SitesBLAST
Comparing 350911 FitnessBrowser__Btheta:350911 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)
1vp5A Crystal structure of 2,5-diketo-d-gluconic acid reductase (tm1009) from thermotoga maritima at 2.40 a resolution
58% identity, 99% coverage: 4:278/278 of query aligns to 5:283/284 of 1vp5A
- active site: D44 (= D43), Y49 (= Y48), K78 (= K73), H111 (= H106)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G18), V20 (= V19), F21 (≠ Y20), D44 (= D43), Y49 (= Y48), N140 (= N135), Q161 (= Q156), W187 (= W182), G188 (= G183), P189 (= P184), F190 (= F185), E192 (= E187), F198 (= F193), A215 (= A210), I230 (= I225), K232 (= K227), T233 (≠ S228), V234 (≠ T229), R238 (= R233), E241 (= E236), N242 (= N237)
Q9GV41 9,11-endoperoxide prostaglandin H2 reductase; Prostaglandin F2-alpha synthase; EC 1.1.1.- from Trypanosoma brucei brucei
44% identity, 92% coverage: 2:257/278 of query aligns to 5:260/276 of Q9GV41
4g5dA X-ray crystal structure of prostaglandin f synthase from leishmania major friedlin bound to NADPH (see paper)
44% identity, 96% coverage: 4:270/278 of query aligns to 8:277/283 of 4g5dA
- active site: D48 (= D43), Y53 (= Y48), K78 (= K73), H111 (= H106)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G22 (= G18), V23 (= V19), W24 (≠ Y20), D48 (= D43), Y53 (= Y48), H111 (= H106), S148 (= S134), N149 (= N135), Q170 (= Q156), W196 (= W182), S197 (≠ G183), P198 (= P184), L199 (≠ F185), Q201 (≠ E187), G202 (= G188), L205 (≠ F193), I237 (= I225), P238 (= P226), K239 (= K227), S240 (= S228), V241 (≠ T229), H242 (≠ R230), R245 (= R233), E248 (= E236), N249 (= N237)
1vbjA The crystal structure of prostaglandin f synthase from trypanosoma brucei
44% identity, 92% coverage: 2:257/278 of query aligns to 10:265/281 of 1vbjA
- active site: D52 (= D43), Y57 (= Y48), K82 (= K73), H115 (= H106)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G26 (= G18), M27 (≠ V19), W28 (≠ Y20), D52 (= D43), Y57 (= Y48), H115 (= H106), N145 (= N135), Q166 (= Q156), W192 (= W182), S193 (≠ G183), P194 (= P184), L195 (≠ F185), Q197 (≠ E187), G198 (= G188), V201 (≠ F193), A218 (= A210), I233 (= I225), K235 (= K227), S236 (= S228), G237 (≠ T229), R241 (= R233), E244 (= E236), N245 (= N237)
3d3fA Crystal structure of yvgn and cofactor NADPH from bacillus subtilis (see paper)
49% identity, 94% coverage: 2:262/278 of query aligns to 6:266/275 of 3d3fA
- active site: D48 (= D43), Y53 (= Y48), K78 (= K73), H111 (= H106)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G22 (= G18), F24 (≠ Y20), D48 (= D43), Y53 (= Y48), H111 (= H106), S140 (= S134), N141 (= N135), Q162 (= Q156), W188 (= W182), S189 (≠ G183), P190 (= P184), L191 (≠ F185), Q193 (≠ E187), L197 (≠ F193), I229 (= I225), K231 (= K227), S232 (= S228), K234 (≠ R230), R237 (= R233), E240 (= E236), N241 (= N237)
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)
42% identity, 97% coverage: 4:274/278 of query aligns to 5:273/275 of A0QV10
- K262 (≠ E260) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
4fziA Crystal structure of prostaglandin f synthase from trypanosoma cruzi (see paper)
