SitesBLAST
Comparing WP_011840731.1 NCBI__GCF_000015985.1:WP_011840731.1 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)
50% identity, 100% coverage: 1:272/272 of query aligns to 1:272/275 of A0QV10
- K262 (≠ T262) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
3wbwA Crystal structure of gox0644 in complex with NADPH
50% identity, 99% coverage: 3:270/272 of query aligns to 4:268/271 of 3wbwA
- active site: D45 (= D44), Y50 (= Y49), K71 (= K74), H104 (= H107)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G20 (= G19), H104 (= H107), N136 (= N139), W183 (= W186), R184 (≠ S187), P185 (= P188), L186 (= L189), L192 (≠ F195), A209 (= A212), K226 (≠ R229), S227 (= S230), V228 (≠ T231), R232 (≠ G235), E235 (= E238), N236 (= N239)
4g5dA X-ray crystal structure of prostaglandin f synthase from leishmania major friedlin bound to NADPH (see paper)
45% identity, 98% coverage: 3:268/272 of query aligns to 6:278/283 of 4g5dA
- active site: D48 (= D44), Y53 (= Y49), K78 (= K74), H111 (= H107)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G22 (= G19), V23 (≠ L20), W24 (= W21), D48 (= D44), Y53 (= Y49), H111 (= H107), S148 (= S138), N149 (= N139), Q170 (= Q160), W196 (= W186), S197 (= S187), P198 (= P188), L199 (= L189), Q201 (≠ R191), G202 (= G192), L205 (≠ F195), I237 (= I227), P238 (= P228), K239 (≠ R229), S240 (= S230), V241 (≠ T231), H242 (≠ R232), R245 (≠ G235), E248 (= E238), N249 (= N239)
4gieA Crystal structure of prostaglandin f synthase from trypanosoma cruzi bound to NADP (see paper)
44% identity, 99% coverage: 4:271/272 of query aligns to 14:283/288 of 4gieA
- active site: D55 (= D44), Y60 (= Y49), K85 (= K74), H118 (= H107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G29 (= G19), W31 (= W21), D55 (= D44), Y60 (= Y49), H118 (= H107), W119 (= W108), N148 (= N139), Q169 (= Q160), W195 (= W186), S196 (= S187), P197 (= P188), L198 (= L189), S200 (≠ R191), L207 (≠ F195), A224 (= A212), I239 (= I227), P240 (= P228), K241 (≠ R229), S242 (= S230), R247 (≠ G235), E250 (= E238), N251 (= N239)
4fziA Crystal structure of prostaglandin f synthase from trypanosoma cruzi (see paper)
45% identity, 97% coverage: 7:271/272 of query aligns to 6:272/277 of 4fziA
Q9GV41 9,11-endoperoxide prostaglandin H2 reductase; Prostaglandin F2-alpha synthase; EC 1.1.1.- from Trypanosoma brucei brucei
43% identity, 100% coverage: 1:271/272 of query aligns to 3:272/276 of Q9GV41
1vbjA The crystal structure of prostaglandin f synthase from trypanosoma brucei
43% identity, 100% coverage: 1:271/272 of query aligns to 8:277/281 of 1vbjA
- active site: D52 (= D44), Y57 (= Y49), K82 (= K74), H115 (= H107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G26 (= G19), M27 (≠ L20), W28 (= W21), D52 (= D44), Y57 (= Y49), H115 (= H107), N145 (= N139), Q166 (= Q160), W192 (= W186), S193 (= S187), P194 (= P188), L195 (= L189), Q197 (≠ R191), G198 (= G192), V201 (≠ F195), A218 (= A212), I233 (= I227), K235 (≠ R229), S236 (= S230), G237 (≠ T231), R241 (≠ G235), E244 (= E238), N245 (= N239)
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)
47% identity, 96% coverage: 4:265/272 of query aligns to 5:268/278 of P06632
- Y50 (= Y49) active site, Proton donor
- H108 (= H107) binding substrate
- 188:242 (vs. 187:239, 44% identical) binding NADP(+)
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)
47% identity, 96% coverage: 4:265/272 of query aligns to 4:267/277 of 1a80A
