SitesBLAST
Comparing SMa1410 FitnessBrowser__Smeli:SMa1410 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)
3b3dA B.Subtilis ytbe (see paper)
37% identity, 90% coverage: 16:263/277 of query aligns to 21:271/280 of 3b3dA
1vbjA The crystal structure of prostaglandin f synthase from trypanosoma brucei
34% identity, 88% coverage: 16:258/277 of query aligns to 24:266/281 of 1vbjA
- active site: D52 (= D43), Y57 (= Y48), K82 (= K73), H115 (= H106)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G26 (= G18), M27 (≠ T19), W28 (≠ Y20), D52 (= D43), Y57 (= Y48), H115 (= H106), N145 (= N137), Q166 (= Q158), W192 (≠ Y184), S193 (≠ C185), P194 (≠ S186), L195 (≠ V187), Q197 (≠ R189), G198 (= G190), V201 (≠ F193), A218 (= A210), I233 (≠ N225), K235 (≠ M227), S236 (= S228), G237 (≠ T229), R241 (≠ N233), E244 (≠ A236), N245 (= N237)
Q9GV41 9,11-endoperoxide prostaglandin H2 reductase; Prostaglandin F2-alpha synthase; EC 1.1.1.- from Trypanosoma brucei brucei
34% identity, 88% coverage: 16:258/277 of query aligns to 19:261/276 of Q9GV41
3d3fA Crystal structure of yvgn and cofactor NADPH from bacillus subtilis (see paper)
37% identity, 87% coverage: 16:257/277 of query aligns to 20:261/275 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 (= S136), N141 (= N137), Q162 (= Q158), W188 (≠ Y184), S189 (≠ C185), P190 (≠ S186), L191 (≠ V187), Q193 (≠ R189), L197 (≠ F193), I229 (≠ N225), K231 (≠ M227), S232 (= S228), K234 (= K230), R237 (≠ N233), E240 (≠ A236), 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)
35% identity, 88% coverage: 14:256/277 of query aligns to 15:258/275 of A0QV10
Sites not aligning to the query:
- 262 modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
4g5dA X-ray crystal structure of prostaglandin f synthase from leishmania major friedlin bound to NADPH (see paper)
34% identity, 90% coverage: 14:262/277 of query aligns to 18:273/283 of 4g5dA
- active site: D48 (= D43), Y53 (= Y48), K78 (= K73), H111 (= H106)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G22 (= G18), V23 (≠ T19), W24 (≠ Y20), D48 (= D43), Y53 (= Y48), H111 (= H106), S148 (= S136), N149 (= N137), Q170 (= Q158), W196 (≠ Y184), S197 (≠ C185), P198 (≠ S186), L199 (≠ V187), Q201 (≠ R189), G202 (= G190), L205 (≠ F193), I237 (≠ N225), P238 (≠ T226), K239 (≠ M227), S240 (= S228), V241 (≠ T229), H242 (≠ K230), R245 (≠ N233), E248 (≠ A236), N249 (= 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)
33% identity, 89% coverage: 16:262/277 of query aligns to 26:274/283 of A0QV09
- G196 (≠ C185) binding
- L198 (≠ V187) binding
- V200 (≠ R189) binding
- I236 (≠ N225) binding
- R238 (≠ M227) binding
- S239 (= S228) binding
- A240 (≠ T229) binding
- R244 (≠ N233) binding
- S247 (≠ A236) binding
- N248 (= N237) binding
- R274 (= R262) binding
2wzmA Crystal structure of a mycobacterium aldo-keto reductase in its apo and liganded form (see paper)
33% identity, 89% coverage: 16:262/277 of query aligns to 17:265/274 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 (= Y184), G187 (≠ C185), P188 (≠ S186), L189 (≠ V187), G190 (≠ A188), V191 (≠ R189), G192 (= G190), L195 (≠ F193), A212 (= A210), I227 (≠ N225), R229 (≠ M227), S230 (= S228), R235 (≠ N233), N239 (= N237), R265 (= R262)
4fziA Crystal structure of prostaglandin f synthase from trypanosoma cruzi (see paper)
