46), Y53 (= Y51), K78 (= K76), H111 (= H107)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G22 (= G21), F24 (≠ W23), D48 (= D46), Y53 (= Y51), H111 (= H107), S140 (≠ C138), N141 (= N139), Q162 (= Q160), W188 (= W186), S189 (= S187), P190 (= P188), L191 (= L189), Q193 (= Q191), L197 (≠ F197), I229 (= I229), K231 (= K231), S232 (= S232), K234 (≠ T234), R237 (= R237), E240 (= E240), N241 (= N241)
3b3dA B.Subtilis ytbe (see paper)
47% identity, 96% coverage: 9:273/275 of query aligns to 11:278/280 of 3b3dA
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)
40% identity, 95% coverage: 6:266/275 of query aligns to 11:300/312 of P14065
- Q29 (= Q24) mutation to K: Decreases catalytic activity.
- Y56 (= Y51) mutation to L: Loss of catalytic activity.
- K264 (= K231) mutation to R: Decreases catalytic activity.
- N267 (≠ T234) mutation to Q: Decreases catalytic activity.
- R270 (= R237) mutation R->H,Y,K: Decreases catalytic activity.
H9JTG9 Aldo-keto reductase AKR2E4; 3-dehydroecdysone reductase; Aldo-keto reductase 2E; EC 1.1.1.- from Bombyx mori (Silk moth) (see paper)
41% identity, 95% coverage: 6:266/275 of query aligns to 7:294/308 of H9JTG9
- 22:29 (vs. 21:25, 13% identical) binding
- D53 (= D46) binding
- SN 158:159 (≠ CN 138:139) binding
- R215 (≠ Q191) binding
- 259:269 (vs. 231:241, 55% identical) binding
3wczA Crystal structure of bombyx mori aldo-keto reductase (akr2e4) in complex with NADP (see paper)
41% identity, 95% coverage: 6:266/275 of query aligns to 6:293/307 of 3wczA
- active site: D52 (= D46), Y57 (= Y51), K86 (= K76), H119 (= H107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G21 (= G21), T22 (≠ V22), G23 (≠ W23), T26 (vs. gap), D52 (= D46), Y57 (= Y51), H119 (= H107), Q179 (= Q160), Y205 (≠ W186), S206 (= S187), P207 (= P188), F208 (≠ L189), R214 (≠ Q191), I256 (= I229), P257 (= P230), K258 (= K231), S259 (= S232), T260 (≠ V233), R264 (= R237), N268 (= N241)
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)
36% identity, 95% coverage: 5:265/275 of query aligns to 4:297/325 of P14550
- Y50 (= Y51) active site, Proton donor; mutation to F: Complete loss of enzymatic activity.; mutation to H: Complete loss of enzymatic activity.
- N52 (= N53) to S: reduced activity towards daunorubicin; dbSNP:rs2229540
- E55 (≠ G56) to D: reduced activity towards daunorubicin; dbSNP:rs6690497
- K80 (= K76) Lowers pKa of active site Tyr; mutation to M: Complete loss of enzymatic activity.
- H113 (= H107) binding ; mutation to Q: Strong decrease in enzymatic activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 299 I→A: No change in enzymatic activity.; I→C: No change in enzymatic activity.
- 300 V→C: No change in enzymatic activity.
7s5fB Crystal structure of mannose-6-phosphate reductase from celery (apium graveolens) leaves with NADP+ and mannonic acid bound (see paper)
37% identity, 94% coverage: 7:265/275 of query aligns to 3:295/309 of 7s5fB
- binding d-mannonic acid: W19 (= W23), D46 (≠ A50), Y47 (= Y51), W78 (= W78), H107 (= H107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G17 (= G21), V18 (= V22), W19 (= W23), D42 (= D46), Y47 (= Y51), N161 (= N139), Q182 (= Q160), H208 (≠ W186), T209 (≠ S187), P210 (= P188), L211 (= L189), G213 (≠ Q191), A214 (vs. gap), A244 (= A214), I259 (= I229), K261 (= K231), S262 (= S232), S263 (≠ V233), R267 (= R237), E270 (= E240), N271 (= N241)
Query Sequence
>17089 FitnessBrowser__Keio:17089
MANPTVIKLQDGNVMPQLGLGVWQASNEEVITAIQKALEVGYRSIDTAAAYKNEEGVGKA
LKNASVNREELFITTKLWNDDHKRPREALLDSLKKLQLDYIDLYLMHWPVPAIDHYVEAW
KGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHK
IQTESWSPLAQGGKGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAE
NFDVWDFRLDKDELGEIAKLDQGKRLGPDPDQFGG
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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