- active site: D44 (= D44), Y49 (= Y49), K74 (= K74), H107 (= H107)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), F21 (≠ W21), D44 (= D44), Y49 (= Y49), H107 (= H107), S138 (= S138), Q160 (= Q160), W186 (= W186), G187 (≠ S187), P188 (= P188), L189 (= L189), Q191 (≠ R191), A214 (= A212), F229 (≠ I227), K231 (≠ R229), S232 (= S230), V233 (≠ T231), R234 (= R232), R237 (≠ G235), E240 (= E238), N241 (= N239)
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)
47% identity, 96% coverage: 4:265/272 of query aligns to 4:267/277 of 1m9hA
- active site: D44 (= D44), Y49 (= Y49), K74 (= K74), H107 (= H107)
- binding nicotinamide-adenine-dinucleotide: G19 (= G19), Y21 (≠ W21), Y49 (= Y49), H107 (= H107), Q160 (= Q160), W186 (= W186), G187 (≠ S187), P188 (= P188), L189 (= L189), Q191 (≠ R191), A214 (= A212), F229 (≠ I227), P230 (= P228), G231 (≠ R229), H237 (≠ G235), N241 (= N239)
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)
44% identity, 99% coverage: 4:271/272 of query aligns to 13:280/283 of A0QV09
- G196 (≠ S187) binding NADPH
- L198 (= L189) binding NADPH
- V200 (≠ R191) binding NADPH
- I236 (= I227) binding NADPH
- R238 (= R229) binding NADPH
- S239 (= S230) binding NADPH
- A240 (≠ T231) binding NADPH
- R244 (≠ G235) binding NADPH
- S247 (≠ E238) binding NADPH
- N248 (= N239) binding NADPH
- R274 (≠ G265) binding NADPH
2wzmA Crystal structure of a mycobacterium aldo-keto reductase in its apo and liganded form (see paper)
44% identity, 99% coverage: 4:271/272 of query aligns to 4:271/274 of 2wzmA
- active site: D44 (= D44), Y49 (= Y49), K74 (= K74), 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 (= G190), V191 (≠ R191), G192 (= G192), L195 (≠ F195), A212 (= A212), I227 (= I227), R229 (= R229), S230 (= S230), R235 (≠ G235), N239 (= N239), R265 (≠ G265)
3d3fA Crystal structure of yvgn and cofactor NADPH from bacillus subtilis (see paper)
44% identity, 99% coverage: 1:268/272 of query aligns to 4:270/275 of 3d3fA
- active site: D48 (= D44), Y53 (= Y49), K78 (= K74), H111 (= H107)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G22 (= G19), F24 (≠ W21), D48 (= D44), Y53 (= Y49), H111 (= H107), S140 (= S138), N141 (= N139), Q162 (= Q160), W188 (= W186), S189 (= S187), P190 (= P188), L191 (= L189), Q193 (≠ R191), L197 (≠ F195), I229 (= I227), K231 (≠ R229), S232 (= S230), K234 (≠ R232), R237 (≠ G235), E240 (= E238), N241 (= N239)
3b3dA B.Subtilis ytbe (see paper)
43% identity, 100% coverage: 1:271/272 of query aligns to 5:278/280 of 3b3dA
1vp5A Crystal structure of 2,5-diketo-d-gluconic acid reductase (tm1009) from thermotoga maritima at 2.40 a resolution
40% identity, 94% coverage: 7:261/272 of query aligns to 7:264/284 of 1vp5A
- active site: D44 (= D44), Y49 (= Y49), K78 (= K74), H111 (= H107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G19), V20 (≠ L20), F21 (≠ W21), D44 (= D44), Y49 (= Y49), N140 (= N139), Q161 (= Q160), W187 (= W186), G188 (≠ S187), P189 (= P188), F190 (≠ L189), E192 (vs. gap), F198 (= F195), A215 (= A212), I230 (= I227), K232 (≠ R229), T233 (≠ S230), V234 (≠ T231), R238 (≠ G235), E241 (= E238), N242 (= N239)
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)
37% identity, 94% coverage: 2:258/272 of query aligns to 9:291/312 of P14065
- Q29 (= Q22) mutation to K: Decreases catalytic activity.
- Y56 (= Y49) mutation to L: Loss of catalytic activity.
- K264 (≠ R229) mutation to R: Decreases catalytic activity.
- N267 (≠ R232) mutation to Q: Decreases catalytic activity.
- R270 (≠ G235) mutation R->H,Y,K: Decreases catalytic activity.