44% identity, 93% coverage: 4:262/278 of query aligns to 4:265/277 of 4fziA
4gieA Crystal structure of prostaglandin f synthase from trypanosoma cruzi bound to NADP (see paper)
44% identity, 93% coverage: 4:262/278 of query aligns to 15:276/288 of 4gieA
- active site: D55 (= D43), Y60 (= Y48), K85 (= K73), H118 (= H106)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G29 (= G18), W31 (≠ Y20), D55 (= D43), Y60 (= Y48), H118 (= H106), W119 (≠ Q107), N148 (= N135), Q169 (= Q156), W195 (= W182), S196 (≠ G183), P197 (= P184), L198 (≠ F185), S200 (≠ E187), L207 (≠ F193), A224 (= A210), I239 (= I225), P240 (= P226), K241 (= K227), S242 (= S228), R247 (= R233), E250 (= E236), N251 (= N237)
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)
41% identity, 94% coverage: 1:261/278 of query aligns to 3:266/278 of P06632
- Y50 (= Y48) active site, Proton donor
- H108 (= H106) binding
- 188:242 (vs. 183:237, 40% identical) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1a80A Native 2,5-diketo-d-gluconic acid reductase a from corynbacterium sp. Complexed with NADPH (see paper)
41% identity, 94% coverage: 1:261/278 of query aligns to 2:265/277 of 1a80A
- active site: D44 (= D43), Y49 (= Y48), K74 (= K73), H107 (= H106)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G19 (= G18), F21 (≠ Y20), D44 (= D43), Y49 (= Y48), H107 (= H106), S138 (= S134), Q160 (= Q156), W186 (= W182), G187 (= G183), P188 (= P184), L189 (≠ F185), Q191 (≠ E187), A214 (= A210), F229 (≠ I225), K231 (= K227), S232 (= S228), V233 (≠ T229), R234 (= R230), R237 (= R233), E240 (= E236), N241 (= N237)
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)
40% identity, 94% coverage: 1:261/278 of query aligns to 2:265/277 of 1m9hA
- active site: D44 (= D43), Y49 (= Y48), K74 (= K73), H107 (= H106)
- binding nicotinamide-adenine-dinucleotide: G19 (= G18), Y21 (= Y20), Y49 (= Y48), H107 (= H106), Q160 (= Q156), W186 (= W182), G187 (= G183), P188 (= P184), L189 (≠ F185), Q191 (≠ E187), A214 (= A210), F229 (≠ I225), P230 (= P226), G231 (≠ K227), H237 (≠ R233), N241 (= N237)
3b3dA B.Subtilis ytbe (see paper)
45% identity, 91% coverage: 6:258/278 of query aligns to 11:267/280 of 3b3dA
3wbwA Crystal structure of gox0644 in complex with NADPH
36% identity, 97% coverage: 4:274/278 of query aligns to 6:271/271 of 3wbwA
- active site: D45 (= D43), Y50 (= Y48), K71 (= K73), H104 (= H106)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G20 (= G18), H104 (= H106), N136 (= N135), W183 (= W182), R184 (≠ G183), P185 (= P184), L186 (≠ F185), L192 (≠ F193), A209 (= A210), K226 (= K227), S227 (= S228), V228 (≠ T229), R232 (= R233), E235 (= E236), N236 (= N237)
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)
38% identity, 92% coverage: 1:257/278 of query aligns to 11:268/283 of A0QV09
- G196 (= G183) binding
- L198 (≠ F185) binding
- V200 (≠ E187) binding
- I236 (= I225) binding
- R238 (≠ K227) binding
- S239 (= S228) binding
- A240 (≠ T229) binding
- R244 (= R233) binding
- S247 (≠ E236) binding
- N248 (= N237) binding