33% identity, 88% coverage: 14:257/277 of query aligns to 14:260/277 of 4fziA
4gieA Crystal structure of prostaglandin f synthase from trypanosoma cruzi bound to NADP (see paper)
33% identity, 88% coverage: 14:257/277 of query aligns to 25:271/288 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 (= W107), N148 (= N137), Q169 (= Q158), W195 (≠ Y184), S196 (≠ C185), P197 (≠ S186), L198 (≠ V187), S200 (≠ R189), L207 (≠ F193), A224 (= A210), I239 (≠ N225), P240 (≠ T226), K241 (≠ M227), S242 (= S228), R247 (≠ N233), E250 (≠ A236), N251 (= 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)
35% identity, 88% coverage: 14:257/277 of query aligns to 15:261/277 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 (= Q158), W186 (≠ Y184), G187 (≠ C185), P188 (≠ S186), L189 (≠ V187), Q191 (≠ R189), A214 (= A210), F229 (≠ N225), P230 (≠ T226), G231 (≠ M227), H237 (≠ N233), N241 (= N237)
5uxfA Crystal structure of mouse recon (akr1c13) in complex with cyclic di- amp (see paper)
33% identity, 94% coverage: 16:275/277 of query aligns to 23:310/316 of 5uxfA
- active site: D53 (= D43), Y58 (= Y48), K87 (= K73), H120 (= H106)
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: Y27 (= Y20), G220 (≠ C185), L222 (≠ V187), T224 (≠ R189), A246 (= A210), Q263 (≠ M227), S264 (= S228), E269 (≠ N233), N273 (= N237), L299 (= L264)
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 1.1.1.372; EC 1.1.1.54; EC 1.1.1.19; EC 1.1.1.20 from Rattus norvegicus (Rat) (see paper)
29% identity, 90% coverage: 16:264/277 of query aligns to 18:299/325 of P51635
- K23 (= K23) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K30 (= K28) Not glycated
- K34 (≠ R32) Not glycated
- K61 (≠ A59) Not glycated
- K68 (vs. gap) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K80 (= K73) Not glycated
- K85 (≠ N78) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K97 (≠ A90) Not glycated
- K127 (vs. gap) Not glycated
- K134 (vs. gap) Not glycated
- K141 (≠ A115) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K145 (≠ R119) Not glycated
- K153 (≠ I127) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K157 (≠ R131) Not glycated
- K240 (≠ R204) Not glycated
- K257 (≠ G221) Not glycated
- K263 (≠ M227) Not glycated
- K287 (= K251) Not glycated
- K294 (≠ T259) Not glycated
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylthreonine
- 13 Not glycated
- 308 Not glycated
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)
35% identity, 88% coverage: 14:257/277 of query aligns to 16:262/278 of P06632
- Y50 (= Y48) active site, Proton donor
- H108 (= H106) binding
- 188:242 (vs. 185:237, 35% 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)
35% identity, 88% coverage: 14:257/277 of query aligns to 15:261/277 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 (= S136), Q160 (= Q158), W186 (≠ Y184), G187 (≠ C185), P188 (≠ S186), L189 (≠ V187), Q191 (≠ R189), A214 (= A210), F229 (≠ N225), K231 (≠ M227), S232 (= S228), V233 (≠ T229), R234 (≠ K230), R237 (≠ N233), E240 (≠ A236), N241 (= N237)
5jh2A Crystal structure of the holo form of akr4c7 from maize (see paper)
32% identity, 85% coverage: 16:250/277 of query aligns to 16:247/257 of 5jh2A
- active site: D43 (= D43), Y48 (= Y48), K77 (= K73), H110 (= H106)