P14550 Aldo-keto reductase family 1 member A1; Alcohol dehydrogenase [NADP(+)]; Aldehyde reductase; Glucuronate reductase; Glucuronolactone reductase; S-nitroso-CoA reductase; ScorR; 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; EC 1.6.-.- from Homo sapiens (Human) (see 5 papers)
34% identity, 94% coverage: 7:263/272 of query aligns to 8:297/325 of P14550
- Y50 (= Y49) active site, Proton donor; mutation to A: Abolished reductase activity.; mutation to F: Complete loss of enzymatic activity.; mutation to H: Complete loss of enzymatic activity.
- N52 (= N51) to S: reduced activity towards daunorubicin; dbSNP:rs2229540
- E55 (≠ G54) to D: reduced activity towards daunorubicin; dbSNP:rs6690497
- K80 (= K74) Lowers pKa of active site Tyr; mutation to M: Complete loss of enzymatic activity.
- H113 (= H107) mutation to Q: Strong decrease in enzymatic activity.
- K127 (= K112) mutation to A: Abolished S-nitroso-CoA reductase activity without affecting ability to reduce S-nitrosoglutathione, glyceraldehyde or glucuronate.
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.
- 312 R→A: Abolished S-nitrosoglutathione reductase activity without affecting ability to reduce S-nitroso-CoA.
P51635 Aldo-keto reductase family 1 member A1; 3-DG-reducing enzyme; Alcohol dehydrogenase [NADP(+)]; Aldehyde reductase; Glucuronate reductase; Glucuronolactone reductase; S-nitroso-CoA reductase; ScorR; 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; EC 1.6.-.- from Rattus norvegicus (Rat) (see paper)
34% identity, 97% coverage: 1:263/272 of query aligns to 1:297/325 of P51635
- M1 (= M1) modified: Initiator methionine, Removed
- T2 (= T2) modified: N-acetylthreonine
- K13 (≠ R12) Not glycated
- K23 (≠ Q22) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K30 (≠ A29) Not glycated
- K34 (≠ R33) Not glycated
- K61 (≠ R60) Not glycated
- K68 (vs. gap) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K80 (= K74) Not glycated
- K85 (≠ A79) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K97 (≠ E91) Not glycated
- K127 (= K112) Not glycated
- K134 (vs. gap) Not glycated
- K141 (≠ V117) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K145 (≠ R121) Not glycated
- K153 (≠ E129) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K157 (≠ T133) Not glycated
- K240 (≠ R206) Not glycated
- K257 (≠ G223) Not glycated
- K263 (≠ R229) Not glycated
- K287 (≠ A253) Not glycated
- K294 (≠ A260) Not glycated
Sites not aligning to the query:
H9JTG9 Aldo-keto reductase AKR2E4; 3-dehydroecdysone reductase; Aldo-keto reductase 2E; EC 1.1.1.- from Bombyx mori (Silk moth) (see paper)
38% identity, 96% coverage: 5:264/272 of query aligns to 8:294/308 of H9JTG9
- 22:29 (vs. 17:24, 25% identical) binding NADP(+)
- D53 (= D44) binding NADP(+)
- SN 158:159 (= SN 138:139) binding NADP(+)
- R215 (= R191) binding NADP(+)
- 259:269 (vs. 229:239, 36% identical) binding NADP(+)
Q9JII6 Aldo-keto reductase family 1 member A1; Alcohol dehydrogenase [NADP(+)]; Aldehyde reductase; Glucuronate reductase; Glucuronolactone reductase; S-nitroso-CoA reductase; ScorR; 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; EC 1.6.-.- from Mus musculus (Mouse)
34% identity, 97% coverage: 1:263/272 of query aligns to 1:297/325 of Q9JII6
- M1 (= M1) modified: Initiator methionine, Removed
- T2 (= T2) modified: N-acetylthreonine
Query Sequence
>WP_011840731.1 NCBI__GCF_000015985.1:WP_011840731.1
MTATLEFHDGSRIPQLGFGLWQVPEERTAEVVREALELGYRLADGAAIYGNEEGLGHGLR
TSGLPRDEVFVTTKVWNDAQGFEAALRAVEESLKRLGLDRLDLCLIHWPAPKRNLYVETW
RALIRLRDEGRITSIGVSNFDLDQIDRLTAETGVTPVLNQIELHPMLQQAELRAGHAERG
IVTQSWSPLGRGMAFETPIIREIAERTGRSPAQVVLRWHIELGCSVIPRSTRRAGLAENL
ALFDFELTEADHAAISALDAGTRTGPDPQSFG
Or try a new SitesBLAST search
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