Sites not aligning to the query:
2wzmA Crystal structure of a mycobacterium aldo-keto reductase in its apo and liganded form (see paper)
38% identity, 92% coverage: 1:257/278 of query aligns to 2:259/274 of 2wzmA
- active site: D44 (= D43), Y49 (= Y48), K74 (= K73), H107 (= H106)
- 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 (≠ W182), G187 (= G183), P188 (= P184), L189 (≠ F185), G190 (≠ A186), V191 (≠ E187), G192 (= G188), L195 (≠ F193), A212 (= A210), I227 (= I225), R229 (≠ K227), S230 (= S228), R235 (= R233), N239 (= N237)
Sites not aligning to the query:
3h7uA Crystal structure of the plant stress-response enzyme akr4c9 (see paper)
38% identity, 87% coverage: 5:245/278 of query aligns to 6:271/312 of 3h7uA
- active site: S24 (≠ T23), D44 (= D43), Y49 (= Y48), K78 (= K73), H111 (= H106)
- binding acetate ion: W21 (≠ Y20), Y49 (= Y48), H111 (= H106)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G18), T20 (≠ V19), W21 (≠ Y20), D44 (= D43), Y49 (= Y48), H111 (= H106), W112 (≠ Q107), N156 (= N135), Q177 (= Q156), Y203 (≠ W182), S204 (≠ G183), P205 (= P184), L206 (≠ F185), S208 (≠ E187), P209 (≠ G188), G210 (≠ R189), A236 (= A210), L251 (≠ I225), P252 (= P226), K253 (= K227), S254 (= S228), R259 (= R233), E262 (= E236), N263 (= N237)
Q0PGJ6 NADPH-dependent aldo-keto reductase, chloroplastic; AtChlAKR; Aldo-keto reductase family 4 member C9; EC 1.1.1.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
38% identity, 87% coverage: 5:245/278 of query aligns to 9:274/315 of Q0PGJ6
5jh2A Crystal structure of the holo form of akr4c7 from maize (see paper)
40% identity, 86% coverage: 6:245/278 of query aligns to 6:243/257 of 5jh2A
- active site: D43 (= D43), Y48 (= Y48), K77 (= K73), H110 (= H106)
- binding adenosine-2'-5'-diphosphate: S185 (≠ G183), P186 (= P184), L187 (≠ F185), G188 (≠ A186), A208 (= A210), K225 (= K227), S226 (= S228), T227 (= T229), R231 (= R233), N235 (= N237)
5zcmA Crystal structure of xylose reductase from debaryomyces nepalensis in complex with NADP-dtt adduct (see paper)
36% identity, 93% coverage: 1:258/278 of query aligns to 9:309/329 of 5zcmA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G26 (= G18), C27 (≠ V19), W28 (≠ Y20), D51 (= D43), Y56 (= Y48), H118 (= H106), Q195 (= Q156), Y221 (≠ V179), S222 (≠ M180), F224 (≠ W182), Q227 (vs. gap), S228 (vs. gap), F244 (= F193), A261 (= A210), I276 (= I225), K278 (= K227), S279 (= S228), R284 (= R233), N288 (= N237)
O80944 Aldo-keto reductase family 4 member C8; EC 1.1.1.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
38% identity, 86% coverage: 6:245/278 of query aligns to 10:270/311 of O80944
Query Sequence
>350911 FitnessBrowser__Btheta:350911
METVRLNNGVEMPILGYGVYQVTPEECERCVLDAISVGYRSIDTAQAYYNEEGVGNAVRK
CGVPREELFITTKVWISNGGYEKAKASIDESLRKLQSDYVDLLLIHQPFNDYYGTYRAME
EAYKAGKARAIGVSNFYPDRFIDLAEFCEIKPAVNQVETHVFNQQVKPQEIMKKYDTKVM
SWGPFAEGRNNFFSNEVLKAIGEQYGKSVAQVALRFLIQRDIIVIPKSTRKERMIENFDV
FDFTLSVKDMEEIAGLDKKESLFFSHYDPEMVNFLINL
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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