- binding adenosine-2'-5'-diphosphate: S185 (≠ C185), P186 (≠ S186), L187 (≠ V187), G188 (= G190), A208 (= A210), K225 (≠ M227), S226 (= S228), T227 (= T229), R231 (≠ N233), N235 (= N237)
3h4gA Structure of aldehyde reductase holoenzyme in complex with potent aldose reductase inhibitor fidarestat: implications for inhibitor binding and selectivity (see paper)
30% identity, 93% coverage: 16:273/277 of query aligns to 18:307/320 of 3h4gA
- active site: D45 (= D43), Y50 (= Y48), K80 (= K73), H113 (= H106)
- binding (2s,4s)-2-aminoformyl-6-fluoro-spiro[chroman-4,4'-imidazolidine]-2',5'-dione: W22 (≠ Y20), Y50 (= Y48), H113 (= H106), W114 (= W107), W220 (vs. gap), I299 (≠ L264), V300 (≠ A266), P301 (≠ G267)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G18), T21 (= T19), W22 (≠ Y20), D45 (= D43), Y50 (= Y48), H113 (= H106), S162 (= S136), N163 (= N137), Q184 (= Q158), Y210 (= Y184), S211 (≠ C185), P212 (≠ S186), L213 (≠ V187), S215 (≠ R189), D217 (≠ E191), A246 (= A210), I261 (≠ N225), P262 (≠ T226), K263 (≠ M227), S264 (= S228), V265 (≠ T229), T266 (≠ K230), R269 (≠ N233), Q272 (≠ A236), N273 (= N237)
3fx4A Porcine aldehyde reductase in ternary complex with inhibitor (see paper)
29% identity, 90% coverage: 16:264/277 of query aligns to 18:299/325 of 3fx4A
- active site: D45 (= D43), Y50 (= Y48), K80 (= K73), H113 (= H106)
- binding [(5Z)-5-{[3-(carboxymethoxy)-4-methoxyphenyl]methylidene}-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid: W22 (≠ Y20), Y50 (= Y48), H113 (= H106), R218 (vs. gap), A219 (vs. gap), F298 (≠ I263), I299 (≠ L264)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G18), T21 (= T19), W22 (≠ Y20), D45 (= D43), Y50 (= Y48), H113 (= H106), Q184 (= Q158), Y210 (= Y184), S211 (≠ C185), P212 (≠ S186), L213 (≠ V187), S215 (≠ R189), A246 (= A210), I261 (≠ N225), P262 (≠ T226), K263 (≠ M227), S264 (= S228), V265 (≠ T229), T266 (≠ K230), R269 (≠ N233), Q272 (≠ A236), N273 (= N237)
Sites not aligning to the query:
P50578 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 Sus scrofa (Pig) (see paper)
29% identity, 90% coverage: 16:264/277 of query aligns to 18:299/325 of P50578
- Y50 (= Y48) active site, Proton donor
- H113 (= H106) binding
- 211:273 (vs. 185:237, 22% identical) binding
3cv7A Crystal structure of porcine aldehyde reductase ternary complex (see paper)
29% identity, 90% coverage: 16:264/277 of query aligns to 18:299/322 of 3cv7A
- active site: D45 (= D43), Y50 (= Y48), K80 (= K73), H113 (= H106)
- binding 3,5-dichloro-2-hydroxybenzoic acid: W22 (≠ Y20), Y50 (= Y48), W82 (≠ H75), H113 (= H106)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G18), T21 (= T19), W22 (≠ Y20), Y50 (= Y48), H113 (= H106), Q184 (= Q158), Y210 (= Y184), S211 (≠ C185), P212 (≠ S186), L213 (≠ V187), S215 (≠ R189), A246 (= A210), I261 (≠ N225), P262 (≠ T226), K263 (≠ M227), S264 (= S228), V265 (≠ T229), T266 (≠ K230), R269 (≠ N233), Q272 (≠ A236), N273 (= N237)
Sites not aligning to the query:
Query Sequence
>SMa1410 FitnessBrowser__Smeli:SMa1410
MGGPMSVYFEKSYQRGFGTYPLKGEPLKAAVREAITVGYRAFDTAQMYGNEAETGEALAE
SGLARDELCITTKVHPDNYSEEAFLPSVEASLKALRVDQADVLMLHWPEINGENARSLRL
LQKAFDIGLARNIGVSNYTAPMMREAQSIVEAPLVTNQVEFHPLIDQSRLLDAAEETKIA
LSSYCSVARGEVFKHPVFAEIGARYGKTAAQTVLRWILQKGVSMNTMSTKPENIRANFEI
LDFALSPHDMKRIDAMNATNYRILKAGMLPWVPDWDR
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